ID   MGP_MOUSE               Reviewed;         104 AA.
AC   P19788; Q6LD77; Q8JZW0;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   24-JAN-2024, entry version 166.
DE   RecName: Full=Matrix Gla protein;
DE            Short=MGP;
DE   Flags: Precursor;
GN   Name=Mgp; Synonyms=Mglap;
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=C57BL/6J;
RX   PubMed=1686347; DOI=10.1002/jbmr.5650060916;
RA   Ikeda T., Yamaguchi A., Icho T., Tsuchida N., Yoshiki S.;
RT   "cDNA and deduced amino acid sequence of mouse matrix gla protein: one of
RT   five glutamic acid residues potentially modified to gla is not conserved in
RT   the mouse sequence.";
RL   J. Bone Miner. Res. 6:1013-1017(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   PubMed=7754814; DOI=10.1002/jbmr.5650100221;
RA   Luo G., D'Souza R., Hogue D., Karsenty G.;
RT   "The matrix Gla protein gene is a marker of the chondrogenesis cell lineage
RT   during mouse development.";
RL   J. Bone Miner. Res. 10:325-334(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
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).
CC   -!- FUNCTION: Associates with the organic matrix of bone and cartilage.
CC       Thought to act as an inhibitor of bone formation.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: Requires vitamin K-dependent gamma-carboxylation for its function.
CC   -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC       {ECO:0000305}.
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DR   EMBL; D00613; BAA00488.1; -; mRNA.
DR   EMBL; S77350; AAP31997.1; -; Genomic_DNA.
DR   EMBL; AK018719; BAB31365.1; -; mRNA.
DR   EMBL; BC036991; AAH36991.1; -; mRNA.
DR   CCDS; CCDS20659.1; -.
DR   PIR; JQ0455; GEMSM1.
DR   RefSeq; NP_032623.1; NM_008597.4.
DR   AlphaFoldDB; P19788; -.
DR   SMR; P19788; -.
DR   BioGRID; 201414; 18.
DR   IntAct; P19788; 17.
DR   STRING; 10090.ENSMUSP00000032342; -.
DR   PhosphoSitePlus; P19788; -.
DR   MaxQB; P19788; -.
DR   PaxDb; 10090-ENSMUSP00000032342; -.
DR   PeptideAtlas; P19788; -.
DR   ProteomicsDB; 295564; -.
DR   Pumba; P19788; -.
DR   Antibodypedia; 2842; 349 antibodies from 30 providers.
DR   DNASU; 17313; -.
DR   Ensembl; ENSMUST00000032342.3; ENSMUSP00000032342.2; ENSMUSG00000030218.3.
DR   GeneID; 17313; -.
DR   KEGG; mmu:17313; -.
DR   UCSC; uc009eml.1; mouse.
DR   AGR; MGI:96976; -.
DR   CTD; 4256; -.
DR   MGI; MGI:96976; Mgp.
DR   VEuPathDB; HostDB:ENSMUSG00000030218; -.
DR   eggNOG; ENOG502S45A; Eukaryota.
DR   GeneTree; ENSGT00390000003753; -.
DR   HOGENOM; CLU_177119_1_0_1; -.
DR   InParanoid; P19788; -.
DR   OMA; NANTFMS; -.
DR   OrthoDB; 3885479at2759; -.
DR   PhylomeDB; P19788; -.
DR   TreeFam; TF330920; -.
DR   BioGRID-ORCS; 17313; 1 hit in 78 CRISPR screens.
DR   ChiTaRS; Mgp; mouse.
DR   PRO; PR:P19788; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; P19788; Protein.
DR   Bgee; ENSMUSG00000030218; Expressed in aorta tunica media and 260 other cell types or tissues.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR   GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR   GO; GO:0048754; P:branching morphogenesis of an epithelial tube; ISO:MGI.
DR   GO; GO:0051216; P:cartilage development; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0030324; P:lung development; ISO:MGI.
DR   GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR   GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
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.
DR   Genevisible; P19788; MM.
PE   3: Inferred from homology;
KW   Chondrogenesis; Developmental protein; Differentiation; Disulfide bond;
KW   Gamma-carboxyglutamic acid; Osteogenesis; Phosphoprotein;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT   CHAIN           20..104
FT                   /note="Matrix Gla protein"
FT                   /id="PRO_0000011111"
FT   DOMAIN          51..97
FT                   /note="Gla"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         21
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07507,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         22
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P07507"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P07507"
FT   MOD_RES         28
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P07507"
FT   MOD_RES         60
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07507,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         67
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07507,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         71
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07507,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   DISULFID        73..79
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT   CONFLICT        25
FT                   /note="S -> I (in Ref. 2; AAP31997)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        103
FT                   /note="K -> R (in Ref. 4; AAH36991)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   104 AA;  12359 MW;  9056F6D47ABF3413 CRC64;
     MKSLLPLAIL AALAVATLCY ESHESMESYE ISPFINRRNA NTFMSPQQRW RAKAQKRVQE
     RNKPAYEINR EACDDYKLCE RYAMVYGYNA AYNRYFRQRR GAKY
//