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OSTC2_SOLSE
ID   OSTC2_SOLSE             Reviewed;          46 AA.
AC   P86863; P86864;
DT   07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT   07-SEP-2016, sequence version 1.
DT   03-AUG-2022, entry version 9.
DE   RecName: Full=Osteocalcin 2 {ECO:0000303|PubMed:24185858};
DE            Short=SseOC2 {ECO:0000303|PubMed:24185858};
DE   AltName: Full=Bone Gla protein {ECO:0000303|PubMed:24185858};
DE            Short=BGP {ECO:0000250|UniProtKB:Q800Y1};
DE   AltName: Full=Gamma-carboxyglutamic acid-containing protein {ECO:0000250|UniProtKB:Q800Y1};
GN   Name=bglap2 {ECO:0000305};
OS   Solea senegalensis (Senegalese sole).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Soleidae; Solea.
OX   NCBI_TaxID=28829 {ECO:0000303|PubMed:24185858};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND PHOSPHORYLATION AT THR-6.
RC   TISSUE=Bone {ECO:0000303|PubMed:24185858};
RX   PubMed=24185858; DOI=10.1007/s10695-013-9880-9;
RA   Cavaco S., Williamson M.K., Rosa J., Roberto V., Cordeiro O., Price P.A.,
RA   Leonor Cancela M., Laize V., Simes D.C.;
RT   "Teleost fish osteocalcin 1 and 2 share the ability to bind the calcium
RT   mineral phase.";
RL   Fish Physiol. Biochem. 40:731-738(2014).
CC   -!- FUNCTION: Binds strongly to apatite and calcium. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent
CC       carboxylation. These residues are essential for the binding of calcium.
CC       {ECO:0000255|PROSITE-ProRule:PRU00463}.
CC   -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC       {ECO:0000305}.
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DR   iPTMnet; P86863; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR   GO; GO:0060348; P:bone development; IEA:InterPro.
DR   GO; GO:0030500; P:regulation of bone mineralization; IEA:InterPro.
DR   GO; GO:1900076; P:regulation of cellular response to insulin stimulus; IEA:InterPro.
DR   GO; GO:0032571; P:response to vitamin K; IEA:InterPro.
DR   InterPro; IPR035972; GLA-like_dom_SF.
DR   InterPro; IPR000294; GLA_domain.
DR   InterPro; IPR039176; Osteocalcin.
DR   InterPro; IPR002384; Osteocalcin/MGP.
DR   PANTHER; PTHR14235; PTHR14235; 1.
DR   PRINTS; PR00002; GLABONE.
DR   SUPFAM; SSF57630; SSF57630; 1.
DR   PROSITE; PS00011; GLA_1; 1.
DR   PROSITE; PS50998; GLA_2; 1.
PE   1: Evidence at protein level;
KW   Biomineralization; Calcium; Direct protein sequencing; Disulfide bond;
KW   Gamma-carboxyglutamic acid; Metal-binding; Phosphoprotein; Secreted.
FT   CHAIN           1..46
FT                   /note="Osteocalcin 2"
FT                   /evidence="ECO:0000269|PubMed:24185858"
FT                   /id="PRO_0000436924"
FT   DOMAIN          1..43
FT                   /note="Gla"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT   BINDING         13
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02820"
FT   BINDING         17
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P02820"
FT   BINDING         20
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P02820"
FT   BINDING         20
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P02820"
FT   BINDING         26
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P02820"
FT   MOD_RES         6
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000303|PubMed:24185858"
FT   MOD_RES         13
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:Q800Y1"
FT   MOD_RES         17
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         20
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         27
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:Q800Y1"
FT   DISULFID        19..25
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
SQ   SEQUENCE   46 AA;  4799 MW;  A73876C40A181EF6 CRC64;
     AVPAGTLSPL QMESLREVCE VNVACDEMAD TAGIVAAYTX FYGPVP
 
 
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