ID   CYTC_MACMU              Reviewed;         146 AA.
AC   O19092; Q5EG77;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Cystatin-C;
DE   AltName: Full=Cystatin-3;
DE   Flags: Precursor;
GN   Name=CST3;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Cao W.G., Jia Y.B., Mah K., Slayden O.D., Brenner R.M.;
RT   "Rhesus monkey DNA sequencing.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
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; U51912; AAB64050.1; -; mRNA.
DR   EMBL; AY885223; AAW79565.1; -; mRNA.
DR   RefSeq; NP_001028096.1; NM_001032924.2.
DR   RefSeq; XP_015005078.1; XM_015149592.1.
DR   AlphaFoldDB; O19092; -.
DR   SMR; O19092; -.
DR   STRING; 9544.ENSMMUP00000012060; -.
DR   MEROPS; I25.004; -.
DR   Ensembl; ENSMMUT00000108399; ENSMMUP00000061250; ENSMMUG00000050596.
DR   GeneID; 574313; -.
DR   KEGG; mcc:574313; -.
DR   CTD; 1471; -.
DR   VEuPathDB; HostDB:ENSMMUG00000050596; -.
DR   eggNOG; ENOG502SC50; Eukaryota.
DR   GeneTree; ENSGT00940000154755; -.
DR   HOGENOM; CLU_118168_0_1_1; -.
DR   InParanoid; O19092; -.
DR   OMA; YTVPWLG; -.
DR   OrthoDB; 1565344at2759; -.
DR   Proteomes; UP000006718; Chromosome 10.
DR   Bgee; ENSMMUG00000050596; Expressed in Ammon's horn and 21 other tissues.
DR   ExpressionAtlas; O19092; baseline.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR   GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR   GO; GO:0006952; P:defense response; IEA:Ensembl.
DR   GO; GO:0060313; P:negative regulation of blood vessel remodeling; IEA:Ensembl.
DR   GO; GO:0010711; P:negative regulation of collagen catabolic process; IEA:Ensembl.
DR   GO; GO:2000117; P:negative regulation of cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0060311; P:negative regulation of elastin catabolic process; IEA:Ensembl.
DR   GO; GO:0010716; P:negative regulation of extracellular matrix disassembly; IEA:Ensembl.
DR   GO; GO:0097435; P:supramolecular fiber organization; IEA:Ensembl.
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;
KW   Reference proteome; Secreted; Signal; Thiol protease inhibitor.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000250"
FT   CHAIN           27..146
FT                   /note="Cystatin-C"
FT                   /id="PRO_0000006640"
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;  15857 MW;  F0B3BB774A29DF26 CRC64;
     MAGPLRAPLL LLAILAVALA VSPAAGASPG KPPRLVGGPM DASVEEEGVR RALDFAVSEY
     NKASNDMYHS RALQVVRARK QIVAGVNYFL DVELGRTTCT KTQPNLDNCP FHEQPHLKRK
     AFCSFQIYTV PWQGTMTLSK STCQDA