Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005788 | cellular_component | endoplasmic reticulum lumen |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0007596 | biological_process | blood coagulation |
| A | 0008289 | molecular_function | lipid binding |
| A | 0008488 | molecular_function | gamma-glutamyl carboxylase activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016829 | molecular_function | lyase activity |
| A | 0017187 | biological_process | peptidyl-glutamic acid carboxylation |
| A | 0019842 | molecular_function | vitamin binding |
| A | 0036211 | biological_process | protein modification process |
| A | 0042373 | biological_process | vitamin K metabolic process |
| A | 0046929 | biological_process | negative regulation of neurotransmitter secretion |
| A | 0051604 | biological_process | protein maturation |
| A | 1903011 | biological_process | negative regulation of bone development |
| A | 2000225 | biological_process | negative regulation of testosterone biosynthetic process |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0030500 | biological_process | regulation of bone mineralization |
| B | 0032571 | biological_process | response to vitamin K |
| B | 0060348 | biological_process | bone development |
| B | 1900076 | biological_process | regulation of cellular response to insulin stimulus |
Functional Information from PROSITE/UniProt
| site_id | PS00011 |
| Number of Residues | 26 |
| Details | GLA_1 Vitamin K-dependent carboxylation domain. EprREvCelnpdcDeladhigfqe.AY |
| Chain | Residue | Details |
| B | GLU68-TYR93 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 100 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 165 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17073445","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P02820","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
