CYTC_RAT
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 03-AUG-2022, entry version 186.
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 STRING; 10116.ENSRNOP00000007175; -.
DR MEROPS; I25.004; -.
DR GlyGen; P14841; 1 site, 5 N-linked glycans (1 site).
DR iPTMnet; P14841; -.
DR PhosphoSitePlus; P14841; -.
DR SwissPalm; P14841; -.
DR PaxDb; P14841; -.
DR PRIDE; P14841; -.
DR GeneID; 25307; -.
DR KEGG; rno:25307; -.
DR UCSC; RGD:2432; rat.
DR CTD; 1471; -.
DR RGD; 2432; Cst3.
DR VEuPathDB; HostDB:ENSRNOG00000005195; -.
DR eggNOG; ENOG502SC50; Eukaryota.
DR HOGENOM; CLU_118168_0_1_1; -.
DR InParanoid; P14841; -.
DR OMA; YTVPWLG; -.
DR OrthoDB; 1565344at2759; -.
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 tissues.
DR Genevisible; P14841; RN.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005604; C:basement membrane; IDA:RGD.
DR GO; GO:0042995; C:cell projection; IDA:RGD.
DR GO; GO:0043292; C:contractile fiber; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0005764; C:lysosome; IDA: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:0006915; P:apoptotic process; IEP:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0001775; P:cell activation; IEP:RGD.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEP:RGD.
DR GO; GO:0042747; P:circadian sleep/wake cycle, REM sleep; IEP: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:0060548; P:negative regulation of cell death; IMP:RGD.
DR GO; GO:0010711; P:negative regulation of collagen catabolic process; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0010716; P:negative regulation of extracellular matrix disassembly; ISO:RGD.
DR GO; GO:0010466; P:negative regulation of peptidase activity; 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:0043067; P:regulation of programmed cell death; IMP: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:0010035; P:response to inorganic substance; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IMP: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 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; 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
