MGP_ARGRE
ID MGP_ARGRE Reviewed; 118 AA.
AC Q800Y2;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Matrix Gla protein;
DE Short=MGP;
DE Flags: Precursor;
GN Name=mgp;
OS Argyrosomus regius (Meagre).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Sciaenidae; Argyrosomus.
OX NCBI_TaxID=172269;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAO48723.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-56, TISSUE SPECIFICITY,
RP AND PHOSPHORYLATION AT SER-22; SER-25; SER-26 AND SER-28.
RC TISSUE=Cartilage {ECO:0000269|PubMed:12568402}, and
RC Kidney {ECO:0000269|PubMed:12568402};
RX PubMed=12568402; DOI=10.1359/jbmr.2003.18.2.244;
RA Simes D.C., Williamson M.K., Ortiz-Delgado J.B., Viegas C.S., Price P.A.,
RA Cancela M.L.;
RT "Purification of matrix Gla protein from a marine teleost fish, Argyrosomus
RT regius: calcified cartilage and not bone as the primary site of MGP
RT accumulation in fish.";
RL J. Bone Miner. Res. 18:244-259(2003).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 20-48, AND GAMMA-CARBOXYGLUTAMATION AT GLU-21.
RC TISSUE=Cartilage;
RX PubMed=14668966; DOI=10.1007/s00223-003-0079-4;
RA Simes D.C., Williamson M.K., Schaff B.J., Gavaia P.J., Ingleton P.M.,
RA Price P.A., Cancela M.L.;
RT "Characterization of osteocalcin (BGP) and matrix Gla protein (MGP) fish
RT specific antibodies: validation for immunodetection studies in lower
RT vertebrates.";
RL Calcif. Tissue Int. 74:170-180(2004).
CC -!- FUNCTION: Associates with the organic matrix of calcified cartilage.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, calcified cartilage (branchial
CC arches), vertebra, gills and kidney. Within the gills, MGP is found
CC mainly in the proliferating chondrocytes and the pericellular cartilage
CC matrix in the incipient calcified cartilage of branchial arches and
CC filaments. {ECO:0000269|PubMed:12568402}.
CC -!- PTM: Requires vitamin K-dependent gamma-carboxylation for its function.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC {ECO:0000305}.
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DR EMBL; AF334473; AAO48723.1; -; mRNA.
DR AlphaFoldDB; Q800Y2; -.
DR SMR; Q800Y2; -.
DR iPTMnet; Q800Y2; -.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:UniProtKB.
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:0030502; P:negative regulation of bone mineralization; TAS:UniProtKB.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR InterPro; IPR035972; GLA-like_dom_SF.
DR InterPro; IPR000294; GLA_domain.
DR InterPro; IPR027118; MGP.
DR PANTHER; PTHR10109; PTHR10109; 1.
DR SMART; SM00069; GLA; 1.
DR SUPFAM; SSF57630; SSF57630; 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; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:12568402,
FT ECO:0000269|PubMed:14668966"
FT CHAIN 20..118
FT /note="Matrix Gla protein"
FT /id="PRO_0000011118"
FT DOMAIN 56..102
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 21
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:14668966"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12568402"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12568402"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12568402"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12568402"
FT MOD_RES 72
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P56620,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 76
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P56620,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 79
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P56620,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT DISULFID 78..84
FT /evidence="ECO:0000250|UniProtKB:P07507,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT CONFLICT 54
FT /note="P -> G (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 118 AA; 13393 MW; F3FCDC36DD8FB09B CRC64;
MRSLLQFLAL SAAIALCVCY ESHESSESAE DLFVPPQQAN SFMTPQRGNA YSPPRGNGNN
FNLMRTVKSP AERRAETCED YSPCRFYAYR HGFQQAYQRY FGSGTHPQQR PAAAARRY
