Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005509 | molecular_function | calcium ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue CA A 301 |
Chain | Residue |
A | ASP246 |
A | VAL247 |
A | GLU249 |
A | ASN264 |
A | THR265 |
Functional Information from PROSITE/UniProt
site_id | PS00010 |
Number of Residues | 12 |
Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CiNtvgsFeCkC |
Chain | Residue | Details |
A | CYS262-CYS273 | |
site_id | PS00022 |
Number of Residues | 12 |
Details | EGF_1 EGF-like domain signature 1. ClCqkGyiGThC |
Chain | Residue | Details |
A | CYS134-CYS145 | |
A | CYS166-CYS177 | |
site_id | PS01186 |
Number of Residues | 12 |
Details | EGF_2 EGF-like domain signature 2. ClCqkGYigth....C |
Chain | Residue | Details |
A | CYS134-CYS145 | |
A | CYS166-CYS177 | |
site_id | PS01187 |
Number of Residues | 26 |
Details | EGF_CA Calcium-binding EGF-like domain signature. DvDECqaipgl........Cqggn...CiNtvgsFeC |
Chain | Residue | Details |
A | ASP246-CYS271 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 31 |
Details | Domain: {"description":"EGF-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 31 |
Details | Domain: {"description":"EGF-like 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 52 |
Details | Domain: {"description":"TB 1"} |
site_id | SWS_FT_FI4 |
Number of Residues | 41 |
Details | Domain: {"description":"EGF-like 4; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI5 |
Number of Residues | 26 |
Details | Region: {"description":"Hybrid domain 1","evidences":[{"source":"PubMed","id":"19446531","evidenceCode":"ECO:0000305"}]} |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"O-linked (Glc) serine","evidences":[{"source":"PubMed","id":"34411563","evidenceCode":"ECO:0000269"}]} |