Q9V3A6
Gene name |
Ero1L (CG1333) |
Protein name |
Ero1-like protein |
Names |
Endoplasmic reticulum oxidoreductin-1-like protein |
Species |
Drosophila melanogaster (Fruit fly) |
KEGG Pathway |
dme:Dmel_CG1333 |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q9V3A6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9V3A6-F1 | Predicted | AlphaFoldDB |
No variants for Q9V3A6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9V3A6 | |||||
No associated diseases with Q9V3A6
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| FAD binding | Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. |
| oxidoreductase activity | Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. |
| protein-disulfide reductase activity | Catalysis of the reaction: a protein with reduced sulfide groups = a protein with oxidized disulfide bonds. |
| thiol oxidase activity | Catalysis of the reaction: 4 R'C(R)SH + O2 = 2 R'C(R)S-S(R)CR' + 2 H2O2. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| chaperone cofactor-dependent protein refolding | The process of assisting in the correct posttranslational noncovalent assembly of proteins, which is dependent on additional protein cofactors. This process occurs over one or several cycles of nucleotide hydrolysis-dependent binding and release. |
| protein folding in endoplasmic reticulum | A protein folding process that takes place in the endoplasmic reticulum (ER). Secreted, plasma membrane and organelle proteins are folded in the ER, assisted by chaperones and foldases (protein disulphide isomerases), and additional factors required for optimal folding (ATP, Ca2+ and an oxidizing environment to allow disulfide bond formation). |
5 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q03103 | ERO1 | Endoplasmic oxidoreductin-1 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| Q96HE7 | ERO1A | ERO1-like protein alpha | Homo sapiens (Human) | PR |
| Q7X9I4 | AERO2 | Endoplasmic reticulum oxidoreductin-2 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| B1H1F9 | ero1a | ERO1-like protein alpha | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) | PR |
| Q7T3D1 | ero1a | ERO1-like protein alpha | Danio rerio (Zebrafish) (Brachydanio rerio) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTTRTVQRNL | WASAAVVLVL | LLLWTDTTGG | YFAAIDETET | SKNCFCELEG | SINDCSCDVD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TVDHFNNMKI | YPRLQSLLVK | NFFRFYKVNL | RQECPFWPDD | SRCAMRFCQV | ENCEEQAIPQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GIKDKGEHKE | KAAFKYTREA | QVGGSACSDG | EDFDSSLGFL | DTSISDQAHR | EFELWAKHDE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AEEDFCIVDD | HEEGSQYVDL | LLNPERYTGY | KGESAHRIWK | SIYLENCFGG | NNETANKFSN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| YVPHLDLRNV | CLEQRAFYRI | ISGLHSSINI | HLCSKYLLSE | SKDFLDPQGI | WGPNVKEFKR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RFSPETTSGE | GPHWLRNLYF | IYLIELRALA | KAAPYLRRED | YYTGIAEEDD | EVKLAINDML |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SVIENFQSHF | DENALFSNGI | ASIKFKHDYK | EKFRNISRIM | SCVGCDKCKL | WGKLQTQGLG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| TALKILYSEK | LNLATESGLW | DKPHIEADPI | FRLSRTEIVA | LFNAFGRLSN | SIYEMENFRC |
| VLR |