SwissProt Database

A494_ARATH

ID   A494_ARATH     STANDARD;      PRT;   313 AA.
AC   P43295;
DT   01-NOV-1995 (REL. 32, CREATED)
DT   01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   PROBABLE CYSTEINE PROTEINASE A494 PRECURSOR (EC 3.4.22.-) (FRAGMENT).
OS   ARABIDOPSIS THALIANA (MOUSE-EAR CRESS).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE;
OC   CAPPARALES; CRUCIFERAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=CV. LANDSBERG ERECTA;
RX   MEDLINE; 94289649.
RA   WILLIAMS J., BULMAN M., HUTTLY A., PHILLIPS A., NEILL S.;
RL   PLANT MOL. BIOL. 25:259-270(1994).
CC   -!- INDUCTION: BY WILTING AND ABSCISIC ACID (ABA).
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; X74359; G516865; -.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL; GLYCOPROTEIN.
FT   NON_TER       1      1
FT   PROPEP       <1     83       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN        84    313       CYSTEINE PROTEINASE A494.
FT   ACT_SITE    108    108       BY SIMILARITY.
FT   ACT_SITE    251    251       BY SIMILARITY.
FT   ACT_SITE    278    278       BY SIMILARITY.
FT   DISULFID    105    155       BY SIMILARITY.
FT   DISULFID    139    189       BY SIMILARITY.
FT   DISULFID    245    299       BY SIMILARITY.
SQ   SEQUENCE   313 AA;  34307 MW;  90E80911 CRC32;
     ALFKKKFGKV YGSIEEHYYR FSVFKANLLR AMRHQKMDPS ARHGVTQFSD LTRSEFRRKH
     LGVKGGFKLP KDANQAPILP TQNLPEEFDW RDRGAVTPVK NQGSCGSCWS FSTTGALEGA
     HFLATGKLVS LSEQQLVDCD HECDPEEEGS CDSGCNGGLM NSAFEYTLKT GGLMREKDYP
     YTGTDGGSCK LDRSKIVASV SNFSVVSINE DQIAANLIKN GPLAVAINAA YMQTYIGGVS
     CPYICSRRLN HGVLLVGYGS AGFSQARLKE KPYWIIKNSW GESWGENGFY KICKGRNICG
     VDSLVSTVAA TTS

SwissProt Database

ACP1_ENTHI

ID   ACP1_ENTHI     STANDARD;      PRT;   284 AA.
AC   P36184;
DT   01-JUN-1994 (REL. 29, CREATED)
DT   01-JUN-1994 (REL. 29, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE ACP1 PRECURSOR (EC 3.4.22.-) (FRAGMENT).
GN   ACP1.
OS   ENTAMOEBA HISTOLYTICA.
OC   EUKARYOTA; PROTOZOA; SARCOMASTIGOPHORA; SARCODINA; RHIZOPODA; LOBOSA;
OC   AMOEBIDA.
RN   [1]
RP   SEQUENCE FROM N.A., AND SEQUENCE OF 70-77.
RC   STRAIN=HM-1;
RX   MEDLINE; 93232277.
RA   REED S., BOUVIER J., POLLACK A.S., ENGEL J.C., BROWN M., HIRATA K.,
RA   QUE X., EAKIN A., HAGBLOM P., GILLIN F., MCKERROW J.H.;
RL   J. CLIN. INVEST. 91:1532-1540(1993).
RN   [2]
RP   SEQUENCE OF 86-250 FROM N.A.
RX   MEDLINE; 90158686.
RA   EAKIN A.E., BOUVIER J., SAKANARI J.A., CRAIK C.S., MCKERROW J.H.;
RL   MOL. BIOCHEM. PARASITOL. 39:1-8(1990).
CC   -!- FUNCTION: INVOLVED IN PATHOGENICITY. ITS PRESENCE CORRELATES WITH
CC       INCREASED PROTEINASE EXPRESSION AND ACTIVITY IN PATHOGENIC
CC       ISOLATES. PROBABLY INVOLVED IN TISSUE INVASION.
CC   -!- SUBCELLULAR LOCATION: EXTRACELLULAR.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; S58669; G385333; -.
DR   EMBL; M27307; G158934; -.
DR   HSSP; P10056; 1PPO.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; MULTIGENE FAMILY; SIGNAL.
FT   NON_TER       1      1
FT   SIGNAL       <1      ?       POTENTIAL.
FT   PROPEP        ?     69       ACTIVATION PEPTIDE.
FT   CHAIN        70    284       CYSTEINE PROTEINASE ACP1.
FT   ACT_SITE     92     92       BY SIMILARITY.
FT   ACT_SITE    227    227       BY SIMILARITY.
FT   ACT_SITE    247    247       BY SIMILARITY.
FT   DISULFID     89    130       BY SIMILARITY.
FT   DISULFID    123    162       BY SIMILARITY.
FT   CONFLICT    133    133       G -> GH (IN REF. 2).
FT   CONFLICT    245    246       IR -> VK (IN REF. 2).
SQ   SEQUENCE   284 AA;  31273 MW;  9F0EB5B5 CRC32;
     THNKVFANRA EYLYRFAVFL DNKKFVEANA NTELNVFGDM THEEFIQTHL GMTYEVPETT
     SNVKAAVKAA PESVDWRSIM NPAKDQGQCG SCWTFCTTAV LEGRVNKDLG KLYSFSEQQL
     VDCDASDNGC ERGPSNSLKF IQENNGLGLE SDYPYKAVAG TCKKVKNVAT VTGSRRVTDG
     SETGLQTIIA ENGPVAVGMD ASRPSFQLYK KGTIYSDTKC RSRMMNHCVT AVGYGSNSNG
     KYWIIRNSWG TSWGDAGYFL LARDSNNMCG IGRDSNYPTG VKLI

SwissProt Database

ACP2_ENTHI

ID   ACP2_ENTHI     STANDARD;      PRT;   310 AA.
AC   P36185;
DT   01-JUN-1994 (REL. 29, CREATED)
DT   01-JUN-1994 (REL. 29, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE ACP2 PRECURSOR (EC 3.4.22.-) (FRAGMENT).
GN   ACP2.
OS   ENTAMOEBA HISTOLYTICA.
OC   EUKARYOTA; PROTOZOA; SARCOMASTIGOPHORA; SARCODINA; RHIZOPODA; LOBOSA;
OC   AMOEBIDA.
RN   [1]
RP   SEQUENCE FROM N.A., AND SEQUENCE OF 90-97.
RC   STRAIN=HM-1;
RX   MEDLINE; 93232277.
RA   REED S., BOUVIER J., POLLACK A.S., ENGEL J.C., BROWN M., HIRATA K.,
RA   QUE X., EAKIN A., HAGBLOM P., GILLIN F., MCKERROW J.H.;
RL   J. CLIN. INVEST. 91:1532-1540(1993).
CC   -!- FUNCTION: CYSTEINE PROTEINASE PRESENT IN PATHOGENIC AND IN
CC       NONPATHOGENIC ISOLATES.
CC   -!- SUBCELLULAR LOCATION: EXTRACELLULAR.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; S58670; G385335; -.
DR   HSSP; P00785; 1AEC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; MULTIGENE FAMILY; SIGNAL.
FT   NON_TER       1      1
FT   SIGNAL       <1      ?       POTENTIAL.
FT   PROPEP        ?     89       ACTIVATION PEPTIDE.
FT   CHAIN        90    310       CYSTEINE PROTEINASE ACP2.
FT   ACT_SITE    114    114       BY SIMILARITY.
FT   ACT_SITE    254    254       BY SIMILARITY.
FT   ACT_SITE    274    274       BY SIMILARITY.
FT   DISULFID    111    156       BY SIMILARITY.
FT   DISULFID    147    188       BY SIMILARITY.
SQ   SEQUENCE   310 AA;  34204 MW;  37B61BC7 CRC32;
     AAGIRIASAI DFNTWASKNN KHFTAIEKLR RRAIFNMNAK FVDSFNKIGS FKLSVDGPFA
     AMTNEEYRTL LKSKRTTEEN GQVKYLNIQA PESVDWRKEG KVTPLRDQAQ CGSCYTFGSL
     AALEGRLLIE KGGDANTLDL SEEHMQCTRD NGNNGCNGGL GSNVYDYIIE HGVAKESDYP
     YTGSDSTCKT NVKSFRKITG YTKVPRNNEA ELKAALSQGL LDVSIDVSSA KFQLYKSGAY
     TDTKCKNNYF ALNHEVCAVG YGVVDGKECW IVRNSWGTSW GDKGYINMVI EGNTCGVATD
     PLYPTGVQYL

SwissProt Database

ACTN_ACTCH

ID   ACTN_ACTCH     STANDARD;      PRT;   380 AA.
AC   P00785;
DT   21-JUL-1986 (REL. 01, CREATED)
DT   01-JAN-1990 (REL. 13, LAST SEQUENCE UPDATE)
DT   01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE)
DE   ACTINIDAIN PRECURSOR (EC 3.4.22.14) (ACTINIDIN).
OS   ACTINIDIA CHINENSIS (KIWI) (YANGTAO).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE; THEALES;
OC   ACTINIDIACEAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=CV. DELICIOSA;
RX   MEDLINE; 90045955.
RA   PODIVINSKY E., FORSTER R.L.S., GARDNER R.C.;
RL   NUCLEIC ACIDS RES. 17:8363-8363(1989).
RN   [2]
RP   SEQUENCE OF 70-371 FROM N.A.
RA   PRAEKELT U.M., MCKEE R.A., SMITH H.;
RL   PLANT MOL. BIOL. 10:193-202(1988).
RN   [3]
RP   SEQUENCE OF 127-346.
RX   MEDLINE; 78256777.
RA   CARNE A., MOORE C.H.;
RL   BIOCHEM. J. 173:73-83(1978).
RN   [4]
RP   SEQUENCE OF 1-13 FROM N.A.
RX   MEDLINE; 91346716.
RA   KEELING J., MAXWELL P., GARDNER R.C.;
RL   PLANT MOL. BIOL. 15:787-788(1990).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), AND REVISIONS.
RX   MEDLINE; 81072298.
RA   BAKER E.N.;
RL   J. MOL. BIOL. 141:441-484(1980).
CC   -!- CATALYTIC ACTIVITY: SPECIFICITY CLOSE TO THAT OF PAPAIN.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; X16466; G15984; -.
DR   EMBL; X13013; G15957; -.
DR   EMBL; X13139; G15959; -.
DR   EMBL; X57551; G21095; -.
DR   PIR; A00975; TAGB.
DR   PIR; S06587; S06587.
DR   PDB; 2ACT; 15-JAN-86.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL; 3D-STRUCTURE.
FT   SIGNAL        1      ?       POTENTIAL.
FT   PROPEP        ?    126       ACTIVATION PEPTIDE.
FT   CHAIN       127    346       ACTINIDIN.
FT   ACT_SITE    151    151
FT   ACT_SITE    288    288
FT   ACT_SITE    308    308
FT   DISULFID    148    191
FT   DISULFID    182    224
FT   DISULFID    282    332
FT   CONFLICT     96     96       D -> G (IN REF. 2).
FT   CONFLICT    108    108       S -> G (IN REF. 2).
FT   CONFLICT    123    124       FG -> VS (IN REF. 2).
FT   CONFLICT    167    170       VTGV -> TSGS (IN REF. 3).
FT   CONFLICT    181    181       D -> G (IN REF. 2).
FT   CONFLICT    184    184       R -> G (IN REF. 2).
FT   CONFLICT    192    192       N -> D (IN REF. 3).
FT   CONFLICT    206    206       N -> D (IN REF. 3).
FT   CONFLICT    212    212       E -> G (IN REF. 2).
FT   CONFLICT    223    227       ECNLD -> DCDVA (IN REF. 3).
FT   CONFLICT    230    231       NE -> DQ (IN REF. 3).
FT   CONFLICT    240    240       E -> G (IN REF. 2).
FT   CONFLICT    272    274       HYS -> QYA (IN REF. 3).
FT   CONFLICT    286    286       I -> V (IN REF. 3).
FT   CONFLICT    290    291       VT -> IV (IN REF. 3).
FT   CONFLICT    301    301       I -> V (IN REF. 3).
FT   CONFLICT    307    307       K -> E (IN REF. 2).
FT   CONFLICT    349    349       H -> Y (IN REF. 2).
FT   CONFLICT    360    360       P -> S (IN REF. 2).
FT   CONFLICT    371    380       GVDDGQRYSA -> E (IN REF. 2).
FT   STRAND      131    132
FT   HELIX       133    136
FT   TURN        137    137
FT   STRAND      144    144
FT   TURN        146    147
FT   HELIX       151    168
FT   STRAND      174    174
FT   HELIX       176    182
FT   STRAND      185    185
FT   TURN        186    187
FT   STRAND      188    188
FT   HELIX       190    192
FT   HELIX       196    206
FT   TURN        207    207
FT   STRAND      209    209
FT   STRAND      211    211
FT   TURN        212    214
FT   HELIX       226    230
FT   STRAND      234    234
FT   STRAND      238    241
FT   TURN        244    245
FT   HELIX       247    256
FT   STRAND      259    263
FT   HELIX       268    272
FT   STRAND      277    278
FT   STRAND      288    298
FT   TURN        299    300
FT   STRAND      301    307
FT   STRAND      310    310
FT   TURN        312    313
FT   TURN        315    315
FT   STRAND      316    316
FT   TURN        317    318
FT   STRAND      319    323
FT   TURN        328    329
FT   HELIX       331    333
FT   TURN        334    335
FT   STRAND      339    342
SQ   SEQUENCE   380 AA;  42158 MW;  0F4C1A35 CRC32;
     MGLPKSFVSM SLLFFSTLLI LSLAFNAKNL TQRTNDEVKA MYESWLIKYG KSYNSLGEWE
     RRFEIFKETL RFIDEHNADT NRSYKVGLNQ FADLTDEEFR STYLGFTSGS NKTKVSNRYE
     PRFGQVLPSY VDWRSAGAVV DIKSQGECGG CWAFSAIATV EGINKIVTGV LISLSEQELI
     DCGRTQNTRG CNGGYITDGF QFIINNGGIN TEENYPYTAQ DGECNLDLQN EKYVTIDTYE
     NVPYNNEWAL QTAVTYQPVS VALDAAGDAF KHYSSGIFTG PCGTAIDHAV TIVGYGTEGG
     IDYWIVKNSW DTTWGEEGYM RILRNVGGAG TCGIATMPSY PVKYNNQNHP KPYSSLINPP
     AFSMSKDGPV GVDDGQRYSA

SwissProt Database

ALEU_HORVU

ID   ALEU_HORVU     STANDARD;      PRT;   362 AA.
AC   P05167;
DT   13-AUG-1987 (REL. 05, CREATED)
DT   13-AUG-1987 (REL. 05, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   THIOL PROTEASE ALEURAIN PRECURSOR (EC 3.4.22.16).
OS   HORDEUM VULGARE (BARLEY).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; MONOCOTYLEDONEAE;
OC   CYPERALES; GRAMINEAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 86016732.
RA   ROGERS J.C., DEAN D., HECK G.R.;
RL   PROC. NATL. ACAD. SCI. U.S.A. 82:6512-6516(1985).
RN   [2]
RP   REVISIONS.
RA   ROGERS J.C.;
RL   SUBMITTED (MAR-1987) TO EMBL/GENBANK/DDBJ DATA BANKS.
CC   -!- CATALYTIC ACTIVITY: HYDROLYSIS OF PROTEINS; ACTS ALSO AS AN
CC       AMINOPEPTIDASE ON PEPTIDE SUBSTRATES WITH FREE N-TERMINI.
CC   -!- SUBCELLULAR LOCATION: VACUOLE-LIKE SUBCELLULAR COMPARTMENT.
CC   -!- INDUCTION: ALEURAIN IS SYNTHESIZED BY THE ALEURONE CELLS
CC       STIMULATED BY GIBBERELLIC OR ABSCISIC ACID.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; X05167; G19021; -.
DR   PIR; A25492; KHBH.
DR   HSSP; P00785; 1AEC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; GLYCOPROTEIN; ZYMOGEN; SIGNAL; GERMINATION.
FT   SIGNAL        1      ?       POTENTIAL.
FT   PROPEP        ?    143       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN       144    362       ALEUREIN.
FT   ACT_SITE    168    168       BY SIMILARITY.
FT   ACT_SITE    308    308       BY SIMILARITY.
FT   ACT_SITE    328    328       BY SIMILARITY.
FT   DISULFID    165    208       BY SIMILARITY.
FT   DISULFID    199    241       BY SIMILARITY.
FT   DISULFID    299    349       BY SIMILARITY.
FT   CARBOHYD    188    188       POTENTIAL.
FT   CARBOHYD    257    257       POTENTIAL.
SQ   SEQUENCE   362 AA;  39122 MW;  B6F24D43 CRC32;
     MAHARVLLLA LAVLATAAVA VASSSSFADS NPIRPVTDRA ASTLESAVLG ALGRTRHALR
     FARFAVRYGK SYESAAEVRR RFRIFSESLE EVRSTNRKGL PYRLGINRFS DMSWEEFQAT
     RLGAAQTCSA TLAGNHLMRD AAALPETKDW REDGIVSPVK NQAHCGSCWT FSTTGALEAA
     YTQATGKNIS LSEQQLVDCA GGFNNFGCNG GLPSQAFEYI KYNGGIDTEE SYPYKGVNGV
     CHYKAENAAV QVLDSVNITL NAEDELKNAV GLVRPVSVAF QVIDGFRQYK SGVYTSDHCG
     TTPDDVNHAV LAVGYGVENG VPYWLIKNSW GADWGDNGYF KMEMGKNMCA IATCASYPVV
     AA

SwissProt Database

BROM_ANACO

ID   BROM_ANACO     STANDARD;      PRT;   212 AA.
AC   P14518;
DT   01-JAN-1990 (REL. 13, CREATED)
DT   01-JAN-1990 (REL. 13, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   BROMELAIN, STEM (EC 3.4.22.32).
OS   ANANAS COMOSUS (PINEAPPLE).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; MONOCOTYLEDONEAE;
OC   BROMELIALES; BROMELIACEAE.
RN   [1]
RP   SEQUENCE.
RX   MEDLINE; 89232167.
RA   RITONJA A., ROWAN A.D., BUTTLE D.J., RAWLINGS N.D., TURK V.,
RA   BARRETT A.J.;
RL   FEBS LETT. 247:419-424(1989).
RN   [2]
RP   STRUCTURE OF CARBOHYDRATE.
RA   VAN KUIK J.A., HOFFMANN R.A., MUTSAERS J.H.G.M., VAN HALBEEK H.,
RA   KAMERLING J.P., VLIEGENTHART J.F.G.;
RL   GLYCOCONJ. J. 3:27-34(1986).
CC   -!- CATALYTIC ACTIVITY: BROAD SPECIFICITY FOR CLEAVAGE OF PROTEINS,
CC       BUT STRONG PREFERENCE FOR Z-ARG-ARG-|-NHMEC AMONGST SMALL
CC       MOLECULE SUBSTRATES.
CC   -!- THE GEOMETRY & THE REACTIVITY OF THE CATALYTIC SITE ARE DIFFERENT
CC       FROM THOSE OF OTHER CYSTEINE PROTEINASES.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   PIR; S03964; S03964.
DR   HSSP; P00785; 1AEC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; GLYCOPROTEIN.
FT   ACT_SITE     26     26       BY SIMILARITY.
FT   ACT_SITE    158    158       BY SIMILARITY.
FT   DISULFID     23     63       BY SIMILARITY.
FT   DISULFID     57     96       BY SIMILARITY.
FT   DISULFID    152    199       BY SIMILARITY.
FT   CARBOHYD    117    117
SQ   SEQUENCE   212 AA;  22831 MW;  1DF2FEA5 CRC32;
     AVPQSIDWRD YGAVTSVKNQ NPCGACWAFA AIATVESIYK IKKGILEPLS EQQVLDCAKG
     YGCKGGWEFR AFEFIISNKG VASGAIYPYK AAKGTCKTDG VPNSAYITGY ARVPRNNESS
     MMYAVSKQPI TVAVDANANF QYYKSGVFNG PCGTSLNHAV TAIGYGQDSI IYPKKWGAKW
     GEAGYIRMAR DVSSSSGICG IAIDPLYPTL EE

SwissProt Database

CAT3_FASHE

ID   CAT3_FASHE     STANDARD;      PRT;    19 AA.
AC   P80532;
DT   01-FEB-1996 (REL. 33, CREATED)
DT   01-FEB-1996 (REL. 33, LAST SEQUENCE UPDATE)
DT   01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE)
DE   PUTATIVE CATHEPSIN L3 (EC 3.4.22.15) (NEWLY EXCYSTED JUVENILE PROTEIN
DE   8) (FRAGMENT).
OS   FASCIOLA HEPATICA (LIVER FLUKE).
OC   EUKARYOTA; METAZOA; ACOELOMATES; PLATYHELMINTHES; TREMATODA.
RN   [1]
RP   SEQUENCE.
RA   TKALCEVIC J., ASHMAN K., MEEUSEN E.;
RL   BIOCHEM. BIOPHYS. RES. COMMUN. 213:167-174(1995).
CC   -!- FUNCTION: THIOL PROTEASE.
CC   -!- SUBUNIT: DIMER OF AN HEAVY AND A LIGHT CHAIN LINKED BY DISULFIDE
CC       BONDS (POTENTIAL).
CC   -!- SUBCELLULAR LOCATION: LYSOSOMAL (POTENTIAL).
CC   -!- DEVELOPMENTAL STAGE: EXPRESSED AT THE NEWLY EXCYSTED JUVENILE
CC       STAGE.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
KW   HYDROLASE; THIOL PROTEASE; LYSOSOME.
FT   NON_TER      19     19
SQ   SEQUENCE   19 AA;  2242 MW;  363E4116 CRC32;
     DVPASIDWRE YGYVTEVKD

SwissProt Database

CATB_BOVIN

ID   CATB_BOVIN     STANDARD;      PRT;   335 AA.
AC   P07688;
DT   01-APR-1988 (REL. 07, CREATED)
DT   01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE)
DT   01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE)
DE   CATHEPSIN B PRECURSOR (EC 3.4.22.1).
GN   CTSB.
OS   BOS TAURUS (BOVINE).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; ARTIODACTYLA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=SPLEEN;
RX   MEDLINE; 93385163.
RA   MORDIER S., BECHET D., ROUX M.-P., OBLED A., FERRARA M.;
RL   BIOCHIM. BIOPHYS. ACTA 1174:305-311(1993).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 91310702.
RA   BECHET D.M., FERRARA M.J., MORDIER S.B., ROUX M.-P., DEVAL C.,
RA   OBLED A.;
RL   J. BIOL. CHEM. 266:14104-14112(1991).
RN   [3]
RP   SEQUENCE OF 80-332.
RX   MEDLINE; 88243785.
RA   MELOUN B., BAUDYS M., POHL J., PAVLIK M., KOSTKA V.;
RL   J. BIOL. CHEM. 263:9087-9093(1988).
RN   [4]
RP   PRELIMINARY SEQUENCE OF 80-332.
RA   MELOUN B., POHL J., KOSTKA V.;
RL   (IN) CYSTEINE PROTEINASES AND THEIR INHIBITORS, TURK V., ED.,
RL   PP.19-29, WALTER DE GRUYTER, BERLIN AND NEW YORK, (1986).
RN   [5]
RP   SEQUENCE OF 80-126.
RX   MEDLINE; 82262056.
RA   POHL J., BAUDYS M., TOMASEK V., KOSTKA V.;
RL   FEBS LETT. 142:23-26(1982).
RN   [6]
RP   DISULFIDE BONDS.
RX   MEDLINE; 90359056.
RA   BAUDYS M., MELOUN B., GAN-ERDENE T., POHL J., KOSTKA V.;
RL   BIOL. CHEM. HOPPE-SEYLER 371:485-491(1990).
CC   -!- FUNCTION: THIOL PROTEASE WHICH IS BELIEVED TO PARTICIPATE IN
CC       INTRACELLULAR DEGRADATION AND TURNOVER OF PROTEINS. HAS ALSO
CC       BEEN IMPLICATED IN TUMOR INVASION AND METASTASIS.
CC   -!- CATALYTIC ACTIVITY: HYDROLYSES PROTEINS, WITH A SPECIFICITY
CC       RESEMBLING THAT OF PAPAIN.
CC   -!- SUBUNIT: DIMER OF A HEAVY CHAIN AND A LIGHT CHAIN CROSS-LINKED
CC       BY A DISULFIDE BOND.
CC   -!- SUBCELLULAR LOCATION: LYSOSOMAL.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; U16336; G809479; -.
DR   EMBL; U16337; G809479; JOINED.
DR   EMBL; U16338; G809479; JOINED.
DR   EMBL; U16339; G809479; JOINED.
DR   EMBL; U16341; G809479; JOINED.
DR   EMBL; U16342; G809479; JOINED.
DR   EMBL; U16343; G809479; JOINED.
DR   EMBL; L06075; G289402; -.
DR   EMBL; M64620; G162813; -.
DR   PIR; A28103; KHBOB.
DR   PIR; A05143; A05143.
DR   HSSP; P07858; 1HUC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; LYSOSOME; GLYCOPROTEIN; ZYMOGEN; SIGNAL.
FT   SIGNAL        1     17       POTENTIAL.
FT   PROPEP       18     79       ACTIVATION PEPTIDE.
FT   CHAIN        80    126       CATHEPSIN B LIGHT CHAIN.
FT   CHAIN       129    332       CATHEPSIN B HEAVY CHAIN.
FT   PROPEP      333    335
FT   ACT_SITE    108    108
FT   ACT_SITE    278    278
FT   ACT_SITE    298    298
FT   DISULFID     93    122
FT   DISULFID    105    150
FT   DISULFID    141    207
FT   DISULFID    142    146
FT   DISULFID    179    211
FT   DISULFID    187    198
FT   DISULFID    227    331
FT   CARBOHYD    192    192
FT   VARIANT     208    208       N -> S.
FT   CONFLICT    154    154       F -> E (IN REF. 2 AND 3).
FT   CONFLICT    297    297       G -> A (IN REF. 2 AND 3).
SQ   SEQUENCE   335 AA;  36688 MW;  2DF5A3FE CRC32;
     MWRLLATLSC LLVLTSARSS LYFPPLSDEL VNFVNKQNTT WKAGHNFYNV DLSYVKKLCG
     AILGGPKLPQ RDAFAADVVL PESFDAREQW PNCPTIKEIR DQGSCGSCWA FGAVEAISDR
     ICIHSNGRVN VEVSAEDMLT CCGGECGDGC NGGFPSGAWN FWTKKGLVSG GLYNSHVGCR
     PYSIPPCEHH VNGSRPPCTG EGDTPKCNKT CEPGYSPSYK EDKHFGCSSY SVANNEKEIM
     AEIYKNGPVE GAFSVYSDFL LYKSGVYQHV SGEIMGGHAI RILGWGVENG TPYWLVGNSW
     NTDWGDNGFF KILRGQDHCG IESEIVAGMP CTHQY

SwissProt Database

CATB_CHICK

ID   CATB_CHICK     STANDARD;      PRT;   340 AA.
AC   P43233;
DT   01-NOV-1995 (REL. 32, CREATED)
DT   01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CATHEPSIN B PRECURSOR (EC 3.4.22.1) (CATHEPSIN B1).
OS   GALLUS GALLUS (CHICKEN).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; AVES; NEOGNATHAE;
OC   GALLIFORMES.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=WHITE LEGHORN; TISSUE=BONE;
RX   MEDLINE; 95375017.
RA   DONG S.S., STRANSKY G.I., WHITAKER C.H., JORDAN S.E.,
RA   SCHLESINGER P.H., EDWARDS J.C., BLAIR H.C.;
RL   BIOCHIM. BIOPHYS. ACTA 1251:69-73(1995).
CC   -!- FUNCTION: THIOL PROTEASE WHICH IS BELIEVED TO PARTICIPATE IN
CC       INTRACELLULAR DEGRADATION AND TURNOVER OF PROTEINS. HAS ALSO
CC       BEEN IMPLICATED IN TUMOR INVASION AND METASTASIS.
CC   -!- CATALYTIC ACTIVITY: HYDROLYSES PROTEINS, WITH A SPECIFICITY
CC       RESEMBLING THAT OF PAPAIN.
CC   -!- SUBUNIT: DIMER OF A HEAVY CHAIN AND A LIGHT CHAIN CROSS-LINKED
CC       BY A DISULFIDE BOND.
CC   -!- SUBCELLULAR LOCATION: LYSOSOMAL.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; U18083; G603203; -.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; LYSOSOME; GLYCOPROTEIN; ZYMOGEN; SIGNAL.
FT   SIGNAL        1     17       POTENTIAL.
FT   PROPEP       18     79       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN        80    340       CATHEPSIN B.
FT   CHAIN        80    126       CATHEPSIN B LIGHT CHAIN (BY SIMILARITY).
FT   CHAIN       129    340       CATHEPSIN B HEAVY CHAIN (BY SIMILARITY).
FT   ACT_SITE    108    108       BY SIMILARITY.
FT   ACT_SITE    279    279       BY SIMILARITY.
FT   ACT_SITE    299    299       BY SIMILARITY.
FT   DISULFID     93    122       BY SIMILARITY.
FT   DISULFID    105    150       BY SIMILARITY.
FT   DISULFID    141    208       BY SIMILARITY.
FT   DISULFID    142    146       BY SIMILARITY.
FT   DISULFID    179    212       BY SIMILARITY.
FT   DISULFID    187    198       BY SIMILARITY.
FT   CARBOHYD     38     38       POTENTIAL.
FT   CARBOHYD    192    192       POTENTIAL.
SQ   SEQUENCE   340 AA;  37587 MW;  F2229B05 CRC32;
     MSWSRSILCL LGAFANARSI PYYPPLSSDL VNHINKLNTT GRAGHNFHNT DMSYVKKLCG
     TFLGGPKAPE RVDFAEDMDL PDTFDTRKQW PNCPTISEIR DQGSCGSCWA FGAVEAISDR
     ICVHTNAKVS VEVSAEDLLS CCGFECGMGC NGGYPSGAWR YWTERGLVSG GLYDSHVGCR
     AYTIPPCEHH VNGSRPPCTG EGGETPRCSR HCEPGYSPSY KEDKHYGITS YGVPRSEKEI
     MAEIYKNGPV EGAFIVYEDF LMYKSGVYQH VSGEQVGGHA IRILGWGVEN GTPYWLAANS
     WNTDWGITGF FKILRGEDHC GIESEIVAGV PRMEQYWTRV

SwissProt Database

CATB_HUMAN

ID   CATB_HUMAN     STANDARD;      PRT;   339 AA.
AC   P07858;
DT   01-AUG-1988 (REL. 08, CREATED)
DT   01-JUL-1989 (REL. 11, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CATHEPSIN B PRECURSOR (EC 3.4.22.1) (CATHEPSIN B1) (APP SECRETASE).
GN   CTSB.
OS   HOMO SAPIENS (HUMAN).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; PRIMATES.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 87017021.
RA   CHAN S.J., SAN SEGUNDO B., MCCORMICK M.B., STEINER D.F.;
RL   PROC. NATL. ACAD. SCI. U.S.A. 83:7721-7725(1986).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   TISSUE=GASTRIC CARCINOMA;
RX   MEDLINE; 94156194.
RA   CAO L., TAGGART R.T., BERQUIN I.M., MOIN K., FONG D., SLOANE B.F.;
RL   GENE 139:163-169(1994).
RN   [3]
RP   SEQUENCE OF 80-126 AND 129-333.
RC   TISSUE=LIVER;
RX   MEDLINE; 85127484.
RA   RITONJA A., POPOVIC T., TURK V., WIEDENMANN K., MACHLEIDT W.;
RL   FEBS LETT. 181:169-172(1985).
RN   [4]
RP   SEQUENCE OF 131-339 FROM N.A.
RX   MEDLINE; 86206063.
RA   FONG D., CALHOUN D.H., HSIEH W.-T., LEE B., WELLS R.D.;
RL   PROC. NATL. ACAD. SCI. U.S.A. 83:2909-2913(1986).
RN   [5]
RP   SEQUENCE OF 80-91 AND 129-139.
RC   TISSUE=LIVER;
RX   MEDLINE; 92344620.
RA   MOIN K., DAY N.A., SAMENI M., HASNAIN S., HIRAMA T., SLOANE B.F.;
RL   BIOCHEM. J. 285:427-434(1992).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
RX   MEDLINE; 91330854.
RA   MUSIL D., ZUCIC D., TURK D., ENGH R.A., MAYR I., HUBER R., POPOVIC T.,
RA   TURK V., TOWATARI T., KATUNUMA N., BODE W.;
RL   EMBO J. 10:2321-2330(1991).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
RX   MEDLINE; 96197789.
RA   TURK D., PODOBNIK M., KUHELJ R., DOLINAR M., TURK V.;
RL   FEBS LETT. 384:211-214(1996).
CC   -!- FUNCTION: THIOL PROTEASE WHICH IS BELIEVED TO PARTICIPATE IN
CC       INTRACELLULAR DEGRADATION AND TURNOVER OF PROTEINS. HAS ALSO
CC       BEEN IMPLICATED IN TUMOR INVASION AND METASTASIS.
CC   -!- CATALYTIC ACTIVITY: HYDROLYSES PROTEINS, WITH A SPECIFICITY
CC       RESEMBLING THAT OF PAPAIN.
CC   -!- SUBUNIT: DIMER OF A HEAVY CHAIN AND A LIGHT CHAIN CROSS-LINKED
CC       BY A DISULFIDE BOND.
CC   -!- SUBCELLULAR LOCATION: LYSOSOMAL.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; M14221; G181192; -.
DR   EMBL; L16510; G291888; -.
DR   EMBL; M13230; G181178; -.
DR   PIR; A26498; KHHUB.
DR   PIR; A25432; A25432.
DR   PIR; S16513; S16513.
DR   PIR; S16514; S16514.
DR   PDB; 1HUC; 26-JAN-95.
DR   SWISS-2DPAGE; P07858; HUMAN.
DR   MIM; 116810; -.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; LYSOSOME; GLYCOPROTEIN; ZYMOGEN; SIGNAL;
KW   POLYMORPHISM; 3D-STRUCTURE.
FT   SIGNAL        1     17       POTENTIAL.
FT   PROPEP       18     79       ACTIVATION PEPTIDE.
FT   CHAIN        80    333       CATHEPSIN B.
FT   CHAIN        80    126       CATHEPSIN B LIGHT CHAIN.
FT   CHAIN       129    333       CATHEPSIN B HEAVY CHAIN.
FT   PROPEP      334    339
FT   ACT_SITE    108    108
FT   ACT_SITE    278    278
FT   ACT_SITE    298    298
FT   DISULFID     93    122
FT   DISULFID    105    150
FT   DISULFID    141    207
FT   DISULFID    142    146
FT   DISULFID    179    211
FT   DISULFID    187    198
FT   CARBOHYD    192    192
FT   VARIANT      26     26       V -> L.
FT   CONFLICT    228    228       N -> D (IN REF. 4).
SQ   SEQUENCE   339 AA;  37807 MW;  B81D3A7B CRC32;
     MWQLWASLCC LLVLANARSR PSFHPVSDEL VNYVNKRNTT WQAGHNFYNV DMSYLKRLCG
     TFLGGPKPPQ RVMFTEDLKL PASFDAREQW PQCPTIKEIR DQGSCGSCWA FGAVEAISDR
     ICIHTNAHVS VEVSAEDLLT CCGSMCGDGC NGGYPAEAWN FWTRKGLVSG GLYESHVGCR
     PYSIPPCEHH VNGSRPPCTG EGDTPKCSKI CEPGYSPTYK QDKHYGYNSY SVSNSEKDIM
     AEIYKNGPVE GAFSVYSDFL LYKSGVYQHV TGEMMGGHAI RILGWGVENG TPYWLVANSW
     NTDWGDNGFF KILRGQDHCG IESEVVAGIP RTDQYWEKI

SwissProt Database

CATB_MOUSE

ID   CATB_MOUSE     STANDARD;      PRT;   339 AA.
AC   P10605;
DT   01-JUL-1989 (REL. 11, CREATED)
DT   01-FEB-1991 (REL. 17, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CATHEPSIN B PRECURSOR (EC 3.4.22.1) (CATHEPSIN B1).
GN   CTSB.
OS   MUS MUSCULUS (MOUSE).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; RODENTIA.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 91190267.
RA   QIAN F., FRANKFATER A., CHAN S.J., STEINER D.F.;
RL   DNA CELL BIOL. 10:159-168(1991).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 91032179.
RA   FERRARA M., WOJCIK F., RHAISSI H., MORDIER S., ROUX M.-P., BECHET D.;
RL   FEBS LETT. 273:195-199(1990).
RN   [3]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 87017021.
RA   CHAN S.J., SAN SEGUNDO B., MCCORMICK M.B., STEINER D.F.;
RL   PROC. NATL. ACAD. SCI. U.S.A. 83:7721-7725(1986).
RN   [4]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 92082172.
RA   QIAN F., FRANKFATER A., STEINER D.F., BAJKOWSKI A.S., CHAN S.J.;
RL   ANTICANCER RES. 11:1445-1451(1991).
RN   [5]
RP   SEQUENCE OF 314-339 FROM N.A.
RX   MEDLINE; 91365255.
RA   FRIEMERT C., CLOSS E.I., SILBERMANN M., ERFLE V., STRAUSS P.G.;
RL   GENE 103:259-261(1991).
CC   -!- FUNCTION: THIOL PROTEASE WHICH IS BELIEVED TO PARTICIPATE IN
CC       INTRACELLULAR DEGRADATION AND TURNOVER OF PROTEINS. HAS ALSO
CC       BEEN IMPLICATED IN TUMOR INVASION AND METASTASIS.
CC   -!- CATALYTIC ACTIVITY: HYDROLYSES PROTEINS, WITH A SPECIFICITY
CC       RESEMBLING THAT OF PAPAIN.
CC   -!- SUBUNIT: DIMER OF A HEAVY CHAIN AND A LIGHT CHAIN CROSS-LINKED
CC       BY A DISULFIDE BOND.
CC   -!- SUBCELLULAR LOCATION: LYSOSOMAL.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; M65270; G309152; -.
DR   EMBL; M65263; G309152; JOINED.
DR   EMBL; M65264; G309152; JOINED.
DR   EMBL; M65265; G309152; JOINED.
DR   EMBL; M65266; G309152; JOINED.
DR   EMBL; M65267; G309152; JOINED.
DR   EMBL; M65268; G309152; JOINED.
DR   EMBL; M65269; G309152; JOINED.
DR   EMBL; M14222; G309202; -.
DR   EMBL; X54966; G50597; -.
DR   EMBL; S69034; G239907; -.
DR   PIR; B26498; KHMSB.
DR   PIR; S12901; S12901.
DR   PIR; A38458; A38458.
DR   PIR; A49826; A49826.
DR   HSSP; P07858; 1HUC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; LYSOSOME; GLYCOPROTEIN; ZYMOGEN; SIGNAL.
FT   SIGNAL        1     17       POTENTIAL.
FT   PROPEP       18     79       ACTIVATION PEPTIDE.
FT   CHAIN        80    333       CATHEPSIN B.
FT   CHAIN        80    126       CATHEPSIN B LIGHT CHAIN (BY SIMILARITY).
FT   CHAIN       129    333       CATHEPSIN B HEAVY CHAIN (BY SIMILARITY).
FT   PROPEP      334    339       BY SIMILARITY.
FT   ACT_SITE    108    108       BY SIMILARITY.
FT   ACT_SITE    278    278       BY SIMILARITY.
FT   ACT_SITE    298    298       BY SIMILARITY.
FT   DISULFID     93    122       BY SIMILARITY.
FT   DISULFID    105    150       BY SIMILARITY.
FT   DISULFID    141    207       BY SIMILARITY.
FT   DISULFID    142    146       BY SIMILARITY.
FT   DISULFID    179    211       BY SIMILARITY.
FT   DISULFID    187    198       BY SIMILARITY.
FT   CARBOHYD    192    192       PROBABLE.
FT   CONFLICT    160    160       S -> N (IN REF. 3).
FT   CONFLICT    174    174       N -> D (IN REF. 3).
FT   CONFLICT    177    177       V -> I (IN REF. 3).
FT   CONFLICT    284    284       G -> V (IN REF. 3).
SQ   SEQUENCE   339 AA;  37280 MW;  30694B74 CRC32;
     MWWSLILLSC LLALTSAHDK PSFHPLSDDL INYINKQNTT WQAGRNFYNV DISYLKKLCG
     TVLGGPKLPG RVAFGEDIDL PETFDAREQW SNCPTIGQIR DQGSCGSCWA FGAVEAISDR
     TCIHTNGRVN VEVSAEDLLT CCGIQCGDGC NGGYPSGAWS FWTKKGLVSG GVYNSHVGCL
     PYTIPPCEHH VNGSRPPCTG EGDTPRCNKS CEAGYSPSYK EDKHFGYTSY SVSNSVKEIM
     AEIYKNGPVE GAFTVFSDFL TYKSGVYKHE AGDMMGGHAI RILGWGVENG VPYWLAANSW
     NLDWGDNGFF KILRGENHCG IESEIVAGIP RTDQYWGRF

