ID   CYTC_RAT                Reviewed;         140 AA.
AC   P14841; Q5M968;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   04-NOV-2026, entry version 204.
DE   RecName: Full=Cystatin-C;
DE   AltName: Full=Cystatin-3;
DE   Flags: Precursor;
GN   Name=Cst3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 14-140.
RC   STRAIN=Buffalo;
RX   PubMed=2689174; DOI=10.1111/j.1432-1033.1989.tb15174.x;
RA   Cole T., Dickson P.W., Esnard F., Averill F., Risbridger G., Gauthier F.,
RA   Schreiber G.;
RT   "The cDNA structure and expression analysis of the genes for the cysteine
RT   proteinase inhibitor cystatin C and for beta 2-microglobulin in rat
RT   brain.";
RL   Eur. J. Biochem. 186:35-42(1989).
RN   [3]
RP   PROTEIN SEQUENCE OF 21-140.
RX   PubMed=2400577;
RA   Esnard F., Esnard A., Faucher D., Capony J.-P., Derancourt J., Brillard M.,
RA   Gauthier F.;
RT   "Rat cystatin C: the complete amino acid sequence reveals a site for N-
RT   glycosylation.";
RL   Biol. Chem. Hoppe-Seyler 371:161-166(1990).
RN   [4]
RP   PROTEIN SEQUENCE OF 21-62.
RX   PubMed=3044831; DOI=10.1016/0014-5793(88)80080-2;
RA   Esnard A., Esnard F., Faucher D., Gauthier F.;
RT   "Two rat homologues of human cystatin C.";
RL   FEBS Lett. 236:475-478(1988).
RN   [5]
RP   PROTEIN SEQUENCE OF 42-54.
RC   TISSUE=Sertoli cell;
RX   PubMed=1563513; DOI=10.1016/0014-5793(92)80180-o;
RA   Esnard A., Esnard F., Guillou F., Gauthier F.;
RT   "Production of the cysteine proteinase inhibitor cystatin C by rat Sertoli
RT   cells.";
RL   FEBS Lett. 300:131-135(1992).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-99, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=24090084; DOI=10.1021/pr400783j;
RA   Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA   Graham M.E., Packer N.H., Cordwell S.J.;
RT   "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT   heterogeneity.";
RL   J. Proteome Res. 12:5791-5800(2013).
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. Known to inhibit cathepsin B, H, and L.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the cystatin family. {ECO:0000305}.
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DR   EMBL; BC087591; AAH87591.1; -; mRNA.
DR   EMBL; X16957; CAA34831.1; -; mRNA.
DR   PIR; S07085; S07085.
DR   PIR; S10587; S10587.
DR   RefSeq; NP_036969.1; NM_012837.1.
DR   AlphaFoldDB; P14841; -.
DR   SMR; P14841; -.
DR   FunCoup; P14841; 167.
DR   STRING; 10116.ENSRNOP00000007175; -.
DR   MEROPS; I25.004; -.
DR   GlyCosmos; P14841; 1 site, 5 glycans.
DR   GlyGen; P14841; 1 site, 5 N-linked glycans (1 site).
DR   iPTMnet; P14841; -.
DR   PhosphoSitePlus; P14841; -.
DR   SwissPalm; P14841; -.
DR   PaxDb; 10116-ENSRNOP00000007175; -.
DR   Ensembl; ENSRNOT00000007175.8; ENSRNOP00000007175.6; ENSRNOG00000005195.8.
DR   GeneID; 25307; -.
DR   KEGG; rno:25307; -.
DR   UCSC; RGD:2432; rat.
DR   AGR; RGD:2432; -.
DR   CTD; 1471; -.
DR   RGD; 2432; Cst3.
DR   VEuPathDB; HostDB:ENSRNOG00000005195; -.
DR   eggNOG; ENOG502SC50; Eukaryota.
DR   GeneTree; ENSGT00940000154755; -.
DR   HOGENOM; CLU_118168_0_1_1; -.
DR   InParanoid; P14841; -.
DR   OMA; AADIQHC; -.
DR   OrthoDB; 51676at9989; -.
DR   PhylomeDB; P14841; -.
