Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 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. CiNtlgsFeCqC |
| Chain | Residue | Details |
| A | CYS429-CYS440 | |
| A | CYS467-CYS478 | |
| A | CYS505-CYS516 | |
| site_id | PS00022 |
| Number of Residues | 12 |
| Details | EGF_1 EGF-like domain signature 1. CqClqGytGPrC |
| Chain | Residue | Details |
| A | CYS438-CYS449 | |
| A | CYS476-CYS487 | |
| A | CYS514-CYS525 | |
| site_id | PS01186 |
| Number of Residues | 12 |
| Details | EGF_2 EGF-like domain signature 2. CqClqGYtgpr....C |
| Chain | Residue | Details |
| A | CYS438-CYS449 | |
| A | CYS476-CYS487 | |
| A | CYS514-CYS525 | |
| site_id | PS01187 |
| Number of Residues | 27 |
| Details | EGF_CA Calcium-binding EGF-like domain signature. DvDECslganp........Cehagk..CiNtlgsFeC |
| Chain | Residue | Details |
| A | ASP412-CYS438 | |
| A | ASP452-CYS476 | |
| A | ASN490-CYS514 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 38 |
| Details | Domain: {"description":"EGF-like 11; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| Details | Domain: {"description":"EGF-like 12; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 36 |
| Details | Domain: {"description":"EGF-like 13; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 5 |
| Details | Region: {"description":"Interaction with DLL4","evidences":[{"source":"UniProtKB","id":"Q07008","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q07008","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Interaction with DLL4","evidences":[{"source":"UniProtKB","id":"Q07008","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"O-linked (Glc...) serine","evidences":[{"source":"PubMed","id":"30127001","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"O-linked (Glc...) serine","evidences":[{"source":"UniProtKB","id":"Q07008","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"O-linked (Fuc...) threonine","evidences":[{"source":"UniProtKB","id":"Q07008","evidenceCode":"ECO:0000250"}]} |