MGP_RAT
ID MGP_RAT Reviewed; 103 AA.
AC P08494;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Matrix Gla protein;
DE Short=MGP;
DE Flags: Precursor;
GN Name=Mgp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3317405; DOI=10.1073/pnas.84.23.8335;
RA Price P.A., Fraser J.D., Metz-Virca G.;
RT "Molecular cloning of matrix Gla protein: implications for substrate
RT recognition by the vitamin K-dependent gamma-carboxylase.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:8335-8339(1987).
RN [2]
RP PHOSPHORYLATION AT SER-22; SER-25 AND SER-28.
RX PubMed=8061611; DOI=10.1002/pro.5560030511;
RA Price P.A., Rice J.S., Williamson M.K.;
RT "Conserved phosphorylation of serines in the Ser-X-Glu/Ser(P) sequences of
RT the vitamin K-dependent matrix Gla protein from shark, lamb, rat, cow, and
RT human.";
RL Protein Sci. 3:822-830(1994).
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; J03026; AAA41597.1; -; mRNA.
DR PIR; A39974; GERTM1.
DR RefSeq; NP_036994.1; NM_012862.1.
DR AlphaFoldDB; P08494; -.
DR SMR; P08494; -.
DR STRING; 10116.ENSRNOP00000007577; -.
DR iPTMnet; P08494; -.
DR PhosphoSitePlus; P08494; -.
DR PaxDb; P08494; -.
DR GeneID; 25333; -.
DR KEGG; rno:25333; -.
DR UCSC; RGD:3088; rat.
DR CTD; 4256; -.
DR RGD; 3088; Mgp.
DR eggNOG; ENOG502S45A; Eukaryota.
DR InParanoid; P08494; -.
DR OrthoDB; 1512503at2759; -.
DR PhylomeDB; P08494; -.
DR PRO; PR:P08494; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0005509; F:calcium ion binding; IDA:RGD.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:RGD.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:RGD.
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; IMP:RGD.
DR GO; GO:0001503; P:ossification; IEP:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; IPI:RGD.
DR GO; GO:0030500; P:regulation of bone mineralization; IEA:InterPro.
DR GO; GO:0051592; P:response to calcium ion; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0009725; P:response to hormone; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
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 1: Evidence at protein level;
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..103
FT /note="Matrix Gla protein"
FT /id="PRO_0000011116"
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:0000269|PubMed:8061611"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8061611"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8061611"
FT MOD_RES 56
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P07507,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
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"
SQ SEQUENCE 103 AA; 12037 MW; F93536D35F48A5C7 CRC64;
MKSLLPLAIL AALAVAALCY ESHESMESYE VSPFTTRRNA NTFISPQQRW HAKAQERVRE
LNKPAQEINR EACDDYKLCE RYALIYGYNA AYNRYFRQRR GAK
