ID   CYTC_SAISC              Reviewed;         146 AA.
AC   O19093;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Cystatin-C;
DE   AltName: Full=Cystatin-3;
DE   Flags: Precursor;
GN   Name=CST3;
OS   Saimiri sciureus (Common squirrel monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Saimiriinae; Saimiri.
OX   NCBI_TaxID=9521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8898820; DOI=10.1161/01.str.27.11.2080;
RA   Wei L.H., Walker L.C., Levy E.;
RT   "Cystatin C. Icelandic-like mutation in an animal model of cerebrovascular
RT   beta-amyloidosis.";
RL   Stroke 27:2080-2085(1996).
CC   -!- FUNCTION: As an inhibitor of cysteine proteinases, this protein is
CC       thought to serve an important physiological role as a local regulator
CC       of this enzyme activity.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cystatin family. {ECO:0000305}.
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DR   EMBL; U52028; AAB64051.1; -; mRNA.
DR   AlphaFoldDB; O19093; -.
DR   SMR; O19093; -.
DR   MEROPS; I25.004; -.
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   2: Evidence at transcript level;
KW   Amyloid; Disulfide bond; Phosphoprotein; Protease inhibitor; Secreted;
KW   Signal; Thiol protease inhibitor.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000250"
FT   CHAIN           27..146
FT                   /note="Cystatin-C"
FT                   /id="PRO_0000006641"
FT   MOTIF           81..85
FT                   /note="Secondary area of contact"
FT   SITE            37
FT                   /note="Reactive site"
FT   MOD_RES         43
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01034"
FT   DISULFID        99..109
FT                   /evidence="ECO:0000250"
FT   DISULFID        123..143
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   146 AA;  15946 MW;  08196353C0306AA3 CRC64;
     MAGPLRAPLL LLAILAVALA LSPAAGASPG RTPRLLGGPM DASVEEEGVR RALDFAVSEY
     NKASNDMYHS RALQVVRARK QIVAGVNYFL DVEMGRTTCT KNQPNLDNCP FHEQPHLKRK
     AFCSFQIYSV PWQGIMTLSK STCQDA