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CYT_CYPCA
ID   CYT_CYPCA               Reviewed;         129 AA.
AC   P35481;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Cystatin;
DE   AltName: Full=Ovarian cystatin;
DE   AltName: Full=P12;
DE   Flags: Precursor;
OS   Cyprinus carpio (Common carp).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Cyprinus.
OX   NCBI_TaxID=7962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 19-57; 74-80 AND
RP   92-129.
RC   TISSUE=Ovary;
RX   PubMed=8829807; DOI=10.1016/0305-0491(95)02070-5;
RA   Tsai Y.-J., Chang G.-D., Huang C.-J., Chang Y.-S., Huang F.-L.;
RT   "Purification and molecular cloning of carp ovarian cystatin.";
RL   Comp. Biochem. Physiol. 113B:573-580(1996).
CC   -!- FUNCTION: Cysteine proteinase inhibitor.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Detected in ovary but not in all the other examined
CC       tissues.
CC   -!- PTM: Proteolytically processed to produce two chains linked by a
CC       disulfide bridge.
CC   -!- SIMILARITY: Belongs to the cystatin family. {ECO:0000305}.
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DR   EMBL; L23572; AAB48011.1; -; mRNA.
DR   AlphaFoldDB; P35481; -.
DR   SMR; P35481; -.
DR   Proteomes; UP000694384; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   CDD; cd00042; CY; 1.
DR   InterPro; IPR000010; Cystatin_dom.
DR   InterPro; IPR046350; Cystatin_sf.
DR   InterPro; IPR018073; Prot_inh_cystat_CS.
DR   Pfam; PF00031; Cystatin; 1.
DR   SMART; SM00043; CY; 1.
DR   SUPFAM; SSF54403; SSF54403; 1.
DR   PROSITE; PS00287; CYSTATIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW   Reference proteome; Secreted; Signal; Thiol protease inhibitor.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:8829807"
FT   CHAIN           19..129
FT                   /note="Cystatin"
FT                   /id="PRO_0000006664"
FT   MOTIF           67..71
FT                   /note="Secondary area of contact"
FT   SITE            23
FT                   /note="Reactive site"
FT                   /evidence="ECO:0000250"
FT   SITE            91..92
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000305"
FT   DISULFID        85..94
FT                   /evidence="ECO:0000250"
FT   DISULFID        108..128
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   129 AA;  14236 MW;  732760DF347515BC CRC64;
     MYLKVIVLFL AVTLVVESTG IPGGLVDADI NDKDVQKALR FAVDHYNGQS NDAFVRKVSK
     VIKVQQQVAA GMKYIFTVKM EVASCKKGGV KTMCAVPKNP SIEQVIQCKI TVWSQPWLNS
     LKVTENTCM
 
 
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