CYTC_MOUSE
ID CYTC_MOUSE Reviewed; 140 AA.
AC P21460; Q544Y0;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Cystatin-C;
DE AltName: Full=Cystatin-3;
DE Flags: Precursor;
GN Name=Cst3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=2241983; DOI=10.1016/0006-291x(90)90767-h;
RA Solem M., Rawson C., Lindburg K., Barnes D.;
RT "Transforming growth factor beta regulates cystatin C in serum-free mouse
RT embryo (SFME) cells.";
RL Biochem. Biophys. Res. Commun. 172:945-951(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv; TISSUE=Liver;
RX PubMed=7835704; DOI=10.1016/0378-1119(94)00728-b;
RA Huh C., Nagle J.W., Kozak C.A., Abrahamson M., Karlsson S.;
RT "Structural organization, expression and chromosomal mapping of the mouse
RT cystatin-C-encoding gene (Cst3).";
RL Gene 152:221-226(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ILS, and ISS;
RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT "High-throughput sequence identification of gene coding variants within
RT alcohol-related QTLs.";
RL Mamm. Genome 12:657-663(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J;
RC TISSUE=Bone marrow, Head, Hippocampus, Kidney, Mammary gland,
RC Medulla oblongata, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; M59470; AAA63298.1; -; mRNA.
DR EMBL; U10098; AAB41056.1; -; Unassigned_DNA.
DR EMBL; AF483486; AAL90760.1; -; mRNA.
DR EMBL; AF483487; AAL90761.1; -; mRNA.
DR EMBL; AK002438; BAB22101.1; -; mRNA.
DR EMBL; AK013676; BAB28949.1; -; mRNA.
DR EMBL; AK014368; BAB29303.1; -; mRNA.
DR EMBL; AK131728; BAE20785.1; -; mRNA.
DR EMBL; AK146333; BAE27088.1; -; mRNA.
DR EMBL; AK151160; BAE30165.1; -; mRNA.
DR EMBL; AK161856; BAE36608.1; -; mRNA.
DR EMBL; AK166430; BAE38771.1; -; mRNA.
DR EMBL; BC002072; AAH02072.1; -; mRNA.
DR CCDS; CCDS16852.1; -.
DR PIR; A36163; A36163.
DR RefSeq; NP_034106.2; NM_009976.4.
DR AlphaFoldDB; P21460; -.
DR SMR; P21460; -.
DR BioGRID; 198955; 12.
DR IntAct; P21460; 3.
DR STRING; 10090.ENSMUSP00000028938; -.
DR MEROPS; I25.004; -.
DR GlyConnect; 2245; 8 N-Linked glycans (1 site).
DR GlyGen; P21460; 1 site, 8 N-linked glycans (1 site).
DR iPTMnet; P21460; -.
DR PhosphoSitePlus; P21460; -.
DR SwissPalm; P21460; -.
DR CPTAC; non-CPTAC-3702; -.
DR EPD; P21460; -.
DR MaxQB; P21460; -.
DR PaxDb; P21460; -.
DR PeptideAtlas; P21460; -.
DR PRIDE; P21460; -.
DR ProteomicsDB; 285407; -.
DR DNASU; 13010; -.
DR Ensembl; ENSMUST00000028938; ENSMUSP00000028938; ENSMUSG00000027447.
DR GeneID; 13010; -.
DR KEGG; mmu:13010; -.
DR UCSC; uc008mtt.1; mouse.
DR CTD; 1471; -.
DR MGI; MGI:102519; Cst3.
DR VEuPathDB; HostDB:ENSMUSG00000027447; -.
DR eggNOG; ENOG502SC50; Eukaryota.
DR GeneTree; ENSGT00940000154755; -.
DR InParanoid; P21460; -.
DR OMA; YTVPWLG; -.
DR OrthoDB; 1565344at2759; -.
DR PhylomeDB; P21460; -.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 13010; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Cst3; mouse.
DR PRO; PR:P21460; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P21460; protein.
DR Bgee; ENSMUSG00000027447; Expressed in skin of external ear and 266 other tissues.
DR ExpressionAtlas; P21460; baseline and differential.
DR Genevisible; P21460; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005604; C:basement membrane; ISO:MGI.
DR GO; GO:0042995; C:cell projection; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0043292; C:contractile fiber; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0005771; C:multivesicular body; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; ISO:MGI.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0030414; F:peptidase inhibitor activity; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:2000117; P:negative regulation of cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
DR GO; GO:0043067; P:regulation of programmed cell death; ISO:MGI.
DR GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
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 Disulfide bond; Protease inhibitor; Reference proteome; Secreted; Signal;
KW Thiol protease inhibitor.
FT SIGNAL 1..20
FT CHAIN 21..140
FT /note="Cystatin-C"
FT /id="PRO_0000006642"
FT MOTIF 75..79
FT /note="Secondary area of contact"
FT SITE 31
FT /note="Reactive site"
FT DISULFID 93..103
FT /evidence="ECO:0000250"
FT DISULFID 117..137
FT /evidence="ECO:0000250"
FT CONFLICT 16
FT /note="A -> G (in Ref. 1; AAA63298)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="L -> F (in Ref. 1; AAA63298)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 140 AA; 15531 MW; 3A563406DD58D0F5 CRC64;
MASPLRSLLF LLAVLAVAWA ATPKQGPRML GAPEEADANE EGVRRALDFA VSEYNKGSND
AYHSRAIQVV RARKQLVAGV NYFLDVEMGR TTCTKSQTNL TDCPFHDQPH LMRKALCSFQ
IYSVPWKGTH SLTKFSCKNA
