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