SwissProt Database

CATB_RAT

ID   CATB_RAT       STANDARD;      PRT;   339 AA.
AC   P00787;
DT   21-JUL-1986 (REL. 01, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CATHEPSIN B PRECURSOR (EC 3.4.22.1) (CATHEPSIN B1) (RSG-2).
GN   CTSB.
OS   RATTUS NORVEGICUS (RAT).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; RODENTIA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=SPRAGUE-DAWLEY; TISSUE=MAMMARY GLAND;
RX   MEDLINE; 95094788.
RA   GUENETTE R.S., MOOIBROEK M., WONG K., WONG P., TENNISWOOD M.;
RL   EUR. J. BIOCHEM. 226:311-321(1994).
RN   [2]
RP   SEQUENCE OF 69-339 FROM N.A.
RX   MEDLINE; 85190489.
RA   SAN SEGUNDO B., CHAN S.J., STEINER D.F.;
RL   PROC. NATL. ACAD. SCI. U.S.A. 82:2320-2324(1985).
RN   [3]
RP   SEQUENCE OF 80-126 AND 129-333.
RC   TISSUE=LIVER;
RX   MEDLINE; 83221657.
RA   TAKIO K., TOWATARI T., KATUNUMA N., TELLER D.C., TITANI K.;
RL   PROC. NATL. ACAD. SCI. U.S.A. 80:3666-3670(1983).
RN   [4]
RP   PROCESSING.
RX   MEDLINE; 92348471.
RA   ROWAN A.D., MASON P., MACH L., MORT J.S.;
RL   J. BIOL. CHEM. 267:15993-15999(1992).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX   MEDLINE; 95197558.
RA   JIA Z., HASNAIN S., HIRAMA T., LEE X., MORT J.S., TO R., HUBER C.P.;
RL   J. BIOL. CHEM. 270:5527-5533(1995).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-339.
RX   MEDLINE; 96311276.
RA   CYGLER M., SIVARAMAN J., GROCHULSKI P., COULOMBE R., STORER A.C.,
RA   MORT J.S.;
RL   STRUCTURE 4:405-416(1996).
CC   -!- FUNCTION: THIOL PROTEASE WHICH IS BELIEVED TO PARTICIPATE IN
CC       INTRACELLULAR DEGRADATION AND TURNOVER OF PROTEINS. HAS ALSO
CC       BEEN IMPLICATED IN TUMOR INVASION AND METASTASIS.
CC   -!- CATALYTIC ACTIVITY: HYDROLYSES PROTEINS, WITH A SPECIFICITY
CC       RESEMBLING THAT OF PAPAIN.
CC   -!- SUBUNIT: DIMER OF A HEAVY CHAIN AND A LIGHT CHAIN CROSS-LINKED
CC       BY A DISULFIDE BOND.
CC   -!- SUBCELLULAR LOCATION: LYSOSOMAL.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; S74711; G797343; -.
DR   EMBL; M11305; G203648; -.
DR   PIR; A00977; KHRTB.
DR   PDB; 1MIN; PRELIMINARY.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; LYSOSOME; GLYCOPROTEIN; ZYMOGEN; SIGNAL;
KW   3D-STRUCTURE.
FT   SIGNAL        1     17       POTENTIAL.
FT   PROPEP       18     79       ACTIVATION PEPTIDE.
FT   CHAIN        80    333       CATHEPSIN B.
FT   CHAIN        80    126       CATHEPSIN B LIGHT CHAIN.
FT   CHAIN       129    333       CATHEPSIN B HEAVY CHAIN.
FT   PROPEP      334    339
FT   ACT_SITE    108    108
FT   ACT_SITE    278    278
FT   ACT_SITE    298    298
FT   DISULFID     93    122       BY SIMILARITY.
FT   DISULFID    105    150       BY SIMILARITY.
FT   DISULFID    141    207       BY SIMILARITY.
FT   DISULFID    142    146       BY SIMILARITY.
FT   DISULFID    179    211       BY SIMILARITY.
FT   DISULFID    187    198
FT   CARBOHYD    192    192
FT   VARIANT     302    302       V -> A.
FT   CONFLICT    159    159       W -> G (IN REF. 3).
SQ   SEQUENCE   339 AA;  37470 MW;  12DBA727 CRC32;
     MWWSLIPLSC LLALTSAHDK PSSHPLSDDM INYINKQNTT WQAGRNFYNV DISYLKKLCG
     TVLGGPNLPE RVGFSEDINL PESFDAREQW SNCPTIAQIR DQGSCGSCWA FGAVEAMSDR
     ICIHTNGRVN VEVSAEDLLT CCGIQCGDGC NGGYPSGAWN FWTRKGLVSG GVYNSHIGCL
     PYTIPPCEHH VNGSRPPCTG EGDTPKCNKM CEAGYSTSYK EDKHYGYTSY SVSDSEKEIM
     AEIYKNGPVE GAFTVFSDFL TYKSGVYKHE AGDVMGGHAI RILGWGIENG VPYWLVANSW
     NVDWGDNGFF KILRGENHCG IESEIVAGIP RTQQYWGRF

SwissProt Database

CATC_HUMAN

ID   CATC_HUMAN     STANDARD;      PRT;   463 AA.
AC   P53634;
DT   01-OCT-1996 (REL. 34, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   DIPEPTIDYL-PEPTIDASE I PRECURSOR (EC 3.4.14.1) (CATHEPSIN C)
DE   (CATHEPSIN J) (DIPEPTIDYL TRANSFERASE).
GN   CTSC.
OS   HOMO SAPIENS (HUMAN).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; PRIMATES.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=ILEUM;
RX   MEDLINE; 95377428.
RA   PARIS A., STRUKELJ B., PUNGERCAR J., RENKO M., DOLENC I., TURK V.;
RL   FEBS LETT. 369:326-330(1995).
CC   -!- FUNCTION: THIOL PROTEASE. HAS DIPEPTIDYLPEPTIDASE ACTIVITY. CAN
CC       DEGRADE GLUCAGON.
CC   -!- CATALYTIC ACTIVITY: RELEASE OF AN N-TERMINAL DIPEPTIDE, XAA-XBB-|-
CC       XCC-, EXCEPT WHEN XAA IS ARG OR LYS, OR XBB OR XCC IS PRO.
CC   -!- SUBUNIT: DIMER OF AN ALPHA CHAIN AND A BETA CHAIN CROSS-LINKED
CC       BY A DISULFIDE BOND.
CC   -!- SUBCELLULAR LOCATION: LYSOSOMAL.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; X87212; G1006657; -.
KW   HYDROLASE; THIOL PROTEASE; LYSOSOME; GLYCOPROTEIN; ZYMOGEN; SIGNAL.
FT   SIGNAL        1     24       BY SIMILARITY.
FT   PROPEP       25    230       BY SIMILARITY.
FT   CHAIN       231    394       BETA CHAIN (LIGHT CHAIN).
FT   CHAIN       395    463       ALPHA CHAIN (HEAVY CHAIN).
FT   ACT_SITE    258    258       BY SIMILARITY.
FT   ACT_SITE    405    405       BY SIMILARITY.
FT   ACT_SITE    427    427       BY SIMILARITY.
FT   CARBOHYD     29     29       POTENTIAL.
FT   CARBOHYD     53     53       POTENTIAL.
FT   CARBOHYD    119    119       POTENTIAL.
FT   CARBOHYD    276    276       POTENTIAL.
SQ   SEQUENCE   463 AA;  51841 MW;  4E1C9E01 CRC32;
     MGAGPSLLLA ALLLLLSGDG AVRCDTPANC TYLDLLGTWV FQVGSSGSQR DVNCSVMGPQ
     EKKVVVYLQK LDTAYDDLGN SGHFTIIYNQ GFEIVLNDYK WFAFFKYKEE GSKVTTYCNE
     TMTGWVHDVL GRNWACFTGK KVGTASENVY VNTAHLKNSQ EKYSNRLYKY DHNFVKAINA
     IQKSWTATTY MEYETLTLGD MIRRSGGHSR KIPRPKPAPL TAEIQQKILH LPTSWDWRNV
     HGINFVSPVR NQASCGSCYS FASMGMLEAR IRILTNNSQT PILSPQEVVS CSQYAQGCEG
     GFPYLIAGKY AQDFGLVEEA CFPYTGTDSP CKMKEDCFRY YSSEYHYVGG FYGGCNEALM
     KLELVHHGPM AVAFEVYDDF LHYKKGIYHH TGLRDPFNPF ELTNHAVLLV GYGTDSASGM
     DYWIVKNSWG TGWGENGYFR IRRGTDECAI ESIAVAATPI PKL

SwissProt Database

CATC_RAT

ID   CATC_RAT       STANDARD;      PRT;   462 AA.
AC   P80067; P80068;
DT   01-MAY-1992 (REL. 22, CREATED)
DT   01-DEC-1992 (REL. 24, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   DIPEPTIDYL-PEPTIDASE I PRECURSOR (EC 3.4.14.1) (CATHEPSIN C)
DE   (CATHEPSIN J) (DIPEPTIDYL TRANSFERASE).
GN   CTSC.
OS   RATTUS NORVEGICUS (RAT).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; RODENTIA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=WISTAR; TISSUE=KIDNEY;
RX   MEDLINE; 92384938.
RA   KOMINAMI E., ISHIDOH K., MUNO D., SATO N.;
RL   BIOL. CHEM. HOPPE-SEYLER 373:367-373(1992).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 91358405.
RA   ISHIDOH K., MUNO D., SATO N., KOMINAMI E.;
RL   J. BIOL. CHEM. 266:16312-16317(1991).
RN   [3]
RP   SEQUENCE OF 25-47; 230-251 AND 393-427.
RC   TISSUE=LIVER;
RX   MEDLINE; 92155229.
RA   NIKAWA T., TOWATARI T., KATUNUMA N.;
RL   EUR. J. BIOCHEM. 204:381-393(1992).
CC   -!- FUNCTION: THIOL PROTEASE. HAS DIPEPTIDYLPEPTIDASE ACTIVITY. CAN
CC       DEGRADE GLUCAGON.
CC   -!- CATALYTIC ACTIVITY: RELEASE OF AN N-TERMINAL DIPEPTIDE, XAA-XBB-|-
CC       XCC-, EXCEPT WHEN XAA IS ARG OR LYS, OR XBB OR XCC IS PRO.
CC   -!- SUBUNIT: DIMER OF AN ALPHA CHAIN AND A BETA CHAIN CROSS-LINKED
CC       BY A DISULFIDE BOND.
CC   -!- SUBCELLULAR LOCATION: LYSOSOMAL.
CC   -!- TISSUE SPECIFICITY: BROADLY DISTRIBUTED, BUT HIGHER LEVELS FOUND
CC       IN LIVER, SPLEEN, INTESTINE, LUNG AND KIDNEY.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; D90404; G220686; -.
DR   PIR; A41158; A41158.
DR   PIR; S23953; S23953.
DR   HSSP; P07858; 1HUC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; LYSOSOME; GLYCOPROTEIN; ZYMOGEN; SIGNAL.
FT   SIGNAL        1     24
FT   PROPEP       25    229       BY SIMILARITY.
FT   CHAIN       230    393       BETA CHAIN (LIGHT CHAIN).
FT   CHAIN       394    462       ALPHA CHAIN (HEAVY CHAIN).
FT   ACT_SITE    257    257       BY SIMILARITY.
FT   ACT_SITE    404    404       BY SIMILARITY.
FT   ACT_SITE    426    426       BY SIMILARITY.
FT   CARBOHYD     29     29
FT   CARBOHYD     53     53       POTENTIAL.
FT   CARBOHYD    144    144       POTENTIAL.
FT   CARBOHYD    275    275       POTENTIAL.
FT   CONFLICT     30     30       C -> E (IN REF. 3).
FT   CONFLICT    129    129       Y -> V (IN REF. 2).
FT   CONFLICT    171    171       H -> N (IN REF. 2).
FT   CONFLICT    191    192       RR -> EE (IN REF. 2).
FT   CONFLICT    263    263       I -> L (IN REF. 2).
SQ   SEQUENCE   462 AA;  52376 MW;  9743605E CRC32;
     MGPWTHSLRA ALLLVLLGVC TVSSDTPANC TYPDLLGTWV FQVGPRHPRS HINCSVMEPT
     EEKVVIHLKK LDTAYDEVGN SGYFTLIYNQ GFEIVLNDYK WFAFFKYEVK GSRAISYCHE
     TMTGWVHDYL GRNWACFVGK KMANHSEKVY VNVAHLGGLQ EKYSERLYSH HHNFVKAINS
     VQKSWTATTY RRYEKLSIRD LIRRSGHSGR ILRPKPAPIT DEIQQQILSL PESWDWRNVR
     GINFVSPVRN QESCGSCYSF ASIGMLEARI RILTNNSQTP ILSPQEVVSC SPYAQGCDGG
     FPYLIAGKYA QDFGVVEENC FPYTATDAPC KPKENCLRYY SSEYYYVGGF YGGCNEALMK
     LELVKHGPMA VAFEVHDDFL HYHSGIYHHT GLSDPFNPFE LTNHAVLLVG YGKDPVTGLD
     YWIVKNSWGS QWGESGYFRI RRGTDECAIE SIAMAAIPIP KL

SwissProt Database

CATH_HUMAN

ID   CATH_HUMAN     STANDARD;      PRT;   335 AA.
AC   P09668;
DT   01-MAR-1989 (REL. 10, CREATED)
DT   01-JAN-1990 (REL. 13, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CATHEPSIN H PRECURSOR (EC 3.4.22.16).
GN   CTSH.
OS   HOMO SAPIENS (HUMAN).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; PRIMATES.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=LIVER;
RX   MEDLINE; 90067944.
RA   FUCHS R., GASSEN H.G.;
RL   NUCLEIC ACIDS RES. 17:9471-9471(1989).
RN   [2]
RP   SEQUENCE OF 88-335 FROM N.A.
RC   TISSUE=KIDNEY;
RX   MEDLINE; 89076480.
RA   FUCHS R., MACHLEIDT W., GASSEN H.G.;
RL   BIOL. CHEM. HOPPE-SEYLER 369:469-475(1988).
RN   [3]
RP   SEQUENCE OF 98-105 AND 114-335.
RC   TISSUE=KIDNEY;
RX   MEDLINE; 88137635.
RA   RITONJA A., POPOVIC T., KOTNIK M., MACHLEIDT W., TURK V.;
RL   FEBS LETT. 228:341-345(1988).
RN   [4]
RP   SEQUENCE OF 99-105; 116-159 AND 294-335.
RA   MACHLEIDT W., RITONJA A., POPOVIC T., KOTNIK M., BRZIN J., TURK V.,
RA   MACHLEIDT I., MULLER-ESTERL W.;
RL   (IN) CYSTEINE PROTEINASES AND THEIR INHIBITORS, TURK V., ED.,
RL   PP.3-18, WALTER DE GRUYTER, BERLIN AND NEW YORK, (1986).
CC   -!- FUNCTION: IMPORTANT FOR THE OVERALL DEGRADATION OF PROTEINS IN
CC       LYSOSOMES.
CC   -!- CATALYTIC ACTIVITY: HYDROLYSIS OF PROTEINS; ACTS ALSO AS AN
CC       AMINOPEPTIDASE ON PEPTIDE SUBSTRATES WITH FREE N-TERMINI.
CC   -!- SUBUNIT: COMPOSED OF A MINICHAIN AND A LARGE CHAIN. THE LARGE
CC       CHAIN MAY BE SPLIT INTO HEAVY AND LIGHT CHAIN. ALL CHAINS ARE
CC       HELD TOGETHER BY DISULFIDE BONDS.
CC   -!- SUBCELLULAR LOCATION: LYSOSOMAL.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; X07549; G29708; -.
DR   EMBL; X07549; E3832; ALT_SEQ.
DR   EMBL; X16832; G29710; -.
DR   PIR; S12486; KHHUH.
DR   HSSP; P00784; 1PPN.
DR   MIM; 116820; -.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; LYSOSOME; GLYCOPROTEIN; ZYMOGEN; SIGNAL.
FT   SIGNAL        1     22
FT   PROPEP       23     97       ACTIVATION PEPTIDE.
FT   PEPTIDE      98    105       CATHEPSIN H MINICHAIN.
FT   CHAIN       116    335       CATHEPSIN H.
FT   CHAIN       116    292       CATHEPSIN H HEAVY CHAIN.
FT   CHAIN       293    335       CATHEPSIN H LIGHT CHAIN.
FT   ACT_SITE    141    141       BY SIMILARITY.
FT   ACT_SITE    281    281       BY SIMILARITY.
FT   ACT_SITE    301    301       BY SIMILARITY.
FT   DISULFID    138    181       BY SIMILARITY.
FT   DISULFID    172    214       BY SIMILARITY.
FT   DISULFID    272    322       BY SIMILARITY.
FT   CARBOHYD    230    230       BY SIMILARITY.
FT   CONFLICT    179    179       Y -> H (IN REF. 3).
FT   CONFLICT    306    306       Q -> E (IN REF. 3 AND 4).
SQ   SEQUENCE   335 AA;  37403 MW;  E548EDD4 CRC32;
     MWATLPLLCA GAWLLGVPVC GAAELSVNSL EKFHFKSWMS KHRKTYSTEE YHHRLQTFAS
     NWRKINAHNN GNHTFKMALN QFSDMSFAEI KHKYLWSEPQ NCSATKSNYL RGTGPYPPSV
     DWRKKGNFVS PVKNQGACGS CWTFSTTGAL ESAIAIATGK MLSLAEQQLV DCAQDFNNYG
     CQGGLPSQAF EYILYNKGIM GEDTYPYQGK DGYCKFQPGK AIGFVKDVAN ITIYDEEAMV
     EAVALYNPVS FAFEVTQDFM MYRTGIYSST SCHKTPDKVN HAVLAVGYGE KNGIPYWIVK
     NSWGPQWGMN GYFLIERGKN MCGLAACASY PIPLV

SwissProt Database

CATH_MOUSE

ID   CATH_MOUSE     STANDARD;      PRT;   333 AA.
AC   P49935;
DT   01-OCT-1996 (REL. 34, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CATHEPSIN H PRECURSOR (EC 3.4.22.16) (CATHEPSIN B3) (CATHEPSIN BA).
GN   CTSH.
OS   MUS MUSCULUS (MOUSE).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; RODENTIA.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 95239085.
RA   LAFUSE W.P., BROWN D., CASTLE L., ZWILLING B.S.;
RL   J. LEUKOC. BIOL. 57:663-669(1995).
CC   -!- FUNCTION: IMPORTANT FOR THE OVERALL DEGRADATION OF PROTEINS IN
CC       LYSOSOMES.
CC   -!- CATALYTIC ACTIVITY: HYDROLYSIS OF PROTEINS; ACTS ALSO AS AN
CC       AMINOPEPTIDASE ON PEPTIDE SUBSTRATES WITH FREE N-TERMINI.
CC   -!- SUBUNIT: COMPOSED OF A MINICHAIN AND A LARGE CHAIN. THE LARGE
CC       CHAIN MAY BE SPLIT INTO HEAVY AND LIGHT CHAIN. ALL CHAINS ARE
CC       HELD TOGETHER BY DISULFIDE BONDS.
CC   -!- SUBCELLULAR LOCATION: LYSOSOMAL.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; U06119; G454101; -.
KW   HYDROLASE; THIOL PROTEASE; LYSOSOME; GLYCOPROTEIN; ZYMOGEN; SIGNAL.
FT   SIGNAL        1     20       POTENTIAL.
FT   PROPEP       21     95       ACTIVATION PEPTIDE.
FT   CHAIN        96    102       CATHEPSIN H MINICHAIN (BY SIMILARITY).
FT   CHAIN       114    333       CATHEPSIN H (BY SIMILARITY).
FT   CHAIN       114    290       CATHEPSIN H HEAVY CHAIN (BY SIMILARITY).
FT   CHAIN       291    333       CATHEPSIN H LIGHT CHAIN (BY SIMILARITY).
FT   ACT_SITE    139    139       BY SIMILARITY.
FT   ACT_SITE    279    279       BY SIMILARITY.
FT   ACT_SITE    299    299       BY SIMILARITY.
FT   DISULFID    136    179       BY SIMILARITY.
FT   DISULFID    170    212       BY SIMILARITY.
FT   DISULFID    270    320       BY SIMILARITY.
FT   CARBOHYD     70     70       POTENTIAL.
FT   CARBOHYD     99     99       POTENTIAL.
FT   CARBOHYD    228    228       POTENTIAL.
SQ   SEQUENCE   333 AA;  37184 MW;  8362D4A7 CRC32;
     MWAALPLLCA GAWLLSTGAT AELTVNAIEK FHFKSWMKQH QKTYSSVEYN HRLQMFANNW
     RKIQAHNQRN HTFKMALNQF SDMSFAEIKH KFLWSEPQNC SATKSNYLRG TGPYPSSMDW
     RKKGNVVSPV KNQGACASCW TFSTTGALES AVAIASGKML SLAEQQLVDC AQAFNNHGCK
     GGLPSQAFEY ILYNKGIMEE DSYPYIGKDS SCRFNPQKAV AFVKNVVNIT LNDEAAMVEA
     VALYNPVSFA FEVTEDFLMY KSGVYSSKSC HKTPDKVNHA VLAVGYGEQN GLLYWIVKNS
     WGSQWGENGY FLIERGKNMC GLAACASYPI PQV

SwissProt Database

CATH_RAT

ID   CATH_RAT       STANDARD;      PRT;   333 AA.
AC   P00786;
DT   21-JUL-1986 (REL. 01, CREATED)
DT   01-AUG-1988 (REL. 08, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CATHEPSIN H PRECURSOR (EC 3.4.22.16) (CATHEPSIN B3) (CATHEPSIN BA).
GN   CTSH.
OS   RATTUS NORVEGICUS (RAT).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; RODENTIA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=WISTAR; TISSUE=KIDNEY;
RX   MEDLINE; 88083632.
RA   ISHIDOH K., IMAJOH S., EMORI Y., OHNO S., KAWASAKI H., MINAMI Y.,
RA   KOMINAMI E., KATUNUMA N., SUZUKI K.;
RL   FEBS LETT. 226:33-37(1987).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   TISSUE=LIVER;
RX   MEDLINE; 89338722.
RA   ISHIDOH K., KOMINAMI E., KATUNUMA N., SUZUKI K.;
RL   FEBS LETT. 253:103-107(1989).
RN   [3]
RP   SEQUENCE OF 4-333 FROM N.A.
RC   TISSUE=LIVER;
RX   MEDLINE; 91114797.
RA   QIAN F., FRANKFATER A., MILLER R.V., CHAN S.J., STEINER D.F.;
RL   INT. J. BIOCHEM. 22:1457-1464(1990).
RN   [4]
RP   SEQUENCE OF 114-333.
RC   TISSUE=LIVER;
RX   MEDLINE; 83221657.
RA   TAKIO K., TOWATARI T., KATUNUMA N., TELLER D.C., TITANI K.;
RL   PROC. NATL. ACAD. SCI. U.S.A. 80:3666-3670(1983).
CC   -!- FUNCTION: IMPORTANT FOR THE OVERALL DEGRADATION OF PROTEINS IN
CC       LYSOSOMES.
CC   -!- CATALYTIC ACTIVITY: HYDROLYSIS OF PROTEINS; ACTS ALSO AS AN
CC       AMINOPEPTIDASE ON PEPTIDE SUBSTRATES WITH FREE N-TERMINI.
CC   -!- SUBUNIT: COMPOSED OF A MINICHAIN AND A LARGE CHAIN. THE LARGE
CC       CHAIN MAY BE SPLIT INTO HEAVY AND LIGHT CHAIN. ALL CHAINS ARE
CC       HELD TOGETHER BY DISULFIDE BONDS.
CC   -!- SUBCELLULAR LOCATION: LYSOSOMAL.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; M36320; G203343; -.
DR   EMBL; Y00708; G55886; -.
DR   EMBL; M38135; G203341; ALT_INIT.
DR   PIR; S00211; KHRTH.
DR   HSSP; P10056; 1PPO.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; LYSOSOME; GLYCOPROTEIN; ZYMOGEN; SIGNAL.
FT   SIGNAL        1     20       POTENTIAL.
FT   PROPEP       21     95       ACTIVATION PEPTIDE.
FT   CHAIN        96    102       CATHEPSIN H MINICHAIN.
FT   CHAIN       114    333       CATHEPSIN H.
FT   CHAIN       114    290       CATHEPSIN H HEAVY CHAIN.
FT   CHAIN       291    333       CATHEPSIN H LIGHT CHAIN.
FT   ACT_SITE    139    139       BY SIMILARITY.
FT   ACT_SITE    279    279       BY SIMILARITY.
FT   ACT_SITE    299    299       BY SIMILARITY.
FT   DISULFID    136    179       BY SIMILARITY.
FT   DISULFID    170    212       BY SIMILARITY.
FT   DISULFID    270    320       BY SIMILARITY.
FT   CARBOHYD    228    228
FT   VARIANT     287    287       G -> A.
SQ   SEQUENCE   333 AA;  37104 MW;  A1F7E0AB CRC32;
     MWTALPLLCA GAWLLSAGAT AELTVNAIEK FHFTSWMKQH QKTYSSREYS HRLQVFANNW
     RKIQAHNQRN HTFKMGLNQF SDMSFAEIKH KYLWSEPQNC SATKSNYLRG TGPYPSSMDW
     RKKGNVVSPV KNQGACGSCW TFSTTGALES AVAIASGKMM TLAEQQLVDC AQNFNNHGCQ
     GGLPSQAFEY ILYNKGIMGE DSYPYIGKNG QCKFNPEKAV AFVKNVVNIT LNDEAAMVEA
     VALYNPVSFA FEVTEDFMMY KSGVYSSNSC HKTPDKVNHA VLAVGYGEQN GLLYWIVKNS
     WGSNWGNNGY FLIERGKNMC GLAACASYPI PQV

SwissProt Database

CATK_HUMAN

ID   CATK_HUMAN     STANDARD;      PRT;   329 AA.
AC   P43235;
DT   01-NOV-1995 (REL. 32, CREATED)
DT   01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CATHEPSIN K PRECURSOR (EC 3.4.22.38) (CATHESPIN O) (CATHEPSIN X)
DE   (CATHEPSIN O2).
GN   CTSK.
OS   HOMO SAPIENS (HUMAN).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; PRIMATES.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=BLOOD;
RX   MEDLINE; 95104457.
RA   SHI G.-P., CHAPMAN H.A., BHAIRI S.M., DELEEUW C., REDDY V.Y.,
RA   WEISS S.J.;
RL   FEBS LETT. 357:129-134(1995).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   TISSUE=BONE;
RX   MEDLINE; 95118380.
RA   INAOKA T., BILBE G., ISHIBASHI O., TEZUKA K.-I., KUMEGAWA M.,
RA   KOKUBO T.;
RL   BIOCHEM. BIOPHYS. RES. COMMUN. 206:89-96(1995).
RN   [3]
RP   SEQUENCE FROM N.A.
RC   TISSUE=OSTEOCLASTOMA;
RX   MEDLINE; 96172222.
RA   LI Y., ALEXANDER M., WUCHERPFENNIG A.L., YELICK P., CHEN W.,
RA   STASHENKO P.;
RL   J. BONE MINER. RES. 10:1197-1202(1995).
RN   [4]
RP   SEQUENCE FROM N.A.
RC   TISSUE=SPLEEN;
RX   MEDLINE; 96082523.
RA   BROMME D., OKAMOTO K.;
RL   BIOL. CHEM. HOPPE-SEYLER 376:379-384(1995).
CC   -!- FUNCTION: CLOSELY INVOLVED IN OSTEOCLASTIC BONE RESORPTION AND MAY
CC       PARTICIPATE PARTIALLY IN THE DISORDER OF BONE REMODELING. DISPLAYS
CC       POTENT ENDOPROTEASE ACTIVITY AGAINST FIBRINOGEN AT ACID PH. MAY
CC       PLAY AN IMPORTANT ROLE IN EXTRACELLULAR MATRIX DEGRADATION.
CC   -!- TISSUE SPECIFICITY: PREDOMINANTLY EXPRESSED IN OSTECLASTS (BONES).
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; U13665; G606923; -.
DR   EMBL; X82153; G562757; -.
DR   EMBL; U20280; G836934; -.
DR   EMBL; S79895; G1195556; -.
DR   MIM; 601105; -.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL.
FT   SIGNAL        1     15       POTENTIAL.
FT   PROPEP       16    114       ACTIVATION PEPTIDE.
FT   CHAIN       115    329       CATHEPSIN K.
FT   ACT_SITE    139    139       BY SIMILARITY.
FT   ACT_SITE    276    276       BY SIMILARITY.
FT   ACT_SITE    296    296       BY SIMILARITY.
FT   DISULFID    136    177       BY SIMILARITY.
FT   DISULFID    170    210       BY SIMILARITY.
FT   DISULFID    269    318       BY SIMILARITY.
FT   CARBOHYD    103    103       POTENTIAL.
FT   CONFLICT     46     46       R -> P (IN REF. 3).
SQ   SEQUENCE   329 AA;  36966 MW;  E1FB169F CRC32;
     MWGLKVLLLP VVSFALYPEE ILDTHWELWK KTHRKQYNNK VDEISRRLIW EKNLKYISIH
     NLEASLGVHT YELAMNHLGD MTSEEVVQKM TGLKVPLSHS RSNDTLYIPE WEGRAPDSVD
     YRKKGYVTPV KNQGQCGSCW AFSSVGALEG QLKKKTGKLL NLSPQNLVDC VSENDGCGGG
     YMTNAFQYVQ KNRGIDSEDA YPYVGQEESC MYNPTGKAAK CRGYREIPEG NEKALKRAVA
     RVGPVSVAID ASLTSFQFYS KGVYYDESCN SDNLNHAVLA VGYGIQKGNK HWIIKNSWGE
     NWGNKGYILM ARNKNNACGI ANLASFPKM

SwissProt Database

CATK_MOUSE

ID   CATK_MOUSE     STANDARD;      PRT;   329 AA.
AC   P55097;
DT   01-OCT-1996 (REL. 34, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CATHEPSIN K PRECURSOR (EC 3.4.22.38).
GN   CTSK.
OS   MUS MUSCULUS (MOUSE).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; RODENTIA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=C57BL; TISSUE=CALVARIA;
RA   RANTAKOKKO J.A., ARO H.T., VUORIO E.;
RL   SUBMITTED (JAN-1996) TO EMBL/GENBANK/DDBJ DATA BANKS.
CC   -!- FUNCTION: CLOSELY INVOLVED IN OSTEOCLASTIC BONE RESORPTION AND MAY
CC       PARTICIPATE PARTIALLY IN THE DISORDER OF BONE REMODELING. DISPLAYS
CC       POTENT ENDOPROTEASE ACTIVITY AGAINST FIBRINOGEN AT ACID PH. MAY
CC       PLAY AN IMPORTANT ROLE IN EXTRACELLULAR MATRIX DEGRADATION (BY
CC       SIMILARITY).
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; X94444; E217091; -.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL.
FT   SIGNAL        1     15       POTENTIAL.
FT   PROPEP       16    114       ACTIVATION PEPTIDE.
FT   CHAIN       115    329       CATHEPSIN K.
FT   ACT_SITE    139    139       BY SIMILARITY.
FT   ACT_SITE    276    276       BY SIMILARITY.
FT   ACT_SITE    296    296       BY SIMILARITY.
FT   DISULFID    136    177       BY SIMILARITY.
FT   DISULFID    170    210       BY SIMILARITY.
FT   DISULFID    269    318       BY SIMILARITY.
FT   CARBOHYD    103    103       POTENTIAL.
FT   CARBOHYD    213    213       POTENTIAL.
SQ   SEQUENCE   329 AA;  36749 MW;  4C08A1FB CRC32;
     MWGLKVLLLP MVSFALSPEE MLDTQWELWK KTHQKQYNSK VDEISRRLIW EKNLKQISAH
     NLEASLGVHT YELAMNHLGD MTSEEVVQKM TGLRIPPSRS YSNDTLYTPE WEGRVPDSID
     YRKKGYVTPV KNQGQCGSCW AFSSAGALEG QLKKKTGKLL ALSPQNLVDC VTENYGCGGG
     YMTTAFQYVQ QNGGIDSEDA FPYVGQDESC MYNATAKAAK CRGYREIPVG NEKALKRAVA
     RVGPISVSID ASLASFQFYS RGVYYDENCD RDNVNHAVLV VGYGTQKGSK HWIIKNSWGE
     SWGNKGYALL ARNKNNACGI TNMASFPKM

SwissProt Database

CATK_RABIT

ID   CATK_RABIT     STANDARD;      PRT;   329 AA.
AC   P43236;
DT   01-NOV-1995 (REL. 32, CREATED)
DT   01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CATHEPSIN K PRECURSOR (EC 3.4.22.38) (OC-2 PROTEIN).
GN   CTSK.
OS   ORYCTOLAGUS CUNICULUS (RABBIT).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; LAGOMORPHA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=BONE;
RX   MEDLINE; 94117413.
RA   TEZUKA K.-I., TEZUKA Y., MAEJIMA A., SATO T., NEMOTO K.,
RA   KAMIOKA H., HAKEDA Y., KUMEGAWA M.;
RL   J. BIOL. CHEM. 269:1106-1109(1994).
CC   -!- FUNCTION: CLOSELY INVOLVED IN OSTEOCLASTIC BONE RESORPTION AND MAY
CC       PARTICIPATE PARTIALLY IN THE DISORDER OF BONE REMODELING. DISPLAYS
CC       POTENT ENDOPROTEASE ACTIVITY AGAINST FIBRINOGEN AT ACID PH. MAY
CC       PLAY AN IMPORTANT ROLE IN EXTRACELLULAR MATRIX DEGRADATION.
CC   -!- TISSUE SPECIFICITY: PREDOMINANTLY EXPRESSED IN OSTECLASTS (BONES).
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; D14036; G454187; -.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL.
FT   SIGNAL        1     15       POTENTIAL.
FT   PROPEP       16    114       ACTIVATION PEPTIDE.
FT   CHAIN       115    329       CATHEPSIN K.
FT   ACT_SITE    139    139       BY SIMILARITY.
FT   ACT_SITE    276    276       BY SIMILARITY.
FT   ACT_SITE    296    296       BY SIMILARITY.
FT   DISULFID    136    177       BY SIMILARITY.
FT   DISULFID    170    210       BY SIMILARITY.
FT   DISULFID    269    318       BY SIMILARITY.
FT   CARBOHYD    103    103       POTENTIAL.
FT   CARBOHYD    268    268       POTENTIAL.
SQ   SEQUENCE   329 AA;  36870 MW;  93ED765E CRC32;
     MWGLKVLLLP VVSFALHPEE ILDTQWELWK KTYSKQYNSK VDEISRRLIW EKNLKHISIH
     NLEASLGVHT YELAMNHLGD MTSEEVVQKM TGLKVPPSRS HSNDTLYIPD WEGRTPDSID
     YRKKGYVTPV KNQGQCGSCW AFSSVGALEG QLKKKTGKLL NLSPQNLVDC VSENYGCGGG
     YMTNAFQYVQ RNRGIDSEDA YPYVGQDESC MYNPTGKAAK CRGYREIPEG NEKALKRAVA
     RVGPVSVAID ASLTSFQFYS KGVYYDENCS SDNVNHAVLA VGYGIQKGNK HWIIKNSWGE
     SWGNKGYILM ARNKNNACGI ANLASFPKM

SwissProt Database

CATL_BOVIN

ID   CATL_BOVIN     STANDARD;      PRT;   334 AA.
AC   P25975;
DT   01-MAY-1992 (REL. 22, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CATHEPSIN L PRECURSOR (EC 3.4.22.15).
GN   CTSL.
OS   BOS TAURUS (BOVINE).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; ARTIODACTYLA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=RETINAL PIGMENT EPITHELIUM;
RA   VOELKEL H., SCHULTZ J.E., KURZ U.;
RL   SUBMITTED (SEP-1996) TO EMBL/GENBANK/DDBJ DATA BANKS.
RN   [2]
RP   SEQUENCE OF 114-132 AND 293-311.
RX   MEDLINE; 91257334.
RA   RITONJA A., COLIC A., DOLENC I., OGRINC T., PODOBNIK M., TURK V.;
RL   FEBS LETT. 283:329-331(1991).
RN   [3]
RP   SEQUENCE OF 114-132 AND 293-311.
RC   TISSUE=KIDNEY;
RX   MEDLINE; 92384944.
RA   DOLENC I., RITONJA A., COLIC A., PODOBNIK M., OGRINC T., TURK V.;
RL   BIOL. CHEM. HOPPE-SEYLER 373:407-412(1992).
CC   -!- FUNCTION: IMPORTANT FOR THE OVERALL DEGRADATION OF PROTEINS IN
CC       LYSOSOMES.
CC   -!- SUBUNIT: DIMER OF AN HEAVY AND A LIGHT CHAIN LINKED BY DISULFIDE
CC       BONDS.
CC   -!- SUBCELLULAR LOCATION: LYSOSOMAL.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; X91755; E200700; -.
DR   PIR; S15845; S15845.
DR   PIR; S24184; S24184.
DR   HSSP; P00784; 1PAD.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; GLYCOPROTEIN; LYSOSOME; ZYMOGEN; SIGNAL.
FT   SIGNAL        1     17       POTENTIAL.
FT   PROPEP       18    117       ACTIVATION PEPTIDE.
FT   CHAIN       118    289       CATHEPSIN L HEAVY CHAIN.
FT   PROPEP      290    291
FT   CHAIN       292    334       CATHEPSIN L LIGHT CHAIN.
FT   ACT_SITE    138    138       BY SIMILARITY.
FT   ACT_SITE    277    277       BY SIMILARITY.
FT   ACT_SITE    301    301       BY SIMILARITY.
FT   DISULFID    135    178       BY SIMILARITY.
FT   DISULFID    169    212       BY SIMILARITY.
FT   DISULFID    270    323       INTERCHAIN (BY SIMILARITY).
FT   CARBOHYD    222    222       POTENTIAL.
FT   CONFLICT    116    116       K -> W (IN REF. 2 AND 3).
FT   CONFLICT    305    305       P -> G (IN REF. 2 AND 3).
FT   CONFLICT    310    310       N -> G (IN REF. 2 AND 3).
SQ   SEQUENCE   334 AA;  37377 MW;  20786901 CRC32;
     MNPSFFLTVL CLGVASAAPK LDPNLDAHWH QWKATHRRLY GMNEEEWRRA VWEKNKKIID
     LHNQEYSEGK HAFRMAMNAF GDMTNEEFRQ VMNGFQNQKH KKGKLFHEPL LVDVPKSVDW
     TKKGYVTPVK NQGQCGSCWA FSATGALEGQ MFRKTGKLVS LSEQNLVDCS RAQGNQGCNG
     GLMDNAFQYI KDNGGLDSEE SYPYLATDTN SCNYKPECSA ANDTGFVDIP QREKALMKAV
     ATVGPISVAI DAGHTSFQFY KSGIYYDPDC SCKDLDHGVL VVGYGFEGTD SNNNKFWIVK
     NSWGPEWGWN GYVKMAKDQN NHCGIATAAS YPTV

