Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008236 | molecular_function | serine-type peptidase activity |
| L | 0005509 | molecular_function | calcium ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA L 1 |
| Chain | Residue |
| L | ASP333 |
| L | ILE334 |
| L | LEU350 |
| L | GLY353 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 2 |
| Chain | Residue |
| A | ASP360 |
| A | ALA328 |
| A | ALA330 |
| A | VAL333 |
| A | THR335 |
| A | CYS358 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA L 3 |
| Chain | Residue |
| L | GLU296 |
| L | ASP310 |
Functional Information from PROSITE/UniProt
| site_id | PS00010 |
| Number of Residues | 12 |
| Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CnDlkigYeClC |
| Chain | Residue | Details |
| L | CYS308-CYS319 | |
| L | CYS347-CYS358 | |
| site_id | PS01186 |
| Number of Residues | 15 |
| Details | EGF_2 EGF-like domain signature 2. ClCpdGFqlvaqrr.C |
| Chain | Residue | Details |
| L | CYS317-CYS331 | |
| L | CYS356-CYS371 | |
| site_id | PS01187 |
| Number of Residues | 24 |
| Details | EGF_CA Calcium-binding EGF-like domain signature. DiDECqdpdt.........Csql....CvNleggYkC |
| Chain | Residue | Details |
| L | ASP333-CYS356 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| L | LEU691 | |
| A | HIS226 | |
| A | SER386 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| L | THR482 | |
| Chain | Residue | Details |
| L | ASN624 | |
| Chain | Residue | Details |
| A | ASN533 | |
