Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005509 | molecular_function | calcium ion binding |
| D | 0005509 | molecular_function | calcium ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 300 |
| Chain | Residue |
| A | GLU48 |
| A | ASP56 |
| A | ASP101 |
| A | SER103 |
| A | ASN104 |
| A | HOH419 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue CA A 301 |
| Chain | Residue |
| A | ASN139 |
| A | TYR140 |
| A | GLY143 |
| A | HOH408 |
| A | ASP119 |
| A | VAL120 |
| A | GLU122 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 302 |
| Chain | Residue |
| A | GLU215 |
| A | ASP225 |
| A | ASP262 |
| A | SER264 |
| A | HOH417 |
| A | HOH420 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue CA D 300 |
| Chain | Residue |
| D | GLU48 |
| D | ASP56 |
| D | ASP101 |
| D | SER103 |
| D | ASN104 |
| D | HOH415 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue CA D 301 |
| Chain | Residue |
| D | ASP119 |
| D | VAL120 |
| D | GLU122 |
| D | ASN139 |
| D | TYR140 |
| D | GLY143 |
| D | HOH411 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue CA D 302 |
| Chain | Residue |
| D | GLU215 |
| D | ASP225 |
| D | ASP262 |
| D | SER264 |
| D | HOH413 |
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 | 224 |
| Details | Domain: {"description":"CUB 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00059","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"(3R)-3-hydroxyasparagine","evidences":[{"source":"PubMed","id":"12743029","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 234 |
| Details | Domain: {"description":"CUB 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00059","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 86 |
| Details | Domain: {"description":"EGF-like; calcium-binding"} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12743029","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
