CST10_MOUSE
ID CST10_MOUSE Reviewed; 148 AA.
AC Q9JM84; A2ART7;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Cystatin 10 {ECO:0000303|PubMed:13679380};
DE AltName: Full=Carminerin {ECO:0000303|PubMed:16680148};
DE Flags: Precursor;
GN Name=Cst10 {ECO:0000312|MGI:MGI:1930004};
GN Synonyms=DD72 {ECO:0000303|PubMed:11856874};
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] {ECO:0000312|EMBL:BAA95411.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INDUCTION
RP BY HIGH PHOSPHATE DIET.
RX PubMed=11856874; DOI=10.1159/000048809;
RA Koshizuka Y., Ikegawa S., Sano M., Nakamura K., Nakamura Y.;
RT "Isolation of novel mouse genes associated with ectopic ossification by
RT differential display method using ttw, a mouse model for ectopic
RT ossification.";
RL Cytogenet. Cell Genet. 94:163-168(2001).
RN [2] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000312|EMBL:AAH48364.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND INDUCTION BY HIGH PHOSPHATE DIET.
RX PubMed=13679380; DOI=10.1074/jbc.m211639200;
RA Koshizuka Y., Yamada T., Hoshi K., Ogasawara T., Chung U.I., Kawano H.,
RA Nakamura Y., Nakamura K., Ikegawa S., Kawaguchi H.;
RT "Cystatin 10, a novel chondrocyte-specific protein, may promote the last
RT steps of the chondrocyte differentiation pathway.";
RL J. Biol. Chem. 278:48259-48266(2003).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16680148; DOI=10.1038/nm1409;
RA Yamada T., Kawano H., Koshizuka Y., Fukuda T., Yoshimura K., Kamekura S.,
RA Saito T., Ikeda T., Kawasaki Y., Azuma Y., Ikegawa S., Hoshi K.,
RA Chung U.I., Nakamura K., Kato S., Kawaguchi H.;
RT "Carminerin contributes to chondrocyte calcification during endochondral
RT ossification.";
RL Nat. Med. 12:665-670(2006).
CC -!- FUNCTION: May play a role in the last steps of the chondrocyte
CC differentiation pathway as an inducer of maturation (PubMed:13679380).
CC Induces chondrocyte calcification during endochondral ossification by
CC playing a role in the transcriptional inhibition of ENPP1, a generator
CC of pyrophosphate which inhibits calcification (PubMed:16680148).
CC Possibly impairs the binding of a transcription factor to the ENPP1
CC promoter (PubMed:16680148). Unlike other cystatins, does not have thiol
CC protease inhibitor activity (PubMed:16680148).
CC {ECO:0000269|PubMed:13679380, ECO:0000269|PubMed:16680148}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:13679380}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9JM84-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JM84-2; Sequence=VSP_058422;
CC -!- TISSUE SPECIFICITY: In cartilage, expressed mainly in mature
CC chondrocytes including prehypertrophic and hypertrophic cells (at
CC protein level) (PubMed:13679380). Expressed exclusively in cartilage
CC (PubMed:11856874). {ECO:0000269|PubMed:11856874,
CC ECO:0000269|PubMed:13679380}.
CC -!- DEVELOPMENTAL STAGE: In maturing chondrocytes, expression appears at
CC day 3 and increases thereafter. {ECO:0000269|PubMed:13679380}.
CC -!- INDUCTION: By high phosphate diet. {ECO:0000269|PubMed:11856874,
CC ECO:0000269|PubMed:13679380}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Microscopic decrease in the
CC calcification of hypertrophic chondrocytes at the growth plate.
CC {ECO:0000269|PubMed:16680148}.
CC -!- SIMILARITY: Belongs to the cystatin family. {ECO:0000255,
CC ECO:0000255|RuleBase:RU362130}.
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DR EMBL; AB036743; BAA95411.1; -; mRNA.
DR EMBL; AL845478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC048364; AAH48364.1; -; mRNA.
