Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005509 | molecular_function | calcium ion binding |
| B | 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. ChNyiggYyCsC |
| Chain | Residue | Details |
| A | CYS138-CYS149 | |
| site_id | PS01186 |
| Number of Residues | 16 |
| Details | EGF_2 EGF-like domain signature 2. CsCrfGYilhtdnrtC |
| Chain | Residue | Details |
| A | CYS147-CYS162 | |
| site_id | PS01187 |
| Number of Residues | 28 |
| Details | EGF_CA Calcium-binding EGF-like domain signature. DvDECkeredeels.....Cdhy....ChNyiggYyC |
| Chain | Residue | Details |
| A | ASP120-CYS147 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLU49 | |
| A | GLY144 | |
| A | GLU216 | |
| A | ASP226 | |
| A | ASP263 | |
| A | SER265 | |
| B | GLU49 | |
| B | ASP57 | |
| B | ASP102 | |
| B | SER104 | |
| B | ASP120 | |
| A | ASP57 | |
| B | VAL121 | |
| B | GLU123 | |
| B | ASN140 | |
| B | TYR141 | |
| B | GLY144 | |
| B | GLU216 | |
| B | ASP226 | |
| B | ASP263 | |
| B | SER265 | |
| A | ASP102 | |
| A | SER104 | |
| A | ASP120 | |
| A | VAL121 | |
| A | GLU123 | |
| A | ASN140 | |
| A | TYR141 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: (3R)-3-hydroxyasparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN140 | |
| B | ASN140 | |
| Chain | Residue | Details |
| A | ASN30 | |
| B | ASN30 | |
| Chain | Residue | Details |
| A | ASN159 | |
| B | ASN159 | |
