Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005509 | molecular_function | calcium ion binding |
| G | 0005509 | molecular_function | calcium ion binding |
Functional Information from PROSITE/UniProt
| site_id | PS00010 |
| Number of Residues | 12 |
| Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. ChNylggYyCsC |
| Chain | Residue | Details |
| A | CYS137-CYS148 | |
| site_id | PS01186 |
| Number of Residues | 16 |
| Details | EGF_2 EGF-like domain signature 2. CsCrvGYilhqnkhtC |
| Chain | Residue | Details |
| A | CYS146-CYS161 | |
| site_id | PS01187 |
| Number of Residues | 28 |
| Details | EGF_CA Calcium-binding EGF-like domain signature. DvDECrtslgdsvp.....Cdhy....ChNylggYyC |
| Chain | Residue | Details |
| A | ASP119-CYS146 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | TYR55 | |
| G | GLY110 | |
| G | PHE111 | |
| G | VAL150 | |
| A | GLY63 | |
| A | PHE108 | |
| A | GLY110 | |
| A | PHE111 | |
| A | VAL150 | |
| G | TYR55 | |
| G | GLY63 | |
| G | PHE108 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | SER126 | |
| A | LEU127 | |
| A | SER147 | |
| G | SER126 | |
| G | LEU127 | |
| G | SER147 | |
| Chain | Residue | Details |
| A | CYS146 | |
| G | CYS146 | |
| Chain | Residue | Details |
| A | GLY91 | |
| G | GLY91 | |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | HIS273 | |
| G | HIS273 | |
