MGP_BOVIN
ID MGP_BOVIN Reviewed; 103 AA.
AC P07507; Q54A30;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Matrix Gla protein;
DE Short=MGP;
DE Contains:
DE RecName: Full=Matrix Gla protein long form;
DE Contains:
DE RecName: Full=Matrix Gla protein short form;
DE Flags: Precursor;
GN Name=MGP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3387234; DOI=10.1093/nar/16.11.5213;
RA Kiefer M.C., Bauer D.M., Young D., Hermsen K.M., Masiarz F.K., Barr P.J.;
RT "The cDNA and derived amino acid sequences for human and bovine matrix Gla
RT protein.";
RL Nucleic Acids Res. 16:5213-5213(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chapman K.L., Newman B., Freemont A.J., Hillarby M.C., Grant M.E.,
RA Boot-Handford R.P., Wallis G.A.;
RT "Differential expression of matrix Gla protein, alpha enolase, and annexin
RT V within the epiphyseal growth plate and in human osteoarthritic tissue.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12658628; DOI=10.1002/mrd.10292;
RA Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H., Takahashi T.,
RA Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y., Tsujimoto G.,
RA Izaike Y., Todoroki J., Hashizume K.;
RT "Characterization of gene expression profiles in early bovine pregnancy
RT using a custom cDNA microarray.";
RL Mol. Reprod. Dev. 65:9-18(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 20-98, AND GAMMA-CARBOXYGLUTAMATION AT GLU-21; GLU-56;
RP GLU-60; GLU-67 AND GLU-71.
RX PubMed=3877721; DOI=10.1016/s0021-9258(18)95688-7;
RA Price P.A., Williamson M.K.;
RT "Primary structure of bovine matrix Gla protein, a new vitamin K-dependent
RT bone protein.";
RL J. Biol. Chem. 260:14971-14975(1985).
RN [6]
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).
RN [7]
RP PARTIAL PROTEIN SEQUENCE, AND PROTEOLYTIC PROCESSING OF C-TERMINAL.
RX PubMed=1939157; DOI=10.1016/s0021-9258(18)54832-8;
RA Hale J.E., Williamson M.K., Price P.A.;
RT "Carboxyl-terminal proteolytic processing of matrix Gla protein.";
RL J. Biol. Chem. 266:21145-21149(1991).
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; X07363; CAA30288.1; -; mRNA.
DR EMBL; AF210379; AAF25880.1; -; mRNA.
DR EMBL; AB098895; BAC56385.1; -; mRNA.
DR EMBL; BC102587; AAI02588.1; -; mRNA.
DR PIR; S01232; GEBOM.
DR RefSeq; NP_777132.1; NM_174707.3.
DR AlphaFoldDB; P07507; -.
DR SMR; P07507; -.
DR iPTMnet; P07507; -.
DR PRIDE; P07507; -.
DR GeneID; 282660; -.
DR KEGG; bta:282660; -.
DR CTD; 4256; -.
DR InParanoid; P07507; -.
DR OrthoDB; 1512503at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; 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;
KW Direct protein sequencing; Disulfide bond; Gamma-carboxyglutamic acid;
KW Osteogenesis; Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:3877721"
FT CHAIN 20..102
FT /note="Matrix Gla protein long form"
FT /evidence="ECO:0000269|PubMed:1939157"
FT /id="PRO_0000011104"
FT CHAIN 20..98
FT /note="Matrix Gla protein short form"
FT /evidence="ECO:0000269|PubMed:1939157"
FT /id="PRO_0000011105"
FT PROPEP 99..102
FT /note="Removed in short form; probably by carboxypeptidase
FT N"
FT /id="PRO_0000011106"
FT PROPEP 103
FT /note="Removed in long form; probably by carboxypeptidase
FT H"
FT /id="PRO_0000011107"
FT DOMAIN 51..97
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 21
FT /note="4-carboxyglutamate; partial"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3877721"
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:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3877721"
FT MOD_RES 60
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3877721"
FT MOD_RES 67
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3877721"
FT MOD_RES 71
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3877721"
FT DISULFID 73..79
SQ SEQUENCE 103 AA; 12217 MW; 86A89984F92BF38A CRC64;
MKSLLLLSIL AALAVAALCY ESHESLESYE INPFINRRNA NSFISPQQRW RAKAQERIRE
LNKPQYELNR EACDDFKLCE RYAMVYGYNA AYDRYFRQRR GAK
