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Protein

Endoplasmic oxidoreductin-1

Gene

ERO1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly PDI1 isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on PDI1 to transfer oxidizing equivalent. Also able to oxidize directly the PDI related protein MPD2. Does not oxidize all PDI related proteins, suggesting that it can discriminate between PDI1 and related proteins. Reoxidation of ERO1 probably involves electron transfer to molecular oxygen via FAD. Acts independently of glutathione. May be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress.5 Publications

Cofactori

FAD1 Publication

Enzyme regulationi

Enzyme activity is tightly regulated to prevent the accumulation of reactive oxygen species in the endoplasmic reticulum. Reversibly down-regulated by the formation of disulfide bonds between Cys-150 and Cys-295.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei187FAD1 Publication1
Binding sitei189FAD1 Publication1
Binding sitei200FAD1 Publication1
Binding sitei228FAD1 Publication1
Binding sitei231FAD1 Publication1
Binding sitei260FAD1 Publication1
Active sitei352Nucleophile1 Publication1
Active sitei3551 Publication1

GO - Molecular functioni

  • oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor Source: InterPro
  • protein disulfide isomerase activity Source: SGD
  • protein disulfide oxidoreductase activity Source: GO_Central
  • thiol oxidase activity Source: SGD

GO - Biological processi

  • cellular protein modification process Source: GO_Central
  • oxidation-reduction process Source: SGD
  • protein folding in endoplasmic reticulum Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:G3O-32708-MONOMER.
YEAST:G3O-32708-MONOMER.
ReactomeiR-SCE-3299685. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoplasmic oxidoreductin-1 (EC:1.8.4.-)
Alternative name(s):
Endoplasmic reticulum oxidoreductase protein 1
Gene namesi
Name:ERO1
Ordered Locus Names:YML130C
ORF Names:YM4987.05C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YML130C.
SGDiS000004599. ERO1.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: SGD
  • endoplasmic reticulum membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi90C → A: No effect. 2 Publications1
Mutagenesisi100C → A: Impairs the capture of mixed-disulfide with PDI1 thereby blocking its function. Loss of activity; when associated with A-105. 2 Publications1
Mutagenesisi105C → A: Loss of activity. 2 Publications1
Mutagenesisi143C → A: No effect; when associated with A-166. 1 Publication1
Mutagenesisi150C → A: Loss of regulatory disulfide bond and strongly increased activity towards PDI; when associated with A-295. 1 Publication1
Mutagenesisi166C → A: No effect; when associated with A-143. 1 Publication1
Mutagenesisi208C → A: No effect. 1 Publication1
Mutagenesisi229G → S in ERO1-1; induces defective folding of disulfide proteins. 1 Publication1
Mutagenesisi231H → Y in ERO1-2; induces defective folding of disulfide proteins. 1 Publication1
Mutagenesisi295C → A: Loss of regulatory disulfide bond and strongly increased activity towards PDI; when associated with A-150. 1 Publication1
Mutagenesisi349C → A: Does not affect activity but increases by twofold the amount of protein found in mixed disulfide with PDI1 or MPD2. 1 Publication1
Mutagenesisi352C → A: Loss of activity. Prevents its reoxidation thereby blocking its function. 2 Publications1
Mutagenesisi355C → A: Loss of activity. Prevents its reoxidation thereby blocking its function. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000000842919 – 563Endoplasmic oxidoreductin-1Add BLAST545

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi21N-linked (GlcNAc...)Sequence analysis1
Glycosylationi35N-linked (GlcNAc...)Sequence analysis1
Glycosylationi53N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi90 ↔ 349Combined sources1 Publication
Disulfide bondi100 ↔ 105Redox-activeCombined sources1 Publication
Glycosylationi130N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi143 ↔ 166Combined sources1 Publication
Disulfide bondi150 ↔ 295Combined sources1 Publication
Glycosylationi342N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi352 ↔ 355Redox-activeCombined sources1 Publication
Glycosylationi425N-linked (GlcNAc...)Sequence analysis1
Glycosylationi458N-linked (GlcNAc...)Sequence analysis1
Glycosylationi468N-linked (GlcNAc...)Sequence analysis1
Glycosylationi491N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

The Cys-100/Cys-105 and Cys-352/Cys-355 disulfide bonds constitute the redox-active center. The Cys-100/Cys-105 disulfide bond may accept electron from PDI1 and funnel them to the active site disulfide Cys-352/Cys-355.
N-glycosylated.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ03103.
PRIDEiQ03103.

Expressioni

Inductioni

By unfolded protein response (UPR).2 Publications

Interactioni

Subunit structurei

May function both as a monomer and a homodimer.1 Publication

Protein-protein interaction databases

BioGridi35075. 46 interactors.
DIPiDIP-4515N.
IntActiQ03103. 11 interactors.
MINTiMINT-503775.

