ID Q8VEK8_MOUSE Unreviewed; 93 AA. AC Q8VEK8; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 08-NOV-2023, entry version 98. DE RecName: Full=Matrix Gla protein {ECO:0000256|ARBA:ARBA00017145, ECO:0000256|RuleBase:RU361261}; DE Short=MGP {ECO:0000256|RuleBase:RU361261}; DE Flags: Fragment; GN Name=Mgp {ECO:0000313|EMBL:AAH18338.1, ECO:0000313|MGI:MGI:96976}; GN Synonyms=Mglap {ECO:0000313|MGI:MGI:96976}; 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 {ECO:0000313|EMBL:AAH18338.1}; RN [1] {ECO:0000313|EMBL:AAH18338.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N {ECO:0000313|EMBL:AAH18338.1}; RC TISSUE=Mammary tumor. Metallothionien-TGF alpha model. 10 month old RC virgin mouse. Taken by biopsy. {ECO:0000313|EMBL:AAH18338.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; 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). CC -!- FUNCTION: Associates with the organic matrix of bone and cartilage. CC Thought to act as an inhibitor of bone formation. CC {ECO:0000256|ARBA:ARBA00025316}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613, CC ECO:0000256|RuleBase:RU361261}. CC -!- PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent CC carboxylation. These residues are essential for the binding of calcium. CC {ECO:0000256|PIRSR:PIRSR602384-3}. CC -!- PTM: Requires vitamin K-dependent gamma-carboxylation for its function. CC {ECO:0000256|RuleBase:RU361261}. CC -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family. CC {ECO:0000256|ARBA:ARBA00008850, ECO:0000256|RuleBase:RU361261}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC018338; AAH18338.1; -; mRNA. DR AlphaFoldDB; Q8VEK8; -. DR AGR; MGI:96976; -. DR MGI; MGI:96976; Mgp. DR ChiTaRS; Mgp; mouse. DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0051216; P:cartilage development; IEA:UniProtKB-KW. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW. DR GO; GO:0030500; P:regulation of bone mineralization; IEA:InterPro. DR InterPro; IPR035972; GLA-like_dom_SF. DR InterPro; IPR000294; GLA_domain. DR InterPro; IPR027118; MGP. DR InterPro; IPR002384; Osteocalcin/MGP. DR PANTHER; PTHR10109; MATRIX GLA PROTEIN; 1. DR PANTHER; PTHR10109:SF0; MATRIX GLA PROTEIN; 1. DR PRINTS; PR00002; GLABONE. DR SMART; SM00069; GLA; 1. DR SUPFAM; SSF57630; GLA-domain; 1. DR PROSITE; PS00011; GLA_1; 1. DR PROSITE; PS50998; GLA_2; 1. PE 2: Evidence at transcript level; KW Calcium {ECO:0000256|PIRSR:PIRSR602384-1}; KW Chondrogenesis {ECO:0000256|ARBA:ARBA00023188}; KW Developmental protein {ECO:0000256|ARBA:ARBA00022473}; KW Differentiation {ECO:0000256|ARBA:ARBA00022782}; KW Disulfide bond {ECO:0000256|PIRSR:PIRSR602384-2}; KW Gamma-carboxyglutamic acid {ECO:0000256|PIRSR:PIRSR602384-3, KW ECO:0000256|RuleBase:RU361261}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR602384-1}; KW Osteogenesis {ECO:0000256|ARBA:ARBA00022855}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Secreted {ECO:0000256|RuleBase:RU361261}. FT DOMAIN 56..86 FT /note="Gla" FT /evidence="ECO:0000259|PROSITE:PS50998" FT BINDING 60 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR602384-1" FT MOD_RES 60 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000256|PIRSR:PIRSR602384-3" FT DISULFID 62..68 FT /evidence="ECO:0000256|PIRSR:PIRSR602384-2" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAH18338.1" SQ SEQUENCE 93 AA; 11236 MW; 0BC6BA44A0141AE1 CRC64; ALAVATLCYE SHESMESYEI SPFINRRNAN TFMSPQQRWR AKAQKRVQER NKPAYEINRE ACDDYKLCER YAMVYGYNAA YNRYFRQRRG ARY //