SwissProt Database

CATL_CHICK

ID   CATL_CHICK     STANDARD;      PRT;   218 AA.
AC   P09648;
DT   01-MAR-1989 (REL. 10, CREATED)
DT   01-MAR-1989 (REL. 10, LAST SEQUENCE UPDATE)
DT   01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE)
DE   CATHEPSIN L (EC 3.4.22.15).
OS   GALLUS GALLUS (CHICKEN).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; AVES; NEOGNATHAE;
OC   GALLIFORMES.
RN   [1]
RP   SEQUENCE.
RX   MEDLINE; 87304227.
RA   WADA K., TAKAI T., TANABE T.;
RL   EUR. J. BIOCHEM. 167:13-18(1987).
RN   [2]
RP   SEQUENCE OF 1-37 AND 177-216.
RC   TISSUE=LIVER;
RX   MEDLINE; 87080783.
RA   WADA K., TANABE T.;
RL   FEBS LETT. 209:330-334(1986).
RN   [3]
RP   SEQUENCE.
RC   TISSUE=LIVER;
RX   MEDLINE; 88050863.
RA   DUFOUR E., OBLED A., VALIN C., BECHET D., RIBADEAU-DUMAS B.,
RA   HUET J.C.;
RL   BIOCHEMISTRY 26:5689-5695(1987).
CC   -!- FUNCTION: IMPORTANT FOR THE OVERALL DEGRADATION OF PROTEINS IN
CC       LYSOSOMES.
CC   -!- SUBUNIT: DIMER OF AN HEAVY AND A LIGHT CHAIN LINKED BY DISULFIDE
CC       BONDS.
CC   -!- SUBCELLULAR LOCATION: LYSOSOMAL.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   PIR; A26818; KHCHL.
DR   PIR; A25654; A25654.
DR   PIR; S00081; S00081.
DR   HSSP; P00785; 1AEC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; GLYCOPROTEIN; LYSOSOME.
FT   CHAIN         1    176       HEAVY CHAIN.
FT   NON_CONS    176    177
FT   CHAIN       177    217       LIGHT CHAIN.
FT   ACT_SITE     25     25       BY SIMILARITY.
FT   ACT_SITE    165    165       BY SIMILARITY.
FT   ACT_SITE    185    185       BY SIMILARITY.
FT   CARBOHYD    109    109
FT   DISULFID     22     65       BY SIMILARITY.
FT   DISULFID     56     99       BY SIMILARITY.
FT   DISULFID    158    207       INTERCHAIN (BY SIMILARITY).
FT   CONFLICT     21     21       Q -> I (IN REF. 3).
FT   CONFLICT     29     29       S -> N (IN REF. 3).
FT   CONFLICT     40     42       RTK -> FKT (IN REF. 3).
FT   CONFLICT     97     98       MISSING (IN REF. 3).
FT   CONFLICT    109    109       N -> K (IN REF. 3).
FT   CONFLICT    177    177       MISSING (IN REF. 3).
FT   CONFLICT    197    197       I -> Q (IN REF. 3).
SQ   SEQUENCE   218 AA;  23963 MW;  9CD1C0FF CRC32;
     APRSVDWREK GYVTPVKDQG QCGSCWAFST TGALEGQHFR TKGKLVSLSE QNLVDCSRPE
     GNQGCNGGLM DQAFQYVQDN GGIDSEESYP YTAKDDEDCR YKAEYNAAND TGFVDIPQGH
     ERALMKAVAS VGPVSVAIDA GHSSFQFYQS GIYYEPDCSS EDLDHGVLVV GYGFEGGKKY
     WIVKNSWGEK WGDKGYIYMA KDRKNHCGIA TAASYPLV

SwissProt Database

CATL_FELCA

ID   CATL_FELCA     STANDARD;      PRT;   139 AA.
AC   P25773;
DT   01-MAY-1992 (REL. 22, CREATED)
DT   01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE)
DT   01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE)
DE   CATHEPSIN L (EC 3.4.22.15) (PROGESTERONE-DEPENDENT PROTEIN) (PDP)
DE   (FRAGMENT).
GN   CTSL.
OS   FELIS SILVESTRIS CATUS (CAT).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; CARNIVORA.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 90114185.
RA   JAFFE R.C., DONNELLY K.M., MAVROGIANIS P.A., VERHAGE H.G.;
RL   MOL. ENDOCRINOL. 3:1807-1814(1989).
CC   -!- FUNCTION: IMPORTANT FOR THE OVERALL DEGRADATION OF PROTEINS IN
CC       LYSOSOMES. MAY BE RESPONSIBLE FOR PREPARING THE ENDOMETRIUM FOR
CC       BLASTOCYST IMPLANTATION.
CC   -!- SUBUNIT: DIMER OF AN HEAVY AND A LIGHT CHAIN LINKED BY DISULFIDE
CC       BONDS.
CC   -!- SUBCELLULAR LOCATION: LYSOSOMAL.
CC   -!- INDUCTION: BY PROGESTERONE.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; M31652; E26301; -.
DR   PIR; A41404; A41404.
DR   HSSP; P00785; 1AEC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; GLYCOPROTEIN; LYSOSOME.
FT   NON_TER       1      1
FT   ACT_SITE     97     97       BY SIMILARITY.
FT   ACT_SITE    121    121       BY SIMILARITY.
FT   DISULFID     <1     32       BY SIMILARITY.
FT   DISULFID     90   >139       BY SIMILARITY.
FT   CARBOHYD     42     42       POTENTIAL.
FT   NON_TER     139    139
SQ   SEQUENCE   139 AA;  15490 MW;  1C17AA3D CRC32;
     GGLIDDAFQY VKDNGGLDSE ESYPYHAQGD SCKYRPENSV ANVTDYWDIP SKENELMITL
     AAVGPISAAI DASLDTFRFY KEGIYYDPSC SSEDVDHGVL VVGYGADGTE TENKKYWIIK
     NSWGTDWGMD GYIKMAKDR

SwissProt Database

CATL_HUMAN

ID   CATL_HUMAN     STANDARD;      PRT;   333 AA.
AC   P07711;
DT   01-APR-1988 (REL. 07, CREATED)
DT   01-OCT-1989 (REL. 12, LAST SEQUENCE UPDATE)
DT   01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE)
DE   CATHEPSIN L PRECURSOR (EC 3.4.22.15) (MAJOR EXCRETED PROTEIN) (MEP).
GN   CTSL.
OS   HOMO SAPIENS (HUMAN).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; PRIMATES.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 88339905.
RA   GAL S., GOTTESMAN M.M.;
RL   BIOCHEM. J. 253:303-306(1988).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 88213715.
RA   JOSEPH L.J., CHANG L.C., STAMENKOVICH D., SUKHATME V.P.;
RL   J. CLIN. INVEST. 81:1621-1629(1988).
RN   [3]
RP   SEQUENCE OF 114-288 AND 292-333.
RX   MEDLINE; 88137635.
RA   RITONJA A., POPOVIC T., KOTNIK M., MACHLEIDT W., TURK V.;
RL   FEBS LETT. 228:341-345(1988).
RN   [4]
RP   SEQUENCE OF 114-155 FROM N.A.
RX   MEDLINE; 87174843.
RA   JOSEPH L., LAPID S., SUKHATME V.;
RL   NUCLEIC ACIDS RES. 15:3186-3186(1987).
RN   [5]
RP   SEQUENCE OF 114-154 AND 292-333.
RX   MEDLINE; 87127952.
RA   MASON R.W., WALKER J.E., NORTHROP F.D.;
RL   BIOCHEM. J. 240:373-377(1986).
CC   -!- FUNCTION: IMPORTANT FOR THE OVERALL DEGRADATION OF PROTEINS IN
CC       LYSOSOMES.
CC   -!- SUBUNIT: DIMER OF AN HEAVY AND A LIGHT CHAIN LINKED BY DISULFIDE
CC       BONDS.
CC   -!- SUBCELLULAR LOCATION: LYSOSOMAL.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; X12451; G29715; -.
DR   EMBL; X05256; E12639; -.
DR   EMBL; M20496; G190418; -.
DR   PIR; S01002; KHHUL.
DR   PIR; A26069; A26069.
DR   HSSP; P00784; 1PAD.
DR   MIM; 116880; -.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; GLYCOPROTEIN; LYSOSOME; ZYMOGEN; SIGNAL.
FT   SIGNAL        1     17       POTENTIAL.
FT   PROPEP       18    113       ACTIVATION PEPTIDE.
FT   CHAIN       114    288       CATHEPSIN L HEAVY CHAIN.
FT   PROPEP      289    291
FT   CHAIN       292    333       CATHEPSIN L LIGHT CHAIN.
FT   ACT_SITE    138    138       BY SIMILARITY.
FT   ACT_SITE    276    276       BY SIMILARITY.
FT   ACT_SITE    300    300       BY SIMILARITY.
FT   DISULFID    135    178       BY SIMILARITY.
FT   DISULFID    169    211       BY SIMILARITY.
FT   DISULFID    269    322       INTERCHAIN (BY SIMILARITY).
FT   CARBOHYD    221    221
FT   CARBOHYD    268    268       (IN REF. 3).
FT   CONFLICT    268    268       D -> N (IN REF. 3).
SQ   SEQUENCE   333 AA;  37564 MW;  BBE9592A CRC32;
     MNPTLILAAF CLGIASATLT FDHSLEAQWT KWKAMHNRLY GMNEEGWRRA VWEKNMKMIE
     LHNQEYREGK HSFTMAMNAF GDMTSEEFRQ VMNGFQNRKP RKGKVFQEPL FYEAPRSVDW
     REKGYVTPVK NQGQCGSCWA FSATGALEGQ MFRKTGRLIS LSEQNLVDCS GPQGNEGCNG
     GLMDYAFQYV QDNGGLDSEE SYPYEATEES CKYNPKYSVA NDTGFVDIPK QEKALMKAVA
     TVGPISVAID AGHESFLFYK EGIYFEPDCS SEDMDHGVLV VGYGFESTES DNNKYWLVKN
     SWGEEWGMGG YVKMAKDRRN HCGIASAASY PTV

SwissProt Database

CATL_MOUSE

ID   CATL_MOUSE     STANDARD;      PRT;   334 AA.
AC   P06797;
DT   01-JAN-1988 (REL. 06, CREATED)
DT   01-NOV-1990 (REL. 16, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CATHEPSIN L PRECURSOR (EC 3.4.22.15) (MAJOR EXCRETED PROTEIN) (MEP).
GN   CTSL.
OS   MUS MUSCULUS (MOUSE).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; RODENTIA.
RN   [1]
RP   SEQUENCE FROM N.A., AND PARTIAL SEQUENCE.
RX   MEDLINE; 88076849.
RA   TROEN B.R., GAL S., GOTTESMAN M.M.;
RL   BIOCHEM. J. 246:731-735(1987).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 88213715.
RA   JOSEPH L.J., CHANG L.C., STAMENKOVICH D., SUKHATME V.P.;
RL   J. CLIN. INVEST. 81:1621-1629(1988).
RN   [3]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 87033683.
RA   PORTNOY D.A., ERICKSON A.H., KOCHAN J., RAVETCH J.V., UNKELESS J.C.;
RL   J. BIOL. CHEM. 261:14697-14703(1986).
RN   [4]
RP   SEQUENCE FROM N.A., AND CARBOHYDRATE-BINDING SITE.
RC   TISSUE=LIVER;
RX   MEDLINE; 91112761.
RA   STEARNS N.A., DONG J., PAN J.X., BRENNER D.A., SAHAGIAN G.G.;
RL   ARCH. BIOCHEM. BIOPHYS. 283:447-457(1990).
RN   [5]
RP   SEQUENCE OF 89-300 FROM N.A.
RC   STRAIN=BNL;
RX   MEDLINE; 86271744.
RA   DENHARDT D.T., HAMILTON R.T., PARFETT C.L.J., EDWARDS D.R.,
RA   PIERRE R.S., WATERHOUSE P., NILSON-HAMILTON M.;
RL   CANCER RES. 46:4590-4593(1986).
CC   -!- FUNCTION: IMPORTANT FOR THE OVERALL DEGRADATION OF PROTEINS IN
CC       LYSOSOMES.
CC   -!- SUBUNIT: DIMER OF AN HEAVY AND A LIGHT CHAIN LINKED BY DISULFIDE
CC       BONDS.
CC   -!- SUBCELLULAR LOCATION: LYSOSOMAL.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; X06086; G53047; -.
DR   EMBL; J02583; G309186; -.
DR   EMBL; M20495; G200501; -.
DR   EMBL; X04392; G929719; -.
DR   PIR; S01177; KHMSL.
DR   PIR; S13890; S13890.
DR   HSSP; P00785; 1AEC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; GLYCOPROTEIN; LYSOSOME; ZYMOGEN; SIGNAL.
FT   SIGNAL        1     17       POTENTIAL.
FT   PROPEP       18    113       ACTIVATION PEPTIDE.
FT   CHAIN       114    288       CATHEPSIN L, HEAVY CHAIN.
FT   CHAIN       291    334       CATHEPSIN L, LIGHT CHAIN.
FT   ACT_SITE    138    138       BY SIMILARITY.
FT   ACT_SITE    276    276       BY SIMILARITY.
FT   ACT_SITE    300    300       BY SIMILARITY.
FT   DISULFID    135    178       BY SIMILARITY.
FT   DISULFID    169    211       BY SIMILARITY.
FT   DISULFID    269    322       INTERCHAIN (BY SIMILARITY).
FT   CARBOHYD    221    221
FT   CONFLICT     58     58       M -> I (IN REF. 2).
FT   CONFLICT    177    177       G -> R (IN REF. 3).
SQ   SEQUENCE   334 AA;  37547 MW;  ABF78B3C CRC32;
     MNLLLLLAVL CLGTALATPK FDQTFSAEWH QWKSTHRRLY GTNEEEWRRA IWEKNMRMIQ
     LHNGEYSNGQ HGFSMEMNAF GDMTNEEFRQ VVNGYRHQKH KKGRLFQEPL MLKIPKSVDW
     REKGCVTPVK NQGQCGSCWA FSASGCLEGQ MFLKTGKLIS LSEQNLVDCS HAQGNQGCNG
     GLMDFAFQYI KENGGLDSEE SYPYEAKDGS CKYRAEFAVA NDTGFVDIPQ QEKALMKAVA
     TVGPISVAMD ASHPSLQFYS SGIYYEPNCS SKNLDHGVLL VGYGYEGTDS NKNKYWLVKN
     SWGSEWGMEG YIKIAKDRDN HCGLATAASY PVVN

SwissProt Database

CATL_RAT

ID   CATL_RAT       STANDARD;      PRT;   334 AA.
AC   P07154;
DT   01-APR-1988 (REL. 07, CREATED)
DT   01-FEB-1991 (REL. 17, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CATHEPSIN L PRECURSOR (EC 3.4.22.15) (MAJOR EXCRETED PROTEIN) (MEP)
DE   (CYCLIC PROTEIN-2) (CP-2).
GN   CTSL.
OS   RATTUS NORVEGICUS (RAT).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; RODENTIA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=WISTAR;
RX   MEDLINE; 88030047.
RA   ISHIDOH K., TOWATARI T., IMAJOH S., KAWASAKI H., KOMINAMI E.,
RA   KATUNUMA N., SUZUKI K.;
RL   FEBS LETT. 223:69-73(1987).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 90092543.
RA   ISHIDOH K., KOMINAMI E., SUZUKI K., KATUNUMA N.;
RL   FEBS LETT. 259:71-74(1989).
RN   [3]
RP   SEQUENCE OF 88-334 FROM N.A.
RC   TISSUE=SERTOLI CELLS;
RX   MEDLINE; 92168015.
RA   ERICKSON-LAWRENCE M., ZABLUDOFF S.D., WRIGHT W.W.;
RL   MOL. ENDOCRINOL. 5:1789-1798(1991).
RN   [4]
RP   SEQUENCE OF 114-288 AND 291-334.
RC   TISSUE=LIVER;
RX   MEDLINE; 88296890.
RA   TOWATARI T., KATUNUMA N.;
RL   FEBS LETT. 236:57-61(1988).
CC   -!- FUNCTION: IMPORTANT FOR THE OVERALL DEGRADATION OF PROTEINS IN
CC       LYSOSOMES.
CC   -!- SUBUNIT: DIMER OF AN HEAVY AND A LIGHT CHAIN LINKED BY DISULFIDE
CC       BONDS.
CC   -!- SUBCELLULAR LOCATION: LYSOSOMAL.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; Y00697; G55888; -.
DR   EMBL; S85184; G246148; -.
DR   PIR; S07098; KHRTL.
DR   HSSP; P00785; 1AEC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; GLYCOPROTEIN; LYSOSOME; ZYMOGEN; SIGNAL.
FT   SIGNAL        1     17       POTENTIAL.
FT   PROPEP       18    113       ACTIVATION PEPTIDE.
FT   CHAIN       114    288       CATHEPSIN L, HEAVY CHAIN.
FT   CHAIN       291    334       CATHEPSIN L, LIGHT CHAIN.
FT   ACT_SITE    138    138       BY SIMILARITY.
FT   ACT_SITE    276    276       BY SIMILARITY.
FT   ACT_SITE    300    300       BY SIMILARITY.
FT   DISULFID    135    178       BY SIMILARITY.
FT   DISULFID    169    211       BY SIMILARITY.
FT   DISULFID    269    322       INTERCHAIN (BY SIMILARITY).
FT   CARBOHYD    221    221
FT   CONFLICT    238    238       A -> P (IN REF. 1).
SQ   SEQUENCE   334 AA;  37660 MW;  792CF115 CRC32;
     MTPLLLLAVL CLGTALATPK FDQTFNAQWH QWKSTHRRLY GTNEEEWRRA VWEKNMRMIQ
     LHNGEYSNGK HGFTMEMNAF GDMTNEEFRQ IVNGYRHQKH KKGRLFQEPL MLQIPKTVDW
     REKGCVTPVK NQGQCGSCWA FSASGCLEGQ MFLKTGKLIS LSEQNLVDCS HDQGNQGCNG
     GLMDFAFQYI KENGGLDSEE SYPYEAKDGS CKYRAEYAVA NDTGFVDIPQ QEKALMKAVA
     TVGPISVAMD ASHPSLQFYS SGIYYEPNCS SKDLDHGVLV VGYGYEGTDS NKDKYWLVKN
     SWGKEWGMDG YIKIAKDRNN HCGLATAASY PIVN

SwissProt Database

CATL_SHEEP

ID   CATL_SHEEP     STANDARD;      PRT;   217 AA.
AC   Q10991;
DT   01-OCT-1996 (REL. 34, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CATHEPSIN L (EC 3.4.22.15).
GN   CTSL.
OS   OVIS ARIES (SHEEP).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; ARTIODACTYLA.
RN   [1]
RP   SEQUENCE.
RC   TISSUE=LIVER;
RA   RITONJA A., COETZER T.H.T., PIKE R.N., DENNISON C.;
RL   COMP. BIOCHEM. PHYSIOL. 114B:193-198(1996).
CC   -!- FUNCTION: IMPORTANT FOR THE OVERALL DEGRADATION OF PROTEINS IN
CC       LYSOSOMES.
CC   -!- SUBUNIT: DIMER OF AN HEAVY AND A LIGHT CHAIN LINKED BY DISULFIDE
CC       BONDS.
CC   -!- SUBCELLULAR LOCATION: LYSOSOMAL.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
KW   HYDROLASE; THIOL PROTEASE; GLYCOPROTEIN; LYSOSOME.
FT   CHAIN         1    175       CATHEPSIN L, HEAVY CHAIN.
FT   CHAIN       177    217       CATHEPSIN L, LIGHT CHAIN.
FT   ACT_SITE     25     25       BY SIMILARITY.
FT   ACT_SITE    163    163       BY SIMILARITY.
FT   ACT_SITE    184    184       BY SIMILARITY.
FT   DISULFID     22     65       BY SIMILARITY.
FT   DISULFID    156    206       INTERCHAIN (BY SIMILARITY).
SQ   SEQUENCE   217 AA;  23608 MW;  EC1D8240 CRC32;
     VPKSVDWTKK GYVTPVKNQG QCGSCWAFSA TGALEGQMFR KTGKLVSLSE QNLVDSSRPQ
     GNQGCNGGLM DNAFQYIKEN GGLDSEESYP YEATDTSCNY KPEYSAAKDT GFVDIPQREK
     ALMKAVATVG PISVAIDAGH SSFQFYKSGI YYDPDCSSKD LDHGVLVVGY GFEGTNNKFW
     IVKNSWGPEW GNKGYVKMAK DQNNHCGIAT AASYPTV

SwissProt Database

CATO_HUMAN

ID   CATO_HUMAN     STANDARD;      PRT;   321 AA.
AC   P43234;
DT   01-NOV-1995 (REL. 32, CREATED)
DT   01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CATHEPSIN O PRECURSOR (EC 3.4.22.-).
GN   CTSO.
OS   HOMO SAPIENS (HUMAN).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; PRIMATES.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=BREAST CARCINOMA;
RX   MEDLINE; 95014586.
RA   VELASCO G., FERRANDO A.A., PUENTE X.S., SANCHEZ L.M., LOPEZ-OTIN C.;
RL   J. BIOL. CHEM. 269:27136-27142(1994).
CC   -!- FUNCTION: PROTEOLYTIC ENZYME POSSIBLY INVOLVED IN NORMAL CELLULAR
CC       PROTEIN DEGRADATION AND TURNOVER.
CC   -!- TISSUE SPECIFICITY: EXPRESSED IN ALL EXAMINED TISSUES. HIGH LEVELS
CC       SEEN IN THE OVARY, KIDNEY AND PLACENTA WHILE LOW LEVELS SEEN IN
CC       THYMUS AND SKELETAL MUSCLE.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; X77383; G574804; -.
DR   MIM; 600550; -.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; GLYCOPROTEIN; ZYMOGEN; SIGNAL.
FT   SIGNAL        1     23       POTENTIAL.
FT   PROPEP       24    107       ACTIVATION PEPTIDE.
FT   CHAIN       108    321       CATHEPSIN O.
FT   ACT_SITE    132    132       BY SIMILARITY.
FT   ACT_SITE    269    269       BY SIMILARITY.
FT   ACT_SITE    289    289       BY SIMILARITY.
FT   DISULFID    129    170       BY SIMILARITY.
FT   DISULFID    163    204       BY SIMILARITY.
FT   DISULFID    262    310       BY SIMILARITY.
FT   CARBOHYD     62     62       POTENTIAL.
FT   CARBOHYD    105    105       POTENTIAL.
SQ   SEQUENCE   321 AA;  35957 MW;  95586EAC CRC32;
     MDVRALPWLP WLLWLLCRGG GDADSRAPFT PTWPRSRERE AAAFRESLNR HRYLNSLFPS
     ENSTAFYGIN QFSYLFPEEF KAIYLRSKPS KFPRYSAEVH MSIPNVSLPL RFDWRDKQVV
     TQVRNQQMCG GCWAFSVVGA VESAYAIKGK PLEDLSVQQV IDCSYNNYGC NGGSTLNALN
     WLNKMQVKLV KDSEYPFKAQ NGLCHYFSGS HSGFSIKGYS AYDFSDQEDE MAKALLTFGP
     LVVIVDAVSW QDYLGGIIQH HCSSGEANHA VLITGFDKTG STPYWIVRNS WGSSWGVDGY
     AHVKMGSNVC GIADSVSSIF V

SwissProt Database

CATS_BOVIN

ID   CATS_BOVIN     STANDARD;      PRT;   217 AA.
AC   P25326;
DT   01-MAY-1992 (REL. 22, CREATED)
DT   01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CATHEPSIN S (EC 3.4.22.27).
GN   CTSS.
OS   BOS TAURUS (BOVINE).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; ARTIODACTYLA.
RN   [1]
RP   SEQUENCE.
RC   TISSUE=SPLEEN;
RX   MEDLINE; 91257334.
RA   RITONJA A., COLIC A., DOLENC I., OGRINC T., PODOBNIK M., TURK V.;
RL   FEBS LETT. 283:329-331(1991).
RN   [2]
RP   SEQUENCE.
RC   TISSUE=SPLEEN;
RX   MEDLINE; 92384944.
RA   DOLENC I., RITONJA A., COLIC A., PODOBNIK M., OGRINC T., TURK V.;
RL   BIOL. CHEM. HOPPE-SEYLER 373:407-412(1992).
RN   [3]
RP   SEQUENCE, AND SEQUENCE OF 22-217 FROM N.A.
RC   TISSUE=SPLEEN;
RX   MEDLINE; 91323515.
RA   WIEDERANDERS B., BROEMME D., KIRSCHKE H., KALKKINEN N., RINNE A.,
RA   PAQUETTE T., TOOTHMAN P.;
RL   FEBS LETT. 286:189-192(1991).
RN   [4]
RP   CHARACTERIZATION.
RX   MEDLINE; 90104320.
RA   BROEMME D., STEINERT A., FRIEBE S., FITTKAU S., WIEDERANDERS B.,
RA   KIRSCHKE H.;
RL   BIOCHEM. J. 264:475-481(1989).
CC   -!- FUNCTION: THIOL PROTEASE. THE BOND-SPECIFICITY OF THIS PROTEINASE
CC       IS IN PART SIMILAR TO THE SPECIFICITIES OF CATHEPSIN L AND
CC       CATHEPSIN N.
CC   -!- CATALYTIC ACTIVITY: SIMILAR TO CATHEPSIN L, BUT WITH MUCH LESS
CC       ACTIVITY ON Z-PHE-ARG-|-NHMEC, AND MORE ACTIVITY ON THE Z-VAL-VAL-
CC       ARG-|-XAA COMPOUND.
CC   -!- SUBUNIT: MONOMER.
CC   -!- SUBCELLULAR LOCATION: LYSOSOMAL.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; M95211; G162815; -.
DR   EMBL; X62001; G312895; -.
DR   PIR; S15844; S15844.
DR   PIR; S23957; S23957.
DR   HSSP; P00785; 1AEC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; LYSOSOME.
FT   ACT_SITE     25     25       BY SIMILARITY.
FT   ACT_SITE    164    164       BY SIMILARITY.
FT   ACT_SITE    184    184       BY SIMILARITY.
FT   DISULFID     12    110       BY SIMILARITY.
FT   DISULFID     22     66       BY SIMILARITY.
FT   DISULFID     56     99       BY SIMILARITY.
FT   DISULFID    158    206       BY SIMILARITY.
SQ   SEQUENCE   217 AA;  23678 MW;  607B2D8F CRC32;
     LPDSMDWREK GCVTEVKYQG ACGSCWAFSA VGALEAQVKL KTGKLVSLSA QNLVDCSTAK
     YGNKGCNGGF MTEAFQYIID NNGIDSEASY PYKAMDGKCQ YDVKNRAATC SRYIELPFGS
     EEALKEAVAN KGPVSVGIDA SHSSFFLYKT GVYYDPSCTQ NVNHGVLVVG YGNLDGKDYW
     LVKNSWGLHF GDQGYIRMAR NSGNHCGIAN YPSYPEI

SwissProt Database

CATS_HUMAN

ID   CATS_HUMAN     STANDARD;      PRT;   331 AA.
AC   P25774;
DT   01-MAY-1992 (REL. 22, CREATED)
DT   01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CATHEPSIN S PRECURSOR (EC 3.4.22.27).
GN   CTSS.
OS   HOMO SAPIENS (HUMAN).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; PRIMATES.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=ALVEOLAR MACROPHAGE;
RX   MEDLINE; 92218373.
RA   SHI G.-P., MUNGER J.S., MEARA J.P., RICH D.H., CHAPMAN H.A.;
RL   J. BIOL. CHEM. 267:7258-7262(1992).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 94209337.
RA   SHI G.-P., WEBB A.C., FOSTER K.E., KNOLL J.H.M., LEMERE C.A.,
RA   MUNGER J.S., CHAPMAN H.A.;
RL   J. BIOL. CHEM. 269:11530-11536(1994).
RN   [3]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 92317106.
RA   WIEDERANDERS B., BROMME D., KIRSCHKE H., VON FIGURA K., SCHMIDT B.,
RA   PETERS C.;
RL   J. BIOL. CHEM. 267:13708-13713(1992).
RN   [4]
RP   REVISION TO 211.
RC   TISSUE=TESTIS;
RA   WIEDERANDERS B., BROEMME D., KIRSCHKE H., VON FIGURA K., SCHMIDT B.,
RA   PETERS C.;
RL   SUBMITTED (MAY-1995) TO EMBL/GENBANK/DDBJ DATA BANKS.
CC   -!- FUNCTION: THIOL PROTEASE. THE BOND-SPECIFICITY OF THIS PROTEINASE
CC       IS IN PART SIMILAR TO THE SPECIFICITIES OF CATHEPSIN L AND
CC       CATHEPSIN N.
CC   -!- CATALYTIC ACTIVITY: SIMILAR TO CATHEPSIN L, BUT WITH MUCH LESS
CC       ACTIVITY ON Z-PHE-ARG-|-NHMEC, AND MORE ACTIVITY ON THE Z-VAL-VAL-
CC       ARG-|-XAA COMPOUND.
CC   -!- SUBUNIT: MONOMER.
CC   -!- SUBCELLULAR LOCATION: LYSOSOMAL.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; S93414; G248406; -.
DR   EMBL; M86553; G179959; -.
DR   EMBL; U07374; G530057; -.
DR   EMBL; U07370; G530057; JOINED.
DR   EMBL; U07371; G530057; JOINED.
DR   EMBL; U07372; G530057; JOINED.
DR   EMBL; U07373; G530057; JOINED.
DR   EMBL; S39127; G250803; -.
DR   EMBL; M90696; G179957; -.
DR   PIR; A42482; A42482.
DR   HSSP; P00785; 1AEC.
DR   MIM; 116845; -.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; LYSOSOME; ZYMOGEN; SIGNAL.
FT   SIGNAL        1     16       POTENTIAL.
FT   PROPEP       17    114       ACTIVATION PEPTIDE.
FT   CHAIN       115    331       CATHEPSIN S.
FT   ACT_SITE    139    139       BY SIMILARITY.
FT   ACT_SITE    278    278       BY SIMILARITY.
FT   ACT_SITE    298    298       BY SIMILARITY.
FT   DISULFID    126    224       BY SIMILARITY.
FT   DISULFID    136    180       BY SIMILARITY.
FT   DISULFID    170    213       BY SIMILARITY.
FT   DISULFID    272    320       BY SIMILARITY.
FT   CARBOHYD    104    104       POTENTIAL.
FT   CONFLICT     92     92       T -> M (IN REF. 3).
FT   CONFLICT    161    161       T -> S (IN REF. 3).
SQ   SEQUENCE   331 AA;  37479 MW;  1A8FFF4B CRC32;
     MKRLVCVLLV CSSAVAQLHK DPTLDHHWHL WKKTYGKQYK EKNEEAVRRL IWEKNLKFVM
     LHNLEHSMGM HSYDLGMNHL GDMTSEEVMS LTSSLRVPSQ WQRNITYKSN PNRILPDSVD
     WREKGCVTEV KYQGSCGACW AFSAVGALEA QLKLKTGKLV TLSAQNLVDC STEKYGNKGC
     NGGFMTTAFQ YIIDNKGIDS DASYPYKAMD QKCQYDSKYR AATCSKYTEL PYGREDVLKE
     AVANKGPVSV GVDARHPSFF LYRSGVYYEP SCTQNVNHGV LVVGYGDLNG KEYWLVKNSW
     GHNFGEEGYI RMARNKGNHC GIASFPSYPE I

SwissProt Database

CATS_RAT

ID   CATS_RAT       STANDARD;      PRT;   330 AA.
AC   Q02765;
DT   01-JUL-1993 (REL. 26, CREATED)
DT   01-JUL-1993 (REL. 26, LAST SEQUENCE UPDATE)
DT   01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE)
DE   CATHEPSIN S PRECURSOR (EC 3.4.22.27).
GN   CTSS.
OS   RATTUS NORVEGICUS (RAT).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; RODENTIA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=BRAIN;
RX   MEDLINE; 93100327.
RA   PETANCESKA S., DEVI L.;
RL   J. BIOL. CHEM. 267:26038-26043(1992).
CC   -!- FUNCTION: THIOL PROTEASE. THE BOND-SPECIFICITY OF THIS PROTEINASE
CC       IS IN PART SIMILAR TO THE SPECIFICITIES OF CATHEPSIN L AND
CC       CATHEPSIN N. MAY BE INVOLVED IN THYROID HORMONE BIOSYNTHESIS.
CC   -!- CATALYTIC ACTIVITY: SIMILAR TO CATHEPSIN L, BUT WITH MUCH LESS
CC       ACTIVITY ON Z-PHE-ARG-|-NHMEC, AND MORE ACTIVITY ON THE Z-VAL-VAL-
CC       ARG-|-XAA COMPOUND.
CC   -!- SUBUNIT: MONOMER.
CC   -!- SUBCELLULAR LOCATION: LYSOSOMAL.
CC   -!- TISSUE SPECIFICITY: HIGHEST LEVELS OCCUR IN THE ILEUM FOLLOWED
CC       BY SPLEEN, BRAIN, THYROID, OVARY AND UTERUS. LOW LEVELS ARE
CC       FOUND IN THE LIVER, KIDNEY, JEJUNUM AND LUNG WITH LOWEST LEVELS
CC       IN THE HEART.
CC   -!- INDUCTION: BY THYROID-STIMULATING HORMONE.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; L03201; G203650; -.
DR   PIR; A45087; A45087.
DR   HSSP; P00785; 1AEC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; LYSOSOME; ZYMOGEN; SIGNAL.
FT   SIGNAL        1     17       POTENTIAL.
FT   PROPEP       18    112       ACTIVATION PEPTIDE.
FT   CHAIN       113    330       CATHEPSIN S.
FT   ACT_SITE    137    137       BY SIMILARITY.
FT   ACT_SITE    277    277       BY SIMILARITY.
FT   ACT_SITE    297    297       BY SIMILARITY.
FT   DISULFID    124    222       BY SIMILARITY.
FT   DISULFID    134    179       BY SIMILARITY.
FT   DISULFID    168    211       BY SIMILARITY.
FT   DISULFID    271    319       BY SIMILARITY.
FT   CARBOHYD    100    100       POTENTIAL.
FT   CARBOHYD    110    110       POTENTIAL.
SQ   SEQUENCE   330 AA;  36833 MW;  6C24B85E CRC32;
     MAVLGAPGVL CDNGATAERP TLDHHWDLWK KTRMRRNTDQ NEEDVRRLIW EKNLKFIMLH
     NLEHSMGMHS YSVGMNHMGD MTPEEVIGYM GSLRIPRPWN RSGTLKSSSN QTLPDSVDWR
     EKGCVTNVKY QGSCGSCWAF SAEGALEGQL KLKTGKLVSL SAQNLVDCST EEKYGNKGCG
     GGFMTEAFQY IIDTSIDSEA SYPYKAMDEK CLYDPKNRAA TCSRYIELPF GDEEALKEAV
     ATKGPVSVGI DDASHSSFFL YQSGVYDDPS CTENMNHGVL VVGYGTLDGK DYWLVKNSWG
     LHFGDQGYIR MARNNKNHCG IASYCSYPEI

SwissProt Database

CATV_NPVAC

ID   CATV_NPVAC     STANDARD;      PRT;   323 AA.
AC   P25783;
DT   01-MAY-1992 (REL. 22, CREATED)
DT   01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   VIRAL CATHEPSIN (EC 3.4.22.-) (V-CATH).
GN   VCATH.
OS   AUTOGRAPHA CALIFORNICA NUCLEAR POLYHEDROSIS VIRUS (ACMNPV).
OC   VIRIDAE; DS-DNA ENVELOPED VIRUSES; BACULOVIRIDAE; EUBACULOVIRINAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=C6;
RA   KUZIO J., FAULKNER P.;
RL   (IN) INSECT CELL CULTURE ENGINEERING, GOOSEN M.F.A., DAUGULIS A.J.,
RL   FAULKNER P., EDS., PP.17-50, MARCEL DEKKER INC., NEW YORK, (1993).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   STRAIN=C6;
RX   MEDLINE; 94303173.
RA   AYRES M.D., HOWARD S.C., KUZIO J., LOPEZ-FERBER M., POSSEE R.D.;
RL   VIROLOGY 202:586-605(1994).
RN   [3]
RP   SEQUENCE OF 118-323 FROM N.A.
RX   MEDLINE; 93183398.
RA   RAWLINGS N.D., PEARL L.H., BUTTLE D.J.;
RL   BIOL. CHEM. HOPPE-SEYLER 373:1211-1215(1992).
CC   -!- FUNCTION: MAY PLAY A ROLE IN DEGRADATION OF INFECTED LARVAE TO
CC       FACILITATE HORIZONTAL TRANSMISSION OF THE VIRUS.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; M67451; G332491; -.
DR   EMBL; L22858; G559196; -.
DR   PIR; S27044; S27044.
DR   HSSP; P00785; 1AEC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE.
FT   ACT_SITE    136    136       BY SIMILARITY.
FT   ACT_SITE    269    269       BY SIMILARITY.
FT   ACT_SITE    289    289       BY SIMILARITY.
FT   DISULFID    133    174       BY SIMILARITY.
FT   DISULFID    167    207       BY SIMILARITY.
FT   DISULFID    262    310       BY SIMILARITY.
SQ   SEQUENCE   323 AA;  36938 MW;  42E80FFE CRC32;
     MNKILFYLFV YGVVNSAAYD LLKAPNYFEE FVHRFNKDYG SEVEKLRRFK IFQHNLNEII
     NKNQNDSAKY EINKFSDLSK DETIAKYTGL SLPIQTQNFC KVIVLDQPPG KGPLEFDWRR
     LNKVTSVKNQ GMCGACWAFA TLASLESQFA IKHNQLINLS EQQMIDCDFV DAGCNGGLLH
     TAFEAIIKMG GVQLESDYPY EADNNNCRMN SNKFLVQVKD CYRYITVYEE KLKDLLRLVG
     PIPMAIDAAD IVNYKQGIIK YCFNSGLNHA VLLVGYGVEN NIPYWTFKNT WGTDWGEDGF
     FRVQQNINAC GMRNELASTA VIY

SwissProt Database

CATV_NPVBM

ID   CATV_NPVBM     STANDARD;      PRT;   323 AA.
AC   P41721;
DT   01-NOV-1995 (REL. 32, CREATED)
DT   01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   VIRAL CATHEPSIN (EC 3.4.22.-) (V-CATH).
GN   VCATH.
OS   BOMBYX MORI NUCLEAR POLYHEDROSIS VIRUS (BMNPV).
OC   VIRIDAE; DS-DNA ENVELOPED VIRUSES; BACULOVIRIDAE; EUBACULOVIRINAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=T3;
RX   MEDLINE; 94365965.
RA   OHKAWA T., MAJIMA K., MAEDA S.;
RL   J. VIROL. 68:6619-6625(1994).
CC   -!- FUNCTION: MAY PLAY A ROLE IN DEGRADATION OF INFECTED LARVAE TO
CC       FACILITATE HORIZONTAL TRANSMISSION OF THE VIRUS.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; U12688; G540066; -.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE.
FT   ACT_SITE    136    136       BY SIMILARITY.
FT   ACT_SITE    269    269       BY SIMILARITY.
FT   ACT_SITE    289    289       BY SIMILARITY.
FT   DISULFID    133    174       BY SIMILARITY.
FT   DISULFID    167    207       BY SIMILARITY.
FT   DISULFID    262    310       BY SIMILARITY.
SQ   SEQUENCE   323 AA;  36922 MW;  A3E34B9E CRC32;
     MNKILFYLFV YAVVKSAAYD PLKAPNYFEE FVHRFNKNYS SEVEKLRRFK IFQHNLNEII
     NKNQNDSAKY EINKFSDLSK DETIAKYTGL SLPTQTQNFC KVILLDQPPG KGPLEFDWRR
     LNKVTSVKNQ GMCGACWAFA TLGSLESQFA IKHNELINLS EQQMIDCDFV DAGCNGGLLH
     TAFEAIIKMG GVQLESDYPY EADNNNCRMN SNKFLVQVKD CYRYIIVYEE KLKDLLPLVG
     PIPMAIDAAD IVNYKQGIIK YCFDSGLNHA VLLVGYGVEN NIPYWTFKNT WGTDWGEDGF
     FRVQQNINAC GMRNELASTA VIY

SwissProt Database

CATV_NPVCF

ID   CATV_NPVCF     STANDARD;      PRT;   324 AA.
AC   P41715;
DT   01-NOV-1995 (REL. 32, CREATED)
DT   01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   VIRAL CATHEPSIN (EC 3.4.22.-) (V-CATH).
GN   VCATH.
OS   CHORISTONEURA FUMIFERANA NUCLEAR POLYHEDROSIS VIRUS (CFMNPV).
OC   VIRIDAE; DS-DNA ENVELOPED VIRUSES; BACULOVIRIDAE; EUBACULOVIRINAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 96138547.
RA   HILL J.E., KUZIO J., FAULKNER P.;
RL   BIOCHIM. BIOPHYS. ACTA 1264:275-278(1995).
CC   -!- FUNCTION: MAY PLAY A ROLE IN DEGRADATION OF INFECTED LARVAE TO
CC       FACILITATE HORIZONTAL TRANSMISSION OF THE VIRUS.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; M97906; G332509; -.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE.
FT   ACT_SITE    137    137       BY SIMILARITY.
FT   ACT_SITE    270    270       BY SIMILARITY.
FT   ACT_SITE    290    290       BY SIMILARITY.
FT   DISULFID    134    175       BY SIMILARITY.
FT   DISULFID    168    208       BY SIMILARITY.
FT   DISULFID    263    311       BY SIMILARITY.
SQ   SEQUENCE   324 AA;  36681 MW;  B931788E CRC32;
     MNKIVLYLLV YGAVQCAAYD VLKAPNYFED FLHKFNKSYS SESEKLRRFQ IFRHNLEEII
     NKNHNDSTAQ YEINKFADLS KDETISKYTG LSLPLQTQNF CEVVVLDRPP DKGPLEFDWR
     RLNKVTSVKN QGMCGACWAF ATLGSLESQF AIKHNQFINL SEQQLIDCDF VDAGCDGGLL
     HTAFEAVMNM GGIQAESDYP YEANNGDCRA NAAKFVVKVK KCYRYITVFE EKLKDLLRSV
     GPIPVAIDAS DIVNYKRGIM KYCANHGLNH AVLLVGYAVE NGVPFWILKN TWGADWGEQG
     YFRVQQNINA CGIQNELPSS AEIY

