OST2A_ONCMY
ID OST2A_ONCMY Reviewed; 167 AA.
AC A0A024QYT3; K9J9B5; P86869;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Osteocalcin 2a {ECO:0000312|EMBL:DAA64603.1};
DE Short=OmyOC2a {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};
DE Flags: Precursor;
GN ORFNames=GSONMT00044887001 {ECO:0000312|EMBL:CDQ79800.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000312|EMBL:DAA64603.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION [MRNA], AND PROTEIN
RP SEQUENCE OF 119-131.
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).
RN [2] {ECO:0000312|EMBL:CDQ79800.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24755649; DOI=10.1038/ncomms4657;
RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA Guiguen Y.;
RT "The rainbow trout genome provides novel insights into evolution after
RT whole-genome duplication in vertebrates.";
RL Nat. Commun. 5:3657-3657(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 EMBL; BK006865; DAA64603.1; -; mRNA.
DR EMBL; FR905504; CDQ79800.1; -; Genomic_DNA.
DR EMBL; GQ241718; ACS32163.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024QYT3; -.
DR SMR; A0A024QYT3; -.
DR Ensembl; ENSOMYT00000070078; ENSOMYP00000064382; ENSOMYG00000029798.
DR GeneTree; ENSGT00710000107036; -.
DR OrthoDB; 1520921at2759; -.
DR Proteomes; UP000193380; Unassembled WGS sequence.
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: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 PANTHER; PTHR14235; PTHR14235; 1.
DR SUPFAM; SSF57630; SSF57630; 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; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..118
FT /evidence="ECO:0000305|PubMed:24185858"
FT /id="PRO_0000436921"
FT CHAIN 119..167
FT /note="Osteocalcin 2a"
FT /evidence="ECO:0000305"
FT /id="PRO_5005739342"
FT DOMAIN 131..163
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT REGION 28..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P02820"
FT BINDING 137
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02820"
FT BINDING 140
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02820"
FT BINDING 140
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02820"
FT MOD_RES 133
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:Q800Y1"
FT MOD_RES 137
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 140
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT DISULFID 139..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT CONFLICT 90
FT /note="T -> M (in Ref. 1; ACS32163)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 167 AA; 16746 MW; CD3766D988C926EB CRC64;
MKSLTLLTIC AVLSVSLSMN DLALDVVLDP APDPATEPAP AADSSASSSA SSSSSSASDS
SASASDSSDS DSSSASSSSS SSESASAEVT TEDPAAATEP EVVIMKRDLA SVLLRRKRAA
GQAAAAFTLT QVESLSEVCE LNLACEHMAE TAGIVAAYTA YYGPPPF
