| IED ID |
IndEnz0002006764 |
| Enzyme Type ID |
protease006764 |
| Protein Name |
Degradation in the endoplasmic reticulum protein 1
|
| Gene Name |
DER1 YBR201W YBR1413 |
| Organism |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage |
cellular organisms
Eukaryota
Opisthokonta
Fungi
Dikarya
Ascomycota
saccharomyceta
Saccharomycotina (true yeasts)
Saccharomycetes
Saccharomycetales
Saccharomycetaceae
Saccharomyces
Saccharomyces cerevisiae (Baker's yeast)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
| Enzyme Sequence |
MDAVILNLLGDIPLVTRLWTIGCLVLSGLTSLRIVDPGKVVYSYDLVFKKGQYGRLLYSIFDYGAFNWISMINIFVSANHLSTLENSFNLRRKFCWIIFLLLVILVKMTSIEQPAASLGVLLHENLVYYELKKNGNQMNVRFFGAIDVSPSIFPIYMNAVMYFVYKRSWLEIAMNFMPGHVIYYMDDIIGKIYGIDLCKSPYDWFRNTETP |
| Enzyme Length |
211 |
| Uniprot Accession Number |
P38307 |
| Absorption |
|
| Active Site |
|
| Activity Regulation |
|
| Binding Site |
|
| Calcium Binding |
|
| catalytic Activity |
|
| DNA Binding |
|
| EC Number |
|
| Enzyme Function |
FUNCTION: Component of the endoplasmic reticulum-associated degradation (ERAD) pathway. Specifically required for the ERAD-L pathway which mediates the degradation of proteins with misfolded lumenal domains within the endoplasmic reticulum (ER). Facilitates retrotranslocation of misfolded proteins from the ER lumen through the ER membrane in conjunction with HRD1 (PubMed:32327568). Both proteins have lateral gates facing each other and distort the membrane region between the lateral gates, making it much thinner than a normal phospholipid bilayer (PubMed:32327568). Substrates insert into the membrane as a hairpin loop with one strand interacting with DER1 and the other with HRD1 (PubMed:32327568). {ECO:0000269|PubMed:16873066, ECO:0000269|PubMed:20005842, ECO:0000269|PubMed:23363603, ECO:0000269|PubMed:32327568, ECO:0000269|PubMed:8631297}. |
| Temperature Dependency |
|
| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
|
| Features |
Chain (1); Frameshift (1); Modified residue (1); Mutagenesis (7); Sequence conflict (1); Topological domain (7); Transmembrane (6) |
| Keywords |
3D-structure;Acetylation;Endoplasmic reticulum;Membrane;Protein transport;Reference proteome;Transmembrane;Transmembrane helix;Transport |
| Interact With |
P25694; Q08109; Q05787; P00729; P53044; Q03714 |
| Induction |
INDUCTION: Up-regulated by the unfolded protein response (UPR). {ECO:0000269|PubMed:10847680}. |
| Subcellular Location |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:8631297}; Multi-pass membrane protein {ECO:0000269|PubMed:8631297}. |
| Modified Residue |
MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0000269|PubMed:23363603 |
| Post Translational Modification |
PTM: N-terminally acetylated by acetyltransferase NatB which enhances DER1 stability and is required for ERAD-L function. {ECO:0000269|PubMed:23363603}. |
| Signal Peptide |
|
| Structure 3D |
Electron microscopy (2) |
| Cross Reference PDB |
6VJZ;
6VK0;
|
| Mapped Pubmed ID |
10407271;
10430031;
11283351;
11406589;
12058050;
12847107;
15215855;
15350974;
15849299;
16168371;
16179952;
16212502;
16316751;
16332527;
16397583;
16619026;
17083136;
17945519;
18180297;
18315532;
18407841;
18719252;
19067491;
19923195;
20118070;
20178855;
20219571;
20519439;
21074049;
21147851;
21222279;
21266254;
21486563;
21664808;
21979948;
22533807;
22829918;
23202731;
23209158;
24292014;
24391512;
25032908;
25231236;
25428985;
26362128;
27321670;
27929418;
9409541;
|
| Motif |
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| Gene Encoded By |
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| Mass |
24,391 |
| Kinetics |
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| Metal Binding |
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| Rhea ID |
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| Cross Reference Brenda |
|