SwissProt Database

CATX_BOVIN

ID   CATX_BOVIN     STANDARD;      PRT;    73 AA.
AC   P05689;
DT   01-NOV-1988 (REL. 09, CREATED)
DT   01-NOV-1988 (REL. 09, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CATHEPSIN (EC 3.4.22.-) (FRAGMENT).
OS   BOS TAURUS (BOVINE).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; ARTIODACTYLA.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 85149242.
RA   GAY N.J., WALKER J.E.;
RL   BIOCHEM. J. 225:707-712(1985).
RN   [2]
RP   SEQUENCE FROM N.A.
RA   SALVESEN G., GAY N.J., WALKER J.E.;
RL   (IN) CYSTEINE PROTEINASES AND THEIR INHIBITORS, TURK V., ED.,
RL   PP.55-62, WALTER DE GRUYTER, BERLIN AND NEW YORK, (1986).
CC   -!- FUNCTION: THIS IS A FRAGMENT FROM AN UNIDENTIFIED THIOL PROTEASE
CC       FROM THE CATHEPSIN FAMILY.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; X01809; G833778; -.
DR   PIR; A29172; A29172.
DR   PIR; A27014; A27014.
DR   HSSP; P00785; 1AEC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE.
FT   NON_TER       1      1
FT   ACT_SITE     11     11       BY SIMILARITY.
FT   ACT_SITE     31     31       BY SIMILARITY.
SQ   SEQUENCE   73 AA;  8228 MW;  45A94EB2 CRC32;
     SEYNDQAFIN HIVSVAGWGV SDGMEYWIVR NSWGEPWGEH GWMRIVTSTY KGGEGARYNL
     AIEESCTFGD PIV

SwissProt Database

CC1_CARCN

ID   CC1_CARCN      STANDARD;      PRT;    43 AA.
AC   P32954;
DT   01-OCT-1993 (REL. 27, CREATED)
DT   01-OCT-1993 (REL. 27, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE I (EC 3.4.22.-) (CC-I) (FRAGMENT).
OS   CARICA CANDAMARCENSIS (HOOK).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE;
OC   VIOLALES; CARICACEAE.
RN   [1]
RP   SEQUENCE.
RC   TISSUE=LATEX;
RX   MEDLINE; 94030669.
RA   WALREAVENS V., JAZIRI M., VAN BEEUMEN J., SCHNEK A.G.,
RA   KLEINSCHMIDT T., LOOZE Y.;
RL   BIOL. CHEM. HOPPE-SEYLER 374:501-506(1993).
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   HSSP; P00784; 1PAD.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE.
FT   ACT_SITE     25     25       BY SIMILARITY.
FT   NON_TER      43     43
SQ   SEQUENCE   43 AA;  4550 MW;  12C0088C CRC32;
     IVASIDWRQK GAVTPVRNQG SCGSCWTFSS VAAVEGIIKI RGT

SwissProt Database

CC2_CARCN

ID   CC2_CARCN      STANDARD;      PRT;    43 AA.
AC   P32955;
DT   01-OCT-1993 (REL. 27, CREATED)
DT   01-OCT-1993 (REL. 27, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE II (EC 3.4.22.-) (CC-II) (FRAGMENT).
OS   CARICA CANDAMARCENSIS (HOOK).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE;
OC   VIOLALES; CARICACEAE.
RN   [1]
RP   SEQUENCE.
RC   TISSUE=LATEX;
RX   MEDLINE; 94030669.
RA   WALREAVENS V., JAZIRI M., VAN BEEUMEN J., SCHNEK A.G.,
RA   KLEINSCHMIDT T., LOOZE Y.;
RL   BIOL. CHEM. HOPPE-SEYLER 374:501-506(1993).
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   HSSP; P10056; 1PPO.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE.
FT   ACT_SITE     25     25       BY SIMILARITY.
FT   NON_TER      43     43
SQ   SEQUENCE   43 AA;  4568 MW;  FCF58EA3 CRC32;
     YPGSVDWRQK GAVTPVKDQN PCGSCWAFST VATVEGINKI VTG

SwissProt Database

CC3_CARCN

ID   CC3_CARCN      STANDARD;      PRT;    43 AA.
AC   P32956;
DT   01-OCT-1993 (REL. 27, CREATED)
DT   01-OCT-1993 (REL. 27, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE III (EC 3.4.22.-) (CC-III) (FRAGMENT).
OS   CARICA CANDAMARCENSIS (HOOK).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE;
OC   VIOLALES; CARICACEAE.
RN   [1]
RP   SEQUENCE.
RC   TISSUE=LATEX;
RX   MEDLINE; 94030669.
RA   WALREAVENS V., JAZIRI M., VAN BEEUMEN J., SCHNEK A.G.,
RA   KLEINSCHMIDT T., LOOZE Y.;
RL   BIOL. CHEM. HOPPE-SEYLER 374:501-506(1993).
CC   -!- PTM: GLYCOSYLATED.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   HSSP; P10056; 1PPO.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; GLYCOPROTEIN.
FT   ACT_SITE     25     25       BY SIMILARITY.
FT   NON_TER      43     43
SQ   SEQUENCE   43 AA;  4636 MW;  3E548179 CRC32;
     YPESIDWRKK GAVTPVKNQG SCGSCWAFST IATVEGINKI VHG

SwissProt Database

CC4_CARCN

ID   CC4_CARCN      STANDARD;      PRT;    43 AA.
AC   P32957;
DT   01-OCT-1993 (REL. 27, CREATED)
DT   01-OCT-1993 (REL. 27, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE IV (EC 3.4.22.-) (CC-IV) (FRAGMENT).
OS   CARICA CANDAMARCENSIS (HOOK).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE;
OC   VIOLALES; CARICACEAE.
RN   [1]
RP   SEQUENCE.
RC   TISSUE=LATEX;
RX   MEDLINE; 94030669.
RA   WALREAVENS V., JAZIRI M., VAN BEEUMEN J., SCHNEK A.G.,
RA   KLEINSCHMIDT T., LOOZE Y.;
RL   BIOL. CHEM. HOPPE-SEYLER 374:501-506(1993).
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   HSSP; P00784; 1PAD.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE.
FT   ACT_SITE     25     25       BY SIMILARITY.
FT   NON_TER      43     43
SQ   SEQUENCE   43 AA;  4685 MW;  A7AA708B CRC32;
     YPESIDWRKK GAVTPVKNQG SCGSCWAFST IVTVEGINKI RTG

SwissProt Database

CPP1_ENTHI

ID   CPP1_ENTHI     STANDARD;      PRT;   315 AA.
AC   Q01957;
DT   01-JUN-1994 (REL. 29, CREATED)
DT   01-JUN-1994 (REL. 29, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE 1 PRECURSOR (EC 3.4.22.-).
GN   CPP1 OR CPP.
OS   ENTAMOEBA HISTOLYTICA.
OC   EUKARYOTA; PROTOZOA; SARCOMASTIGOPHORA; SARCODINA; RHIZOPODA; LOBOSA;
OC   AMOEBIDA.
RN   [1]
RP   SEQUENCE FROM N.A., AND PARTIAL SEQUENCE.
RC   STRAIN=HM-1:IMSS;
RX   MEDLINE; 92389981.
RA   TANNICH E., NICKEL R., BUSS H., HORSTMANN R.D.;
RL   MOL. BIOCHEM. PARASITOL. 54:109-111(1992).
RN   [2]
RP   SEQUENCE OF 4-315 FROM N.A.
RC   STRAIN=HM-1:IMSS;
RX   MEDLINE; 91161560.
RA   TANNICH E., SCHOLZE H., NICKE R., HORSTMANN R.D.;
RL   J. BIOL. CHEM. 266:4798-4803(1991).
RN   [3]
RP   SEQUENCE OF 94-99; 101-110 AND 112-113.
RC   STRAIN=HM-1:IMSS;
RX   MEDLINE; 90095985.
RA   SCHULTE W., SCHOLZE H.;
RL   J. PROTOZOOL. 36:538-543(1989).
CC   -!- FUNCTION: INVOLVED IN THE DESTRUCTION OF HUMAN TISSUE BY
CC       E.HISTOLYTICA. CAN ABOLISH ADHESION AND DEGRADE MATRIX PROTEINS
CC       SUCH AS COLLAGEN, LAMININ AND FIBRONECTIN. MAY PLAY A ROLE
CC       IMPORTANT ROLE IN PATHOGENICITY.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; M94162; G158926; -.
DR   EMBL; M64712; G158932; -.
DR   HSSP; P07858; 1HUC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL; MULTIGENE FAMILY.
FT   SIGNAL        1      ?       POTENTIAL.
FT   PROPEP        ?     93       ACTIVATION PEPTIDE.
FT   CHAIN        94    315       CYSTEINE PROTEINASE 1.
FT   ACT_SITE    118    118       BY SIMILARITY.
FT   ACT_SITE    259    259       BY SIMILARITY.
FT   ACT_SITE    279    279       BY SIMILARITY.
FT   DISULFID    115    161       BY SIMILARITY.
FT   DISULFID    152    193       BY SIMILARITY.
FT   CONFLICT      4      4       F -> V (IN REF. 2).
FT   CONFLICT    269    269       V -> A (IN REF. 2).
SQ   SEQUENCE   315 AA;  35056 MW;  9AA2B21F CRC32;
     MFTFILMFYI GYGIDFNTWV ANNNKHFTAV ESLRRRAIFN MNARIVAENN RKETFKLSVD
     GPFAAMTNEE YNSLLKLKRS GEEKGEVRYL NIQAPKAVDW RKKGKVTPIR DQGNCGSCYT
     FGSIAALEGR LLIEKGGDSE TLDLSEEHMV QCTREDGNNG CNGGLGSNVY NYIMENGIAK
     ESDYPYTGSD STCRSDVKAF AKIKSYNRVA RNNEVELKAA ISQGLVDVSI DASSVQFQLY
     KSGAYTDTQC KNNYFALNHE VCAVGYGVVD GKECWIVRNS WGTGWGEKGY INMVIEGNTC
     GVATDPLYPT GVEYL

SwissProt Database

CPP2_ENTHI

ID   CPP2_ENTHI     STANDARD;      PRT;   315 AA.
AC   Q01958;
DT   01-JUN-1994 (REL. 29, CREATED)
DT   01-JUN-1994 (REL. 29, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE 2 PRECURSOR (EC 3.4.22.-).
GN   CPP2.
OS   ENTAMOEBA HISTOLYTICA.
OC   EUKARYOTA; PROTOZOA; SARCOMASTIGOPHORA; SARCODINA; RHIZOPODA; LOBOSA;
OC   AMOEBIDA.
RN   [1]
RP   SEQUENCE FROM N.A., AND PARTIAL SEQUENCE.
RC   STRAIN=HM-1:IMSS;
RX   MEDLINE; 92389981.
RA   TANNICH E., NICKEL R., BUSS H., HORSTMANN R.D.;
RL   MOL. BIOCHEM. PARASITOL. 54:109-111(1992).
CC   -!- FUNCTION: INVOLVED IN THE DESTRUCTION OF HUMAN TISSUE BY
CC       E.HISTOLYTICA. CAN ABOLISH ADHESION AND DEGRADE MATRIX PROTEINS
CC       SUCH AS COLLAGEN, LAMININ AND FIBRONECTIN. MAY PLAY A ROLE
CC       IMPORTANT ROLE IN PATHOGENICITY.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; M94163; G158928; -.
DR   HSSP; P07858; 1HUC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL; MULTIGENE FAMILY.
FT   SIGNAL        1      ?       POTENTIAL.
FT   PROPEP        ?     93       ACTIVATION PEPTIDE.
FT   CHAIN        94    315       CYSTEINE PROTEINASE 2.
FT   ACT_SITE    118    118       BY SIMILARITY.
FT   ACT_SITE    259    259       BY SIMILARITY.
FT   ACT_SITE    279    279       BY SIMILARITY.
FT   DISULFID    115    161       BY SIMILARITY.
FT   DISULFID    152    193       BY SIMILARITY.
SQ   SEQUENCE   315 AA;  34688 MW;  D28A63B7 CRC32;
     MFAFICLLAI ASAIDFNTWA SKNNKHFTAI EKLRRRAIFN MNAKFVDSFN KIGSFKLSVD
     GPFAAMTNEE YRTLLKSKRT TEENGQVKYL NIQAPESVDW RKEGKVTPIR DQAQCGSCYT
     FGSLAALEGR LLIEKGGDAN TLDLSEEHMV QCTRDNGNNG CNGGLGSNVY DYIIEHGVAK
     ESDYPYTGSD STCKTNVKSF AKITGYTKVP RNNEAELKAA LSQGLVDVSI DASSAKFQLY
     KSGAYTDTKC KNNYFALNHE VCAVGYGVVD GKECWIVRNS WGTGWGDKGY INMVIEGNTC
     GVATDPLYPT GVQYL

SwissProt Database

CPP3_ENTHI

ID   CPP3_ENTHI     STANDARD;      PRT;   308 AA.
AC   Q06964;
DT   01-JUN-1994 (REL. 29, CREATED)
DT   01-JUN-1994 (REL. 29, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE 3 PRECURSOR (EC 3.4.22.-) (CYSTEINE PROTEINASE
DE   ACP3) (FRAGMENT).
GN   CPNP.
OS   ENTAMOEBA HISTOLYTICA.
OC   EUKARYOTA; PROTOZOA; SARCOMASTIGOPHORA; SARCODINA; RHIZOPODA; LOBOSA;
OC   AMOEBIDA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=SAW 1734;
RX   MEDLINE; 91161560.
RA   TANNICH E., SCHOLZE H., NICKE R., HORSTMANN R.D.;
RL   J. BIOL. CHEM. 266:4798-4803(1991).
RN   [2]
RP   PARTIAL SEQUENCE FROM N.A., AND SEQUENCE OF 87-94.
RC   STRAIN=HM-1;
RX   MEDLINE; 93232277.
RA   REED S., BOUVIER J., POLLACK A.S., ENGEL J.C., BROWN M., HIRATA K.,
RA   QUE X., EAKIN A., HAGBLOM P., GILLIN F., MCKERROW J.H.;
RL   J. CLIN. INVEST. 91:1532-1540(1993).
CC   -!- FUNCTION: CAN ABOLISH ADHESION AND DEGRADE MATRIX PROTEINS
CC       SUCH AS COLLAGEN, LAMININ AND FIBRONECTIN.
CC   -!- SUBCELLULAR LOCATION: EXTRACELLULAR.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; M64721; G158930; -.
DR   HSSP; P07858; 1HUC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; SIGNAL; MULTIGENE FAMILY; ZYMOGEN.
FT   NON_TER       1      1
FT   SIGNAL       <1      ?       POTENTIAL.
FT   PROPEP        ?     86       ACTIVATION PEPTIDE.
FT   CHAIN        87    308       CYSTEINE PROTEINASE 3.
FT   ACT_SITE    111    111       BY SIMILARITY.
FT   ACT_SITE    252    252       BY SIMILARITY.
FT   ACT_SITE    272    272       BY SIMILARITY.
FT   DISULFID    108    154       BY SIMILARITY.
FT   DISULFID    145    186       BY SIMILARITY.
SQ   SEQUENCE   308 AA;  33680 MW;  C16AD1AB CRC32;
     LAIANAIDFN TWAANNNKHF TAVEALRRRA IFNMNARFVA EFNKKGSFKL SVDGPFAAMT
     NEEYRTLLKS KRTVEENGKV TYLNIQAPES VDWRAQGKVT PIRDQAQCGS CYTFGSLAAL
     EGRLLIEKGG NANTLDLSEE HLVQCTRDNG NNGCNGGLGS NVYDYIIQNG VAKESDYPYT
     GTDSTCKTNV KAFAKITGYN KVPRNNEAEL KAALSQGLVD VSIDASSAKF QLYKSGAYSD
     TKCKNNFFAL NHEVCAVGYG VVDGKECWIV RNSWGTGWGD KGYINMVIEG NTCGVATDPL
     YPTGVQYL

SwissProt Database

CPR3_CAEEL

ID   CPR3_CAEEL     STANDARD;      PRT;   370 AA.
AC   P43507;
DT   01-NOV-1995 (REL. 32, CREATED)
DT   01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE)
DT   01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE)
DE   CATHEPSIN B-LIKE CYSTEINE PROTEINASE 3 PRECURSOR (EC 3.4.22.-).
GN   CPR-3.
OS   CAENORHABDITIS ELEGANS.
OC   EUKARYOTA; METAZOA; ACOELOMATES; NEMATODA; SECERNENTEA; RHABDITIDA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=BRISTOL N2;
RA   LARMINIE C.G.C., JOHNSTONE I.L.;
RL   SUBMITTED (MAR-1995) TO EMBL/GENBANK/DDBJ DATA BANKS.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
CC   -!- SIMILARITY: STRONGEST, TO CATHEPSIN B.
DR   EMBL; L39890; G675494; -.
DR   EMBL; L39925; G675496; -.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL.
FT   SIGNAL        1     16       POTENTIAL.
FT   PROPEP       17     91       POTENTIAL.
FT   CHAIN        92    370       CATHEPSIN B-LIKE CYSTEINE PROTEINASE 3.
FT   ACT_SITE    120    120       BY SIMILARITY.
FT   ACT_SITE    284    284       BY SIMILARITY.
FT   ACT_SITE    304    304       BY SIMILARITY.
FT   DISULFID    105    134       BY SIMILARITY.
FT   DISULFID    117    162       BY SIMILARITY.
FT   DISULFID    153    210       BY SIMILARITY.
FT   DISULFID    154    158       BY SIMILARITY.
FT   DISULFID    190    214       BY SIMILARITY.
FT   DISULFID    198    202       BY SIMILARITY.
FT   CARBOHYD    138    138       POTENTIAL.
SQ   SEQUENCE   370 AA;  40770 MW;  A479AAE7 CRC32;
     MLKVYFLALF LAGCSAFVLD EIRGINIGQS PQKVLVDHVN TVQTSWVAEH NEISEFEMKF
     KVMDVKFAEP LEKDSDVASE LFVRGEIVPE PLPDTFDARE KWPDCNTIKL IRNQATCGSC
     WAFGAAEVIS DRVCIQSNGT QQPVISVEDI LSCCGTTCGY GCKGGYSIEA LRFWASSGAV
     TGGDYGGHGC MPYSFAPCTK NCPESTTPSC KTTCQSSYKT EEYKKDKHYG ASAYKVTTTK
     SVTEIQTEIY HYGPVEASYK VYEDFYHYKS GVYHYTSGKL VGGHAVKIIG WGVENGVDYW
     LIANSWGTSF GEKGFFKIRR GTNECQIEGN VVAGIAKLGT HSETYEDDGG AATSCSFIMC
     TLMVLTYYFV

SwissProt Database

CPR4_CAEEL

ID   CPR4_CAEEL     STANDARD;      PRT;   335 AA.
AC   P43508;
DT   01-NOV-1995 (REL. 32, CREATED)
DT   01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CATHEPSIN B-LIKE CYSTEINE PROTEINASE 4 PRECURSOR (EC 3.4.22.-).
GN   CPR-4 OR F44C4.3.
OS   CAENORHABDITIS ELEGANS.
OC   EUKARYOTA; METAZOA; ACOELOMATES; NEMATODA; SECERNENTEA; RHABDITIDA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=BRISTOL N2;
RA   LARMINIE C.G.C., JOHNSTONE I.L.;
RL   SUBMITTED (MAR-1995) TO EMBL/GENBANK/DDBJ DATA BANKS.
RN   [2]
RP   SEQUENCE FROM N.A.
RC   STRAIN=BRISTOL N2;
RA   WATERSTON R.;
RL   SUBMITTED (FEB-1996) TO EMBL/GENBANK/DDBJ DATA BANKS.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
CC   -!- SIMILARITY: STRONGEST, TO CATHEPSIN B.
DR   EMBL; L39895; G675500; -.
DR   EMBL; L39926; G695293; -.
DR   EMBL; U50313; G1226319; -.
DR   WORMPEP; F44C4.3; CE07251.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL.
FT   SIGNAL        1     15       POTENTIAL.
FT   PROPEP       16     80       POTENTIAL.
FT   CHAIN        81    335       CATHEPSIN B-LIKE CYSTEINE PROTEINASE 4.
FT   ACT_SITE    109    109       BY SIMILARITY.
FT   ACT_SITE    281    281       BY SIMILARITY.
FT   ACT_SITE    301    301       BY SIMILARITY.
FT   DISULFID     94    123       BY SIMILARITY.
FT   DISULFID    106    150       BY SIMILARITY.
FT   DISULFID    142    209       BY SIMILARITY.
FT   DISULFID    143    146       BY SIMILARITY.
FT   DISULFID    179    213       BY SIMILARITY.
FT   DISULFID    187    199       BY SIMILARITY.
FT   CARBOHYD    193    193       POTENTIAL.
SQ   SEQUENCE   335 AA;  36493 MW;  1AF74379 CRC32;
     MKYLILAALV AVTAGLVIPL VPKTQEAITE YVNSKQSLWK AEIPKDITIE QVKKRLMRTE
     FVAPHTPDVE VVKHDINEDT IPATFDARTQ WPNCMSINNI RDQSDCGSCW AFAAAEAASD
     RFCIASNGAV NTLLSAEDVL SCCSNCGYGC EGGYPINAWK YLVKSGFCTG GSYEAQFGCK
     PYSLAPCGET VGNVTWPSCP DDGYDTPACV NKCTNKNYNV AYTADKHFGS TAYAVGKKVS
     QIQAEIIAHG PVEAAFTVYE DFYQYKTGVY VHTTGQELGG HAIRILGWGT DNGTPYWLVA
     NSWNVNWGEN GYFRIIRGTN ECGIEHAVVG GVPKV

SwissProt Database

CPR5_CAEEL

ID   CPR5_CAEEL     STANDARD;      PRT;   344 AA.
AC   P43509;
DT   01-NOV-1995 (REL. 32, CREATED)
DT   01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE)
DT   01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE)
DE   CATHEPSIN B-LIKE CYSTEINE PROTEINASE 5 PRECURSOR (EC 3.4.22.-).
GN   CPR-5.
OS   CAENORHABDITIS ELEGANS.
OC   EUKARYOTA; METAZOA; ACOELOMATES; NEMATODA; SECERNENTEA; RHABDITIDA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=BRISTOL N2;
RA   LARMINIE C.G.C., JOHNSTONE I.L.;
RL   SUBMITTED (MAR-1995) TO EMBL/GENBANK/DDBJ DATA BANKS.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
CC   -!- SIMILARITY: STRONGEST, TO CATHEPSIN B.
DR   EMBL; L39896; G671713; -.
DR   EMBL; L39927; G675502; -.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL.
FT   SIGNAL        1     15       POTENTIAL.
FT   PROPEP       16     81       POTENTIAL.
FT   CHAIN        82    344       CATHEPSIN B-LIKE CYSTEINE PROTEINASE 5.
FT   ACT_SITE    110    110       BY SIMILARITY.
FT   ACT_SITE    286    286       BY SIMILARITY.
FT   ACT_SITE    306    306       BY SIMILARITY.
FT   DISULFID     95    124       BY SIMILARITY.
FT   DISULFID    107    154       BY SIMILARITY.
FT   DISULFID    143    213       BY SIMILARITY.
FT   DISULFID    144    150       BY SIMILARITY.
FT   DISULFID    183    217       BY SIMILARITY.
FT   DISULFID    191    203       BY SIMILARITY.
SQ   SEQUENCE   344 AA;  37391 MW;  EB9789C2 CRC32;
     MWKLSAILLV AAASAVVIPG HREAPALTGQ ALIDYVNSAQ KLWTAGHQVI PKEKITKKLM
     DVKYLVPHKD EDIVATEVSD AIPDHFDARD QWPNCMSINN IRDQSDCGSC WAFAAAEAIS
     DRTCIASNGA VNTLLSSEDL LSCCTGMFSC GNGCEGGYPI QAWKWWVKHG LVTGGSYETQ
     FGCKPYSIAP CGETVNGVKW PACPEDTEPT PKCVDSCTSK NNYATPYLQD KHFGSTAYAV
     GKKVEQIQTE ILTNGPIEVA FTVYEDFYQY TTGVYVHTAG ASLGGHAVKI LGWGVDNGTP
     YWLVANSWNV AWGEKGYFRI IRGLNECGIE HSAVAGIPDL ARHN

SwissProt Database

CPR6_CAEEL

ID   CPR6_CAEEL     STANDARD;      PRT;   379 AA.
AC   P43510;
DT   01-NOV-1995 (REL. 32, CREATED)
DT   01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CATHEPSIN B-LIKE CYSTEINE PROTEINASE 6 PRECURSOR (EC 3.4.22.-).
GN   CPR-6 OR C25B8.3.
OS   CAENORHABDITIS ELEGANS.
OC   EUKARYOTA; METAZOA; ACOELOMATES; NEMATODA; SECERNENTEA; RHABDITIDA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=BRISTOL N2;
RA   LARMINIE C.G.C., JOHNSTONE I.L.;
RL   SUBMITTED (MAR-1995) TO EMBL/GENBANK/DDBJ DATA BANKS.
RN   [2]
RP   SEQUENCE FROM N.A.
RC   STRAIN=BRISTOL N2;
RA   WATERSTON R.;
RL   SUBMITTED (NOV-1995) TO EMBL/GENBANK/DDBJ DATA BANKS.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
CC   -!- SIMILARITY: STRONGEST, TO CATHEPSIN B.
DR   EMBL; L39894; G671715; -.
DR   EMBL; L39939; G695294; -.
DR   EMBL; U41556; G1118083; -.
DR   WORMPEP; C25B8.3; CE04078.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL.
FT   SIGNAL        1     16       POTENTIAL.
FT   PROPEP       17    104       POTENTIAL.
FT   CHAIN       105    379       CATHEPSIN B-LIKE CYSTEINE PROTEINASE 6.
FT   ACT_SITE    133    133       BY SIMILARITY.
FT   ACT_SITE    305    305       BY SIMILARITY.
FT   ACT_SITE    325    325       BY SIMILARITY.
FT   DISULFID    118    147       BY SIMILARITY.
FT   DISULFID    130    174       BY SIMILARITY.
FT   DISULFID    166    233       BY SIMILARITY.
FT   DISULFID    167    170       BY SIMILARITY.
FT   DISULFID    203    237       BY SIMILARITY.
FT   DISULFID    211    223       BY SIMILARITY.
FT   CARBOHYD    196    196       POTENTIAL.
SQ   SEQUENCE   379 AA;  42404 MW;  D782979C CRC32;
     MKTLLFLSCI VVAAYCACND NLESVLDKYR NREIDSEAAE LDGDDLIDYV NENQNLWTAK
     KQRRFSSVYG ENDKAKWGLM GVNHVRLSVK GKQHLSKTKD LDLDIPESFD SRDNWPKCDS
     IKVIRDQSSC GSCWAFGAVE AMSDRICIAS HGELQVTLSA DDLLSCCKSC GFGCNGGDPL
     AAWRYWVKDG IVTGSNYTAN NGCKPYPFPP CEHHSKKTHF DPCPHDLYPT PKCEKKCVSD
     YTDKTYSEDK FFGASAYGVK DDVEAIQKEL MTHGPLEIAF EVYEDFLNYD GGVYVHTGGK
     LGGGHAVKLI GWGIDDGIPY WTVANSWNTD WGEDGFFRIL RGVDECGIES GVVGGIPKLN
     SLTSRLHRHH RRHVYDDNY

SwissProt Database

CYS1_CAEEL

ID   CYS1_CAEEL     STANDARD;      PRT;   329 AA.
AC   P25807;
DT   01-MAY-1992 (REL. 22, CREATED)
DT   01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   GUT-SPECIFIC CYSTEINE PROTEINASE PRECURSOR (EC 3.4.22.-).
GN   GCP-1.
OS   CAENORHABDITIS ELEGANS.
OC   EUKARYOTA; METAZOA; ACOELOMATES; NEMATODA; SECERNENTEA; RHABDITIDA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=BRISTOL N2;
RX   MEDLINE; 92244294.
RA   RAY C., MCKERROW J.H.;
RL   MOL. BIOCHEM. PARASITOL. 51:239-250(1992).
CC   -!- FUNCTION: THIOL PROTEASE. HAS A ROLE AS A DIGESTIVE ENZYME.
CC   -!- TISSUE SPECIFICITY: INTESTINE.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
CC   -!- SIMILARITY: STRONGEST, TO CATHEPSIN B.
DR   EMBL; M74797; G1395200; ALT_SEQ.
DR   HSSP; P07858; 1HUC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL.
FT   SIGNAL        1      ?       POTENTIAL.
FT   PROPEP        ?     84       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN        85    329       GUT-SPECIFIC CYSTEINE PROTEINASE.
FT   ACT_SITE    113    113       BY SIMILARITY.
FT   ACT_SITE    275    275       BY SIMILARITY.
FT   ACT_SITE    295    295       BY SIMILARITY.
FT   DISULFID     98    127       BY SIMILARITY.
FT   DISULFID    110    155       BY SIMILARITY.
FT   DISULFID    146    204       BY SIMILARITY.
FT   DISULFID    147    151       BY SIMILARITY.
FT   DISULFID    183    208       BY SIMILARITY.
FT   DISULFID    191    196       BY SIMILARITY.
SQ   SEQUENCE   329 AA;  35456 MW;  6DF6A1F9 CRC32;
     MEVPYPYPLC AVTLAFVPIN HQSAVETLTG QALVDYVNSA QSLFKTEHVE ITEEEMKFKL
     MDGKYAAAHS DEIRATEQEV VLASVPATFD SRTQWSECKS IKLIRDQATC GSCWAFGAAE
     MISDRTCIET KGAQQPIISP DDLLSCCGSS CGNGCEGGYP IQALRWWDSK GVVTGGDYHG
     AGCKPYPIAP CTSGNCPESK TPSCSMSCQS GYSTAYAKDK HFGVSAYAVP KNAASIQAEI
     YANGPVEAAF SVYEDFYKYK SGVYKHTAGK YLGGHAIKII GWGTESGSPY WLVANSWGVN
     WGESGFFKIY RGDDQCGIES AVVAGKAKV

SwissProt Database

CYS1_DICDI

ID   CYS1_DICDI     STANDARD;      PRT;   343 AA.
AC   P04988;
DT   13-AUG-1987 (REL. 05, CREATED)
DT   13-AUG-1987 (REL. 05, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE 1 PRECURSOR (EC 3.4.22.-).
GN   CPRA OR CP1.
OS   DICTYOSTELIUM DISCOIDEUM (SLIME MOLD).
OC   EUKARYOTA; PROTOZOA; SARCOMASTIGOPHORA; SARCODINA; RHIZOPODA;
OC   EUMYCETOZOA; DICTYOSTELIA.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 85257519.
RA   WILLIAMS J.G., NORTH M.J., MAHBUBANI H.M.;
RL   EMBO J. 4:999-1006(1985).
RN   [2]
RP   CARBOHYDRATES.
RX   MEDLINE; 96210028.
RA   MEHTA D.P., ICHIKAWA M., SALIMATH P.V., ETCHISON J.R., HAAK R.,
RA   MANZI A., FREEZE H.H.;
RL   J. BIOL. CHEM. 271:10897-10903(1996).
CC   -!- FUNCTION: CYSTEINE PROTEINASES 1 AND 2 ARE BELIEVED TO PARTICIPATE
CC       IN THE BREAKDOWN OF PROTEIN DURING DIFFERENTIATION OF DICTOSTELIUM
CC       AS A RESPONSE TO STARVATION.
CC   -!- SUBCELLULAR LOCATION: LYSOSOMAL.
CC   -!- PTM: PHOSPHOGLYCOSYLATED, CONTAINS GLCNAC-ALPHA-1-P-SER RESIDUES.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; X02407; E1716; ALT_INIT.
DR   PIR; A22827; KHDO.
DR   HSSP; P00785; 1AEC.
DR   DICTYDB; DD02003; CPRA.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; LYSOSOME; ZYMOGEN; GLYCOPROTEIN;
KW   PHOSPHORYLATION; SIGNAL.
FT   SIGNAL        1     18       POTENTIAL.
FT   PROPEP       19    117       ACTIVATION PEPTIDE.
FT   CHAIN       118    343       CYSTEINE PROTEINASE 1.
FT   ACT_SITE    142    142       BY SIMILARITY.
FT   ACT_SITE    286    286       BY SIMILARITY.
FT   ACT_SITE    311    311       BY SIMILARITY.
FT   DISULFID    139    190       BY SIMILARITY.
FT   DISULFID    173    224       BY SIMILARITY.
FT   DISULFID    279    332       BY SIMILARITY.
SQ   SEQUENCE   343 AA;  38495 MW;  4647B1CD CRC32;
     MKVILLFVLA VFTVFVSSRG IPPEEQSQFL EFQDKFNKKY SHEEYLERFE IFKSNLGKIE
     ELNLIAINHK ADTKFGVNKF ADLSSDEFKN YYLNNKEAIF TDDLPVADYL DDEFINSIPT
     AFDWRTRGAV TPVKNQGQCG SCWSFSTTGN VEGQHFISQN KLVSLSEQNL VDCDHECMEY
     EGEEACDEGC NGGLQPNAYN YIIKNGGIQT ESSYPYTAET GTQCNFNSAN IGAKISNFTM
     IPKNETVMAG YIVSTGPLAI AADAVEWQFY IGGVFDIPCN PNSLDHGILI VGYSAKNTIF
     RKNMPYWIVK NSWGADWGEQ GYIYLRRGKN TCGVSNFVST SII

SwissProt Database

CYS1_HAECO

ID   CYS1_HAECO     STANDARD;      PRT;   342 AA.
AC   P19092;
DT   01-NOV-1990 (REL. 16, CREATED)
DT   01-NOV-1990 (REL. 16, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CATHEPSIN B-LIKE CYSTEINE PROTEINASE 1 PRECURSOR (EC 3.4.22.-).
GN   AC-1.
OS   HAEMONCHUS CONTORTUS.
OC   EUKARYOTA; METAZOA; ACOELOMATES; NEMATODA; SECERNENTEA; SPIRURIDA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=ISOLATE BPL1;
RX   MEDLINE; 90348715.
RA   COX G.N., PRATT D., HAGEMAN R., BOISVENUE R.J.;
RL   MOL. BIOCHEM. PARASITOL. 41:25-34(1990).
CC   -!- FUNCTION: EXPRESSION OF THE PROTEASE CORRELATES WITH BLOOD-FEEDING
CC       AND SUGGESTS A ROLE FOR THE PROTEASE IN BLOOD DIGESTION.
CC   -!- DEVELOPMENTAL STAGE: AT LOW LEVEL IN THE THIRD AND FOURTH-STAGE
CC       LARVAE, AND ABUNDANT IN ADULT WORMS.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
CC   -!- SIMILARITY: STRONGEST, TO CATHEPSIN B.
DR   EMBL; M31112; G159173; -.
DR   PIR; A45524; A45524.
DR   HSSP; P07858; 1HUC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; GLYCOPROTEIN; SIGNAL;
KW   MULTIGENE FAMILY.
FT   SIGNAL        1      ?       POTENTIAL.
FT   PROPEP        ?     86       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN        87    342       CYSTEINE PROTEINASE 1.
FT   ACT_SITE    114    114       BY SIMILARITY.
FT   ACT_SITE    285    285       BY SIMILARITY.
FT   ACT_SITE    305    305       BY SIMILARITY.
FT   DISULFID    100    128       BY SIMILARITY.
FT   DISULFID    111    156       BY SIMILARITY.
FT   DISULFID    147    214       BY SIMILARITY.
FT   DISULFID    148    152       BY SIMILARITY.
FT   DISULFID    185    218       BY SIMILARITY.
FT   DISULFID    193    205       BY SIMILARITY.
FT   CARBOHYD     99     99       POTENTIAL.
FT   CARBOHYD    138    138       POTENTIAL.
FT   CARBOHYD    198    198       POTENTIAL.
FT   CARBOHYD    296    296       POTENTIAL.
SQ   SEQUENCE   342 AA;  38459 MW;  290E7705 CRC32;
     MKYLVLALCT YLCSQTGADE NAAQGIPLEA QRLTGEPLVA YLRRSQNLFE VNSAPTPNFE
     QKIMDIKYKH QKLNLMVKED PDPEVDIPPS YDPRDVWKNC TTFYIRDQAN CGSCWAVSTA
     AAISDRICIA SKAEKQVNIS ATDIMTCCRP QCGDGCEGGW PIEAWKYFIY DGVVSGGEYL
     TKDVCRPYPI HPCGHHGNDT YYGECRGTAP TPPCKRKCRP GVRKMYRIDK RYGKDAYIVK
     QSVKAIQSEI LRNGPVVASF AVYEDFRHYK SGIYKHTAGE LRGYHAVKMI GWGNENNTDF
     WLIANSWHND WGEKGYFRII RGTNDCGIEG TIAAGIVDTE SL

SwissProt Database

CYS1_HOMAM

ID   CYS1_HOMAM     STANDARD;      PRT;   322 AA.
AC   P13277;
DT   01-JAN-1990 (REL. 13, CREATED)
DT   01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   DIGESTIVE CYSTEINE PROTEINASE 1 PRECURSOR (EC 3.4.22.-).
GN   LCP1.
OS   HOMARUS AMERICANUS (AMERICAN LOBSTER).
OC   EUKARYOTA; METAZOA; ARTHROPODA; CRUSTACEA; MALACOSTRACA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=DIGESTIVE GLAND;
RX   MEDLINE; 92070467.
RA   LAYCOCK M.V., MACKAY R.M., DI FRUSCIO M., GALLANT J.W.;
RL   FEBS LETT. 292:115-120(1991).
RN   [2]
RP   SEQUENCE OF 106-133.
RC   TISSUE=DIGESTIVE JUICE;
RX   MEDLINE; 90088376.
RA   LAYCOCK M.V., HIRAMA T., HASNAIN S., WATSON D., STORER A.C.;
RL   BIOCHEM. J. 263:439-444(1989).
CC   -!- ENZYME REGULATION: INHIBITED BY E-64, ANTIPAIN, LEUPEPTIN, HEAVY
CC       METAL IONS, IODOACETIC ACID, DITHIONITROBENZENE, P-HYDROXYMERCURI-
CC       BENZOATE; ACTIVATED BY MERCAPTOETHANOL AND DITHIOTHREITOL.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
CC   -!- SIMILARITY: STRONGEST, TO PAPAIN AND CATHEPSIN L.
DR   EMBL; X63567; G11051; -.
DR   PIR; S06154; S06154.
DR   PIR; S19649; S19649.
DR   HSSP; P00785; 1AEC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL; MULTIGENE FAMILY.
FT   SIGNAL        1     16       POTENTIAL.
FT   PROPEP       17    105       ACTIVATION PEPTIDE.
FT   CHAIN       106    322       DIGESTIVE CYSTEINE PROTEINASE 1.
FT   ACT_SITE    129    129       BY SIMILARITY.
FT   ACT_SITE    269    269       BY SIMILARITY.
FT   ACT_SITE    289    289       BY SIMILARITY.
FT   DISULFID    126    170       BY SIMILARITY.
FT   DISULFID    160    203       BY SIMILARITY.
FT   DISULFID    262    311       BY SIMILARITY.
FT   CONFLICT    114    114       K -> E (IN REF. 2).
SQ   SEQUENCE   322 AA;  35498 MW;  41628777 CRC32;
     MKVVALFLFG LALAAANPSW EEFKGKFGRK YVDLEEERYR LNVFLDNLQY IEEFNKKYER
     GEVTYNLAIN QFSDMTNEKF NAVMKGYKKG PRPAAVFTST DAAPESTEVD WRTKGAVTPV
     KDQGQCGSCW AFSTTGGIEG QHFLKTGRLV SLSEQQLVDC AGGSYYNQGC NGGWVERAIM
     YVRDNGGVDT ESSYPYEARD NTCRFNSNTI GATCTGYVGI AQGSESALKT ATRDIGPISV
     AIDASHRSFQ SYYTGVYYEP SCSSSQLDHA VLAVGYGSEG GQDFWLVKNS WATSWGESGY
     IKMARNRNNN CGIATDACYP TV

SwissProt Database

CYS1_HORVU

ID   CYS1_HORVU     STANDARD;      PRT;   371 AA.
AC   P25249;
DT   01-MAY-1992 (REL. 22, CREATED)
DT   01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE EP-B 1 PRECURSOR (EC 3.4.22.-).
OS   HORDEUM VULGARE (BARLEY).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; MONOCOTYLEDONEAE;
OC   CYPERALES; GRAMINEAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=CV. HIMALAYA; TISSUE=ALEURONE;
RX   MEDLINE; 93005672.
RA   KOEHLER S.M., HO T.H.D.;
RL   PLANT CELL 2:769-783(1990).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   STRAIN=CV. HIMALAYA;
RA   MIKKONEN A.A., PORALI I.K., CERCOS M., HO T.H.D.;
RL   SUBMITTED (JAN-1996) TO EMBL/GENBANK/DDBJ DATA BANKS.
CC   -!- INDUCTION: SYNTHESIZED BY THE ALEURONE CELLS STIMULATED BY
CC       GIBBERELLIC ACID.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; U19359; G1146116; -.
DR   PIR; JQ1111; JQ1111.
DR   HSSP; P00785; 1AEC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; GLYCOPROTEIN; ZYMOGEN; SIGNAL; GERMINATION;
KW   MULTIGENE FAMILY.
FT   SIGNAL        1     28       POTENTIAL.
FT   PROPEP       29    133       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN       134    371       CYSTEINE PROTEINASE EP-B 1.
FT   ACT_SITE    158    158       BY SIMILARITY.
FT   ACT_SITE    297    297       BY SIMILARITY.
FT   ACT_SITE    318    318       BY SIMILARITY.
FT   DISULFID    155    197       BY SIMILARITY.
FT   DISULFID    189    230       BY SIMILARITY.
FT   DISULFID    291    343       BY SIMILARITY.
FT   CARBOHYD    130    130       POTENTIAL.
SQ   SEQUENCE   371 AA;  40358 MW;  1B5D6AC5 CRC32;
     MGLLSKKLLV ASMVAAVLAV AAVELCSAIP MEDKDLESEE ALWDLYERWQ SAHRVRRHHA
     EKHRRFGTFK SNAHFIHSHN KRGDHPYRLH LNRFGDMDQA EFRATFVGDL RRDTPAKPPS
     VPGFMYAALN VSDLPPSVDW RQKGAVTGVK DQGKCGSCWA FSTVVSVEGI NAIRTGSLVS
     LSEQELIDCD TADNDGCQGG LMDNAFEYIK NNGGLITEAA YPYRAARGTC NVARAAQNSP
     VVVHIDGHQD VPANSEEDLA RAVANQPVSV AVEASGKAFM FYSEGVFTGD CGTELDHGVA
     VVGYGVAEDG KAYWTVKNSW GPSWGEQGYI RVEKDSGASG GLCGIAMEAS YPVKTYNKPM
     PRRALGAWES Q

SwissProt Database

CYS1_LEIPI

ID   CYS1_LEIPI     STANDARD;      PRT;   354 AA.
AC   P35591;
DT   01-JUN-1994 (REL. 29, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE 1 PRECURSOR (EC 3.4.22.-) (AMASTIGOTE CYSTEINE
DE   PROTEINASE A-1).
GN   CYS1.
OS   LEISHMANIA PIFANOI.
OC   EUKARYOTA; PROTOZOA; SARCOMASTIGOPHORA; MASTIGOPHORA; KINETOPLASTIDA;
OC   TRYPANOSOMATIDAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RA   ALMEIDA R.W.;
RL   SUBMITTED (MAR-1996) TO EMBL/GENBANK/DDBJ DATA BANKS.
RN   [2]
RP   SEQUENCE OF 147-311 FROM N.A.
RX   MEDLINE; 93149195.
RA   TRAUB-CSEKO Y.M., DUBOISE M., BOUKAI L.K., MCMAHON-PRATT D.;
RL   MOL. BIOCHEM. PARASITOL. 57:101-115(1993).
CC   -!- FUNCTION: THE CYSTEINE PROTEINASES HAVE A POTENTIAL ROLE IN
CC       HOST-PARASITE INTERACTION AND VIRULENCE.
CC   -!- DEVELOPMENTAL STAGE: PRIMARILY EXPRESSED BY THE AMASTIGOTE STAGE.
CC       EXPRESSED 4 TIMES MORE IN AMASTIGOTES THAN IN PROMASTIGOTES.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; L29168; G1220383; -.
DR   EMBL; L00717; -; NOT_ANNOTATED_CDS.
DR   HSSP; P00785; 1AEC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; GLYCOPROTEIN; ZYMOGEN; SIGNAL.
FT   SIGNAL        1      ?       POTENTIAL.
FT   PROPEP        ?    125       ACTIVATION PEPTIDE (PROBABLE).
FT   CHAIN       126    354       CYSTEINE PROTEINASE 1.
FT   ACT_SITE    153    153       BY SIMILARITY.
FT   ACT_SITE    289    289       BY SIMILARITY.
FT   ACT_SITE    309    309       BY SIMILARITY.
FT   DISULFID    150    191       BY SIMILARITY.
FT   DISULFID    184    229       BY SIMILARITY.
FT   DISULFID    282    330       BY SIMILARITY.
FT   CARBOHYD    208    208       POTENTIAL.
FT   CONFLICT    149    149       L -> Q (IN REF. 2).
FT   CONFLICT    152    152       S -> W (IN REF. 2).
FT   CONFLICT    296    296       F -> S (IN REF. 2).
SQ   SEQUENCE   354 AA;  38746 MW;  9A7841EE CRC32;
     MARRNPLLFA IVVTILFVVC YGSALIAQTP PPVDNFVASA HYGSFKKRHG KAFGGDAEEG
     HRFNAFKQNM QTAYFLNTQN PHAHYDVSGK FADLTPQEFA KLYLNPDYYA RHLKDHKEDV
     HVDDSAPSGV MSVDWRDKGA VTPVKNQGLC GSCWAFSAIG NIEGQWAASG HSLVSLSEQM
     LVSCDNIDEG CNGGLMDQAM NWIMQSHNGS VFTEASYPYT SGGGTRPPCH DEGEVGAKIT
     GFLSLPHDEE RIAEWVEKRG PVAVAVDATT WQLYFGGVVS LCLAWSLNHG VLIVGFNKNA
     KPPYWIVKNS WGSSWGEKGY IRLAMGSNQC MLKNYPVSAT VESPHTPHVP TTTA

SwissProt Database

CYS1_MAIZE

ID   CYS1_MAIZE     STANDARD;      PRT;   371 AA.
AC   Q10716;
DT   01-OCT-1996 (REL. 34, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE 1 PRECURSOR (EC 3.4.22.-).
GN   CCP1.
OS   ZEA MAYS (MAIZE).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; MONOCOTYLEDONEAE;
OC   CYPERALES; GRAMINEAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 96004895.
RA   DOMOTO C., WATANABE H., ABE M., ABE K., ARAI S.;
RL   BIOCHIM. BIOPHYS. ACTA 1263:241-244(1995).
RN   [2]
RP   SEQUENCE OF 227-371 FROM N.A.
RC   STRAIN=CV. DEA; TISSUE=ROOT MERISTEM;
RX   MEDLINE; 95359405.
RA   CHEVALIER C., BOURGEOIS E., PRADET A., RAYMOND P.;
RL   PLANT MOL. BIOL. 28:473-485(1995).
CC   -!- FUNCTION: INVOLVED IN THE DEGRADATION OF THE STORAGE PROTEIN ZEIN.
CC       MAY PLAY A ROLE IN PROTEOLYSIS DURING EMERGENCIES.
CC   -!- TISSUE SPECIFICITY: EXPRESSED DURING THE LATE STAGES OF SEED
CC       RIPENING, IN MATURE SEEDS AND DURING GERMINATION.
CC   -!- SIMILARITY: TO OTHER EUKARYOTIC THIOL PROTEASES.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; D45402; G643597; -.
DR   EMBL; X82185; G559532; -.
DR   MAIZEDB; 24531; -.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; GLYCOPROTEIN; SIGNAL.
FT   SIGNAL        1     18       POTENTIAL.
FT   PROPEP       19    136       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN       137    371       CYSTEINE PROTEINASE 1.
FT   ACT_SITE    161    161       BY SIMILARITY.
FT   ACT_SITE    303    303       BY SIMILARITY.
FT   ACT_SITE    330    330       BY SIMILARITY.
FT   DISULFID    158    208       BY SIMILARITY.
FT   DISULFID    196    241       BY SIMILARITY.
FT   DISULFID    297    345       BY SIMILARITY.
FT   CARBOHYD    254    254       POTENTIAL.
FT   CONFLICT    269    269       L -> R (IN REF. 2).
FT   CONFLICT    318    318       I -> M (IN REF. 2).
SQ   SEQUENCE   371 AA;  40347 MW;  79820DDF CRC32;
     MAHRVLLLLS LASAAAVAAA VDAEDPLIRQ VVPGGDDNDL ELNAESHFLS FVQRFGKSYK
     DADEHAYRLS VFKDNLRRAR RHQLLDPSAE HGVTKFSDLT PAEFRRTYLG LRKSRRALLR
     ELGESAHEAP VLPTDGLPDD FDWRDHGAVG PVKNQGSCGS CWSFSASGAL EGAHYLATGK
     LEVLSEQQFV DCDHECDSSE PDSCDSGCNG GLMTTAFSYL QKAGGLESEK DYPYTGSDGK
     CKFDKSKIVA SVQNFSVVSV DEAQISANLI KHGPLAIGIN AAYMQTYIGG VSCPYICGRH
     LDHGVLLVGY GASGFAPIRL KDKPYWIIKN SWGENWGENG YYKICRGSNV RNKCGVDSMV
     STVSAVHASK E

SwissProt Database

CYS1_OSTOS

ID   CYS1_OSTOS     STANDARD;      PRT;   341 AA.
AC   P25802;
DT   01-MAY-1992 (REL. 22, CREATED)
DT   01-FEB-1996 (REL. 33, LAST SEQUENCE UPDATE)
DT   01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE)
DE   CATHEPSIN B-LIKE CYSTEINE PROTEINASE 1 PRECURSOR (EC 3.4.22.-).
GN   CP-1.
OS   OSTERTAGIA OSTERTAGI.
OC   EUKARYOTA; METAZOA; ACOELOMATES; NEMATODA; SECERNENTEA; RHABDITIDA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=LARVA;
RX   MEDLINE; 93116804.
RA   PRATT D., BOISVENUE R.J., COX G.N.;
RL   MOL. BIOCHEM. PARASITOL. 56:39-48(1992).
CC   -!- FUNCTION: EXPRESSION OF THE PROTEASE CORRELATES WITH BLOOD-FEEDING
CC       AND SUGGESTS A ROLE FOR THE PROTEASE IN BLOOD DIGESTION.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
CC   -!- SIMILARITY: STRONGEST, TO CATHEPSIN B.
DR   EMBL; M88503; G552158; -.
DR   EMBL; M88503; G552159; ALT_SEQ.
DR   EMBL; M88504; G159950; -.
DR   HSSP; P07858; 1HUC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; GLYCOPROTEIN; MULTIGENE FAMILY;
KW   SIGNAL.
FT   SIGNAL        1      ?       POTENTIAL.
FT   PROPEP        ?     88       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN        89    341       CYSTEINE PROTEINASE 1.
FT   ACT_SITE    119    119       BY SIMILARITY.
FT   ACT_SITE    288    288       BY SIMILARITY.
FT   ACT_SITE    308    308       BY SIMILARITY.
FT   DISULFID    104    133       BY SIMILARITY.
FT   DISULFID    116    160       BY SIMILARITY.
FT   DISULFID    152    218       BY SIMILARITY.
FT   DISULFID    153    156       BY SIMILARITY.
FT   DISULFID    189    222       BY SIMILARITY.
FT   DISULFID    197    209       BY SIMILARITY.
FT   CARBOHYD    103    103       POTENTIAL.
FT   CARBOHYD    202    202       POTENTIAL.
SQ   SEQUENCE   341 AA;  38439 MW;  5D8A001B CRC32;
     MKYLFFALCL YLYQGISEAE VPAEQIPLEA QALSGLPLVE YLQKNQRLFE VTATPVPYFK
     QRLMDLKYID QNNIPDEEVE DEELEENNDD IPESYDPRIQ WANCSSLFHI PDQANCGSCW
     AVSSAAAMSD RICIASKGAK QVLISAQDVV SCCTWCGDGC EGGWPISAFR FHADEGVVTG
     GDYNTKGSCR PYEIHPCGHH GNETYYGECV GMADTPRCKR RCLLGYPKSY PSDRYYKKAY
     QLKNSVKAIQ KDIMKNGPVV ATYTVYEDFA HYRSGIYKHK AGRKTGLHAV KVIGWGEEKG
     TPYWIVANSW HDDWGENGFF RMHRGSNDCG FEERMAAGSV Q

SwissProt Database

CYS2_DICDI

ID   CYS2_DICDI     STANDARD;      PRT;   376 AA.
AC   P04989;
DT   13-AUG-1987 (REL. 05, CREATED)
DT   13-AUG-1987 (REL. 05, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE 2 PRECURSOR (EC 3.4.22.-) (PRESTALK CATHEPSIN).
GN   CPRB OR CP2.
OS   DICTYOSTELIUM DISCOIDEUM (SLIME MOLD).
OC   EUKARYOTA; PROTOZOA; SARCOMASTIGOPHORA; SARCODINA; RHIZOPODA;
OC   EUMYCETOZOA; DICTYOSTELIA.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 87172698.
RA   DATTA S., FIRTEL R.A.;
RL   MOL. CELL. BIOL. 7:149-159(1987).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 86093683.
RA   PEARS C.J., MAHBUBANI H.M., WILLIAMS J.G.;
RL   NUCLEIC ACIDS RES. 13:8853-8866(1985).
RN   [3]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 87057653.
RA   GOMER R.H., DATTA S., FIRTEL R.A.;
RL   J. CELL BIOL. 103:1999-2015(1986).
CC   -!- FUNCTION: CYSTEINE PROTEINASES 1 AND 2 ARE BELIEVED TO PARTICIPATE
CC       IN THE BREAKDOWN OF PROTEIN DURING DIFFERENTIATION OF DICTOSTELIUM
CC       AS A RESPONSE TO STARVATION.
CC   -!- SUBCELLULAR LOCATION: LYSOSOMAL.
CC   -!- DEVELOPMENTAL STAGE: EXPRESSED BY PRESTALK CELLS.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; M16039; G167860; -.
DR   EMBL; X03344; E1705; ALT_INIT.
DR   PIR; A25439; KHDOP.
DR   HSSP; P00785; 1AEC.
DR   DICTYDB; DD02004; CPRB.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; LYSOSOME; ZYMOGEN; SIGNAL.
FT   SIGNAL        1     18       POTENTIAL.
FT   PROPEP       19    122       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN       123    376       CYSTEINE PROTEINASE 2.
FT   ACT_SITE    147    147       BY SIMILARITY.
FT   ACT_SITE    286    286       BY SIMILARITY.
FT   ACT_SITE    343    343       BY SIMILARITY.
FT   DISULFID    144    187       BY SIMILARITY.
FT   DISULFID    178    221       BY SIMILARITY.
FT   DISULFID    279    365       BY SIMILARITY.
SQ   SEQUENCE   376 AA;  41851 MW;  035F9652 CRC32;
     MRLLVFLILL IFVNFSFANV RPNGRRFSES QYRTAFTEWT LKFNRQYSSS EFSNRYSIFK
     SNMDYVDNWN SKGDSQTVLG LNNFADITNE EYRKTYLGTR VNAHSYNGYD GREVLNVEDL
     QTNPKSIDWR TKNAVTPIKD QGQCGSCWSF STTGSTEGAH ALKTKKLVSL SEQNLVDCSG
     PEENFGCDGG LMNNAFDYII KNKGIDTESS YPYTAETGST CLFNKSDIGA TIKGYVNITA
     GSEISLENGA QHGPVSVAID ASHNSFQLYT SGIYYEPKCS PTELDHGVLV VGYGVQGKDD
     EGPVLNRKQT IVIHKNEDNK VESSDDSSDS VRPKANNYWI VKNSWGTSWG IKGYILMSKD
     RKNNCGIASV SSYPLA

SwissProt Database

CYS2_HAECO

ID   CYS2_HAECO     STANDARD;      PRT;   342 AA.
AC   P25793;
DT   01-MAY-1992 (REL. 22, CREATED)
DT   01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CATHEPSIN B-LIKE CYSTEINE PROTEINASE 2 PRECURSOR (EC 3.4.22.-).
GN   AC-2.
OS   HAEMONCHUS CONTORTUS.
OC   EUKARYOTA; METAZOA; ACOELOMATES; NEMATODA; SECERNENTEA; SPIRURIDA.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 91218800.
RA   PRATT D., COX G.N., MILHAUSEN M.J., BOISVENUE R.J.;
RL   MOL. BIOCHEM. PARASITOL. 43:181-192(1990).
CC   -!- FUNCTION: EXPRESSION OF THE PROTEASE CORRELATES WITH BLOOD-FEEDING
CC       AND SUGGESTS A ROLE FOR THE PROTEASE IN BLOOD DIGESTION.
CC   -!- DEVELOPMENTAL STAGE: AT LOW LEVEL IN THE THIRD AND FOURTH-STAGE
CC       LARVAE, AND ABUNDANT IN ADULT WORMS.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
CC   -!- SIMILARITY: STRONGEST, TO CATHEPSIN B.
DR   EMBL; M60213; G159165; -.
DR   EMBL; M60212; G159165; JOINED.
DR   PIR; A44965; A44965.
DR   HSSP; P07858; 1HUC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; GLYCOPROTEIN; SIGNAL;
KW   MULTIGENE FAMILY.
FT   SIGNAL        1      ?       POTENTIAL.
FT   PROPEP        ?     86       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN        87    342       CYSTEINE PROTEINASE 2.
FT   ACT_SITE    114    114       BY SIMILARITY.
FT   ACT_SITE    285    285       BY SIMILARITY.
FT   ACT_SITE    305    305       BY SIMILARITY.
FT   DISULFID    100    128       BY SIMILARITY.
FT   DISULFID    111    156       BY SIMILARITY.
FT   DISULFID    147    214       BY SIMILARITY.
FT   DISULFID    148    152       BY SIMILARITY.
FT   DISULFID    185    218       BY SIMILARITY.
FT   DISULFID    193    205       BY SIMILARITY.
FT   CARBOHYD     99     99       POTENTIAL.
FT   CARBOHYD    138    138       POTENTIAL.
FT   CARBOHYD    198    198       POTENTIAL.
FT   CARBOHYD    296    296       POTENTIAL.
SQ   SEQUENCE   342 AA;  38406 MW;  89092341 CRC32;
     MKYLVLALCT YLCSQSGADE NAAQGIPLEA QRLTGEPLVA YLRRSQNLFE VNSDPTPDFE
     QKIMSIKYKH QKLNLMVKED PDPEVDIPPS YDPRDVWKNC TTFYIRDQAN CGSCWAVSTA
     AAISDRICIA SKAEKQVNIS ATDIMTCCRP QCGDGCEGGW PIEAWKYFIY DGVVSGGEYL
     TKDVCRPYPI HPCGHHGNDT YYGECRGTAP TPPCKRKCRP GVRKMYRIDK RYGKDAYIVK
     QSVKAIQSEI LKNGPVVASF AVYEDFRHYK SGIYKHTAGE LRGYHAVKMI GWGNENNTDF
     WLIANSWHND WGEKGYFRIV RGSNDCGIEG TIAAGIVDTE SL

SwissProt Database

CYS2_HOMAM

ID   CYS2_HOMAM     STANDARD;      PRT;   323 AA.
AC   P25782;
DT   01-MAY-1992 (REL. 22, CREATED)
DT   01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   DIGESTIVE CYSTEINE PROTEINASE 2 PRECURSOR (EC 3.4.22.-).
GN   LCP2.
OS   HOMARUS AMERICANUS (AMERICAN LOBSTER).
OC   EUKARYOTA; METAZOA; ARTHROPODA; CRUSTACEA; MALACOSTRACA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=DIGESTIVE GLAND;
RX   MEDLINE; 92070467.
RA   LAYCOCK M.V., MACKAY R.M., DI FRUSCIO M., GALLANT J.W.;
RL   FEBS LETT. 292:115-120(1991).
CC   -!- ENZYME REGULATION: INHIBITED BY E-64, ANTIPAIN, LEUPEPTIN, HEAVY
CC       METAL IONS, IODOACETIC ACID, DITHIONITROBENZENE, P-HYDROXYMERCURI-
CC       BENZOATE; ACTIVATED BY MERCAPTOETHANOL AND DITHIOTHREITOL.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
CC   -!- SIMILARITY: STRONGEST, TO PAPAIN AND CATHEPSIN L.
DR   EMBL; X63568; G11053; -.
DR   PIR; S19650; S19650.
DR   HSSP; P00785; 1AEC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL; MULTIGENE FAMILY.
FT   SIGNAL        1     16       POTENTIAL.
FT   PROPEP       17    107       ACTIVATION PEPTIDE.
FT   CHAIN       108    323       DIGESTIVE CYSTEINE PROTEINASE 2.
FT   ACT_SITE    131    131       BY SIMILARITY.
FT   ACT_SITE    270    270       BY SIMILARITY.
FT   ACT_SITE    290    290       BY SIMILARITY.
FT   DISULFID    128    171       BY SIMILARITY.
FT   DISULFID    162    204       BY SIMILARITY.
FT   DISULFID    263    312       BY SIMILARITY.
SQ   SEQUENCE   323 AA;  35401 MW;  88F1F52A CRC32;
     MKVAVLFLCG VALAAASPSW EHFKGKYGRQ YVDAEEDSYR RVIFEQNQKY IEEFNKKYEN
     GEVTFNLAMN KFGDMTLEEF NAVMKGNIPR RSAPVSVFYP KKETGPQATE VDWRTKGAVT
     PVKDQGQCGS CWAFSTTGSL EGQHFLKTGS LISLAEQQLV DCSRPYGPQG CNGGWMNDAF
     DYIKANNGID TEAAYPYEAR DGSCRFDSNS VAATCSGHTN IASGSETGLQ QAVRDIGPIS
     VTIDAAHSSF QFYSSGVYYE PSCSPSYLDH AVLAVGYGSE GGQDFWLVKN SWATSWGDAG
     YIKMSRNRNN NCGIATVASY PLV

SwissProt Database

CYS2_HORVU

ID   CYS2_HORVU     STANDARD;      PRT;   373 AA.
AC   P25250;
DT   01-MAY-1992 (REL. 22, CREATED)
DT   01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE EP-B 4 PRECURSOR (EC 3.4.22.-).
OS   HORDEUM VULGARE (BARLEY).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; MONOCOTYLEDONEAE;
OC   CYPERALES; GRAMINEAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=CV. HIMALAYA; TISSUE=ALEURONE;
RX   MEDLINE; 93005672.
RA   KOEHLER S.M., HO T.H.D.;
RL   PLANT CELL 2:769-783(1990).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   STRAIN=CV. HIMALAYA;
RA   MIKKONEN A.A., PORALI I.K., CERCOS M., HO T.H.D.;
RL   SUBMITTED (JAN-1996) TO EMBL/GENBANK/DDBJ DATA BANKS.
CC   -!- INDUCTION: SYNTHESIZED BY THE ALEURONE CELLS STIMULATED BY
CC       GIBBERELLIC ACID.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; S45163; G257039; -.
DR   EMBL; U19384; G1146118; -.
DR   PIR; JQ1110; JQ1110.
DR   HSSP; P00785; 1AEC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; GLYCOPROTEIN; ZYMOGEN; SIGNAL; GERMINATION;
KW   MULTIGENE FAMILY.
FT   SIGNAL        1     28       POTENTIAL.
FT   PROPEP       29    133       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN       134    373       CYSTEINE PROTEINASE EP-B 4.
FT   ACT_SITE    158    158       BY SIMILARITY.
FT   ACT_SITE    297    297       BY SIMILARITY.
FT   ACT_SITE    318    318       BY SIMILARITY.
FT   DISULFID    155    197       BY SIMILARITY.
FT   DISULFID    189    230       BY SIMILARITY.
FT   DISULFID    291    343       BY SIMILARITY.
FT   CARBOHYD    130    130       POTENTIAL.
SQ   SEQUENCE   373 AA;  40511 MW;  515E6E2E CRC32;
     MGLLSKKLLV ASMVAAVLAV AAVELCSAIP MEDKDLESEE ALWDLYERWQ SAHRVRRHHA
     EKHRRFGTFK SNAHFIHSHN KRGDHPYRLH LNRFGDMDQA EFRATFVGDL RRDTPSKPPS
     VPGFMYAALN VSDLPPSVDW RQKGAVTGVK DQGKCGSCWA FSTVVSVEGI NAIRTGSLVS
     LSEQELIDCD TADNDGCQGG LMDNAFEYIK NNGGLITEAA YPYRAARGTC NVARAAQNSP
     VVVHIDGHQD VPANSEEDLA RAVANQPVSV AVEASGKAFM FYSEGVFTGE CGTELDHGVA
     VVGYGVAEDG KAYWTVKNSW GPSWGEQGYI RVEKDSGASG GLCGIAMEAS YPVKTYSKPK
     PTPRRALGAR ESL

SwissProt Database

CYS2_LEIPI

ID   CYS2_LEIPI     STANDARD;      PRT;   444 AA.
AC   Q05094;
DT   01-FEB-1994 (REL. 28, CREATED)
DT   01-FEB-1994 (REL. 28, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE 2 PRECURSOR (EC 3.4.22.-) (AMASTIGOTE CYSTEINE
DE   PROTEINASE A-2).
GN   CYS2.
OS   LEISHMANIA PIFANOI.
OC   EUKARYOTA; PROTOZOA; SARCOMASTIGOPHORA; MASTIGOPHORA; KINETOPLASTIDA;
OC   TRYPANOSOMATIDAE.
RN   [1]
RP   SEQUENCE FROM N.A., AND SEQUENCE OF 125-159; 237-266 AND 308-322.
RX   MEDLINE; 93149195.
RA   TRAUB-CSEKO Y.M., DUBOISE M., BOUKAI L.K., MCMAHON-PRATT D.;
RL   MOL. BIOCHEM. PARASITOL. 57:101-115(1993).
CC   -!- FUNCTION: THE CYSTEINE PROTEINASES HAVE A POTENTIAL ROLE IN
CC       HOST-PARASITE INTERACTION AND VIRULENCE.
CC   -!- DEVELOPMENTAL STAGE: PRIMARILY EXPRESSED BY THE AMASTIGOTE STAGE.
CC       EXPRESSED 15 TIMES MORE IN AMASTIGOTES THAN IN PROMASTIGOTES.
CC   -!- SUBCELLULAR LOCATION: ASSOCIATED WITH MEGASOME, A UNIQUE
CC       LYSOSOMAL ORGANELLE FOUND IN INTRACELLULAR AMASTIGOTES OF THE
CC       L.MEXICANA COMPLEX.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; M97695; G159298; -.
DR   PIR; A48566; A48566.
DR   HSSP; P24821; 1HRE.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL; GLYCOPROTEIN.
FT   SIGNAL        1     19       OR 27.
FT   PROPEP       20    124       ACTIVATION PEPTIDE (PROBABLE).
FT   CHAIN       125    444       CYSTEINE PROTEINASE 2.
FT   ACT_SITE    150    150       BY SIMILARITY.
FT   ACT_SITE    289    289       BY SIMILARITY.
FT   ACT_SITE    309    309       BY SIMILARITY.
FT   DISULFID    147    188       BY SIMILARITY.
FT   CARBOHYD    228    228       POTENTIAL.
FT   CARBOHYD    372    372       POTENTIAL.
SQ   SEQUENCE   444 AA;  47857 MW;  F5D39FF4 CRC32;
     MATSRAALCA VAVVCVVLAA ACAPARAIHV GTPAAALFEE FKRTYGRAYE TLAEEQQRLA
     NFERNLELMR EHQARNPHAQ FGITKFFDLS EAEFAARYLN GAAYFAAAKR HAAQHYRKAR
     ADLSAVPDAV DWREKGAVTP VKDQGACGSC WAFSAVGNIE GQWYLAGHEL VSLSEQQLVS
     CDDMNDGCDG GLMLQAFDWL LQNTNGHLHT EDSYPYVSGN GYVPECSNSS EELVVGAQID
     GHVLIGSSEK AMAAWLAKNG PIAIALDASS FMSYKSGVLT ACIGKQLNHG VLLVGYDMTG
     EVPYWVIKNS WGGDWGEQGY VRVVMGVNAC LLSEYPVSAH VRESAAPGTS TSSETPAPRP
     VMVEQVICFD KNCTQGCRKT LIKANECHKN GGGGASMIKC SPQKVTMCTY SNEFCVGGGL
     CFETPDGKCA PYFLGSIMNT CHYT

SwissProt Database

CYS2_MAIZE

ID   CYS2_MAIZE     STANDARD;      PRT;   360 AA.
AC   Q10717;
DT   01-OCT-1996 (REL. 34, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE 2 PRECURSOR (EC 3.4.22.-).
GN   CCP2.
OS   ZEA MAYS (MAIZE).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; MONOCOTYLEDONEAE;
OC   CYPERALES; GRAMINEAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=SEED;
RX   MEDLINE; 96004895.
RA   DOMOTO C., WATANABE H., ABE M., ABE K., ARAI S.;
RL   BIOCHIM. BIOPHYS. ACTA 1263:241-244(1995).
CC   -!- FUNCTION: INVOLVED IN THE DEGRADATION OF THE STORAGE PROTEIN ZEIN.
CC       MAY PLAY A ROLE IN PROTEOLYSIS DURING EMERGENCIES.
CC   -!- TISSUE SPECIFICITY: EXPRESSED AT THE ONSET OF GERMINATION.
CC   -!- SUBCELLULAR LOCATION: PROBABLY ACCUMULATES IN VACUOLES.
CC   -!- SIMILARITY: TO OTHER EUKARYOTIC THIOL PROTEASES.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; D45403; G644490; -.
DR   MAIZEDB; 24531; -.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; GLYCOPROTEIN; SIGNAL.
FT   SIGNAL        1     19       POTENTIAL.
FT   PROPEP       20    142       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN       143    360       CYSTEINE PROTEINASE 2.
FT   ACT_SITE    167    167       BY SIMILARITY.
FT   ACT_SITE    307    307       BY SIMILARITY.
FT   ACT_SITE    327    327       BY SIMILARITY.
FT   CARBOHYD    125    125       POTENTIAL.
FT   CARBOHYD    256    256       POTENTIAL.
SQ   SEQUENCE   360 AA;  39199 MW;  D65545CC CRC32;
     MVPRRLFVLA VVVLADTAAV VNSGFADSNP IRPVTDRAAS ALESTVFAAL GRTRDALRFA
     RFAVRYGKSY ESAAEVHKRF RIFSESLQLV RSTNRKGLSY RLGINRFADM SWEEFRATRL
     GAAQNCSATL TGNHRMRAAA VALPETKDWR EDGIVSPVKN QGHCGSCWTF STTGALEAAY
     TQATGKPISL SEQQLVDCGF AFNNFGCNGG LPSQAFEYIK YNGGLDTEES YPYQGVNGIC
     KFKNENVGVK VLDSVNITLG AEDELKDAVG LVRPVSVAFE VITGFRLYKS GVYTSDHCGT
     TPMDVNHAVL AVGYGVEDGV PYWLIKNSWG ADWGDEGYFK MEMGKNMCGV ATCASYPIVA

SwissProt Database

CYS3_HOMAM

ID   CYS3_HOMAM     STANDARD;      PRT;   321 AA.
AC   P25784;
DT   01-MAY-1992 (REL. 22, CREATED)
DT   01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   DIGESTIVE CYSTEINE PROTEINASE 3 PRECURSOR (EC 3.4.22.-).
GN   LCP3.
OS   HOMARUS AMERICANUS (AMERICAN LOBSTER).
OC   EUKARYOTA; METAZOA; ARTHROPODA; CRUSTACEA; MALACOSTRACA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=DIGESTIVE GLAND;
RX   MEDLINE; 92070467.
RA   LAYCOCK M.V., MACKAY R.M., DI FRUSCIO M., GALLANT J.W.;
RL   FEBS LETT. 292:115-120(1991).
CC   -!- ENZYME REGULATION: INHIBITED BY E-64, ANTIPAIN, LEUPEPTIN, HEAVY
CC       METAL IONS, IODOACETIC ACID, DITHIONITROBENZENE, P-HYDROXYMERCURI-
CC       BENZOATE; ACTIVATED BY MERCAPTOETHANOL AND DITHIOTHREITOL.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
CC   -!- SIMILARITY: STRONGEST, TO PAPAIN AND CATHEPSIN L.
DR   EMBL; X63569; G11055; ALT_INIT.
DR   PIR; S20838; S20838.
DR   HSSP; P00785; 1AEC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL; MULTIGENE FAMILY.
FT   SIGNAL        1     16       POTENTIAL.
FT   PROPEP       17    106       ACTIVATION PEPTIDE.
FT   CHAIN       107    321       DIGESTIVE CYSTEINE PROTEINASE 3.
FT   ACT_SITE    130    130       BY SIMILARITY.
FT   ACT_SITE    268    268       BY SIMILARITY.
FT   ACT_SITE    288    288       BY SIMILARITY.
FT   DISULFID    127    170       BY SIMILARITY.
FT   DISULFID    161    203       BY SIMILARITY.
FT   DISULFID    261    310       BY SIMILARITY.
SQ   SEQUENCE   321 AA;  35366 MW;  49556405 CRC32;
     MKVAALFLCG LALATASPSW DHFKTQYGRK YGDAKEELYR QRVFQQNEQL IEDFNKKFEN
     GEVTFKVAMN QFGDMTNEEF NAVMKGYKKG SRGEPKAVFT AEAGPMAADV DWRTKALVTP
     VKDQEQCGSC WAFSATGALE GQHFLKNDEL VSLSEQQLVD CSTDYGNDGC GGGWMTSAFD
     YIKDNGGIDT ESSYPYEAED RSCRFDANSI GAICTGSVEV QHTEEALQEA VSGVGPISVA
     IDASHFSFQF YSSGVYYEQN CSPTFLDHGV LAVGYGTEST KDYWLVKNSW GSSWGDAGYI
     KMSRNRDNNC GIASEPSYPT V

SwissProt Database

CYS3_OSTOS

ID   CYS3_OSTOS     STANDARD;      PRT;   174 AA.
AC   Q06544;
DT   01-FEB-1995 (REL. 31, CREATED)
DT   01-FEB-1995 (REL. 31, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CATHEPSIN B-LIKE CYSTEINE PROTEINASE 3 (EC 3.4.22.-) (FRAGMENT).
GN   CP-3.
OS   OSTERTAGIA OSTERTAGI.
OC   EUKARYOTA; METAZOA; ACOELOMATES; NEMATODA; SECERNENTEA; RHABDITIDA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=LARVA;
RX   MEDLINE; 93116804.
RA   PRATT D., BOISVENUE R.J., COX G.N.;
RL   MOL. BIOCHEM. PARASITOL. 56:39-48(1992).
CC   -!- FUNCTION: EXPRESSION OF THE PROTEASE CORRELATES WITH BLOOD-FEEDING
CC       AND SUGGESTS A ROLE FOR THE PROTEASE IN BLOOD DIGESTION.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
CC   -!- SIMILARITY: STRONGEST, TO CATHEPSIN B.
DR   EMBL; M88505; G159952; -.
DR   EMBL; S51920; -; NOT_ANNOTATED_CDS.
DR   PIR; B48454; B48454.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; GLYCOPROTEIN; MULTIGENE FAMILY.
FT   NON_TER       1      1
FT   ACT_SITE    122    122       BY SIMILARITY.
FT   ACT_SITE    142    142       BY SIMILARITY.
FT   DISULFID     22     55       BY SIMILARITY.
FT   DISULFID     30     42       BY SIMILARITY.
SQ   SEQUENCE   174 AA;  19939 MW;  3194AE20 CRC32;
     AWQYFALEGV VTGGNYRKQG CCRPYEFPPC GRHGKEPYYG ECYDTAKTPK CQKTCQRGYL
     KAYKEDKHFG KSAYRLPNNV KAIQRDIMKN GPVVAGFIVY EDFAHYKSGI YKHTAGRMTG
     GHAVKIIGWG KEKGTPYWLI ANSWHDDWGE KGFYRMIRGI NNCRIEEMVF AGIV

SwissProt Database

CYS4_BRANA

ID   CYS4_BRANA     STANDARD;      PRT;   328 AA.
AC   P25251;
DT   01-MAY-1992 (REL. 22, CREATED)
DT   01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE COT44 PRECURSOR (EC 3.4.22.-).
OS   BRASSICA NAPUS (RAPE).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE;
OC   CAPPARALES; CRUCIFERAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=SEED;
RX   MEDLINE; 92386055.
RA   DIETRICH R.A., MASLYAR D.J., HEUPEL R.C., HARADA J.J.;
RL   PLANT CELL 1:73-80(1989).
CC   -!- FUNCTION: MAY FUNCTION IN AN EARLY EVENT IN CORTICAL CELL
CC       DIFFERENTIATION.
CC   -!- TISSUE SPECIFICITY: PRESENT IN BOTH COTYLEDONS AND AXES.
CC   -!- DEVELOPMENTAL STAGE: EXPRESSED MAXIMALLY DURING POSTGERMINATIVE
CC       GROWTH.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   PIR; JQ1121; JQ1121.
DR   HSSP; P00785; 1AEC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; GLYCOPROTEIN; ZYMOGEN; SIGNAL; GERMINATION.
FT   SIGNAL        1      ?       POTENTIAL.
FT   PROPEP        ?      ?       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN         ?    328       CYSTEINE PROTEINASE COT44.
FT   ACT_SITE    124    124       BY SIMILARITY.
FT   ACT_SITE    260    260       BY SIMILARITY.
FT   ACT_SITE    280    280       BY SIMILARITY.
FT   DISULFID    121    163       BY SIMILARITY.
FT   DISULFID    155    196       BY SIMILARITY.
FT   DISULFID    254    305       BY SIMILARITY.
FT   CARBOHYD     48     48       POTENTIAL.
FT   CARBOHYD     60     60       POTENTIAL.
SQ   SEQUENCE   328 AA;  36276 MW;  D3C76889 CRC32;
     MSIYLRWSLE HGKSNSNSNG IINQQDERFN IFKDNLRFID LHNENNKNAT YKLGLTIFAN
     LTNDEYRSLY LGARTEPVRR ITKAKNVNMK YSAAVNVDEV PVTVDWRQKG AVNAIKDQGT
     CGSCWAFSTA AAVEGINKIV TGELVSLSEQ ELVDCDKSYN QGCNGGLMDY AFQFIMKNGG
     LNTEKDYPYH GTNGKCNSLL KNSRVVTIDG YEDVPSKDET ALKRAVSYQP VSVAIDAGGR
     AFQHYQSGIF TGKCGTNMDH AVVAVGYGSE NGVDYWIVRN SWGTRWGEDG YIRMERNVAS
     KSGKCGIAIE ASYPVKYSPN PVRGTSSV

SwissProt Database

CYS4_DICDI

ID   CYS4_DICDI     STANDARD;      PRT;   442 AA.
AC   P54639;
DT   01-OCT-1996 (REL. 34, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE 4 PRECURSOR (EC 3.4.22.-).
GN   CPRD OR CP4.
OS   DICTYOSTELIUM DISCOIDEUM (SLIME MOLD).
OC   EUKARYOTA; PROTOZOA; SARCOMASTIGOPHORA; SARCODINA; RHIZOPODA;
OC   EUMYCETOZOA; DICTYOSTELIA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=AX4;
RX   MEDLINE; 96081966.
RA   SOUZA G.M., HIRAI J., MEHTA D.P., FREEZE H.H.;
RL   J. BIOL. CHEM. 270:28938-28945(1995).
CC   -!- SUBCELLULAR LOCATION: LYSOSOMAL.
CC   -!- PTM: PHOSPHOGLYCOSYLATED, CONTAINS GLCNAC-ALPHA-1-P-SER RESIDUES.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; L36204; G1222695; -.
DR   DICTYDB; DD0????; CPRD.
KW   HYDROLASE; THIOL PROTEASE; LYSOSOME; ZYMOGEN; GLYCOPROTEIN;
KW   PHOSPHORYLATION; SIGNAL.
FT   SIGNAL        1     17       POTENTIAL.
FT   PROPEP       18      ?       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN         ?    442       CYSTEINE PROTEINASE 4.
FT   ACT_SITE    135    135       BY SIMILARITY.
FT   ACT_SITE    277    277       BY SIMILARITY.
FT   ACT_SITE    406    406       BY SIMILARITY.
FT   DISULFID    132    178       BY SIMILARITY.
FT   DISULFID    169    212       BY SIMILARITY.
FT   DISULFID    270    428       BY SIMILARITY.
FT   DOMAIN      286    296       POLY-SER.
FT   DOMAIN      299    304       POLY-SER.
FT   DOMAIN      310    315       POLY-SER.
FT   DOMAIN      319    323       POLY-SER.
FT   DOMAIN      327    332       POLY-SER.
SQ   SEQUENCE   442 AA;  45690 MW;  42B40EDE CRC32;
     MRVLSFLCLL LVSYASAKQQ FSELQYRNAF TNWMQAHQRT YSSEEFNARY QIFKSNMDYV
     HQWNSKGGET VLGLNVFADI TNQEYRTTYL GTPFDGSALI GTEEEKIFST PAPTVDWRAQ
     GAVTPIKNQG QCGGCWSFST TGSTEGAHFI ASGTKKDLVS LSEQNLIDCS KSYGNNGCEG
     GLMTLGFEYI INNKGIDTES SYPYTAEDGK ECKFKTSNIG AQIVSYQNVT SGSEASLQSA
     SNNAPVSVAI DASNESFQLY ESGIYYEPAC TPTQLDHGVL VVGYGSGSSS SSGSSSGKSS
     SSSSTGGKTS SSSSSGKASS SSSGKASSSS SSGKTSSAAS STSGSQSGSQ SGSQSGQSTG
     SQSGQTSASG QASASGSGSG SGSGSGSGSG SGAVEASSGN YWIVKNSWGT SWGMDGYIFM
     SKDRNNNCGI ATMASFPTAS SN

SwissProt Database

CYS5_DICDI

ID   CYS5_DICDI     STANDARD;      PRT;   344 AA.
AC   P54640;
DT   01-OCT-1996 (REL. 34, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE 5 PRECURSOR (EC 3.4.22.-).
GN   CPRE OR CP5.
OS   DICTYOSTELIUM DISCOIDEUM (SLIME MOLD).
OC   EUKARYOTA; PROTOZOA; SARCOMASTIGOPHORA; SARCODINA; RHIZOPODA;
OC   EUMYCETOZOA; DICTYOSTELIA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=AX4;
RX   MEDLINE; 96081966.
RA   SOUZA G.M., HIRAI J., MEHTA D.P., FREEZE H.H.;
RL   J. BIOL. CHEM. 270:28938-28945(1995).
CC   -!- SUBCELLULAR LOCATION: LYSOSOMAL.
CC   -!- PTM: PHOSPHOGLYCOSYLATED, CONTAINS GLCNAC-ALPHA-1-P-SER RESIDUES.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; L36205; G1222694; -.
DR   DICTYDB; DD0????; CPRE.
KW   HYDROLASE; THIOL PROTEASE; LYSOSOME; ZYMOGEN; GLYCOPROTEIN;
KW   PHOSPHORYLATION; SIGNAL.
FT   SIGNAL        1     17       POTENTIAL.
FT   PROPEP       18      ?       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN         ?    344       CYSTEINE PROTEINASE 4.
FT   ACT_SITE    136    136       BY SIMILARITY.
FT   ACT_SITE    272    272       BY SIMILARITY.
FT   ACT_SITE    311    311       BY SIMILARITY.
SQ   SEQUENCE   344 AA;  37212 MW;  25D35FB9 CRC32;
     MKVLSFLCVL LVSVATAKQQ FSELQYRNAF TDWMITHQKS YTSEEFGARY NIFTANMDYV
     QQWNSKGSET VLGLNNFADI TNEEYRNTYL GTKFDASSLI GTQEEKVHTN SSAASKDWRS
     EGAVTPVKNQ GQCGGCWSFS TTGSTEGAHF QSKGELVSLS EQNLIDCSTE NSGCDGGLMT
     YAFEYIINNN GIDTESSYPY KAENGKCEYK SENSGATLSS YKTVTAGSES SLESAVNVNP
     VSVAIDASHQ SFQLYTSGIY YEPECSSENL DHGVLAVGYG SGSGSSSGQS SGQSSGNLSA
     SSSNEYWIVK NSWGTSWGIE GYILMSRNRD NNCGIASSAS FPVV

SwissProt Database

CYSL_LYCES

ID   CYSL_LYCES     STANDARD;      PRT;   346 AA.
AC   P20721;
DT   01-FEB-1991 (REL. 17, CREATED)
DT   01-FEB-1991 (REL. 17, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   LOW-TEMPERATURE-INDUCED CYSTEINE PROTEINASE PRECURSOR (EC 3.4.22.-)
DE   (FRAGMENT).
OS   LYCOPERSICON ESCULENTUM (TOMATO).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE;
OC   SOLANALES; SOLANACEAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=CV. VFNT CHERRY;
RA   SCHAFFER M.A., FISCHER R.L.;
RL   PLANT PHYSIOL. 87:431-436(1988).
CC   -!- INDUCTION: IN RESPONSE TO LOW TEMPERATURE.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; M21444; G806314; -.
DR   PIR; JA0159; JA0159.
DR   HSSP; P00785; 1AEC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; GLYCOPROTEIN.
FT   NON_TER       1      1
FT   PROPEP       <1     17       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN        18    346       LOW-TEMPERATURE-INDUCED CYSTEINE
FT                                PROTEINASE.
FT   ACT_SITE     42     42       BY SIMILARITY.
FT   ACT_SITE    178    178       BY SIMILARITY.
FT   ACT_SITE    198    198       BY SIMILARITY.
FT   DISULFID     39     81       BY SIMILARITY.
FT   DISULFID     73    114       BY SIMILARITY.
FT   DISULFID    172    223       BY SIMILARITY.
FT   CARBOHYD    215    215       POTENTIAL.
SQ   SEQUENCE   346 AA;  37429 MW;  C760F25E CRC32;
     KLSKNKSDRY LPKVGDSLPE SIDWREKGVL VGVKDQGSCG SCWAFSAVAA MESINAIVTG
     NLISLSEQEL VDCDRSYNEG CDGGLMDYAF EFVIKNGGID TEEDYPYKER NGVCDQYRKN
     AKVVKIDSYE DVPVNNEKAL QKAVAHQPVS IALEAGGRDF QHYKSGIFTG KCGTAVDHGV
     VIAGYGTENG MDYWIVRNSW GANCRENGYL RVQRNVSSSS GLCGLAIEPS YPVKTGPNPP
     KPAPSPPSPV KPPTECDEYS QCAVGTTCCC ILQFRRSCFS WGCCPLEGAT CCEDHYSCCP
     HDYPICNVRQ GTCSMSKGNP LGVKAMKRIL AQPIGAFGNG GKKSSS

SwissProt Database

CYSP_HEMSP

ID   CYSP_HEMSP     STANDARD;      PRT;   360 AA.
AC   P43156;
DT   01-NOV-1995 (REL. 32, CREATED)
DT   01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   THIOL PROTEASE SEN102 PRECURSOR (EC 3.4.22.-).
GN   SEN102.
OS   HEMEROCALLIS SP. (DAYLILY).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; MONOCOTYLEDONEAE;
OC   LILIALES; LILIACEAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=CV. CRADDLE SONG; TISSUE=PETAL/SEPAL;
RX   MEDLINE; 95359413.
RA   VALPUESTA V., LANGE N., GUERRERO C., REID M.;
RL   PLANT MOL. BIOL. 28:575-582(1995).
CC   -!- SUBCELLULAR LOCATION: ENDOPLASMIC RETICULUM LUMEN (POTENTIAL).
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; X74406; G396568; -.
DR   PROSITE; PS00014; ER_TARGET.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; GLYCOPROTEIN; SIGNAL;
KW   ENDOPLASMIC RETICULUM.
FT   SIGNAL        1     20       POTENTIAL.
FT   PROPEP       21    133       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN       134    360       THIOL PROTEASE SEN102.
FT   ACT_SITE    154    154       BY SIMILARITY.
FT   ACT_SITE    289    289       BY SIMILARITY.
FT   ACT_SITE    310    310       BY SIMILARITY.
FT   CARBOHYD    353    353       POTENTIAL.
FT   SITE        357    360       PREVENT SECRETION FROM ER (POTENTIAL).
SQ   SEQUENCE   360 AA;  39914 MW;  E68E709D CRC32;
     MAKPKFIALA LVALSFLSIA QSIPFTEKDL ASEDSLWNLY EKWRTHHTVA RDLDEKNRRF
     NVFKENVKFI HEFNQKKDAP YKLALNKFGD MTNQEFRSKY AGSKIQHHRS QRGIQKNTGS
     FMYENVGSLP AASIDWRAKG AVTGVKDQGQ CGSCWAFSTI ASVEGINQIK TGELVSLSEQ
     ELVDCDTSYN EGCNGGLMDY AFEFIQKNGI TTEDSYPYAE QDGTCASNLL NSPVVSIDGH
     QDVPANNENA LMQAVANQPI SVSIEASGYG FQFYSEGVFT GRCGTELDHG VAIVGYGATR
     DGTKYWIVKN SWGEEWGESG YIRMQRGISD KRGKCGIAME ASYPIKTSAN PKNSSTRDEL

SwissProt Database

CYSP_PEA

ID   CYSP_PEA       STANDARD;      PRT;   363 AA.
AC   P25804;
DT   01-MAY-1992 (REL. 22, CREATED)
DT   01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE 15A PRECURSOR (EC 3.4.22.-) (TURGOR-RESPONSIVE
DE   PROTEIN 15A).
OS   PISUM SATIVUM (GARDEN PEA).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE; FABALES;
OC   FABACEAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=CV. PROGRESS NO. 9;
RX   MEDLINE; 91355842.
RA   GUERRERO F.D., JONES J.T., MULLET J.E.;
RL   PLANT MOL. BIOL. 15:11-26(1990).
CC   -!- INDUCTION: BY DEHYDRATION OF SHOOTS BUT NOT ROOTS AND NOT BY
CC       HEAT SHOCK OR ABA.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; X54358; G20679; -.
DR   PIR; S11862; S11862.
DR   HSSP; P07858; 1HUC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; GLYCOPROTEIN; SIGNAL.
FT   SIGNAL        1     18       POTENTIAL.
FT   PROPEP       19    131       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN       132    363       CYSTEINE PROTEINASE 15A.
FT   ACT_SITE    156    156       BY SIMILARITY.
FT   ACT_SITE    299    299       BY SIMILARITY.
FT   ACT_SITE    326    326       BY SIMILARITY.
FT   DISULFID    153    203       BY SIMILARITY.
FT   DISULFID    187    236       BY SIMILARITY.
FT   DISULFID    292    347       BY SIMILARITY.
FT   CARBOHYD    249    249       POTENTIAL.
SQ   SEQUENCE   363 AA;  40126 MW;  CB86647F CRC32;
     MDRRFLFALF LFAAVATAVT DDTNNDDFII RQVVDNEEDH LLNAEHHFTS FKSKFSKSYA
     TKEEHDYRFG VFKSNLIKAK LHQNRDPTAE HGITKFSDLT ASEFRRQFLG LKKRLRLPAH
     AQKAPILPTT NLPEDFDWRE KGAVTPVKDQ GSCGSCWAFS TTGALEGAHY LATGKLVSLS
     EQQLVDCDHV CDPEQAGSCD SGCNGGLMNN AFEYLLESGG VVQEKDYAYT GRDGSCKFDK
     SKVVASVSNF SVVTLDEDQI AANLVKNGPL AVAINAAWMQ TYMSGVSCPY VCAKSRLDHG
     VLLVGFGKGA YAPIRLKEKP YWIIKNSWGQ NWGEQGYYKI CRGRNVCGVD SMVSTVAAAQ
     SNH

SwissProt Database

CYSP_PHAVU

ID   CYSP_PHAVU     STANDARD;      PRT;   362 AA.
AC   P25803;
DT   01-MAY-1992 (REL. 22, CREATED)
DT   01-JUN-1994 (REL. 29, LAST SEQUENCE UPDATE)
DT   01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE)
DE   VIGNAIN PRECURSOR (EC 3.4.22.-) (BEAN ENDOPEPTIDASE) (CYSTEINE
DE   PROTEINASE EP-C1).
OS   PHASEOLUS VULGARIS (KIDNEY BEAN) (FRENCH BEAN).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE; FABALES;
OC   FABACEAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=CV. SAXA; TISSUE=SEEDLING;
RX   MEDLINE; 92329731.
RA   OGUSHI Y., TANAKA T., YAMAUCHI D., MINAMIKAWA T.;
RL   PLANT MOL. BIOL. 19:705-706(1992).
RN   [2]
RP   SEQUENCE OF 2-362 FROM N.A.
RC   STRAIN=CV. GOLDSTAR; TISSUE=FRUIT;
RX   MEDLINE; 91322501.
RA   TANAKA T., YAMAUCHI D., MINAMIKAWA T.;
RL   PLANT MOL. BIOL. 16:1083-1084(1991).
CC   -!- FUNCTION: THOUGHT TO BE INVOLVED IN THE HYDROLYSIS OF STORED
CC       SEED PROTEINS.
CC   -!- SUBUNIT: MONOMER.
CC   -!- SUBCELLULAR LOCATION: ENDOPLASMIC RETICULUM LUMEN.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; X63102; G20994; -.
DR   EMBL; X56753; E33857; -.
DR   PIR; S16251; S16251.
DR   HSSP; P00785; 1AEC.
DR   PROSITE; PS00014; ER_TARGET.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; GLYCOPROTEIN; SIGNAL;
KW   ENDOPLASMIC RETICULUM.
FT   SIGNAL        1     20       POTENTIAL.
FT   PROPEP       21    131       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN       132    362       VIGNAIN.
FT   ACT_SITE    152    152       BY SIMILARITY.
FT   ACT_SITE    288    288       BY SIMILARITY.
FT   ACT_SITE    309    309       BY SIMILARITY.
FT   CARBOHYD    326    326       POTENTIAL.
FT   CARBOHYD    346    346       POTENTIAL.
FT   SITE        359    362       PREVENT SECRETION FROM ER.
FT   CONFLICT    107    107       P -> H (IN REF. 2).
SQ   SEQUENCE   362 AA;  40212 MW;  5B448E27 CRC32;
     MATKKLLWVV LSFSLVLGVA NSFDFHDKDL ASEESLWDLY ERWRSHHTVS RSLGEKHKRF
     NVFKANLMHV HNTNKMDKPY KLKLNKFADM TNHEFRSTYA GSKVNHPRMF RGTPHENGAF
     MYEKVVSVPP SVDWRKKGAV TDVKDQGQCG SCWAFSTVVA VEGINQIKTN KLVALSEQEL
     VDCDKEENQG CNGGLMESAF EFIKQKGGIT TESNYPYKAQ EGTCDASKVN DLAVSIDGHE
     NVPANDEDAL LKAVANQPVS VAIDAGGSDF QFYSEGVFTG DCSTDLNHGV AIVGYGTTVD
     GTNYWIVRNS WGPEWGEHGY IRMQRNISKK EGLCGIAMLP SYPIKNSSDN PTGSFSSPKD
     EL

SwissProt Database

CYSP_PLAFA

ID   CYSP_PLAFA     STANDARD;      PRT;   569 AA.
AC   P25805;
DT   01-MAY-1992 (REL. 22, CREATED)
DT   01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   THROPHOZOITE CYSTEINE PROTEINASE PRECURSOR (EC 3.4.22.-) (TCP).
OS   PLASMODIUM FALCIPARUM.
OC   EUKARYOTA; PROTOZOA; APICOMPLEXA; SPOROZOA; COCCIDIA; EUCOCCIDIIDA.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 92228005.
RA   ROSENTHAL P.J., NELSON R.G.;
RL   MOL. BIOCHEM. PARASITOL. 51:143-152(1992).
CC   -!- FUNCTION: PROBABLY DEGRADES ERYTHROCYTE HEMOGLOBIN.
CC   -!- DEVELOPMENTAL STAGE: THROPHOZOITE.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
CC   -!- SIMILARITY: STRONGEST SIMILARITY TO CATHEPSIN L.
DR   EMBL; M81341; G160248; -.
DR   PIR; A45624; A45624.
DR   HSSP; P07858; 1HUC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; GLYCOPROTEIN; SIGNAL.
FT   SIGNAL        1      ?       POTENTIAL.
FT   PROPEP        ?    332       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN       333    569       THROPHOZOITE CYSTEINE PROTEINASE.
FT   DOMAIN       64     70       POLY-ASN.
FT   ACT_SITE    357    357       BY SIMILARITY.
FT   ACT_SITE    488    488       BY SIMILARITY.
FT   ACT_SITE    533    533       BY SIMILARITY.
FT   DISULFID    354    395       BY SIMILARITY.
FT   CARBOHYD     58     58       POTENTIAL.
FT   CARBOHYD     98     98       POTENTIAL.
FT   CARBOHYD    121    121       POTENTIAL.
FT   CARBOHYD    127    127       POTENTIAL.
FT   CARBOHYD    479    479       POTENTIAL.
FT   CARBOHYD    487    487       POTENTIAL.
SQ   SEQUENCE   569 AA;  66880 MW;  9B8F0096 CRC32;
     MVAIKEMKEL AFARPSLVET LNKKKKFLKK KEKRTFVLSI YAFITFIIFC IGILYFTNKS
     SAHNNNNNKN EHSLKKEEIE LLRVLLEKYK KQKDGILNES SNEEDEEKYT LNSETYNNKN
     NVSNIKNDSI KSKKEEYINL ERILLEKYKK FINENNEENR KELSNILHKL LEINKLILRE
     EKDDKKVYLI NDNYDEKGAL EIGMNEEMKY KKEDPINNIK YASKFFKFMK EHNKVYKNID
     EQMRKFEIFK INYISIKNHN KLNKNAMYKK KVNQFSDYSE EELKEYFKTL LHVPNHMIEK
     YSKPFENHLK DNILISEFYT NGKRNEKDIF SKVPEILDYR EKGIVHEPKD QGLCGSCWAF
     ASVGNIESVF AKKNKNILSF SEQEVVDCSK DNFGCDGGHP FYSFLYVLQN ELCLGDEYKY
     KAKDDMFCLN YRCKRKVSLS SIGAVKENQL ILALNEVGPL SVNVGVNNDF VAYSEGVYNG
     TCSEELNHSV LLVGYGQVEK TKLNYNNKIQ TYNTKENSNQ PDDNIIYYWI IKNSWSKKWG
     ENGFMRLSRN KNGDNVFCGI GEEVFYPIL

SwissProt Database

CYSP_PLAFA

ID   CYSP_PLAFA     STANDARD;      PRT;   569 AA.
AC   P25805;
DT   01-MAY-1992 (REL. 22, CREATED)
DT   01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   THROPHOZOITE CYSTEINE PROTEINASE PRECURSOR (EC 3.4.22.-) (TCP).
OS   PLASMODIUM FALCIPARUM.
OC   EUKARYOTA; PROTOZOA; APICOMPLEXA; SPOROZOA; COCCIDIA; EUCOCCIDIIDA.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 92228005.
RA   ROSENTHAL P.J., NELSON R.G.;
RL   MOL. BIOCHEM. PARASITOL. 51:143-152(1992).
CC   -!- FUNCTION: PROBABLY DEGRADES ERYTHROCYTE HEMOGLOBIN.
CC   -!- DEVELOPMENTAL STAGE: THROPHOZOITE.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
CC   -!- SIMILARITY: STRONGEST SIMILARITY TO CATHEPSIN L.
DR   EMBL; M81341; G160248; -.
DR   PIR; A45624; A45624.
DR   HSSP; P07858; 1HUC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; GLYCOPROTEIN; SIGNAL.
FT   SIGNAL        1      ?       POTENTIAL.
FT   PROPEP        ?    332       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN       333    569       THROPHOZOITE CYSTEINE PROTEINASE.
FT   DOMAIN       64     70       POLY-ASN.
FT   ACT_SITE    357    357       BY SIMILARITY.
FT   ACT_SITE    488    488       BY SIMILARITY.
FT   ACT_SITE    533    533       BY SIMILARITY.
FT   DISULFID    354    395       BY SIMILARITY.
FT   CARBOHYD     58     58       POTENTIAL.
FT   CARBOHYD     98     98       POTENTIAL.
FT   CARBOHYD    121    121       POTENTIAL.
FT   CARBOHYD    127    127       POTENTIAL.
FT   CARBOHYD    479    479       POTENTIAL.
FT   CARBOHYD    487    487       POTENTIAL.
SQ   SEQUENCE   569 AA;  66880 MW;  9B8F0096 CRC32;
     MVAIKEMKEL AFARPSLVET LNKKKKFLKK KEKRTFVLSI YAFITFIIFC IGILYFTNKS
     SAHNNNNNKN EHSLKKEEIE LLRVLLEKYK KQKDGILNES SNEEDEEKYT LNSETYNNKN
     NVSNIKNDSI KSKKEEYINL ERILLEKYKK FINENNEENR KELSNILHKL LEINKLILRE
     EKDDKKVYLI NDNYDEKGAL EIGMNEEMKY KKEDPINNIK YASKFFKFMK EHNKVYKNID
     EQMRKFEIFK INYISIKNHN KLNKNAMYKK KVNQFSDYSE EELKEYFKTL LHVPNHMIEK
     YSKPFENHLK DNILISEFYT NGKRNEKDIF SKVPEILDYR EKGIVHEPKD QGLCGSCWAF
     ASVGNIESVF AKKNKNILSF SEQEVVDCSK DNFGCDGGHP FYSFLYVLQN ELCLGDEYKY
     KAKDDMFCLN YRCKRKVSLS SIGAVKENQL ILALNEVGPL SVNVGVNNDF VAYSEGVYNG
     TCSEELNHSV LLVGYGQVEK TKLNYNNKIQ TYNTKENSNQ PDDNIIYYWI IKNSWSKKWG
     ENGFMRLSRN KNGDNVFCGI GEEVFYPIL

SwissProt Database

CYSP_PLAVI

ID   CYSP_PLAVI     STANDARD;      PRT;   583 AA.
AC   P42666;
DT   01-NOV-1995 (REL. 32, CREATED)
DT   01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE PRECURSOR (EC 3.4.22.-).
OS   PLASMODIUM VIVAX.
OC   EUKARYOTA; PROTOZOA; APICOMPLEXA; SPOROZOA; COCCIDIA; EUCOCCIDIIDA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=SALVADOR I;
RX   MEDLINE; 94334995.
RA   ROSENTHAL P.J., RING C.S., CHEN X., COHEN F.E.;
RL   J. MOL. BIOL. 241:312-316(1994).
CC   -!- FUNCTION: PROBABLY DEGRADES ERYTHROCYTE HEMOGLOBIN.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
CC   -!- SIMILARITY: STRONGEST SIMILARITY TO CATHEPSIN L.
DR   EMBL; L26362; G431434; -.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; GLYCOPROTEIN; SIGNAL.
FT   SIGNAL        1      ?       POTENTIAL.
FT   PROPEP        ?    338       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN       339    583       CYSTEINE PROTEINASE.
FT   ACT_SITE    363    363       BY SIMILARITY.
FT   ACT_SITE    495    495       BY SIMILARITY.
FT   ACT_SITE    547    547       BY SIMILARITY.
FT   DISULFID    360    402       BY SIMILARITY.
FT   CARBOHYD     70     70       POTENTIAL.
FT   CARBOHYD    195    195       POTENTIAL.
FT   CARBOHYD    272    272       POTENTIAL.
FT   CARBOHYD    381    381       POTENTIAL.
FT   CARBOHYD    486    486       POTENTIAL.
FT   CARBOHYD    494    494       POTENTIAL.
SQ   SEQUENCE   583 AA;  65721 MW;  4078A8D5 CRC32;
     MAQDIKIMNL TKSSLEALNR NQMLSKKSSR KILKICMYAI LTFAMCGVVL ICLTAMSNSD
     GSLTQSGSHN QSGSLKGLSS TPGDGEILNK AEIETLRFIF SNYPHGNRDP TGDDVEKPAD
     AALPNEEDQK VKIADAGKHI KLMKQYNEIV ADMSEDNKEQ LAKMLRELLK KKINERKKKR
     EDPNGNNEEG KEVINISVPS FNYKRVSANQ DDSDDEEEVS VAQIEGLFVN LKYASKFFNF
     MNKYKRSYKD INEQMEKYKN FKMNYLKIKK HNETNQMYKM KVNQFSDYSK KDFESYFRKL
     VPIPDHLKKK YVVPFSSMNN GKGKNVVTSS SGANLLADVP EILDYREKGI VHEPKDQGLC
     GSCWAFASVG NVECMYAKEH NKTILTLSEQ EVVDCSKLNF GCDGGHPFYS FIYAIENGIC
     MGDDYKYKAM DNLFCLNYRC KNKVTLSSVG GVKENELIRA LNEVGPVSVN VGVTDDFSFY
     GGGIFNGTCT EELNHSVLLV GYGQVQSSKI FQEKNAYDDA SGVTKKGALS YPSKADDGIQ
     YYWIIKNSWS KFWGENGFMR ISRNKEGDNV FCGIGVEVFY PIL

SwissProt Database

CYSP_PLAVN

ID   CYSP_PLAVN     STANDARD;      PRT;   506 AA.
AC   P46102;
DT   01-NOV-1995 (REL. 32, CREATED)
DT   01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE PRECURSOR (EC 3.4.22.-).
OS   PLASMODIUM VINCKEI.
OC   EUKARYOTA; PROTOZOA; APICOMPLEXA; SPOROZOA; COCCIDIA; EUCOCCIDIIDA.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 93250055.
RA   ROSENTHAL P.J.;
RL   BIOCHIM. BIOPHYS. ACTA 1173:91-93(1993).
CC   -!- FUNCTION: PROBABLY DEGRADES ERYTHROCYTE HEMOGLOBIN.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
CC   -!- SIMILARITY: STRONGEST SIMILARITY TO CATHEPSIN L.
DR   EMBL; L08500; -; NOT_ANNOTATED_CDS.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; GLYCOPROTEIN; SIGNAL.
FT   SIGNAL        1      ?       POTENTIAL.
FT   PROPEP        ?    262       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN       263    506       CYSTEINE PROTEINASE.
FT   ACT_SITE    287    287       BY SIMILARITY.
FT   ACT_SITE    419    419       BY SIMILARITY.
FT   ACT_SITE    470    470       BY SIMILARITY.
FT   DISULFID    284    326       BY SIMILARITY.
FT   CARBOHYD     21     21       POTENTIAL.
FT   CARBOHYD    133    133       POTENTIAL.
FT   CARBOHYD    258    258       POTENTIAL.
FT   CARBOHYD    418    418       POTENTIAL.
SQ   SEQUENCE   506 AA;  58255 MW;  0856C8B6 CRC32;
     MSDNIGQINF TIPGIQSLDE NDTYLKINHK KTIKICAYAI TAIALFFIGG VFFKNQAKIN
     ALDAIDEAVL MNKEIAHLRE ILNKYKATIN EDDEFVYQAY DNKNGDSENQ LLLMLHKLLK
     NNANKVNTFD VNNESNKNID PTYIFRQKLE SMQDNIKYAS KFFKYMKENN KKYENMDEQL
     QRFENFKIRY MKTQKHNEMV GKNGLTYVQK VNQYSDFSKE EFDNYFKKLL SVPMDLKSKY
     IVPLKKHLAN TNLISVDNKS KDFPDSRDYR SKFNFLPPKD QGNCGSCWAF AAIGNFEYLY
     VHTRHEMPIS FSEQQMVDCS TENYGCDGGN PFYAFLYMIN NGVCLGDEYP YKGHEDFFCL
     NYRCSLLGRV HFIGDVKPNE LIMALNYVGP VTIAVGASED FVLYSGGVFD GECNPELNHS
     VLLVGYGQVK KSLAFEDSHS NVDSNLIKKY KENIKGDDDD DIIYYWIVRN SWGPNWGEGG
     YIRIKRNKAG DDGFCGVGSD VFFPIY

SwissProt Database

CYSP_SCHJA

ID   CYSP_SCHJA     STANDARD;      PRT;   342 AA.
AC   P43157;
DT   01-NOV-1995 (REL. 32, CREATED)
DT   01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CATHEPSIN B-LIKE CYSTEINE PROTEINASE PRECURSOR (EC 3.4.22.-)
DE   (ANTIGEN SJ31).
GN   CATB.
OS   SCHISTOSOMA JAPONICUM (BLOOD FLUKE).
OC   EUKARYOTA; METAZOA; ACOELOMATES; PLATYHELMINTHES; TREMATODA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=CHINESE MAINLAND;
RX   MEDLINE; 95207690.
RA   MERCKELBACH A., HASSE S., DELL R., ESCHLBECK A., RUPPEL A.;
RL   TROP. MED. PARASITOL. 45:193-198(1994).
CC   -!- FUNCTION: THIOL PROTEASE. HAS A ROLE AS A DIGESTIVE ENZYME.
CC   -!- TISSUE SPECIFICITY: INTESTINE (GUT).
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
CC   -!- SIMILARITY: STRONGEST, TO CATHEPSIN B.
DR   EMBL; X70968; G11167; -.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL; ANTIGEN.
FT   SIGNAL        1     17       POTENTIAL.
FT   PROPEP       18     89       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN        90    342       CATHEPSIN B-LIKE CYSTEINE PROTEINASE.
FT   ACT_SITE    118    118       BY SIMILARITY.
FT   ACT_SITE    288    288       BY SIMILARITY.
FT   ACT_SITE    308    308       BY SIMILARITY.
FT   DISULFID    103    132       BY SIMILARITY.
FT   DISULFID    115    159       BY SIMILARITY.
FT   DISULFID    151    217       BY SIMILARITY.
FT   DISULFID    152    155       BY SIMILARITY.
FT   DISULFID    188    221       BY SIMILARITY.
FT   DISULFID    196    207       BY SIMILARITY.
SQ   SEQUENCE   342 AA;  38796 MW;  3B8F44AB CRC32;
     MLKIAVYIVS LFTFLEAHVT TRNNQRIEPL SDEMISFINE HPDAGWKADK SDRFHSLDDA
     RILMGARKED AEMKRNRRPT VDHHDLNVEI PSQFDSRKKW PHCKSISQIR DQSRCGSCWA
     FGAVEAMTDR ICIQSGGGQS AELSALDLIS CCKDCGDGCQ GGFPGVAWDY WVKRGIVTGG
     SKENHTGCQP YPFPKCEHHT KGKYPACGTK IYKTPQCKQT CQKGYKTPYE QDKHYGDESY
     NVQNNEKVIQ RDIMMYGPVE AAFDVYEDFL NYKSGIYRHV TGSIVGGHAI RIIGWGVEKR
     TPYWLIANSW NEDWGEKGLF RMVRGRDECS IESDVVAGLI KT

SwissProt Database

CYSP_SCHMA

ID   CYSP_SCHMA     STANDARD;      PRT;   340 AA.
AC   P25792;
DT   01-MAY-1992 (REL. 22, CREATED)
DT   01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CATHEPSIN B-LIKE CYSTEINE PROTEINASE PRECURSOR (EC 3.4.22.-)
DE   (ANTIGEN SM31).
OS   SCHISTOSOMA MANSONI (BLOOD FLUKE).
OC   EUKARYOTA; METAZOA; ACOELOMATES; PLATYHELMINTHES; TREMATODA.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 89261925.
RA   KLINKERT M.-Q., FELLEISEN R., LINK G., RUPPEL A., BECK E.;
RL   MOL. BIOCHEM. PARASITOL. 33:113-122(1989).
CC   -!- FUNCTION: THIOL PROTEASE. HAS A ROLE AS A DIGESTIVE ENZYME.
CC   -!- TISSUE SPECIFICITY: INTESTINE (GUT).
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
CC   -!- SIMILARITY: STRONGEST, TO CATHEPSIN B.
DR   EMBL; M21309; G160950; -.
DR   HSSP; P07858; 1HUC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL; ANTIGEN.
FT   SIGNAL        1     17       POTENTIAL.
FT   PROPEP       18     88       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN        89    340       CATHEPSIN B-LIKE CYSTEINE PROTEINASE.
FT   ACT_SITE    117    117       BY SIMILARITY.
FT   ACT_SITE    287    287       BY SIMILARITY.
FT   ACT_SITE    307    307       BY SIMILARITY.
FT   DISULFID    102    131       BY SIMILARITY.
FT   DISULFID    114    158       BY SIMILARITY.
FT   DISULFID    150    216       BY SIMILARITY.
FT   DISULFID    151    154       BY SIMILARITY.
FT   DISULFID    187    220       BY SIMILARITY.
FT   DISULFID    195    206       BY SIMILARITY.
SQ   SEQUENCE   340 AA;  38592 MW;  3CCE5F85 CRC32;
     MLTSILCIAS LITFLEAHIS VKNEKFEPLS DDIISYINEH PNAGWRAEKS NRFHSLDDAR
     IQMGARREEP DLRRKRRPTV DHNDWNVEIP SNFDSRKKWP GCKSIATIRD QSRCGSCWSF
     GAVEAMSDRS CIQSGGKQNV ELSAVDLLTC CESCGLGCEG GILGPAWDYW VKEGIVTASS
     KENHTGCEPY PFPKCEHHTK GKYPPCGSKI YNTPRCKQTC QRKYKTPYTQ DKHRGKSSYN
     VKNDEKAIQK EIMKYGPVEA SFTVYEDFLN YKSGIYKHIT GEALGGHAIR IIGWGVENKT
     PYWLIANSWN EDWGENGYFR IVRGRDECSI ESEVIAGRIN

SwissProt Database

CYSP_THEAN

ID   CYSP_THEAN     STANDARD;      PRT;   441 AA.
AC   P25781;
DT   01-MAY-1992 (REL. 22, CREATED)
DT   01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE PRECURSOR (EC 3.4.22.-).
GN   TACP.
OS   THEILERIA ANNULATA.
OC   EUKARYOTA; PROTOZOA; APICOMPLEXA; SPOROZOA; COCCIDIA; PIROPLASMIDA.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 92389980.
RA   BAYLIS H.A., MEGSON A., MOTTRAM J.C., HALL R.;
RL   MOL. BIOCHEM. PARASITOL. 54:105-107(1992).
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; M86659; G161887; -.
DR   PIR; A45565; A45565.
DR   HSSP; P00785; 1AEC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL; GLYCOPROTEIN.
FT   SIGNAL        1      ?       POTENTIAL.
FT   PROPEP        ?    227       ACTIVATION PEPTIDE.
FT   CHAIN       228    441       CYSTEINE PROTEINASE.
FT   ACT_SITE    252    252       BY SIMILARITY.
FT   ACT_SITE    381    381       BY SIMILARITY.
FT   ACT_SITE    403    403       BY SIMILARITY.
FT   DISULFID    249    290       BY SIMILARITY.
FT   CARBOHYD    270    270       POTENTIAL.
FT   CARBOHYD    345    345       POTENTIAL.
SQ   SEQUENCE   441 AA;  49653 MW;  AD4F3D96 CRC32;
     MTVLDDHFPQ GDDETVVPTS SSIPILSQMR QIVIKKRLLI SFLLTFFILA LSSASILTYF
     FFRSKSITNF KSLAIEHIES HYPSMDPSKR AGFVEEIVKI RQTGKITSDA ESELDMLIEF
     DAFVEKYKKV HRSFDQRVQR FLTFRKNYHI VKTHKPTEPY SLDLNKFSDL SDEEFKALYP
     VITPPKTYTS LSKHLEFKKM SHKNPIYISK LKKAKGIEEI KDLSLITGEN LNWARTDAVS
     PTKDQGDHCG SCWAFSSIAS VESLYRLYKN KSYFLSEQEL VNCDKSSMGC AGGLPITALE
     YIHSKGVSFE SEVPYTGIVS PCKPSIKNKV FIDSISILKG NDVVNKSLVI SPTVVGIAVT
     KELKLYSGGI FTGKCGGELN HAVLLVGEGV DHETGMRYWI IKNSWGEDWG ENGFLRLQRT
     KKGLDKCGIL TFGLNPILYS S

SwissProt Database

CYSP_THEPA

ID   CYSP_THEPA     STANDARD;      PRT;   439 AA.
AC   P22497;
DT   01-AUG-1991 (REL. 19, CREATED)
DT   01-AUG-1991 (REL. 19, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE PRECURSOR (EC 3.4.22.-).
OS   THEILERIA PARVA.
OC   EUKARYOTA; PROTOZOA; APICOMPLEXA; SPOROZOA; COCCIDIA; PIROPLASMIDA.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 91009278.
RA   NENE V., GOBRIGHT E., MUSOKE A.J., LONSDALE-ECCLES J.D.;
RL   J. BIOL. CHEM. 265:18047-18050(1990).
RN   [2]
RP   SEQUENCE OF 178-439 FROM N.A.
RC   STRAIN=MUGUGA;
RX   MEDLINE; 92228011.
RA   NENE V., IAMS K.P., GOBRIGHT E., MUSOKE A.J.;
RL   MOL. BIOCHEM. PARASITOL. 51:17-27(1992).
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; M37791; G161873; -.
DR   EMBL; M67476; G161879; -.
DR   PIR; A36083; KHQBTT.
DR   HSSP; P10056; 1PPO.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL; GLYCOPROTEIN.
FT   SIGNAL        1     59       POTENTIAL.
FT   PROPEP       60    228       ACTIVATION PEPTIDE.
FT   CHAIN       229    439       CYSTEINE PROTEINASE.
FT   ACT_SITE    252    252       BY SIMILARITY.
FT   ACT_SITE    381    381       BY SIMILARITY.
FT   ACT_SITE    403    403       BY SIMILARITY.
FT   DISULFID    249    290       BY SIMILARITY.
FT   DOMAIN      165    181       INVOLVED IN PROCESSING TO YIELD ACTIVE
FT                                ENZYMES (BY SIMILARITY).
FT   CARBOHYD    205    205       POTENTIAL.
SQ   SEQUENCE   439 AA;  50179 MW;  B4BD9301 CRC32;
     MVSSVVSNPN ERLVNNRVEN DLESSDDTLS TQAKPVSRLL TRKLLLGVVV LFFLAGVSVV
     SYFLFSKYKM LNKFKRELDD HLTKDFPNLE RSKRDTCFDE LTRLFGDGFL SDDPKLEYEV
     YREFEEFNSK YNRRHATQQE RLNRLVTFRS NYLEVKEQKG DEPYVKGINR FSDLTEREFY
     KLFPVMKPPK ATYSNGYYLL SHMANKTYLK NLKKALNTDE DVDLAKLTGE NLDWRRSSSV
     TSVKDQSNCG GCWAFSTVGS VEGYYMSHFD KSYELSVQEL LDCDSFSNGC QGGLLESAYE
     YVRKYGLVSA KDLPFVDKAR RCSVPKAKKV SVPSYHVFKG KEVMTRSLTS SPCSVYLSVS
     PELAKYKSGV FTGECGKSLN HAVVLVGEGY DEVTKKRYWV VQNSWGTDWG ENGYMRLERT
     NMGTDKCGVL DTSMSAFEL

SwissProt Database

CYSP_TRIFO

ID   CYSP_TRIFO     STANDARD;      PRT;    23 AA.
AC   P33403;
DT   01-FEB-1994 (REL. 28, CREATED)
DT   01-FEB-1994 (REL. 28, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE (EC 3.4.22.-) (FRAGMENT).
OS   TRICHOMONAS FOETUS.
OC   EUKARYOTA; PROTOZOA; SARCOMASTIGOPHORA; MASTIGOPHORA; TRICHOMONADIDA;
OC   TRICHOMONADIDAE.
RN   [1]
RP   SEQUENCE.
RX   MEDLINE; 93307628.
RA   IRVINE J.W., COOMBS G.H., NORTH M.J.;
RL   FEMS MICROBIOL. LETT. 110:113-120(1993).
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE.
FT   NON_TER      23     23
SQ   SEQUENCE   23 AA;  2514 MW;  68789EDA CRC32;
     ADSLDWREKG VVNSIKDQAQ XGS

