ID   MGP_GALGA               Reviewed;         102 AA.
AC   P56620;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Matrix Gla protein;
DE            Short=MGP;
GN   Name=mgp;
OS   Galeorhinus galeus (Tope shark) (Galeorhinus australis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Triakidae;
OC   Galeorhinus.
OX   NCBI_TaxID=86063;
RN   [1]
RP   PROTEIN SEQUENCE, AND GAMMA-CARBOXYGLUTAMATION AT GLU-43; GLU-47; GLU-50
RP   AND GLU-51.
RC   TISSUE=Cartilage;
RX   PubMed=8030445; DOI=10.1002/jbmr.5650090417;
RA   Rice J.S., Williamson M.K., Price P.A.;
RT   "Isolation and sequence of the vitamin K-dependent matrix Gla protein from
RT   the calcified cartilage of the soupfin shark.";
RL   J. Bone Miner. Res. 9:567-576(1994).
RN   [2]
RP   PHOSPHORYLATION AT SER-2; SER-3 AND SER-5.
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 calcified cartilage.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Accounts for 35-40% of the total protein in the
CC       acid demineralization extract of calcified cartilage.
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   AlphaFoldDB; P56620; -.
DR   SMR; P56620; -.
DR   iPTMnet; P56620; -.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
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   1: Evidence at protein level;
KW   Chondrogenesis; Developmental protein; Differentiation;
KW   Direct protein sequencing; Disulfide bond; Gamma-carboxyglutamic acid;
KW   Osteogenesis; Phosphoprotein; Secreted.
FT   CHAIN           1..102
FT                   /note="Matrix Gla protein"
FT                   /id="PRO_0000148912"
FT   DOMAIN          27..73
FT                   /note="Gla"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT   REGION          18..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          72..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..102
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:8061611"
FT   MOD_RES         3
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:8061611"
FT   MOD_RES         5
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:8061611"
FT   MOD_RES         43
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:8030445"
FT   MOD_RES         47
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:8030445"
FT   MOD_RES         50
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:8030445"
FT   MOD_RES         51
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:8030445"
FT   DISULFID        49..55
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
SQ   SEQUENCE   102 AA;  12565 MW;  BFE722363DA13851 CRC64;
     DSSESNEIED VLFLGRQDAN SFMRQPRPPN HWDSRDRFKS PRERTREKCE EYRPCERLAR
     QVGLKRAYGK YFGNRRQRPS TSGRLRPRKY RASRYRNHHY RY