| IED ID | IndEnz0002016412 |
| Enzyme Type ID | protease016412 |
| Protein Name |
Derlin-1 Degradation in endoplasmic reticulum protein 1 DERtrin-1 Der1-like protein 1 |
| Gene Name | DERL1 DER1 UNQ243/PRO276 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MSDIGDWFRSIPAITRYWFAATVAVPLVGKLGLISPAYLFLWPEAFLYRFQIWRPITATFYFPVGPGTGFLYLVNLYFLYQYSTRLETGAFDGRPADYLFMLLFNWICIVITGLAMDMQLLMIPLIMSVLYVWAQLNRDMIVSFWFGTRFKACYLPWVILGFNYIIGGSVINELIGNLVGHLYFFLMFRYPMDLGGRNFLSTPQFLYRWLPSRRGGVSGFGVPPASMRRAADQNGGGGRHNWGQGFRLGDQ |
| Enzyme Length | 251 |
| Uniprot Accession Number | Q9BUN8 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins (PubMed:15215856, PubMed:33658201). Forms homotetramers which encircle a large channel traversing the endoplasmic reticulum (ER) membrane (PubMed:33658201). This allows the retrotranslocation of misfolded proteins from the ER into the cytosol where they are ubiquitinated and degraded by the proteasome (PubMed:33658201). The channel has a lateral gate within the membrane which provides direct access to membrane proteins with no need to reenter the ER lumen first (PubMed:33658201). May mediate the interaction between VCP and the misfolded protein (PubMed:15215856). Also involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation (PubMed:26565908). By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway (PubMed:26692333). {ECO:0000269|PubMed:15215856, ECO:0000269|PubMed:26565908, ECO:0000269|PubMed:26692333, ECO:0000269|PubMed:33658201}.; FUNCTION: (Microbial infection) In case of infection by cytomegaloviruses, it plays a central role in the export from the ER and subsequent degradation of MHC class I heavy chains via its interaction with US11 viral protein, which recognizes and associates with MHC class I heavy chains. Also participates in the degradation process of misfolded cytomegalovirus US2 protein. {ECO:0000269|PubMed:15215855, ECO:0000269|PubMed:15215856}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Beta strand (1); Chain (1); Initiator methionine (1); Modified residue (4); Motif (1); Mutagenesis (8); Natural variant (1); Region (1); Topological domain (7); Transmembrane (6) |
| Keywords | 3D-structure;Acetylation;Alternative splicing;Endoplasmic reticulum;Host-virus interaction;Membrane;Phosphoprotein;Protein transport;Reference proteome;Transmembrane;Transmembrane helix;Transport;Unfolded protein response |
| Interact With | Q8TB40; Q13520; P51572; P13569; Q9H5X1; Q96PJ5; O15552; Q05329; Q8TCT9; Q8N6L0; Q8TBB1; Q9H6H4; Q86VR2; Q9NY72; Q14973; Q3KNW5; Q8IWU4; Q8TBB6; Q9UHI5; Q9BQ70; Q53QW1; Q6PL24; Q9Y320; Q13049; Q9Y385 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15215855, ECO:0000269|PubMed:15215856, ECO:0000269|PubMed:16186509, ECO:0000269|PubMed:16449189}; Multi-pass membrane protein {ECO:0000269|PubMed:15215855, ECO:0000269|PubMed:15215856, ECO:0000269|PubMed:16186509, ECO:0000269|PubMed:16449189}. |
| Modified Residue | MOD_RES 2; /note=N-acetylserine; /evidence=ECO:0007744|PubMed:22223895; MOD_RES 201; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:23186163; MOD_RES 202; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:18669648; MOD_RES 226; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:23186163 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | Electron microscopy (1); X-ray crystallography (1) |
| Cross Reference PDB | 5GLF; 7CZB; |
| Mapped Pubmed ID | 11146634; 11740563; 11812794; 15174051; 15358861; 15362974; 15611333; 16168377; 16868077; 16901789; 16954204; 17453418; 17872946; 18048502; 18094046; 18205950; 18227067; 18555783; 18716059; 18927294; 19002207; 19114714; 1998343; 21184741; 22238364; 22311976; 22627700; 23306155; 24019521; 24089527; 24685677; 2475911; 24807418; 25030448; 25416956; 2570460; 26173415; 26210183; 26611529; 26638075; 27572270; 27977784; 28178653; 28219405; 29530993; 29743537; 29768262; 31670413; 31721721; 33658201; 7523390; 7529176; 7553863; 7553864; 8625414; |
| Motif | MOTIF 241..248; /note=SHP-box; /evidence=ECO:0000305|PubMed:27714797 |
| Gene Encoded By | |
| Mass | 28,801 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.105; |