SwissProt Database

CYSP_TRYBB

ID   CYSP_TRYBB     STANDARD;      PRT;   450 AA.
AC   P14658;
DT   01-APR-1990 (REL. 14, CREATED)
DT   01-APR-1990 (REL. 14, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE PRECURSOR (EC 3.4.22.-).
OS   TRYPANOSOMA BRUCEI BRUCEI.
OC   EUKARYOTA; PROTOZOA; SARCOMASTIGOPHORA; MASTIGOPHORA; KINETOPLASTIDA;
OC   TRYPANOSOMATIDAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=I STAR SERODEME;
RX   MEDLINE; 90092471.
RA   MOTTRAM J.C., NORTH M.J., BARRY J.D., COOMBS G.H.;
RL   FEBS LETT. 258:211-215(1989).
RN   [2]
RP   PARTIAL SEQUENCE.
RX   MEDLINE; 89219143.
RA   CAZZULO J.J., COUSO R., RAIMONDI A., WERNSTEDT C., HELLMAN U.;
RL   MOL. BIOCHEM. PARASITOL. 33:33-42(1989).
RN   [3]
RP   SEQUENCE FROM N.A.
RC   STRAIN=RHODESIENSE WRATAT 1.1;
RX   MEDLINE; 91045093.
RA   PAMER E.G., DAVIS C.E., EAKIN A., SO M.;
RL   NUCLEIC ACIDS RES. 18:6141-6141(1990).
CC   -!- FUNCTION: THE CYSTEINE PROTEINASES HAVE A POTENTIAL ROLE IN
CC       HOST-PARASITE INTERACTION AND VIRULENCE.
CC   -!- THE 108-RESIDUE EXTENSION APPEARS LIKELY TO BE PROCESSED IN PART
CC       TO PRODUCE THE MATURE ENZYME, AND MAY BE INVOLVED IN TARGETTING
CC       THE PROTEIN WITHIN THE CELL.
CC   -!- SUBCELLULAR LOCATION: LYSOSOMAL.
CC   -!- DEVELOPMENTAL STAGE: PREDOMINANTYL EXPRESSED BY STUMPY FORMS,
CC       WHICH ARE PREADAPTED FOR DIFFERENTIATION INTO PROCYCLIC
CC       TRYPANOSOMES IN THE TSE TSE MIDGUT.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; X16465; G10393; -.
DR   EMBL; X54353; G10391; -.
DR   PIR; S07051; S07051.
DR   PIR; S12099; S12099.
DR   HSSP; P00784; 1PAD.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL; GLYCOPROTEIN; LYSOSOME.
FT   SIGNAL        1     20       PROBABLE.
FT   PROPEP       21    125       ACTIVATION PEPTIDE (PROBABLE).
FT   CHAIN       126    450       CYSTEINE PROTEINASE.
FT   SIMILAR     126    342       TO OTHER THIOL PROTEASES.
FT   DOMAIN      343    450       108-RESIDUE EXTENSION.
FT   DOMAIN      344    352       POLY-PRO.
FT   ACT_SITE    150    150       BY SIMILARITY.
FT   ACT_SITE    287    287       BY SIMILARITY.
FT   ACT_SITE    307    307       BY SIMILARITY.
FT   DISULFID    147    188       BY SIMILARITY.
FT   CARBOHYD    120    120       POTENTIAL.
FT   CARBOHYD    397    397       POTENTIAL.
FT   VARIANT     115    115       L -> V (IN STRAIN WRATAT 1.1).
FT   VARIANT     143    143       V -> D (IN STRAIN WRATAT 1.1).
FT   VARIANT     186    186       S -> F (IN STRAIN WRATAT 1.1).
FT   VARIANT     189    189       N -> G (IN STRAIN WRATAT 1.1).
FT   VARIANT     267    267       E -> T (IN STRAIN WRATAT 1.1).
FT   VARIANT     283    283       K -> E (IN STRAIN WRATAT 1.1).
SQ   SEQUENCE   450 AA;  48451 MW;  90F7C209 CRC32;
     MPRTEMVRFV RLPVVLLAMA ACLASVALGS LHVEESLEMR FAAFKKKYGK VYKDAKEEAF
     RFRAFEENME QAKIQAAANP YATFGVTPFS DMTREEFRAR YRNGASYFAA AQKRLRKTVN
     VTTGRAPAAV DWREKGAVTP VKVQGQCGSC WAFSTIGNIE GQWQVAGNPL VSLSEQMLVS
     CDTIDSGCNG GLMDNAFNWI VNSNGGNVFT EASYPYVSGN GEQPQCQMNG HEIGAAITDH
     VDLPQDEDAI AAYLAENGPL AIAVDAESFM DYNGGILTSC TSKQLDHGVL LVGYNDNSNP
     PYWIIKNSWS NMWGEDGYIR IEKGTNQCLM NQAVSSAVVG GPTPPPPPPP PPSATFTQDF
     CEGKGCTKGC SHATFPTGEC VQTTGVGSVI ATCGASNLTQ IIYPLSRSCS GPSVPITVPL
     DKCIPILIGS VEYHCSTNPP TKAARLVPHQ

SwissProt Database

CYSP_TRYCR

ID   CYSP_TRYCR     STANDARD;      PRT;   467 AA.
AC   P25779;
DT   01-MAY-1992 (REL. 22, CREATED)
DT   01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CRUZIPAIN PRECURSOR (EC 3.4.22.-) (MAJOR CYSTEINE PROTEINASE)
DE   (CRUZAINE).
OS   TRYPANOSOMA CRUZI.
OC   EUKARYOTA; PROTOZOA; SARCOMASTIGOPHORA; MASTIGOPHORA; KINETOPLASTIDA;
OC   TRYPANOSOMATIDAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=TULAHUEN;
RX   MEDLINE; 92218393.
RA   EAKIN A.E., MILLS A.A., HARTH G., MCKERROW J.H., CRAIK C.S.;
RL   J. BIOL. CHEM. 267:7411-7420(1992).
RN   [2]
RP   SEQUENCE FROM N.A. (CLONES 1800-2 AND 1800-4).
RC   STRAIN=TULAHUEN 2;
RX   MEDLINE; 92158002.
RA   CAMPETELLA O., HENRIKSSON J., ASLUND L., FRASCH A.C.C.,
RA   PETTERSSON U., CAZZULO J.J.;
RL   MOL. BIOCHEM. PARASITOL. 50:225-234(1992).
RN   [3]
RP   SEQUENCE OF 141-306 FROM N.A.
RC   STRAIN=RA;
RX   MEDLINE; 90158686.
RA   EAKIN A.E., BOUVIER J., SAKANARI J.A., CRAIK C.S., MCKERROW J.H.;
RL   MOL. BIOCHEM. PARASITOL. 39:1-8(1990).
RN   [4]
RP   SEQUENCE OF 295-467 FROM N.A.
RC   STRAIN=TULAHUEN 2;
RX   MEDLINE; 91246270.
RA   ASLUND L., HENRIKSSON J., CAMPETELLA O., FRASCH A.C.C.,
RA   PETTERSSON U., CAZZULO J.J.;
RL   MOL. BIOCHEM. PARASITOL. 45:345-348(1991).
RN   [5]
RP   AUTOCATALYSIS OF C-TERMINAL.
RC   STRAIN=TULAHUEN 2;
RX   MEDLINE; 91187061.
RA   HELLMAN U., WERNSTEDT C., CAZZULO J.J.;
RL   MOL. BIOCHEM. PARASITOL. 44:15-21(1991).
RN   [6]
RP   SPECIFICITY.
RC   STRAIN=TULAHUEN 2;
RX   MEDLINE; 90167112.
RA   CAZZULO J.J., CAZZULO FRANKE M.C., MARTINEZ J.,
RA   FRANKE DE CAZZULO B.M.;
RL   BIOCHIM. BIOPHYS. ACTA 1037:186-191(1990).
RN   [7]
RP   SEQUENCE OF 123-146 AND 304-317.
RX   MEDLINE; 89219143.
RA   CAZZULO J.J., COUSO R., RAIMONDI A., WERNSTEDT C., HELLMAN U.;
RL   MOL. BIOCHEM. PARASITOL. 33:33-42(1989).
CC   -!- FUNCTION: HYDROLYSES CHROMOGENIC PEPTIDES AT THE CARBOXYL ARG OR
CC       LYS; REQUIRES AT LEAST ONE MORE AMINO ACID, PREFERABLY ARG, PHE,
CC       VAL OR LEU, BETWEEN THE TERMINAL ARG OR LYS AND THE AMINO-BLOCKING
CC       GROUP.
CC   -!- FUNCTION: THE CYSTEINE PROTEASE MAY PLAY AN IMPORTANT ROLE IN THE
CC       DEVELOPMENT AND DIFFERENTIATION OF THE PARASITES AT SEVERAL STAGES
CC       OF THEIR LIFE CYCLE.
CC   -!- ENZYME REGULATION: STRONGLY INHIBITED BY E-64 (L-TRANS-
CC       EPOXYSUCCINYLLEUCYLAMIDO(4-GUANIDINO)BUTANE, LEUPEPTIN, AND
CC       N-ALPHA-P-TOSYL-L-LYSINE CHLOROMETHYL KETONE.
CC   -!- DEVELOPMENTAL STAGE: PRESENT IN ALL DEVELOPMENTAL STAGES.
CC   -!- PURIFIED CRUZIPAIN IS ABLE TO DEGRADE ITSELF, YIELDING A COMPLEX
CC       MIXTURE OF SMALL PEPTIDES, AND A MAJOR 25 KD FRAGMENT.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; M84342; G162048; -.
DR   EMBL; M69121; G162334; -.
DR   EMBL; M69121; G162335; -.
DR   EMBL; X54414; G10606; -.
DR   EMBL; M27305; G162044; -.
DR   PIR; S16162; S16162.
DR   PIR; A60667; A60667.
DR   HSSP; P00785; 1AEC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL; GLYCOPROTEIN;
KW   MULTIGENE FAMILY.
FT   SIGNAL        1     18       PROBABLE.
FT   PROPEP       19    122       ACTIVATION PEPTIDE (PROBABLE).
FT   CHAIN       123    467       CRUZAIN.
FT   ACT_SITE    147    147       BY SIMILARITY.
FT   ACT_SITE    284    284       BY SIMILARITY.
FT   ACT_SITE    304    304       BY SIMILARITY.
FT   DISULFID    144    185       BY SIMILARITY.
FT   SITE        337    338       CLEAVAGE (AUTO-).
FT   CARBOHYD    169    169       POTENTIAL.
FT   CARBOHYD    292    292       POTENTIAL.
FT   CARBOHYD    377    377       POTENTIAL.
FT   VARIANT       9      9       L -> S (IN CLONE 1800-2).
FT   VARIANT      35     35       T -> A (IN CLONE 1800-2).
FT   VARIANT      39     39       A -> V (IN CLONE 1800-2).
FT   VARIANT      51     51       S -> N (IN CLONE 1800-4).
FT   VARIANT      56     56       A -> R (IN CLONE 1800-2).
FT   VARIANT      76     76       N -> G (IN CLONE 1800-4).
FT   VARIANT     109    109       Q -> G (IN CLONE 1800-4).
FT   VARIANT     117    117       K -> N (IN CLONE 1800-2).
FT   VARIANT     146    146       S -> G (IN REF. 7).
FT   VARIANT     157    158       EC -> SG (IN STRAIN RA).
FT   VARIANT     186    186       S -> G (IN CLONES 1800-2 AND 1800-4).
FT   VARIANT     204    204       A -> G (IN STRAIN RA).
FT   VARIANT     250    251       WL -> CV (IN CLONES 1800-2 AND 1800-4).
FT   VARIANT     261    262       VD -> H (IN STRAIN RA).
FT   VARIANT     286    286       V -> F (IN CLONE 1800-4).
FT   VARIANT     286    286       V -> L (IN STRAIN RA).
FT   VARIANT     308    308       T -> A (IN CLONE 1800-2, AND IN
FT                                REF. 4 AND REF. 7).
FT   VARIANT     313    313       E -> D (IN CLONES 1800-2 AND 1800-4 AND
FT                                REF. 7).
FT   VARIANT     357    357       S -> C (IN REF. 4).
FT   VARIANT     409    409       L -> F (IN CLONE 1800-2).
FT   VARIANT     427    427       K -> Q (IN CLONE 1800-2).
FT   VARIANT     430    430       R -> W (IN CLONE 1800-2).
FT   VARIANT     457    457       H -> Y (IN CLONE 1800-2).
FT   VARIANT     461    461       H -> Q (IN CLONE 1800-2).
SQ   SEQUENCE   467 AA;  49836 MW;  6C8D8174 CRC32;
     MSGWARALLL AAVLVVMACL VPAATASLHA EETLTSQFAE FKQKHGRVYE SAAEEAFRLS
     VFRENLFLAR LHAAANPHAT FGVTPFSDLT REEFRSRYHN GAAHFAAAQE RARVPVKVEV
     VGAPAAVDWR ARGAVTAVKD QGQCGSCWAF SAIGNVECQW FLAGHPLTNL SEQMLVSCDK
     TDSGCSGGLM NNAFEWIVQE NNGAVYTEDS YPYASGEGIS PPCTTSGHTV GATITGHVEL
     PQDEAQIAAW LAVNGPVAVA VDASSWMTYT GGVMTSCVSE QLDHGVLLVG YNDSAAVPYW
     IIKNSWTTQW GEEGYIRIAK GSNQCLVKEE ASSAVVGGPG PTPEPTTTTT TSAPGPSPSY
     FVQMSCTDAA CIVGCENVTL PTGQCLLTTS GVSAIVTCGA ETLTEEVFLT STHCSGPSVR
     SSVPLNKCNR LLRGSVEFFC GSSSSGRLAD VDRQRRHQPY HSRHRRL

SwissProt Database

CYSP_SCHJA

ID   CYSP_SCHJA     STANDARD;      PRT;   342 AA.
AC   P43157;
DT   01-NOV-1995 (REL. 32, CREATED)
DT   01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CATHEPSIN B-LIKE CYSTEINE PROTEINASE PRECURSOR (EC 3.4.22.-)
DE   (ANTIGEN SJ31).
GN   CATB.
OS   SCHISTOSOMA JAPONICUM (BLOOD FLUKE).
OC   EUKARYOTA; METAZOA; ACOELOMATES; PLATYHELMINTHES; TREMATODA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=CHINESE MAINLAND;
RX   MEDLINE; 95207690.
RA   MERCKELBACH A., HASSE S., DELL R., ESCHLBECK A., RUPPEL A.;
RL   TROP. MED. PARASITOL. 45:193-198(1994).
CC   -!- FUNCTION: THIOL PROTEASE. HAS A ROLE AS A DIGESTIVE ENZYME.
CC   -!- TISSUE SPECIFICITY: INTESTINE (GUT).
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
CC   -!- SIMILARITY: STRONGEST, TO CATHEPSIN B.
DR   EMBL; X70968; G11167; -.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL; ANTIGEN.
FT   SIGNAL        1     17       POTENTIAL.
FT   PROPEP       18     89       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN        90    342       CATHEPSIN B-LIKE CYSTEINE PROTEINASE.
FT   ACT_SITE    118    118       BY SIMILARITY.
FT   ACT_SITE    288    288       BY SIMILARITY.
FT   ACT_SITE    308    308       BY SIMILARITY.
FT   DISULFID    103    132       BY SIMILARITY.
FT   DISULFID    115    159       BY SIMILARITY.
FT   DISULFID    151    217       BY SIMILARITY.
FT   DISULFID    152    155       BY SIMILARITY.
FT   DISULFID    188    221       BY SIMILARITY.
FT   DISULFID    196    207       BY SIMILARITY.
SQ   SEQUENCE   342 AA;  38796 MW;  3B8F44AB CRC32;
     MLKIAVYIVS LFTFLEAHVT TRNNQRIEPL SDEMISFINE HPDAGWKADK SDRFHSLDDA
     RILMGARKED AEMKRNRRPT VDHHDLNVEI PSQFDSRKKW PHCKSISQIR DQSRCGSCWA
     FGAVEAMTDR ICIQSGGGQS AELSALDLIS CCKDCGDGCQ GGFPGVAWDY WVKRGIVTGG
     SKENHTGCQP YPFPKCEHHT KGKYPACGTK IYKTPQCKQT CQKGYKTPYE QDKHYGDESY
     NVQNNEKVIQ RDIMMYGPVE AAFDVYEDFL NYKSGIYRHV TGSIVGGHAI RIIGWGVEKR
     TPYWLIANSW NEDWGEKGLF RMVRGRDECS IESDVVAGLI KT

SwissProt Database

CYSP_VIGMU

ID   CYSP_VIGMU     STANDARD;      PRT;   362 AA.
AC   P12412;
DT   01-OCT-1989 (REL. 12, CREATED)
DT   01-OCT-1989 (REL. 12, LAST SEQUENCE UPDATE)
DT   01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE)
DE   VIGNAIN PRECURSOR (EC 3.4.22.-) (BEAN ENDOPEPTIDASE) (CYSTEINE
DE   PROTEINASE) (SULFHYDRYL-ENDOPEPTIDASE) (SH-EP).
OS   VIGNA MUNGO (RICE BEAN) (BLACK GRAM).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE; FABALES;
OC   FABACEAE.
RN   [1]
RP   SEQUENCE FROM N.A., AND SEQUENCE OF 132-140.
RC   TISSUE=SEED COTYLEDON;
RX   MEDLINE; 89386007.
RA   AKASOFU H., YAMAUCHI D., MITSUHASHI W., MINAMIKAWA T.;
RL   NUCLEIC ACIDS RES. 17:6733-6733(1989).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   TISSUE=LEAF;
RX   MEDLINE; 90245586.
RA   AKASOFU H., YAMAUCHI D., MINAMIKAWA T.;
RL   NUCLEIC ACIDS RES. 18:1892-1892(1990).
CC   -!- FUNCTION: THOUGHT TO BE INVOLVED IN THE HYDROLYSIS OF STORED
CC       SEED PROTEINS.
CC   -!- CATALYTIC ACTIVITY: HYDROLYSIS OF PROTEINS, SUCH AS AZOCASEIN.
CC       PREFERENTIAL CLEAVAGE: ASN-|-XAA IN SMALL MOLECULE SUBSTRATES
CC       SUCH AS BOC-ASN-|-OPHNO(2).
CC   -!- SUBCELLULAR LOCATION: ENDOPLASMIC RETICULUM LUMEN.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; X15732; G22062; -.
DR   EMBL; X51900; G22066; -.
DR   PIR; S12581; S12581.
DR   HSSP; P00785; 1AEC.
DR   PROSITE; PS00014; ER_TARGET.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; GLYCOPROTEIN; SIGNAL;
KW   ENDOPLASMIC RETICULUM.
FT   SIGNAL        1     20       POTENTIAL.
FT   PROPEP       21    131       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN       132    362       VIGNAIN.
FT   ACT_SITE    152    152       BY SIMILARITY.
FT   ACT_SITE    288    288       BY SIMILARITY.
FT   ACT_SITE    309    309       BY SIMILARITY.
FT   DISULFID    149    191       BY SIMILARITY.
FT   DISULFID    183    224       BY SIMILARITY.
FT   DISULFID    282    334       BY SIMILARITY.
FT   CARBOHYD    326    326       POTENTIAL.
FT   CARBOHYD    346    346       POTENTIAL.
FT   SITE        359    362       PREVENT SECRETION FROM ER.
SQ   SEQUENCE   362 AA;  40222 MW;  ADF86061 CRC32;
     MAMKKLLWVV LSLSLVLGVA NSFDFHEKDL ESEESLWDLY ERWRSHHTVS RSLGEKHKRF
     NVFKANVMHV HNTNKMDKPY KLKLNKFADM TNHEFRSTYA GSKVNHHKMF RGSQHGSGTF
     MYEKVGSVPA SVDWRKKGAV TDVKDQGQCG SCWAFSTIVA VEGINQIKTN KLVSLSEQEL
     VDCDKEENQG CNGGLMESAF EFIKQKGGIT TESNYPYTAQ EGTCDESKVN DLAVSIDGHE
     NVPVNDENAL LKAVANQPVS VAIDAGGSDF QFYSEGVFTG DCNTDLNHGV AIVGYGTTVD
     GTNYWIVRNS WGPEWGEQGY IRMQRNISKK EGLCGIAMMA SYPIKNSSDN PTGSLSSPKD
     EL

SwissProt Database

EUM1_EURMA

ID   EUM1_EURMA     STANDARD;      PRT;   211 AA.
AC   P25780;
DT   01-MAY-1992 (REL. 22, CREATED)
DT   01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   MITE GROUP I ALLERGEN EUR M I (EC 3.4.22.-) (FRAGMENT).
GN   EURM1.
OS   EUROGLYPHUS MAYNEI (HOUSE-DUST MITE).
OC   EUKARYOTA; METAZOA; ARTHROPODA; CHELICERATA; ARACHNIDA; ACARI.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 93130112.
RA   KENT N.A., HILL M.R., KEEN J.N., HOLLAND P.W., HART B.J.;
RL   INT. ARCH. ALLERGY IMMUNOL. 99:150-152(1992).
CC   -!- FUNCTION: THIS PROTEIN IS AN ALLERGEN, IT IS MOST PROBABLY A THIOL
CC       PROTEASE.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; X60073; E37871; -.
DR   PIR; S21864; S21864.
DR   HSSP; P07858; 1HUC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; GLYCOPROTEIN; ALLERGEN.
FT   NON_TER       1      1
FT   ACT_SITE     35     35       BY SIMILARITY.
FT   ACT_SITE    171    171       BY SIMILARITY.
FT   ACT_SITE    191    191       BY SIMILARITY.
FT   DISULFID     32     72       BY SIMILARITY.
FT   CARBOHYD     53     53       POTENTIAL.
FT   NON_TER     211    211
SQ   SEQUENCE   211 AA;  23630 MW;  DADEE27B CRC32;
     TYACSINSVS LPSELDLRSL RTVTPIRMQG GCGSCWAFSG VASTESAYLA YRNMSLDLAE
     QELVDCASQN GCHGDTIPRG IEYIQQNGVV QEHYYPYVAR EQSCHRPNAQ RYGLKNYCQI
     SPPDSNKIRQ ALTQTHTAVA VIIGIKDLNA FRHYDGRTIM QHDNGYQPNY HAVNIVGYGN
     TQGVDYWIVR NSWDTTWGDN GYGYFAANIN L

SwissProt Database

LCPA_LEIME

ID   LCPA_LEIME     STANDARD;      PRT;   354 AA.
AC   P25775;
DT   01-MAY-1992 (REL. 22, CREATED)
DT   01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE A PRECURSOR (EC 3.4.22.-).
GN   LMCPA.
OS   LEISHMANIA MEXICANA.
OC   EUKARYOTA; PROTOZOA; SARCOMASTIGOPHORA; MASTIGOPHORA; KINETOPLASTIDA;
OC   TRYPANOSOMATIDAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=ISOLATE MNYC/BZ/62/M379;
RX   MEDLINE; 92374843.
RA   MOTTRAM J.C., ROBERTSON C.D., COOMBS G.H., BARRY J.D.;
RL   MOL. MICROBIOL. 6:1925-1932(1992).
CC   -!- DEVELOPMENTAL STAGE: EXPRESSED IN ALL LIFE-CYCLE STAGES BUT AT
CC       HIGHER LEVELS IN THE AMASTIGOTE STAGE IN THE MAMMAL AND IN
CC       STATIONARY PHASE PROMASTIGOTE CULTURES WHICH CONTAIN THE INFECTIVE
CC       METACYCLIC FORM OF THE PARASITE.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; X62163; G9573; -.
DR   PIR; S16856; S16856.
DR   PIR; S25267; S25267.
DR   HSSP; P00784; 1PAD.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL; GLYCOPROTEIN.
FT   SIGNAL        1      ?
FT   PROPEP        ?    125       ACTIVATION PEPTIDE (PROBABLE).
FT   CHAIN       126    354       CYSTEINE PROTEINASE A.
FT   ACT_SITE    153    153       BY SIMILARITY.
FT   ACT_SITE    289    289       BY SIMILARITY.
FT   ACT_SITE    309    309       BY SIMILARITY.
FT   DISULFID    150    191       BY SIMILARITY.
FT   DISULFID    184    229       BY SIMILARITY.
FT   DISULFID    282    330       BY SIMILARITY.
FT   CARBOHYD    208    208       POTENTIAL.
SQ   SEQUENCE   354 AA;  38745 MW;  9928219C CRC32;
     MARRNPLLFA IVVTILFVVC YGSALIAQTP PPVDNFVASA HYGSFKKRHG KAFGGDAEEG
     HRFNAFKQNM QTAYFLNTQN PHAHYDVSGK FADLTPQEFA KLYLNPDYYA RHLKNHKEDV
     HVDDSAPSGV MSVDWRDKGA VTPVKNQGLC GSCWAFSAIG NIEGQWAASG HSLVSLSEQM
     LVSCDNIDEG CNGGLMDQAM NWIMQSHNGS VFTEASYPYT SGGGTRPPCH DEGEVGAKIT
     GFLSLPHDEE RIAEWVEKRG PVAVAVDATT WQLYFGGVVS LCLAWSLNHG VLIVGFNKNA
     KPPYWIVKNS WGSSWGEKGY IRLAMGSNQC MLKNYPVSAT VESPHTPHVP TTTA

SwissProt Database

LCPB_LEIME

ID   LCPB_LEIME     STANDARD;      PRT;   443 AA.
AC   P36400;
DT   01-JUN-1994 (REL. 29, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE B PRECURSOR (EC 3.4.22.-).
GN   LMCPB.
OS   LEISHMANIA MEXICANA.
OC   EUKARYOTA; PROTOZOA; SARCOMASTIGOPHORA; MASTIGOPHORA; KINETOPLASTIDA;
OC   TRYPANOSOMATIDAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=ISOLATE MNYC/BZ/62/M379;
RX   MEDLINE; 93011959.
RA   SOUZA A.E., WAUGH S., COOMBS G.H., MOTTRAM J.C.;
RL   FEBS LETT. 311:124-127(1992).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   STRAIN=ISOLATE MNYC/BZ/62/M379;
RA   MOTTRAM J.C., SOUZA A.E., HUTCHISON J.E., FRAME M.J., COOMBS G.H.;
RL   SUBMITTED (JUN-1995) TO EMBL/GENBANK/DDBJ DATA BANKS.
CC   -!- DEVELOPMENTAL STAGE: PRIMARILY EXPRESSED IN AMASTIGOTES.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; Z14061; G9542; -.
DR   EMBL; Z49962; G899313; -.
DR   PIR; S25003; S25003.
DR   PIR; S29245; S29245.
DR   HSSP; P24821; 1HRE.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL; GLYCOPROTEIN.
FT   SIGNAL        1      ?
FT   PROPEP        ?    125       ACTIVATION PEPTIDE (PROBABLE).
FT   CHAIN       126    443       CYSTEINE PROTEINASE B.
FT   ACT_SITE    150    150       BY SIMILARITY.
FT   ACT_SITE    288    288       BY SIMILARITY.
FT   ACT_SITE    308    308       BY SIMILARITY.
FT   DISULFID    147    188       BY SIMILARITY.
FT   DISULFID    181    226       BY SIMILARITY.
FT   DISULFID    281    329       BY SIMILARITY.
FT   CARBOHYD    228    228       POTENTIAL.
FT   CONFLICT    185    186       ND -> DN (IN REF. 1).
FT   CONFLICT    189    189       D -> S (IN REF. 1).
FT   CONFLICT    361    361       M -> V (IN REF. 1).
FT   CONFLICT    373    374       TQ -> RR (IN REF. 1).
FT   CONFLICT    424    424       P -> H (IN REF. 1).
FT   CONFLICT    429    429       A -> S (IN REF. 1).
FT   CONFLICT    433    433       L -> F (IN REF. 1).
SQ   SEQUENCE   443 AA;  47728 MW;  FC446AF4 CRC32;
     MATSRAALCA VAVVCVVLAA ACAPARAIHV GTPAAALFEE FKRTYGRAYE TLAEEQQRLA
     NFERNLELMR EHQARNPHAQ FGITKFFDLS EAEFAARYLN GAAYFAAAKR HAAQHYRKAR
     ADLSAVPDAV DWREKGAVTP VKDQGACGSC WAFSAVGNIE GQWYLAGHEL VSLSEQQLVS
     CDDMNDGCDG GLMLQAFDWL LQNTNGHLHT EDSYPYVSGN GYVPECSNSS ELVVGAQIDG
     HVLIGSSEKA MAAWLAKNGP IAIALDASSF MSYKSGVLTA CIGKQLNHGV LLVGYDMTGE
     VPYWVIKNSW GGDWGEQGYV RVVMGVNACL LSEYPVSAHV RESAAPGTST SSETPAPRPV
     MVEQVICFDK NCTQGCRKTL IKANECHKNG GGGASMIKCS PQKVTMCTYS NEFCVGGGLC
     FETPDGKCAP YFLGSIMNTC HYT

SwissProt Database

MMAL_DERFA

ID   MMAL_DERFA     STANDARD;      PRT;   321 AA.
AC   P16311;
DT   01-AUG-1990 (REL. 15, CREATED)
DT   01-FEB-1995 (REL. 31, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   MAJOR MITE FECAL ALLERGEN DER F I PRECURSOR (EC 3.4.22.-).
GN   DERF1.
OS   DERMATOPHAGOIDES FARINAE (HOUSE-DUST MITE).
OC   EUKARYOTA; METAZOA; ARTHROPODA; CHELICERATA; ARACHNIDA; ACARI.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 91215493.
RA   DILWORTH R.J., CHUA K.Y., THOMAS W.R.;
RL   CLIN. EXP. ALLERGY 21:25-32(1991).
RN   [2]
RP   SEQUENCE OF 98-309 FROM N.A.
RA   KENT N., HILL M.R., KEEN J.N., HOLLAND P.W., HART B.J.;
RL   SUBMITTED (MAR-1992) TO EMBL/GENBANK/DDBJ DATA BANKS.
RN   [3]
RP   SEQUENCE OF 99-128.
RX   MEDLINE; 88229138.
RA   LIND P., HANSEN O.C., HORN N.;
RL   J. IMMUNOL. 140:4256-4262(1988).
CC   -!- FUNCTION: THIS PROTEIN IS THE MAJOR ALLERGEN OF HOUSE DUST MITE,
CC       IT IS A THIOL PROTEASE THAT HYDROLYSES PROTEINS, WITH A PREFERENCE
CC       FOR PHE OR BASIC RESIDUES.
CC   -!- SUBCELLULAR LOCATION: SECRETED.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; X65196; G7413; -.
DR   PIR; A27634; A27634.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ALLERGEN; GLYCOPROTEIN; ZYMOGEN; SIGNAL.
FT   SIGNAL        1     18       POTENTIAL.
FT   PROPEP       19     98       ACTIVATION PEPTIDE.
FT   CHAIN        99    321       MAJOR MITE FECAL ALLERGEN DER F I.
FT   ACT_SITE    133    133       BY SIMILARITY.
FT   ACT_SITE    269    269       BY SIMILARITY.
FT   ACT_SITE    288    288       BY SIMILARITY.
FT   CARBOHYD    151    151       POTENTIAL.
FT   DISULFID    102    216       BY SIMILARITY.
FT   DISULFID    130    170       BY SIMILARITY.
FT   DISULFID    164    202       BY SIMILARITY.
FT   CONFLICT    201    201       R -> Q (IN REF. 2).
FT   CONFLICT    282    282       D -> V (IN REF. 2).
SQ   SEQUENCE   321 AA;  36435 MW;  4A126DFC CRC32;
     MKFVLAIASL LVLSTVYARP ASIKTFEEFK KAFNKNYATV EEEEVARKNF LESLKYVEAN
     KGAINHLSDL SLDEFKNRYL MSAEAFEQLK TQFDLNAETS ACRINSVNVP SELDLRSLRT
     VTPIRMQGGC GSCWAFSGVA ATESAYLAYR NTSLDLSEQE LVDCASQHGC HGDTIPRGIE
     YIQQNGVVEE RSYPYVAREQ RCRRPNSQHY GISNYCQIYP PDVKQIREAL TQTHTAIAVI
     IGIKDLRAFQ HYDGRTIIQH DNGYQPNYHA VNIVGYGSTQ GDDYWIVRNS WDTTWGDSGY
     GYFQAGNNLM MIEQYPYVVI M

SwissProt Database

MMAL_DERPT

ID   MMAL_DERPT     STANDARD;      PRT;   320 AA.
AC   P08176;
DT   01-AUG-1988 (REL. 08, CREATED)
DT   01-FEB-1995 (REL. 31, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   MAJOR MITE FECAL ALLERGEN DER P I PRECURSOR (EC 3.4.22.-).
GN   DERP1.
OS   DERMATOPHAGOIDES PTERONYSSINUS (HOUSE-DUST MITE).
OC   EUKARYOTA; METAZOA; ARTHROPODA; CHELICERATA; ARACHNIDA; ACARI.
RN   [1]
RP   SEQUENCE FROM N.A., AND POLYMORPHISM.
RX   MEDLINE; 93357682.
RA   CHUA K.Y., KEHAL P.K., THOMAS W.R.;
RL   INT. ARCH. ALLERGY IMMUNOL. 101:364-368(1993).
RN   [2]
RP   SEQUENCE OF 76-320 FROM N.A.
RX   MEDLINE; 88089411.
RA   CHUA K.Y., STEWART G.A., THOMAS W.R., SIMPSON R.J., DILWORTH R.J.,
RA   PLOZZA T.M., TURNER K.J.;
RL   J. EXP. MED. 167:175-182(1988).
RN   [3]
RP   SEQUENCE OF 81-176 FROM N.A.
RX   MEDLINE; 88114080.
RA   THOMAS W.R., STEWART G.A., SIMPSON R.J., CHUA K.Y., PLOZZA T.M.,
RA   DILWORTH R.J., NISBET A., TURNER K.J.;
RL   INT. ARCH. ALLERGY APPL. IMMUNOL. 85:127-129(1988).
RN   [4]
RP   SEQUENCE OF 99-127.
RX   MEDLINE; 88229138.
RA   LIND P., HANSEN O.C., HORN N.;
RL   J. IMMUNOL. 140:4256-4262(1988).
RN   [5]
RP   REVISIONS TO 232-241.
RX   MEDLINE; 91215493.
RA   DILWORTH R.J., CHUA K.Y., THOMAS W.R.;
RL   CLIN. EXP. ALLERGY 21:25-32(1991).
RN   [6]
RP   3D-STRUCTURE MODELLING.
RX   MEDLINE; 95062135.
RA   TOPHAM C.M., SRINIVASAN N., THORPE C.J., OVERINGTON J.P.,
RA   KALSHEKER N.A.;
RL   PROTEIN ENG. 7:869-894(1994).
CC   -!- FUNCTION: THIS PROTEIN IS THE MAJOR ALLERGEN OF HOUSE DUST MITE,
CC       IT IS A THIOL PROTEASE THAT HYDROLYSES PROTEINS, WITH A PREFERENCE
CC       FOR PHE OR BASIC RESIDUES.
CC   -!- SUBCELLULAR LOCATION: SECRETED.
CC   -!- DISEASE: REACTS WITH IGE IN 80% OF PATIENTS WITH HOUSE DUST
CC       ALLERGY.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; U11695; G511953; -.
DR   EMBL; M24794; G387592; ALT_INIT.
DR   PIR; C27634; C27634.
DR   PIR; A27582; A27582.
DR   PIR; JQ0337; JQ0337.
DR   HSSP; P07858; 1HUC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; GLYCOPROTEIN; ALLERGEN; SIGNAL;
KW   POLYMORPHISM.
FT   SIGNAL        1     18       POTENTIAL.
FT   PROPEP       19     98       ACTIVATION PEPTIDE.
FT   CHAIN        99    320       MAJOR MITE FECAL ALLERGEN DER P I.
FT   CARBOHYD    150    150       POTENTIAL.
FT   ACT_SITE    132    132       BY SIMILARITY.
FT   ACT_SITE    268    268       BY SIMILARITY.
FT   ACT_SITE    288    288       BY SIMILARITY.
FT   DISULFID    102    215       BY SIMILARITY.
FT   DISULFID    129    169       BY SIMILARITY.
FT   DISULFID    163    201       BY SIMILARITY.
FT   VARIANT     148    148       Y -> H.
FT   VARIANT     179    179       E -> K.
FT   VARIANT     222    222       V -> A.
FT   VARIANT     234    234       S -> T.
FT   VARIANT     313    313       E -> Q.
SQ   SEQUENCE   320 AA;  36104 MW;  8A18F95B CRC32;
     MKIVLAIASL LALSAVYARP SSIKTFEEYK KAFNKSYATF EDEEAARKNF LESVKYVQSN
     GGAINHLSDL SLDEFKNRFL MSAEAFEHLK TQFDLNAETN ACSINGNAPA EIDLRQMRTV
     TPIRMQGGCG SCWAFSGVAA TESAYLAYRN QSLDLAEQEL VDCASQHGCH GDTIPRGIEY
     IQHNGVVQES YYRYVAREQS CRRPNAQRFG ISNYCQIYPP NVNKIREALA QTHSAIAVII
     GIKDLDAFRH YDGRTIIQRD NGYQPNYHAV NIVGYSNAQG VDYWIVRNSW DTNWGDNGYG
     YFAANIDLMM IEEYPYVVIL

SwissProt Database

ORYA_ORYSA

ID   ORYA_ORYSA     STANDARD;      PRT;   458 AA.
AC   P25776;
DT   01-MAY-1992 (REL. 22, CREATED)
DT   01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   ORYZAIN ALPHA CHAIN PRECURSOR (EC 3.4.22.-).
OS   ORYZA SATIVA (RICE).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; MONOCOTYLEDONEAE;
OC   CYPERALES; GRAMINEAE.
RN   [1]
RP   SEQUENCE FROM N.A., AND SEQUENCE OF 129-135.
RC   STRAIN=CV. NIPPONBARE; TISSUE=SEED;
RX   MEDLINE; 91358494.
RA   WATANABE H., ABE K., EMORI Y., HOSOYAMA H., ARAI S.;
RL   J. BIOL. CHEM. 266:16897-16902(1991).
CC   -!- TISSUE SPECIFICITY: EXPRESSED ONLY IN SEEDS.
CC   -!- INDUCTION: STIMULATED BY GIBBERELLIC ACID.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; D90406; G218181; -.
DR   PIR; JU0388; KHRZOA.
DR   HSSP; P00785; 1AEC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; GLYCOPROTEIN; SIGNAL.
FT   SIGNAL        1     21       POTENTIAL.
FT   PROPEP       22    128       ACTIVATION PEPTIDE.
FT   CHAIN       129    458       ORYZAIN ALPHA CHAIN.
FT   ACT_SITE    153    153       BY SIMILARITY.
FT   ACT_SITE    289    289       BY SIMILARITY.
FT   ACT_SITE    309    309       BY SIMILARITY.
FT   DISULFID    150    192       BY SIMILARITY.
FT   DISULFID    184    225       BY SIMILARITY.
FT   DISULFID    283    334       BY SIMILARITY.
FT   CARBOHYD    445    445       POTENTIAL.
SQ   SEQUENCE   458 AA;  50274 MW;  2BE4B420 CRC32;
     MRISMALAAA ALLLLLSLAA ADMSIVSYGE RSEEEARRLY AEWKAEHGKS YNAVGEEERR
     YAAFRDNLRY IDEHNAAADA GVHSFRLGLN RFADLTNEEY RDTYLGLRNK PRRERKVSDR
     YLAADNEALP ESVDWRTKGA VAEIKDQGGC GSCWAFSAIA AVEDINQIVT GDLISLSEQE
     LVDCDTSYNE GCNGGLMDYA FDFIINNGGI DTEDDYPYKG KDERCDVNRK NAKVVTIDSY
     EDVTPNSETS LQKAVRNQPV SVAIEAGGRA FQLYSSGIFT GKCGTALDHG VAAVGYGTEN
     GKDYWIVRNS WGKSWGESGY VRMERNIKAS SGKCGIAVEP SYPLKKGENP PNPGPTPPSP
     TPPPTVCDNY YTCPDSTTCC CIYEYGKYCY AWGCCPLEGA TCCDDHYSCC PHEYPICNVQ
     QGTCLMAKDS PLAVKALKRT LAKPNLSFLF GNGKKSSA

SwissProt Database

ORYB_ORYSA

ID   ORYB_ORYSA     STANDARD;      PRT;   471 AA.
AC   P25777;
DT   01-MAY-1992 (REL. 22, CREATED)
DT   01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   ORYZAIN BETA CHAIN PRECURSOR (EC 3.4.22.-).
OS   ORYZA SATIVA (RICE).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; MONOCOTYLEDONEAE;
OC   CYPERALES; GRAMINEAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=CV. NIPPONBARE; TISSUE=SEED;
RX   MEDLINE; 91358494.
RA   WATANABE H., ABE K., EMORI Y., HOSOYAMA H., ARAI S.;
RL   J. BIOL. CHEM. 266:16897-16902(1991).
CC   -!- TISSUE SPECIFICITY: EXPRESSED ONLY IN SEEDS.
CC   -!- INDUCTION: STIMULATED BY GIBBERELLIC ACID.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; D90407; G218183; -.
DR   PIR; JU0389; KHRZOB.
DR   HSSP; P00785; 1AEC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; GLYCOPROTEIN; SIGNAL.
FT   SIGNAL        1     21       POTENTIAL.
FT   PROPEP       22    139       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN       140    471       ORYZAIN BETA CHAIN.
FT   ACT_SITE    164    164       BY SIMILARITY.
FT   ACT_SITE    301    301       BY SIMILARITY.
FT   ACT_SITE    321    321       BY SIMILARITY.
FT   DISULFID    161    204       BY SIMILARITY.
FT   DISULFID    195    237       BY SIMILARITY.
FT   DISULFID    295    346       BY SIMILARITY.
FT   CARBOHYD    340    340       POTENTIAL.
FT   CARBOHYD    388    388       POTENTIAL.
SQ   SEQUENCE   471 AA;  50505 MW;  C47EA20B CRC32;
     MAARAAAAAF LLLLIVVGHR ASDMSIISYN AEHGARGLEE GPTEAEARAA YDLWLAENGG
     GSPNALGGEH ERRFLVFWDN LKFVDAHNAR ADEGGGFRLG MNRFADLTNE EFRATFLGAK
     VAERSRAAGE RYRHDGVEEL PESVDWREKG AVAPVKNQGQ CGSCWAFSAV STVESINQLV
     TGEMITLSEQ ELVECSTNGQ NSGCNGGLMA DAFDFIIKNG GIDTEDDYPY KAVDGKCDIN
     RENAKVVSID GFEDVPQNDE KSLQKAVAHQ PVSVAIEAGG REFQLYHSGV FSGRCGTSLD
     HGVVAVGYGT DNGKDYWIVR NSWGPKWGES GYVRMERNIN VTTGKCGIAM MASYPTKSGA
     NPPKPSPTPP TPPTPPPPSA PDHVCDDNFS CPAGSTCCCA FGFRNLCLVW GCCPVEGATC
     CKDHASCCPP DYPVCNTRAG TCSASKNSPL SVKALKRTLA KLNTHELIDN M