DR CCDS; CCDS16853.1; -. [Q9JM84-1]
DR RefSeq; NP_067380.1; NM_021405.2. [Q9JM84-1]
DR AlphaFoldDB; Q9JM84; -.
DR SMR; Q9JM84; -.
DR STRING; 10090.ENSMUSP00000043520; -.
DR PaxDb; Q9JM84; -.
DR PRIDE; Q9JM84; -.
DR ProteomicsDB; 283964; -. [Q9JM84-1]
DR ProteomicsDB; 283965; -. [Q9JM84-2]
DR DNASU; 58214; -.
DR Ensembl; ENSMUST00000047008; ENSMUSP00000043520; ENSMUSG00000033156. [Q9JM84-1]
DR Ensembl; ENSMUST00000109938; ENSMUSP00000105564; ENSMUSG00000033156. [Q9JM84-1]
DR Ensembl; ENSMUST00000109939; ENSMUSP00000105565; ENSMUSG00000033156. [Q9JM84-2]
DR GeneID; 58214; -.
DR KEGG; mmu:58214; -.
DR UCSC; uc008mtu.1; mouse. [Q9JM84-1]
DR CTD; 58214; -.
DR MGI; MGI:1930004; Cst10.
DR VEuPathDB; HostDB:ENSMUSG00000033156; -.
DR eggNOG; ENOG502SC50; Eukaryota.
DR GeneTree; ENSGT00940000154755; -.
DR HOGENOM; CLU_118168_0_1_1; -.
DR InParanoid; Q9JM84; -.
DR OMA; LAFGFCQ; -.
DR OrthoDB; 1565344at2759; -.
DR PhylomeDB; Q9JM84; -.
DR BioGRID-ORCS; 58214; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q9JM84; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9JM84; protein.
DR Bgee; ENSMUSG00000033156; Expressed in parotid gland and 14 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; ISO:MGI.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0110148; P:biomineralization; IMP:MGI.
DR GO; GO:0060349; P:bone morphogenesis; IMP:MGI.
DR GO; GO:0055074; P:calcium ion homeostasis; IMP:MGI.
DR GO; GO:0048469; P:cell maturation; IDA:MGI.
DR GO; GO:0019725; P:cellular homeostasis; IMP:MGI.
DR GO; GO:0002062; P:chondrocyte differentiation; IDA:MGI.
DR GO; GO:0001958; P:endochondral ossification; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0003430; P:growth plate cartilage chondrocyte growth; IMP:MGI.
DR GO; GO:2000117; P:negative regulation of cysteine-type endopeptidase activity; IBA:GO_Central.
DR CDD; cd00042; CY; 1.
DR InterPro; IPR000010; Cystatin_dom.
DR InterPro; IPR046350; Cystatin_sf.
DR InterPro; IPR018073; Prot_inh_cystat_CS.
DR InterPro; IPR001713; Prot_inh_stefin.
DR Pfam; PF00031; Cystatin; 1.
DR PRINTS; PR00295; STEFINA.
DR SMART; SM00043; CY; 1.
DR SUPFAM; SSF54403; SSF54403; 1.
DR PROSITE; PS00287; CYSTATIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Biomineralization; Cytoplasm; Disulfide bond;
KW Reference proteome; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..148
FT /note="Cystatin 10"
FT /id="PRO_5006993922"
FT DOMAIN 36..148
FT /note="Cystatin kininogen-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00979"
FT DISULFID 101..111
FT /evidence="ECO:0000250|UniProtKB:P28325"
FT DISULFID 125..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00979"
FT VAR_SEQ 84..121
FT /note="Missing (in isoform 2)"
FT /id="VSP_058422"
SQ SEQUENCE 148 AA; 16451 MW; 637534CBFC5AA179 CRC64;
MASLLSPSMP VLAAVALTLT LAVIPEASTN AEAKQVVLGG VEPADPKDKE VQKVVKFAVR
TYNDMDNDLY LSKPIRLMSA SQQVVAGKNY YLKIELGRTT CTKTESNLVD CPFNEQPDQQ
KRVICNFQIN VAPWLNKMSM TNFNCYNF
