8SNN
Structure of mature human ADAM17/iRhom2 sheddase complex, conformation 1
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004222 | molecular_function | metalloendopeptidase activity |
A | 0006508 | biological_process | proteolysis |
A | 0008237 | molecular_function | metallopeptidase activity |
B | 0002862 | biological_process | negative regulation of inflammatory response to antigenic stimulus |
B | 0004252 | molecular_function | serine-type endopeptidase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005783 | cellular_component | endoplasmic reticulum |
B | 0005789 | cellular_component | endoplasmic reticulum membrane |
B | 0005796 | cellular_component | Golgi lumen |
B | 0005886 | cellular_component | plasma membrane |
B | 0012505 | cellular_component | endomembrane system |
B | 0015031 | biological_process | protein transport |
B | 0016020 | cellular_component | membrane |
B | 0019838 | molecular_function | growth factor binding |
B | 0042058 | biological_process | regulation of epidermal growth factor receptor signaling pathway |
B | 0050708 | biological_process | regulation of protein secretion |
B | 0050709 | biological_process | negative regulation of protein secretion |
B | 0072659 | biological_process | protein localization to plasma membrane |
B | 0140318 | molecular_function | protein transporter activity |
Functional Information from PROSITE/UniProt
site_id | PS00142 |
Number of Residues | 10 |
Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VTTHELGHNF |
Chain | Residue | Details |
A | VAL402-PHE411 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 160 |
Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 68 |
Details | Region: {"description":"Crambin-like"} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 266 |
Details | Topological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 27 |
Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 22 |
Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
Chain | Residue | Details |