IED ID | IndEnz0002007658 |
Enzyme Type ID | protease007658 |
Protein Name |
Derlin-2 DER1-like protein 2 cDerlin-2 |
Gene Name | R151.6 |
Organism | Caenorhabditis elegans |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
Enzyme Sequence | MNGVVAALEEMPPVTRFYTGACVLLTTAVHLEFVTPFHLYFNWELIIRKYQFWRLITSFCFFGSFGFSFLFNMIFTYRYCMMLEEGSFRGRRADFVYMFLFGAVLMILSGIFVQILFLGQAFTIMLVYIWSRRNPMIQMNFFGVLTFTAPYLPWVLLLFSLLLGNNAVVDFMGIACGHIYFFLEDVFPFQEHGKRFLKTPQWLVYLFDERRPEPLPEDERPGGFEWGDEQPEQEQHD |
Enzyme Length | 237 |
Uniprot Accession Number | Q21997 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: May be required for the degradation process of some specific misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Its precise function remains unclear, but its ability to complement der1 mutations in C.cerevisiae, suggests a similar function in the degradation of ER misfolded proteins. {ECO:0000269|PubMed:15093775, ECO:0000269|PubMed:15215856}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Region (1); Topological domain (5); Transmembrane (4) |
Keywords | Endoplasmic reticulum;Membrane;Protein transport;Reference proteome;Stress response;Transmembrane;Transmembrane helix;Transport |
Interact With | |
Induction | INDUCTION: By endoplasmic reticulum stress. {ECO:0000269|PubMed:15215856}. |
Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9GZP9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9GZP9}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 16184190; 19509052; 21085631; 21177967; 21722281; 22286215; 22560298; 22569626; 23641861; 23800452; 25487147; |
Motif | |
Gene Encoded By | |
Mass | 28,034 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |