ID   Q8VEK8_MOUSE            Unreviewed;        93 AA.
AC   Q8VEK8;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   28-JUN-2023, entry version 96.
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|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}.
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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                   /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
//