Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016020 | cellular_component | membrane |
| A | 0051260 | biological_process | protein homooligomerization |
| B | 0016020 | cellular_component | membrane |
| B | 0051260 | biological_process | protein homooligomerization |
| C | 0016020 | cellular_component | membrane |
| C | 0051260 | biological_process | protein homooligomerization |
Functional Information from PROSITE/UniProt
| site_id | PS00291 |
| Number of Residues | 16 |
| Details | PRION_1 Prion protein signature 1. AGAAAAGAVVGGLGGY |
| Chain | Residue | Details |
| A | ALA113-TYR128 | |
| site_id | PS00706 |
| Number of Residues | 19 |
| Details | PRION_2 Prion protein signature 2. EtDiKIMeRVVeQMCttQY |
| Chain | Residue | Details |
| A | GLU200-TYR218 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"3138115","evidenceCode":"ECO:0000269"}]} |