DR   Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR   PRO; PR:P14841; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000005195; Expressed in Ammon's horn and 20 other cell types or tissues.
DR   ExpressionAtlas; P14841; baseline and differential.
DR   GO; GO:0030424; C:axon; IDA:RGD.
DR   GO; GO:0005604; C:basement membrane; IDA:RGD.
DR   GO; GO:0043292; C:contractile muscle fiber; IDA:RGD.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IDA:RGD.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR   GO; GO:0005771; C:multivesicular body; IDA:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0031965; C:nuclear membrane; IDA:RGD.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0031982; C:vesicle; IDA:RGD.
DR   GO; GO:0001540; F:amyloid-beta binding; ISO:RGD.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; ISO:RGD.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0030414; F:peptidase inhibitor activity; IDA:RGD.
DR   GO; GO:0002020; F:protease binding; IDA:RGD.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IMP:RGD.
DR   GO; GO:0006952; P:defense response; ISO:RGD.
DR   GO; GO:0007566; P:embryo implantation; IEP:RGD.
DR   GO; GO:0001654; P:eye development; IEP:RGD.
DR   GO; GO:0008584; P:male gonad development; IEP:RGD.
DR   GO; GO:0060313; P:negative regulation of blood vessel remodeling; ISO:RGD.
DR   GO; GO:0010711; P:negative regulation of collagen catabolic process; ISO:RGD.
DR   GO; GO:0060311; P:negative regulation of elastin catabolic process; ISO:RGD.
DR   GO; GO:0010716; P:negative regulation of extracellular matrix disassembly; ISO:RGD.
DR   GO; GO:0045861; P:negative regulation of proteolysis; ISO:RGD.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:RGD.
DR   GO; GO:0045740; P:positive regulation of DNA replication; IDA:RGD.
DR   GO; GO:0034103; P:regulation of tissue remodeling; ISO:RGD.
DR   GO; GO:0048678; P:response to axon injury; IEP:RGD.
DR   GO; GO:0009743; P:response to carbohydrate; IEP:RGD.
DR   GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR   GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR   GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR   GO; GO:0007431; P:salivary gland development; IEP:RGD.
DR   GO; GO:0060009; P:Sertoli cell development; IEP:RGD.
DR   GO; GO:0097435; P:supramolecular fiber organization; ISO:RGD.
DR   CDD; cd00042; CY; 1.
DR   FunFam; 3.10.450.10:FF:000004; Cystatin C; 1.
DR   Gene3D; 3.10.450.10; -; 1.
DR   InterPro; IPR000010; Cystatin_dom.
DR   InterPro; IPR046350; Cystatin_sf.
DR   InterPro; IPR018073; Prot_inh_cystat_CS.
DR   PANTHER; PTHR46186; CYSTATIN; 1.
DR   PANTHER; PTHR46186:SF6; CYSTATIN-C; 1.
DR   Pfam; PF00031; Cystatin; 1.
DR   SMART; SM00043; CY; 1.
DR   SUPFAM; SSF54403; Cystatin/monellin; 1.
DR   PROSITE; PS00287; CYSTATIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Protease inhibitor; Reference proteome; Secreted; Signal;
KW   Thiol protease inhibitor.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..140
FT                   /note="Cystatin-C"
FT                   /id="PRO_0000006644"
FT   MOTIF           75..79
FT                   /note="Secondary area of contact"
FT   SITE            31
FT                   /note="Reactive site"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0007744|PubMed:24090084"
FT   DISULFID        93..103
FT                   /evidence="ECO:0000250"
FT   DISULFID        117..137
FT                   /evidence="ECO:0000250"
FT   CONFLICT        38
FT                   /note="A -> E (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   140 AA;  15437 MW;  B785B2958F7824F8 CRC64;
     MASPLRSLML LLAVLAVAWA GTSRPPPRLL GAPQEADASE EGVQRALDFA VSEYNKGSND
     AYHSRAIQVV RARKQLVAGI NYYLDVEMGR TTCTKSQTNL TNCPFHDQPH LMRKALCSFQ
     IYSVPWKGTH TLTKSSCKNA
//