Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| B | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
Functional Information from PROSITE/UniProt
| site_id | PS00019 |
| Number of Residues | 10 |
| Details | ACTININ_1 Actinin-type actin-binding domain signature 1. EEaVFSFWLN |
| Chain | Residue | Details |
| A | GLU196-ASN205 | |
| site_id | PS00141 |
| Number of Residues | 12 |
| Details | ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VIFDTGSSDLWV |
| Chain | Residue | Details |
| A | VAL77-VAL88 | |
| A | ALA264-GLY275 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"P42210","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00415","evidenceCode":"ECO:0000255"}]} |
