Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0006457 | biological_process | protein folding |
| A | 0051082 | molecular_function | unfolded protein binding |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0006457 | biological_process | protein folding |
| B | 0051082 | molecular_function | unfolded protein binding |
Functional Information from PROSITE/UniProt
| site_id | PS00803 |
| Number of Residues | 16 |
| Details | CALRETICULIN_1 Calreticulin family signature 1. KhEQnidCGGGYVKLF |
| Chain | Residue | Details |
| A | LYS98-PHE113 | |
| site_id | PS00804 |
| Number of Residues | 9 |
| Details | CALRETICULIN_2 Calreticulin family signature 2. IMFGPDiCG |
| Chain | Residue | Details |
| A | ILE130-GLY138 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | LYS62 | |
| A | LYS64 | |
| A | GLN26 | |
| B | LYS64 | |
| B | ASP328 | |
| A | ASP328 | |
| B | GLN26 | |
| B | LYS62 | |
| Chain | Residue | Details |
| A | TYR128 | |
| A | ASP135 | |
| A | ASP317 | |
| B | TYR109 | |
| B | LYS111 | |
| B | TYR128 | |
| B | ASP135 | |
| B | ASP317 | |
| A | TYR109 | |
| A | LYS111 | |
| Chain | Residue | Details |
| A | LYS48 | |
| A | LYS159 | |
| B | LYS48 | |
| B | LYS159 | |
| Chain | Residue | Details |
| A | LYS64 | |
| B | LYS64 | |
