Q03103
Gene name |
ERO1 (YML130C, YM4987.05C) |
Protein name |
Endoplasmic oxidoreductin-1 |
Names |
Endoplasmic reticulum oxidoreductase protein 1 |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YML130C |
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
5 structures for Q03103
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1RP4 | X-ray | 220 A | A | 56-424 | PDB |
| 1RQ1 | X-ray | 280 A | A | 56-424 | PDB |
| 3M31 | X-ray | 185 A | A | 56-424 | PDB |
| 3NVJ | X-ray | 320 A | A | 56-424 | PDB |
| AF-Q03103-F1 | Predicted | AlphaFoldDB |
3 variants for Q03103
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s13-13079 | 33 | A>T | No | SGRP | |
| s13-11893 | 428 | E>G | No | SGRP | |
| s13-11717 | 487 | P>S | No | SGRP |
No associated diseases with Q03103
8 regional properties for Q03103
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | THIF-type NAD/FAD binding fold | 54 - 444 | IPR000594-1 |
| domain | THIF-type NAD/FAD binding fold | 450 - 945 | IPR000594-2 |
| conserved_site | Ubiquitin-activating enzyme E1, conserved site | 410 - 418 | IPR018074 |
| domain | Ubiquitin-activating enzyme E1, C-terminal | 922 - 1053 | IPR018965 |
| domain | Ubiquitin-activating enzyme, SCCH domain | 637 - 884 | IPR019572 |
| domain | Ubiquitin-activating enzyme E1, FCCH domain | 226 - 295 | IPR032418 |
| domain | Ubiquitin-activating enzyme E1, four-helix bundle | 297 - 365 | IPR032420 |
| active_site | Ubiquitin-activating enzyme E1, Cys active site | 629 - 637 | IPR033127 |
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. |
3 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. |
| 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. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| 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 |
|---|---|---|---|---|
| Q9V3A6 | Ero1L | Ero1-like protein | Drosophila melanogaster (Fruit fly) | 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 |
| MRLRTAIATL | CLTAFTSATS | NNSYIATDQT | QNAFNDTHFC | KVDRNDHVSP | SCNVTFNELN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AINENIRDDL | SALLKSDFFK | YFRLDLYKQC | SFWDANDGLC | LNRACSVDVV | EDWDTLPEYW |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QPEILGSFNN | DTMKEADDSD | DECKFLDQLC | QTSKKPVDIE | DTINYCDVND | FNGKNAVLID |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LTANPERFTG | YGGKQAGQIW | STIYQDNCFT | IGETGESLAK | DAFYRLVSGF | HASIGTHLSK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EYLNTKTGKW | EPNLDLFMAR | IGNFPDRVTN | MYFNYAVVAK | ALWKIQPYLP | EFSFCDLVNK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EIKNKMDNVI | SQLDTKIFNE | DLVFANDLSL | TLKDEFRSRF | KNVTKIMDCV | QCDRCRLWGK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IQTTGYATAL | KILFEINDAD | EFTKQHIVGK | LTKYELIALL | QTFGRLSESI | ESVNMFEKMY |
| 430 | 440 | 450 | 460 | 470 | 480 |
| GKRLNGSENR | LSSFFQNNFF | NILKEAGKSI | RYTIENINST | KEGKKKTNNS | QSHVFDDLKM |
| 490 | 500 | 510 | 520 | 530 | 540 |
| PKAEIVPRPS | NGTVNKWKKA | WNTEVNNVLE | AFRFIYRSYL | DLPRNIWELS | LMKVYKFWNK |
| 550 | 560 | ||||
| FIGVADYVSE | ETREPISYKL | DIQ |