MGP_CHICK
ID MGP_CHICK Reviewed; 103 AA.
AC O42413;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Matrix Gla protein;
DE Short=MGP;
DE Flags: Precursor;
GN Name=MGP;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cartilage;
RX PubMed=9434150; DOI=10.1016/s0167-4781(97)00155-3;
RA Wiedemann M., Trueb B., Belluoccio D.;
RT "Molecular cloning of avian matrix Gla protein.";
RL Biochim. Biophys. Acta 1395:47-49(1998).
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 -!- TISSUE SPECIFICITY: In 16-day-old embryo, expressed at high level in
CC the sternum and tibia, at low level in skeletal muscle, heart and
CC gizzard. Not present in skin, liver and brain.
CC -!- PTM: Requires vitamin K-dependent gamma-carboxylation for its function.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC {ECO:0000305}.
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DR EMBL; Y13903; CAA74201.1; -; mRNA.
DR RefSeq; NP_990375.1; NM_205044.1.
DR AlphaFoldDB; O42413; -.
DR SMR; O42413; -.
DR STRING; 9031.ENSGALP00000019149; -.
DR PaxDb; O42413; -.
DR Ensembl; ENSGALT00000019173; ENSGALP00000019149; ENSGALG00000011740.
DR GeneID; 395912; -.
DR KEGG; gga:395912; -.
DR CTD; 4256; -.
DR VEuPathDB; HostDB:geneid_395912; -.
DR eggNOG; ENOG502S45A; Eukaryota.
DR GeneTree; ENSGT00390000003753; -.
DR HOGENOM; CLU_177119_1_0_1; -.
DR InParanoid; O42413; -.
DR OMA; MESYEIN; -.
DR OrthoDB; 1512503at2759; -.
DR PhylomeDB; O42413; -.
DR TreeFam; TF330920; -.
DR PRO; PR:O42413; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000011740; Expressed in lung and 9 other tissues.
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 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; PS00011; GLA_1; 1.
DR PROSITE; PS50998; GLA_2; 1.
PE 2: Evidence at transcript level;
KW Chondrogenesis; Developmental protein; Differentiation; Disulfide bond;
KW Gamma-carboxyglutamic acid; Osteogenesis; Phosphoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..103
FT /note="Matrix Gla protein"
FT /id="PRO_0000011117"
FT DOMAIN 52..98
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 MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 57
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 61
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 68
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 72
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT DISULFID 74..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
SQ SEQUENCE 103 AA; 12266 MW; 2BD458980F85047C CRC64;
MRALIVLVLL AVLVMAATCY ESHESMESHE YLNPFLNRQR ANGFIRDDTG LRAVLQERIR
ERNKAPQERQ REICEDFHLC EQYALNHGYP AAYRHYFGRR RNK