OST2B_ONCMY
ID OST2B_ONCMY Reviewed; 164 AA.
AC K9J977; P86868;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Osteocalcin 2b {ECO:0000312|EMBL:ACS32164.1};
DE Short=OmyOC2b {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=GSONMT00015798001 {ECO:0000312|EMBL:CDQ80774.1};
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:ACS32164.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION [MRNA], AND PROTEIN
RP SEQUENCE OF 116-128.
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:CDQ80774.1}
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; BK006866; DAA64604.1; -; mRNA.
DR EMBL; GQ241719; ACS32164.1; -; Genomic_DNA.
DR EMBL; FR905655; CDQ80774.1; -; Genomic_DNA.
DR AlphaFoldDB; K9J977; -.
DR SMR; K9J977; -.
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..115
FT /evidence="ECO:0000305|PubMed:24185858"
FT /id="PRO_0000436922"
FT CHAIN 116..164
FT /note="Osteocalcin 2b"
FT /evidence="ECO:0000305"
FT /id="PRO_5005921925"
FT DOMAIN 128..160
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT REGION 30..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02820"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 137
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P02820"
FT MOD_RES 130
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:Q800Y1"
FT MOD_RES 134
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 137
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT DISULFID 136..142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
SQ SEQUENCE 164 AA; 16406 MW; 80DDD5E8689213C6 CRC64;
MKSLTLLTIC AVLSVSLSMN DLALDVVLDP DPAAEPAPAA DSSASSSASS SSSSASDSSA
SASDSSDSDS SSSSSSSSSS ESASAEAMAE DPAAATEPEV IMKRDLASVL LRRKRAAGPA
AAAFTLTQVE SLSEVCELNL ACEHMAETAG IVAAYTAYYG PPPF