SwissProt Database

ORYC_ORYSA

ID   ORYC_ORYSA     STANDARD;      PRT;   362 AA.
AC   P25778;
DT   01-MAY-1992 (REL. 22, CREATED)
DT   01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   ORYZAIN GAMMA CHAIN PRECURSOR (EC 3.4.22.-).
OS   ORYZA SATIVA (RICE).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; MONOCOTYLEDONEAE;
OC   CYPERALES; GRAMINEAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=CV. NIPPONBARE; TISSUE=SEED;
RX   MEDLINE; 91358494.
RA   WATANABE H., ABE K., EMORI Y., HOSOYAMA H., ARAI S.;
RL   J. BIOL. CHEM. 266:16897-16902(1991).
CC   -!- TISSUE SPECIFICITY: EXPRESSED ONLY IN SEEDS.
CC   -!- INDUCTION: STIMULATED BY GIBBERELLIC ACID.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
CC   -!- SIMILARITY: STRONGEST, TO ALEURAIN AND CATHEPSIN H.
DR   EMBL; D90408; G218185; -.
DR   PIR; JU0390; KHRZOG.
DR   HSSP; P00785; 1AEC.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; GLYCOPROTEIN; SIGNAL.
FT   SIGNAL        1     24       POTENTIAL.
FT   PROPEP       25    144       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN       145    362       ORYZAIN GAMMA CHAIN.
FT   ACT_SITE    169    169       BY SIMILARITY.
FT   ACT_SITE    309    309       BY SIMILARITY.
FT   ACT_SITE    329    329       BY SIMILARITY.
FT   DISULFID    166    209       BY SIMILARITY.
FT   DISULFID    200    242       BY SIMILARITY.
FT   DISULFID    300    350       BY SIMILARITY.
FT   CARBOHYD    128    128       POTENTIAL.
FT   CARBOHYD    258    258       POTENTIAL.
SQ   SEQUENCE   362 AA;  39204 MW;  A80DA3B6 CRC32;
     MAHRRIILLL AVAAVAATSA VAAASSGFDD SNPIRSVTDH AASALESTVI AALGRTRGAL
     RFARFAVRHG KRYGDAAEVQ RRFRIFSESL ELVRSTNRRG LPYRLGINRF ADMSWEEFQA
     SRLGAAQNCS ATLAGNHRMR DAPALPETKD WREDGIVSPV KDQGHCGSCW PFSTTGSLEA
     RYTQATGPPV SLSEQQLADC ATRYNNFGCS GGLPSQAFEY IKYNGGLDTE EAYPYTGVNG
     ICHYKPENAG VKVLDSVNIT LVAEDELKNA VGLVRPVSVA FQVINGFRMY KSGVYTSDHC
     GTSPMDVNHA VLAVGYGVEN GVPYWLIKNS WGADWGDNGY FTMEMGKNMC GIATCASYPI
     VA

SwissProt Database

P34_SOYBN

ID   P34_SOYBN      STANDARD;      PRT;   379 AA.
AC   P22895;
DT   01-AUG-1991 (REL. 19, CREATED)
DT   01-AUG-1991 (REL. 19, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   P34 PROBABLE THIOL PROTEASE PRECURSOR (EC 3.4.22.-).
OS   GLYCINE MAX (SOYBEAN).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE; FABALES;
OC   FABACEAE.
RN   [1]
RP   SEQUENCE FROM N.A., AND SEQUENCE OF 123-147.
RC   STRAIN=CV. CENTURY; TISSUE=SEED;
RX   MEDLINE; 90338001.
RA   KALINSKI A., WEISEMANN J.M., MATTHEWS B.F., HERMAN E.M.;
RL   J. BIOL. CHEM. 265:13843-13848(1990).
RN   [2]
RP   PROCESSING, AND SUBCELLULAR LOCATION.
RX   MEDLINE; 92291086.
RA   KALINSKI A., MELROY D.L., DWIVEDI R.S., HERMAN E.M.;
RL   J. BIOL. CHEM. 267:12068-12076(1992).
CC   -!- FUNCTION: PROBABLE THIOL PROTEASE.
CC   -!- SUBCELLULAR LOCATION: PROTEIN STORAGE VACUOLES OF SEEDS.
CC       THIS PROTEIN WAS WRONGLY THOUGHT TO BE ASSOCIATED WITH SEED OIL
CC       BODIES.
CC   -!- SUBUNIT: HOMODIMER, DISULFIDE-LINKED (PROBABLE).
CC   -!- PTM: N-GLYCOSYLATED ON ITS PROPEPTIDE.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; J05560; G1199563; ALT_SEQ.
DR   PIR; A37126; KHSYO4.
DR   HSSP; P10056; 1PPO.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; LYSOSOME; ZYMOGEN; SIGNAL; GLYCOPROTEIN.
FT   SIGNAL        1     23       POTENTIAL.
FT   PROPEP       24    122       ACTIVATION PEPTIDE.
FT   CHAIN       123    379       P34 PROBABLE THIOL PROTEASE.
FT   SITE        200    200       ANCESTRAL ACTIVE SITE.
FT   ACT_SITE    301    301       BY SIMILARITY.
FT   ACT_SITE    321    321       BY SIMILARITY.
FT   DISULFID    190    230       BY SIMILARITY.
FT   DISULFID    293    346       BY SIMILARITY.
FT   CARBOHYD     70     70       PROBABLE.
FT   CARBOHYD    292    292       POTENTIAL.
SQ   SEQUENCE   379 AA;  42794 MW;  0ACD761D CRC32;
     MGFLVLLLFS LLGLSSSSSI STHRSILDLD LTKFTTQKQV SSLFQLWKSE HGRVYHNHEE
     EAKRLEIFKN NSNYIRDMNA NRKSPHSHRL GLNKFADITP QEFSKKYLQA PKDVSQQIKM
     ANKKMKKEQY SCDHPPASWD WRKKGVITQV KYQGGCGRGW AFSATGAIEA AHAIATGDLV
     SLSEQELVDC VEESEGSYNG WQYQSFEWVL EHGGIATDDD YPYRAKEGRC KANKIQDKVT
     IDGYETLIMS DESTESETEQ AFLSAILEQP ISVSIDAKDF HLYTGGIYDG ENCTSPYGIN
     HFVLLVGYGS ADGVDYWIAK NSWGFDWGED GYIWIQRNTG NLLGVCGMNY FASYPTKEES
     ETLVSARVKG HRRVDHSPL

SwissProt Database

PAP2_CARPA

ID   PAP2_CARPA     STANDARD;      PRT;   218 AA.
AC   P14080;
DT   01-JAN-1990 (REL. 13, CREATED)
DT   01-JAN-1990 (REL. 13, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CHYMOPAPAIN (EC 3.4.22.6) (PAPAYA PROTEINASE II) (PPII).
OS   CARICA PAPAYA (PAPAYA).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE;
OC   VIOLALES; CARICACEAE.
RN   [1]
RP   SEQUENCE.
RX   MEDLINE; 90179730.
RA   WATSON D.C., YAGUCHI M., LYNN K.R.;
RL   BIOCHEM. J. 266:75-81(1990).
RN   [2]
RP   SEQUENCE.
RX   MEDLINE; 89302685.
RA   JACQUET A., KLEINSCHMIDT T., SCHNEK A.G., LOOZE Y., BRAUNITZER G.;
RL   BIOL. CHEM. HOPPE-SEYLER 370:425-434(1989).
CC   -!- CATALYTIC ACTIVITY: SPECIFICITY CLOSE BUT NOT IDENTICAL TO THAT OF
CC       PAPAIN.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   PIR; S04222; S04222.
DR   PIR; S08285; S08285.
DR   HSSP; P10056; 1PPO.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE.
FT   ACT_SITE     25     25
FT   ACT_SITE    159    159
FT   ACT_SITE    179    179
FT   DISULFID     22     63
FT   DISULFID     56     95
FT   DISULFID    153    204
SQ   SEQUENCE   218 AA;  23657 MW;  5B1A4A7A CRC32;
     YPQSIDWRAK GAVTPVKNQG ACGSCWAFST IATVEGINKI VTGNLLELSE QELVDCDKHS
     YGCKGGYQTT SLQYVANNGV HTSKVYPYQA KQYKCRATDK PGPKVKITGY KRVPSNCETS
     FLGALANQPL SVLVEAGGKP FQLYKSGVFD GPCGTKLDHA VTAVGYGTSD GKNYIIIKNS
     WGPNWGEKGY MRLKRQSGNS QGTCGVYKSS YYPFKGFA

SwissProt Database

PAP3_CARPA

ID   PAP3_CARPA     STANDARD;      PRT;   348 AA.
AC   P10056;
DT   01-MAR-1989 (REL. 10, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   CARICAIN PRECURSOR (EC 3.4.22.30) (PAPAYA PROTEINASE OMEGA) (PAPAYA
DE   PROTEINASE III) (PPIII) (PAPAYA PEPTIDASE A).
OS   CARICA PAPAYA (PAPAYA).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE;
OC   VIOLALES; CARICACEAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=LEAF;
RA   BAKER K.C., REVELL D.F., CUMMINGS N.J., COLLINS M.E., GOODENOUGH P.W.;
RL   SUBMITTED (MAY-1995) TO EMBL/GENBANK/DDBJ DATA BANKS.
RN   [2]
RP   SEQUENCE OF 133-348.
RX   MEDLINE; 89105320.
RA   DUBOIS T., KLEINSCHMIDT T., SCHNEK A.G., LOOZE Y., BRAUNITZER G.;
RL   BIOL. CHEM. HOPPE-SEYLER 369:741-754(1988).
RN   [3]
RP   SEQUENCE OF 237-348 FROM N.A.
RC   TISSUE=LEAF;
RA   COLLINS M.E., REVELL D.F., SUMNER I.G., PICKERSGILL R.W.,
RA   GOODENOUGH P.W.;
RL   SUBMITTED (FEB-1990) TO EMBL/GENBANK/DDBJ DATA BANKS.
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RA   PICKERSGILL R.W., RIZKALLAH P., HARRIS G.W., GOODENOUGH P.W.;
RL   ACTA CRYSTALLOGR. B 47:766-771(1991).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT GLU-290.
RX   MEDLINE; 96354872.
RA   KATERELOS N.A., TAYLOR M.A.J., SCOTT M., GOODENOUGH P.W.,
RA   PICKERSGILL R.W.;
RL   FEBS LETT. 392:35-39(1996).
CC   -!- CATALYTIC ACTIVITY: HYDROLYSIS OF PROTEINS WITH BROAD SPECIFICITY
CC       FOR PEPTIDE BONDS, SIMILAR TO THOSE OF PAPAIN AND CHYMOPAPAIN.
CC   -!- SUBUNIT: MONOMER.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; X66060; G18098; -.
DR   EMBL; X51899; E25522; -.
DR   PIR; S01135; S01135.
DR   PIR; S11748; S11748.
DR   PDB; 1PPO; 31-JAN-94.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL; 3D-STRUCTURE.
FT   SIGNAL        1     18       POTENTIAL.
FT   PROPEP       19    132       ACTIVATION PEPTIDE.
FT   CHAIN       133    348       CARICAIN.
FT   ACT_SITE    157    157
FT   ACT_SITE    291    291
FT   ACT_SITE    311    311
FT   DISULFID    154    195
FT   DISULFID    188    227
FT   DISULFID    285    336
FT   STRAND      137    138
FT   TURN        139    143
FT   STRAND      150    150
FT   STRAND      155    155
FT   HELIX       157    174
FT   STRAND      180    180
FT   HELIX       182    188
FT   TURN        194    195
FT   STRAND      196    196
FT   HELIX       200    210
FT   STRAND      212    212
FT   STRAND      214    214
FT   TURN        215    217
FT   HELIX       229    231
FT   STRAND      237    237
FT   STRAND      241    244
FT   HELIX       250    259
FT   STRAND      262    266
FT   HELIX       271    275
FT   STRAND      280    281
FT   STRAND      291    301
FT   TURN        302    303
FT   STRAND      304    310
FT   STRAND      313    313
FT   TURN        318    318
FT   STRAND      319    319
FT   TURN        320    321
FT   STRAND      322    326
FT   HELIX       335    337
FT   TURN        338    339
FT   STRAND      343    346
SQ   SEQUENCE   348 AA;  38788 MW;  7DD70EAF CRC32;
     MAMIPSISKL LFVAICLFVH MSVSFGDFSI VGYSQDDLTS TERLIQLFNS WMLNHNKFYE
     NVDEKLYRFE IFKDNLNYID ETNKKNNSYW LGLNEFADLS NDEFNEKYVG SLIDATIEQS
     YDEEFINEDT VNLPENVDWR KKGAVTPVRH QGSCGSCWAF SAVATVEGIN KIRTGKLVEL
     SEQELVDCER RSHGCKGGYP PYALEYVAKN GIHLRSKYPY KAKQGTCRAK QVGGPIVKTS
     GVGRVQPNNE GNLLNAIAKQ PVSVVVESKG RPFQLYKGGI FEGPCGTKVD HAVTAVGYGK
     SGGKGYILIK NSWGTAWGEK GYIRIKRAPG NSPGVCGLYK SSYYPTKN

SwissProt Database

PAP4_CARPA

ID   PAP4_CARPA     STANDARD;      PRT;   348 AA.
AC   P05994;
DT   01-NOV-1988 (REL. 09, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   PAPAYA PROTEINASE IV PRECURSOR (EC 3.4.22.25) (PPIV) (PAPAYA PEPTIDASE
DE   B) (GLYCYL ENDOPEPTIDASE).
OS   CARICA PAPAYA (PAPAYA).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE;
OC   VIOLALES; CARICACEAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=LEAF;
RX   MEDLINE; 95288290.
RA   TAYLOR M.A., BAKER K.C., BRIGGS G.S., CONNERTON I.F., CUMMINGS N.J.,
RA   PRATT K.A., REVELL D.F., FREEDMAN R.B., GOODENOUGH P.W.;
RL   PROTEIN ENG. 8:59-62(1995).
RN   [2]
RP   SEQUENCE OF 133-348.
RX   MEDLINE; 90076470.
RA   RITONJA A., BUTTLE D.J., RAWLINGS N.D., TURK V., BARRETT A.J.;
RL   FEBS LETT. 258:109-112(1989).
RN   [3]
RP   SEQUENCE OF 133-150.
RX   MEDLINE; 80088401.
RA   LYNN K.R., YAGUCHI M.;
RL   BIOCHIM. BIOPHYS. ACTA 581:363-364(1979).
RN   [4]
RP   SEQUENCE OF 287-348 FROM N.A.
RX   MEDLINE; 87099799.
RA   MCKEE R.A., ADAMS S., MATTHEWS J.A., SMITH C.J., SMITH H.;
RL   BIOCHEM. J. 237:105-110(1986).
RN   [5]
RP   SUBSTRATE SPECIFICITY.
RX   MEDLINE; 90127427.
RA   BUTTLE D.J., RITONJA A., PEARL L.H., TURK V., BARRETT A.J.;
RL   FEBS LETT. 260:195-197(1990).
CC   -!- FUNCTION: THIOL PROTEASE WITH A SUBSTRATE SPECIFICITY VERY
CC       DIFFERENT FROM THE OTHER THIOL PROTEASES.
CC   -!- CATALYTIC ACTIVITY: PREFERENTIAL CLEAVAGE: GLY-|-XAA, IN PROTEINS
CC       AND IN SMALL MOLECULE SUBSTRATES.
CC   -!- ENZYME REGULATION: NOT INHIBITED BY CYSTATIN.
CC   -!- SUBSTITUTION OF THE CONSERVED GLY-23 RESIDUE BY GLU COULD POSSIBLY
CC       EXPLAIN THE UNUSUAL SPECIFICITY.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; X78056; G953176; -.
DR   EMBL; X03970; G18088; -.
DR   PIR; S06837; S06837.
DR   HSSP; P10056; 1PPO.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL.
FT   SIGNAL        1     18       POTENTIAL.
FT   PROPEP       19    132       ACTIVATION PEPTIDE.
FT   CHAIN       133    348       PROTEINASE IV.
FT   ACT_SITE    157    157       BY SIMILARITY.
FT   ACT_SITE    291    291       BY SIMILARITY.
FT   ACT_SITE    311    311       BY SIMILARITY.
FT   DISULFID    154    195       BY SIMILARITY.
FT   DISULFID    188    227       BY SIMILARITY.
FT   DISULFID    285    336       BY SIMILARITY.
FT   CONFLICT    190    190       K -> L (IN REF. 2).
SQ   SEQUENCE   348 AA;  39024 MW;  A9A454F3 CRC32;
     MAIICSFSKL LFVAICLFGH MSLSYCDFSI VGYSQDDLTS TERLIQLFNS WMLKHNKNYK
     NVDEKLYRFE IFKDNLKYID ERNKMINGYW LGLNEFSDLS NDEFKEKYVG SLPEDYTNQP
     YDEEFVNEDI VDLPESVDWR AKGAVTPVKH QGYCESCWAF STVATVEGIN KIKTGNLVEL
     SEQELVDCDK QSYGCNRGYQ STSLQYVAQN GIHLRAKYPY IAKQQTCRAN QVGGPKVKTN
     GVGRVQSNNE GSLLNAIAHQ PVSVVVESAG RDFQNYKGGI FEGSCGTKVD HAVTAVGYGK
     SGGKGYILIK NSWGPGWGEN GYIRIRRASG NSPGVCGVYR SSYYPIKN

SwissProt Database

PAP5_CARPA

ID   PAP5_CARPA     STANDARD;      PRT;    96 AA.
AC   P05993;
DT   01-NOV-1988 (REL. 09, CREATED)
DT   01-NOV-1988 (REL. 09, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE (EC 3.4.22.-) (CLONE PLBPC13) (FRAGMENT).
OS   CARICA PAPAYA (PAPAYA).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE;
OC   VIOLALES; CARICACEAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 87099799.
RA   MCKEE R.A., ADAMS S., MATTHEWS J.A., SMITH C.J., SMITH H.;
RL   BIOCHEM. J. 237:105-110(1986).
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; X03971; G18086; -.
DR   PIR; B26074; B26074.
DR   HSSP; P00784; 1PAD.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE.
FT   NON_TER       1      1
FT   ACT_SITE     31     31       BY SIMILARITY.
FT   ACT_SITE     58     58       BY SIMILARITY.
SQ   SEQUENCE   96 AA;  10474 MW;  B816070E CRC32;
     GPLAVAINAA YMQTYIGGVS CPYICSRRLN HGVLLVGYGS AGYAPIRLKE KPYWVIKNSW
     GENWGENGYY KICRGRNICG VDSMVSTVAA VHTTSQ

SwissProt Database

PAPA_CARPA

ID   PAPA_CARPA     STANDARD;      PRT;   345 AA.
AC   P00784;
DT   21-JUL-1986 (REL. 01, CREATED)
DT   01-JAN-1988 (REL. 06, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   PAPAIN PRECURSOR (EC 3.4.22.2) (PAPAYA PROTEINASE I) (PPI).
OS   CARICA PAPAYA (PAPAYA).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE;
OC   VIOLALES; CARICACEAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 87163525.
RA   COHEN L.W., COGHLAN V.M., DIHEL L.C.;
RL   GENE 48:219-227(1986).
RN   [2]
RP   SEQUENCE OF 134-345.
RX   MEDLINE; 71007899.
RA   MITCHEL R.E.J., CHAIKEN I.M., SMITH E.L.;
RL   J. BIOL. CHEM. 245:3485-3492(1970).
RN   [3]
RP   REVISION TO 197.
RX   MEDLINE; 70141125.
RA   HUSAIN S.S., LOWE G.;
RL   BIOCHEM. J. 116:689-692(1970).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX   MEDLINE; 69006973.
RA   DRENTH J., JANSONIUS J.N., KOEKOEK R., SWEN H.M., WOLTHERS B.G.;
RL   NATURE 218:929-932(1968).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX   MEDLINE; 85058190.
RA   KAMPHUIS I.G., KALK K.H., SWARTE M.B.A., DRENTH J.;
RL   J. MOL. BIOL. 179:233-256(1984).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX   MEDLINE; 90269230.
RA   STUBBS M.T., LABER B., BODE W., HUBER R., JERALA R., LENARCIC B.,
RA   TURK V.;
RL   EMBO J. 9:1939-1947(1990).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX   MEDLINE; 93075728.
RA   YAMAMOTO A., TOMOO K., DOI M., OHISHI H., INOUE M., ISHIDA T.,
RA   YAMAMOTO D., TSUBOI S., OKAMOTO H., OKADA Y.;
RL   BIOCHEMISTRY 31:11305-11309(1992).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RA   PICKERSGILL R.W., HARRIS G.W., GARMAN E.;
RL   ACTA CRYSTALLOGR. B 48:59-67(1992).
CC   -!- CATALYTIC ACTIVITY: PREFERENTIAL CLEAVAGE: ARG-. LYS-, PHE-XAA-.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; M15203; G167391; -.
DR   PIR; A26466; PPPA.
DR   PDB; 1PAD; 17-FEB-84.
DR   PDB; 2PAD; 17-FEB-84.
DR   PDB; 4PAD; 04-MAR-85.
DR   PDB; 5PAD; 17-FEB-84.
DR   PDB; 6PAD; 17-FEB-84.
DR   PDB; 9PAP; 15-JAN-95.
DR   PDB; 1PE6; 15-APR-93.
DR   PDB; 1PIP; 31-OCT-93.
DR   PDB; 1POP; 31-OCT-93.
DR   PDB; 1PPD; 02-JAN-85.
DR   PDB; 1PPN; 31-JAN-94.
DR   PDB; 1PPP; 31-JAN-94.
DR   PDB; 1STF; 31-JAN-94.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; SIGNAL; 3D-STRUCTURE.
FT   SIGNAL        1     18       POTENTIAL.
FT   PROPEP       19    133       ACTIVATION PEPTIDE.
FT   CHAIN       134    345       PAPAIN.
FT   ACT_SITE    158    158
FT   ACT_SITE    292    292
FT   ACT_SITE    308    308
FT   DISULFID    155    196
FT   DISULFID    189    228
FT   DISULFID    286    333
FT   CONFLICT    180    180       E -> Q (IN REF. 2).
FT   CONFLICT    219    220       YP -> PY (IN REF. 2).
FT   CONFLICT    251    251       E -> Q (IN REF. 2).
FT   CONFLICT    268    268       E -> Q (IN REF. 2).
FT   STRAND      138    139
FT   TURN        140    144
FT   STRAND      151    151
FT   TURN        153    154
FT   STRAND      156    156
FT   HELIX       158    175
FT   STRAND      181    181
FT   HELIX       183    189
FT   TURN        191    192
FT   TURN        195    196
FT   STRAND      197    197
FT   STRAND      199    199
FT   HELIX       201    210
FT   TURN        211    211
FT   STRAND      213    213
FT   STRAND      215    215
FT   TURN        216    218
FT   HELIX       231    233
FT   STRAND      238    238
FT   STRAND      242    245
FT   HELIX       251    260
FT   STRAND      263    267
FT   HELIX       272    276
FT   STRAND      281    282
FT   STRAND      292    299
FT   STRAND      303    307
FT   STRAND      310    310
FT   TURN        312    313
FT   TURN        315    315
FT   STRAND      316    316
FT   TURN        317    318
FT   STRAND      319    323
FT   HELIX       332    334
FT   TURN        335    336
FT   STRAND      340    343
SQ   SEQUENCE   345 AA;  38922 MW;  B329F58F CRC32;
     MAMIPSISKL LFVAICLFVY MGLSFGDFSI VGYSQNDLTS TERLIQLFES WMLKHNKIYK
     NIDEKIYRFE IFKDNLKYID ETNKKNNSYW LGLNVFADMS NDEFKEKYTG SIAGNYTTTE
     LSYEEVLNDG DVNIPEYVDW RQKGAVTPVK NQGSCGSCWA FSAVVTIEGI IKIRTGNLNE
     YSEQELLDCD RRSYGCNGGY PWSALQLVAQ YGIHYRNTYP YEGVQRYCRS REKGPYAAKT
     DGVRQVQPYN EGALLYSIAN QPVSVVLEAA GKDFQLYRGG IFVGPCGNKV DHAVAAVGYG
     PNYILIKNSW GTGWGENGYI RIKRGTGNSY GVCGLYTSSF YPVKN

SwissProt Database

RD19_ARATH

ID   RD19_ARATH     STANDARD;      PRT;   368 AA.
AC   P43296;
DT   01-NOV-1995 (REL. 32, CREATED)
DT   01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE RD19A PRECURSOR (EC 3.4.22.-).
GN   RD19A.
OS   ARABIDOPSIS THALIANA (MOUSE-EAR CRESS).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE;
OC   CAPPARALES; CRUCIFERAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=CV. COLUMBIA;
RX   MEDLINE; 93314960.
RA   KOIZUMI M., YAMAGUCHI-SHINOZAKI K., TSUJI H., SHINOZAKI K.;
RL   GENE 129:175-182(1993).
CC   -!- INDUCTION: BY HIGH SALT CONDITIONS.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; D13042; G435618; -.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; GLYCOPROTEIN; SIGNAL.
FT   SIGNAL        1     23       POTENTIAL.
FT   PROPEP       24    134       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN       135    368       CYSTEINE PROTEINASE RD19A.
FT   ACT_SITE    159    159       BY SIMILARITY.
FT   ACT_SITE    302    302       BY SIMILARITY.
FT   ACT_SITE    329    329       BY SIMILARITY.
FT   DISULFID    156    206       BY SIMILARITY.
FT   DISULFID    194    240       BY SIMILARITY.
FT   DISULFID    296    350       BY SIMILARITY.
FT   CARBOHYD    253    253       POTENTIAL.
SQ   SEQUENCE   368 AA;  40418 MW;  0530E4F1 CRC32;
     MDRLKLYFSV FVLSFFIVSV SSSDVNDGDD LVIRQVVGGA EPQVLTSEDH FSLFKRKFGK
     VYASNEEHDY RFSVFKANLR RARRHQKLDP SATHGVTQFS DLTRSEFRKK HLGVRSGFKL
     PKDANKAPIL PTENLPEDFD WRDHGAVTPV KNQGSCGSCW SFSATGALEG ANFLATGKLV
     SLSEQQLVDC DHECDPEEAD SCDSGCNGGL MNSAFEYTLK TGGLMKEEDY PYTGKDGKTC
     KLDKSKIVAS VSNFSVISID EEQIAANLVK NGPLAVAINA GYMQTYIGGV SCPYICTRRL
     NHGVLLVGYG AAGYAPARFK EKPYWIIKNS WGETWGENGF YKICKGRNIC GVDSMVSTVA
     ATVSTTAH

SwissProt Database

RD21_ARATH

ID   RD21_ARATH     STANDARD;      PRT;   462 AA.
AC   P43297;
DT   01-NOV-1995 (REL. 32, CREATED)
DT   01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   CYSTEINE PROTEINASE RD21A PRECURSOR (EC 3.4.22.-).
GN   RD21A.
OS   ARABIDOPSIS THALIANA (MOUSE-EAR CRESS).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE;
OC   CAPPARALES; CRUCIFERAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=CV. COLUMBIA;
RX   MEDLINE; 93314960.
RA   KOIZUMI M., YAMAGUCHI-SHINOZAKI K., TSUJI H., SHINOZAKI K.;
RL   GENE 129:175-182(1993).
CC   -!- INDUCTION: BY HIGH SALT CONDITIONS.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; D13043; G435619; -.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE; ZYMOGEN; GLYCOPROTEIN; SIGNAL.
FT   SIGNAL        1     21       POTENTIAL.
FT   PROPEP       22    136       ACTIVATION PEPTIDE (POTENTIAL).
FT   CHAIN       137    462       CYSTEINE PROTEINASE RD21A.
FT   ACT_SITE    161    161       BY SIMILARITY.
FT   ACT_SITE    297    297       BY SIMILARITY.
FT   ACT_SITE    317    317       BY SIMILARITY.
FT   DISULFID    158    200       BY SIMILARITY.
FT   DISULFID    192    233       BY SIMILARITY.
FT   DISULFID    291    342       BY SIMILARITY.
FT   CARBOHYD     90     90       POTENTIAL.
FT   CARBOHYD    414    414       POTENTIAL.
SQ   SEQUENCE   462 AA;  50966 MW;  E9407B72 CRC32;
     MGFLKPTMAI LFLAMVAVSS AVDMSIISYD EKHGVSTTGG RSEAEVMSIY EAWLVKHGKA
     QSQNSLVEKD RRFEIFKDNL RFVDEHNEKN LSYRLGLTRF ADLTNDEYRS KYLGAKMEKK
     GERRTSLRYE ARVGDELPES IDWRKKGAVA EVKDQGGCGS CWAFSTIGAV EGINQIVTGD
     LITLSEQELV DCDTSYNEGC NGGLMDYAFE FIIKNGGIDT DKDYPYKGVD GTCDQIRKNA
     KVVTIDSYED VPTYSEESLK KAVAHQPISI AIEAGGRAFQ LYDSGIFDGS CGTQLDHGVV
     AVGYGTENGK DYWIVRNSWG KSWGESGYLR MARNIASSSG KCGIAIEPSY PIKNGENPPN
     PGPSPPSPIK PPTQCDSYYT CPESNTCCCL FEYGKYCFAW GCCPLEAATC CDDNYSCCPH
     EYPVCDLDQG TCLLSKNSPF SVKALKRKPA TPFWSQGRKN IA

SwissProt Database

SERA_PLAFG

ID   SERA_PLAFG     STANDARD;      PRT;   989 AA.
AC   P13823;
DT   01-JAN-1990 (REL. 13, CREATED)
DT   01-JAN-1990 (REL. 13, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   SERINE-REPEAT ANTIGEN PROTEIN PRECURSOR (P126) (111 KD ANTIGEN).
GN   SERA.
OS   PLASMODIUM FALCIPARUM (ISOLATE FCR-3 / GAMBIA).
OC   EUKARYOTA; PROTOZOA; APICOMPLEXA; SPOROZOA; COCCIDIA; EUCOCCIDIIDA.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 89219141.
RA   LI W.-B., BZIK D.J., HORII T., INSELBURG J.;
RL   MOL. BIOCHEM. PARASITOL. 33:13-26(1989).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 89040025.
RA   BZIK D.J., LI W.-B., HORII T., INSELBURG J.;
RL   MOL. BIOCHEM. PARASITOL. 30:279-288(1988).
RN   [3]
RP   SEQUENCE FROM N.A.
RC   STRAIN=HONDURAS-1;
RX   MEDLINE; 95198763.
RA   FOX B.A., BZIK D.J.;
RL   MOL. BIOCHEM. PARASITOL. 68:133-144(1994).
RN   [4]
RP   SEQUENCE OF 6-362 FROM N.A.
RX   MEDLINE; 88288340.
RA   HORII T., BZIK D.J., INSELBURG J.;
RL   MOL. BIOCHEM. PARASITOL. 30:9-18(1988).
RN   [5]
RP   SIMILARITY TO THIOL PROTEASES OF A DOMAIN.
RX   MEDLINE; 89365153.
RA   HIGGINS D.G., MCCONNELL D.J., SHARP P.M.;
RL   NATURE 340:604-604(1989).
RN   [6]
RP   SIMILARITY TO THIOL PROTEASES OF A DOMAIN.
RX   MEDLINE; 90044065.
RA   EAKIN A.E., HIGAKI J.N., MCKERROW J.H., CRAIK C.S.;
RL   NATURE 342:132-132(1989).
RN   [7]
RP   SIMILARITY TO THIOL PROTEASES OF A DOMAIN.
RX   MEDLINE; 90044065.
RA   MOTTRAM J.C., COOMBS G.H., NORTH M.J.;
RL   NATURE 342:132-132(1989).
CC   -!- FUNCTION: IT MAY FUNCTION AT THE RED BLOOD CELL MEMBRANE, PERHAPS
CC       AS A COMPONENT THAT INFLUENCES THE INVASION PROCESS.
CC   -!- SUBCELLULAR LOCATION: EXPORTED ANTIGEN THAT ACCUMULATES IN THE
CC       PARASITOPHOROUS VACUOLE.
CC   -!- PTM: CONTAINS NUMEROUS POSSIBLE O-LINKED GLYCOSYLATION AND SERINE
CC       PHOSPHORYLATION SITES.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   EMBL; X06427; E8903; -.
DR   EMBL; J03993; G160681; -.
DR   EMBL; U08113; G607635; -.
DR   EMBL; J04000; G160683; -.
DR   EMBL; M21323; G552180; -.
DR   PIR; A54505; A54505.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   ANTIGEN; MALARIA; GLYCOPROTEIN; SIGNAL; HYDROLASE; THIOL PROTEASE.
FT   SIGNAL        1     16
FT   CHAIN        17    989       SERINE-REPEAT ANTIGEN PROTEIN.
FT   DOMAIN       27    227       SER-RICH.
FT   DOMAIN      191    225       POLY-SER.
FT   DOMAIN      571    989       THIOL-PROTEASE-LIKE.
FT   SITE        588    588       ANCESTRAL ACTIVE SITE.
FT   ACT_SITE    754    754       BY SIMILARITY.
FT   ACT_SITE    779    779       BY SIMILARITY.
FT   CARBOHYD    168    168       POTENTIAL.
FT   CARBOHYD    310    310       POTENTIAL.
FT   CARBOHYD    820    820       POTENTIAL.
FT   VARIANT     178    191       MISSING (IN AN ALLELE).
FT   CONFLICT      6      8       SLF -> EFL (IN REF. 4).
FT   CONFLICT     44     44       A -> T (IN REF. 4).
FT   CONFLICT    356    362       EKENKND -> KKKKKGI (IN REF. 4).
SQ   SEQUENCE   989 AA;  111095 MW;  AEFEA631 CRC32;
     MKSYISLFFI LCVIFNKNVI KCTGESQTGN TGGGQAGNTV GDQAGSTGGS PQGSTGASQP
     GSSEPSNPVS SGHSVSTVSV SQTSTSSEKQ DTIQVKSALL KDYMGLKVTG PCNENFIMFL
     VPHIYIDVDT EDTNIELRTT LKETNNAISF ESNSGSLEKK KYVKLPSNGT TGEQGSSTGT
     VRGDTEPISD SSSSSSSSSS SSSSSSSSSS SSSSSSSSSS SSSSSESLPA NGPDSPTVKP
     PRNLQNICET GKNFKLVVYI KENTLIIKWK VYGETKDTTE NNKVDVRKYL INEKETPFTS
     ILIHAYKEHN GTNLIESKNY ALGSDIPEKC DTLASNCFLS GNFNIEKCFQ CALLVEKENK
     NDVCYKYLSE DIVSNFKEIK AETEDDDEDD YTEYKLTESI DNILVKMFKT NENNDKSELI
     KLEEVDDSLK LELMNYCSLL KDVDTTGTLD NYGMGNEMDI FNNLKRLLIY HSEENINTLK
     NKFRNAAVCL KNVDDWIVNK RGLVLPELNY DLEYFNEHLY NDKNSPEDKD NKGKGVVHVD
     TTLEKEDTLS YDNSDNMFCN KEYCNRLKDE NNCISNLQVE DQGNCDTSWI FASKYHLETI
     RCMKGYEPTK ISALYVANCY KGEHKDRCDE GSSPMEFLQI IEDYGFLPAE SNYPYNYVKV
     GEQCPKVEDH WMNLWDNGKI LHNKNEPNSL DGKGYTAYES ERFHDNMDAF VKIIKTEVMN
     KGSVIAYIKA ENVMGYEFSG KKVQNLCGDD TADHAVNIVG YGNYVNSEGE KKSYWIVRNS
     WGPYWGDEGY FKVDMYGPTH CHFNFIHSVV IFNVDLPMNN KTTKKESKIY DYYLKASPEF
     YHNLYFKNFN VGKKNLFSEK EDNENNKKLG NNYIIFGQDT AGSGQSGKES NTALESAGTS
     NEVSERVHVY HILKHIKDGK IRMGMRKYID TQDVNKKHSC TRSYAFNPEN YEKCVNLCNV
     NWKTCEEKTS PGLCLSKLDT NNECYFCYV

SwissProt Database

TES1_RAT

ID   TES1_RAT       STANDARD;      PRT;   333 AA.
AC   P15242; P15243;
DT   01-APR-1990 (REL. 14, CREATED)
DT   01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE)
DT   01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE)
DE   TESTIN 1/2 PRECURSOR (CMB-22/CMB-23).
OS   RATTUS NORVEGICUS (RAT).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; RODENTIA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=TESTIS;
RX   MEDLINE; 95226598.
RA   GRIMA J., ZHU L., ZONG S.D., CATTERALL J.F., BARDIN C.W.,
RA   CHENG C.Y.;
RL   BIOL. REPROD. 52:340-355(1995).
RN   [2]
RP   SEQUENCE OF 18-49.
RC   STRAIN=SPRAGUE-DAWLEY; TISSUE=SERTOLI CELLS;
RX   MEDLINE; 90078247.
RA   CHENG C.Y., GRIMA J., STAHLER M.S., LOCKSHIN R.A.;
RL   J. BIOL. CHEM. 264:21386-21393(1989).
RN   [3]
RP   LACK OF PROTEASE ACTIVITY.
RX   MEDLINE; 93191698.
RA   CHENG C.Y., MORRIS I., BARDIN C.W.;
RL   BIOCHEM. BIOPHYS. RES. COMMUN. 191:224-231(1993).
CC   -!- FUNCTION: NOT KNOWN.
CC   -!- SUBCELLULAR LOCATION: SERTOLI CELLS SECRETORY PROTEIN.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
CC   -!- CAUTION: SHOULD NOT BE CONFUSED WITH MOUSE TESTIN WHICH IS A
CC       LIM DOMAIN PROTEIN.
DR   EMBL; U16858; G577430; -.
DR   PIR; A34199; A34199.
DR   PIR; B34199; B34199.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   TESTIS; SIGNAL.
FT   SIGNAL        1     17
FT   CHAIN        18    333       TESTIN 2.
FT   CHAIN        20    333       TESTIN 1.
FT   SITE        138    138       ANCESTRAL ACTIVE SITE.
FT   ACT_SITE    276    276       BY SIMILARITY.
FT   ACT_SITE    300    300       BY SIMILARITY.
FT   DISULFID    135    178       BY SIMILARITY.
FT   DISULFID    169    211       BY SIMILARITY.
FT   DISULFID    269    322       BY SIMILARITY.
SQ   SEQUENCE   333 AA;  38033 MW;  3C35DFEF CRC32;
     MIAVLFLAIL CLEVDSTAPT PDPSLDVEWN EWRTKHGKTY NMNEERLKRA VWEKNFKMIE
     LHNWEYLEGR HDFTMAMNAF GDLTNIEFVK MMTGFQRQKI KKTHIFQDHQ FLYVPKRVDW
     RQLGYVTPVK NQGHCASSWA FSATGSLEGQ MFRKTERLIP LSEQNLLDCM GSNVTHGCSG
     GFMQYAFQYV KDNGGLATEE SYPYRGQGRE CRYHAENSAA NVRDFVQIPG SEEALMKAVA
     KVGPISVAVD ASHGSFQFYG SGIYYEPQCK RVHLNHAVLV VGYGFEGEES DGNSFWLVKN
     SWGEEWGMKG YMKLAKDWSN HCGIATYSTY PIV

SwissProt Database

THPA_THADA

ID   THPA_THADA     STANDARD;      PRT;    35 AA.
AC   P21381;
DT   01-MAY-1991 (REL. 18, CREATED)
DT   01-MAY-1991 (REL. 18, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   THAUMATOPAIN (EC 3.4.22.-) (FRAGMENT).
OS   THAUMATOCOCCUS DANIELLII (KATEMFE).
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; MONOCOTYLEDONEAE;
OC   ZINGIBERALES; MARANTACEAE.
RN   [1]
RP   SEQUENCE.
RC   TISSUE=SEED;
RX   MEDLINE; 91158711.
RA   CUSACK M., STEPHEN A.G., POWLS R., BEYNON R.J.;
RL   BIOCHEM. J. 274:231-236(1991).
CC   -!- FUNCTION: SPECIFICITY SIMILAR TO THAT OF PAPAIN.
CC   -!- SUBUNIT: MONOMER.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE
CC       PAPAIN FAMILY OF THIOL PROTEASES.
DR   PIR; S14329; S14329.
DR   HSSP; P00784; 1PAD.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN.
KW   HYDROLASE; THIOL PROTEASE.
FT   ACT_SITE     26     26
FT   NON_TER      35     35
SQ   SEQUENCE   35 AA;  3774 MW;  60B91E55 CRC32;
     NLPNSVDWWK KGAVAAVKNQ RXCGSCXAFS SIKTS