Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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. CvNtpgsFmCiC |
| Chain | Residue | Details |
| B | CYS457-CYS468 | |
| B | CYS572-CYS583 | |
| B | CYS619-CYS630 | |
| site_id | PS00022 |
| Number of Residues | 12 |
| Details | EGF_1 EGF-like domain signature 1. CaCpqGftGPsC |
| Chain | Residue | Details |
| B | CYS541-CYS552 | |
| site_id | PS01186 |
| Number of Residues | 15 |
| Details | EGF_2 EGF-like domain signature 2. CiCktGYiriddys.C |
| Chain | Residue | Details |
| B | CYS466-CYS480 | |
| B | CYS508-CYS521 | |
| B | CYS541-CYS552 | |
| site_id | PS01187 |
| Number of Residues | 27 |
| Details | EGF_CA Calcium-binding EGF-like domain signature. DiDECaegrhy........Crentm..CvNtpgsFmC |
| Chain | Residue | Details |
| B | ASP440-CYS466 | |
| B | ASP555-CYS581 | |
| B | ASP602-CYS628 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| B | ASP440 | |
| B | ASN574 | |
| B | LEU575 | |
| B | TRP578 | |
| B | ASP602 | |
| B | ILE603 | |
| B | GLU605 | |
| B | ASN621 | |
| B | LEU622 | |
| B | GLY625 | |
| B | ILE441 | |
| B | GLU443 | |
| B | ASN459 | |
| B | THR460 | |
| B | SER463 | |
| B | ASP555 | |
| B | ILE556 | |
| B | GLU558 | |
| Chain | Residue | Details |
| B | ASN517 | |
| Chain | Residue | Details |
| B | THR548 | |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| B | ASN615 | |
| B | ASN635 | |
