| General information | | DisProt: | DP00116 | | Name: | Osteocalcin | | Synonym(s): | OSTCN_CANFA
Gamma-carboxyglutamic acid-containing protein
Bone Gla protein
BGP
| | First appeared in release: | Release 1.0 (08/01/2003) | | UniProt: | P81455 | | UniGene: | | | SwissProt: | OSTCN_CANFA | | TrEMBL: | | | NCBI (GI): | 3914247 | | Source organism: | Canis familiaris (dog) | | Sequence length: | 49 | | Percent disordered: | 100% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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YLDSGLGAPV PYPDPLEPKR EVCELNPNCD ELADHIGFQE AYQRFYGPV
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| Functional narrative |
Osteocalcin, a secreted protein, interacts with vitamin K and hydroxyapatite to bind calcium. This complex is involved with bone calcification. Osteocalcin is a member of the osteocalcin / matrix Gla-protein family. Levels of osteocalcin are thought to be associated with bone density.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered - Extended | | Name: | | | Location: | 1 - 49 | | Length: | 49 | | Region sequence: |
YLDSGLGAPVPYPDPLEPKREVCELNPNCDELADHIGFQEAYQRFYGPV | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Substrate/ligand binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 6.8; calcium chloride (buffer) 5 mM; imidazole (buffer) 30 mM; sodium chloride (buffer) 20 mM)
- Size exclusion/gel filtration chromatography (298 K; pH: 6.8; calcium chloride (buffer) 5 mM; imidazole (buffer) 30 mM; sodium chloride (buffer) 20 mM)
| References:
- Colombo G, Fanti P, Yao C, Malluche HH. "Isolation and complete amino acid sequence of osteocalcin from canine bone." J Bone Miner Res. 1993; 8(6): 733-43. PubMed: 8101026
- Isbell DT, Du S, Schroering AG, Colombo G, Shelling JG. "Metal ion binding to dog osteocalcin studied by 1H NMR spectroscopy." Biochemistry. 1993; 32(42): 11352-11362. PubMed: 8218200
| Comments:
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| Comments |
This protein is only disordered in the absence of calcium. When calcium is present, the conformation dramatically changes to a more ordered state.
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