MGP_MOUSE
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 03-AUG-2022, entry version 158.
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; 17.
DR IntAct; P19788; 17.
DR STRING; 10090.ENSMUSP00000032342; -.
DR PhosphoSitePlus; P19788; -.
DR MaxQB; P19788; -.
DR PaxDb; P19788; -.
DR PeptideAtlas; P19788; -.
DR PRIDE; P19788; -.
DR ProteomicsDB; 295564; -.
DR Antibodypedia; 2842; 307 antibodies from 30 providers.
DR DNASU; 17313; -.
DR Ensembl; ENSMUST00000032342; ENSMUSP00000032342; ENSMUSG00000030218.
DR GeneID; 17313; -.
DR KEGG; mmu:17313; -.
DR UCSC; uc009eml.1; mouse.
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; MESYEIN; -.
DR OrthoDB; 1512503at2759; -.
DR PhylomeDB; P19788; -.
DR TreeFam; TF330920; -.
DR BioGRID-ORCS; 17313; 1 hit in 73 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 258 other tissues.
DR Genevisible; P19788; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; 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; PTHR10109; 1.
DR PRINTS; PR00002; GLABONE.
DR SMART; SM00069; GLA; 1.
DR SUPFAM; SSF57630; SSF57630; 1.
DR PROSITE; PS00011; GLA_1; 1.
DR PROSITE; PS50998; GLA_2; 1.
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