Structurei

Secondary structure

1563
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi56 – 73Combined sources18
Turni77 – 79Combined sources3
Beta strandi80 – 86Combined sources7
Beta strandi91 – 93Combined sources3
Beta strandi95 – 98Combined sources4
Turni102 – 105Combined sources4
Beta strandi109 – 111Combined sources3
Helixi113 – 115Combined sources3
Helixi118 – 120Combined sources3
Helixi122 – 125Combined sources4
Turni130 – 132Combined sources3
Beta strandi133 – 135Combined sources3
Beta strandi137 – 139Combined sources3
Helixi141 – 143Combined sources3
Helixi146 – 149Combined sources4
Turni152 – 154Combined sources3
Beta strandi159 – 161Combined sources3
Helixi165 – 168Combined sources4
Beta strandi176 – 180Combined sources5
Turni181 – 183Combined sources3
Helixi193 – 205Combined sources13
Helixi216 – 240Combined sources25
Beta strandi241 – 243Combined sources3
Turni245 – 247Combined sources3
Helixi254 – 260Combined sources7
Turni261 – 263Combined sources3
Helixi265 – 285Combined sources21
Helixi286 – 288Combined sources3
Helixi297 – 311Combined sources15
Helixi316 – 319Combined sources4
Turni325 – 327Combined sources3
Helixi330 – 346Combined sources17
Helixi347 – 349Combined sources3
Helixi353 – 376Combined sources24
Helixi381 – 389Combined sources9
Helixi393 – 424Combined sources32

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RP4X-ray2.20A56-424[»]
1RQ1X-ray2.80A56-424[»]
3M31X-ray1.85A56-424[»]
3NVJX-ray3.20A56-424[»]
ProteinModelPortaliQ03103.
SMRiQ03103.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ03103.

Family & Domainsi

Domaini

The C-terminal part (437-563) is required for the association with the endoplasmic reticulum lumen membrane.1 Publication

Sequence similaritiesi

Belongs to the EROs family.Curated

Keywords - Domaini

Redox-active center, Signal

Phylogenomic databases

GeneTreeiENSGT00390000007753.
HOGENOMiHOG000158050.
InParanoidiQ03103.
OMAiTHICAEY.
OrthoDBiEOG092C1KNC.

Family and domain databases

InterProiIPR007266. Ero1.
[Graphical view]
PANTHERiPTHR12613. PTHR12613. 2 hits.
PfamiPF04137. ERO1. 1 hit.
[Graphical view]
PIRSFiPIRSF017205. ERO1. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q03103-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLRTAIATL CLTAFTSATS NNSYIATDQT QNAFNDTHFC KVDRNDHVSP
60 70 80 90 100
SCNVTFNELN AINENIRDDL SALLKSDFFK YFRLDLYKQC SFWDANDGLC
110 120 130 140 150
LNRACSVDVV EDWDTLPEYW QPEILGSFNN DTMKEADDSD DECKFLDQLC
160 170 180 190 200
QTSKKPVDIE DTINYCDVND FNGKNAVLID LTANPERFTG YGGKQAGQIW
210 220 230 240 250
STIYQDNCFT IGETGESLAK DAFYRLVSGF HASIGTHLSK EYLNTKTGKW
260 270 280 290 300
EPNLDLFMAR IGNFPDRVTN MYFNYAVVAK ALWKIQPYLP EFSFCDLVNK
310 320 330 340 350
EIKNKMDNVI SQLDTKIFNE DLVFANDLSL TLKDEFRSRF KNVTKIMDCV
360 370 380 390 400
QCDRCRLWGK IQTTGYATAL KILFEINDAD EFTKQHIVGK LTKYELIALL
410 420 430 440 450
QTFGRLSESI ESVNMFEKMY GKRLNGSENR LSSFFQNNFF NILKEAGKSI
460 470 480 490 500
RYTIENINST KEGKKKTNNS QSHVFDDLKM PKAEIVPRPS NGTVNKWKKA
510 520 530 540 550
WNTEVNNVLE AFRFIYRSYL DLPRNIWELS LMKVYKFWNK FIGVADYVSE
560
ETREPISYKL DIQ
Length:563
Mass (Da):65,033
Last modified:November 1, 1997 - v1
Checksum:i928CE700AE6137EF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti555P → L in AAT93069 (PubMed:17322287).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z50178 Genomic DNA. Translation: CAA90553.1.
AY693050 Genomic DNA. Translation: AAT93069.1.
BK006946 Genomic DNA. Translation: DAA09769.1.
PIRiS58198.
RefSeqiNP_013576.1. NM_001182493.1.

Genome annotation databases

EnsemblFungiiYML130C; YML130C; YML130C.
GeneIDi854909.
KEGGisce:YML130C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z50178 Genomic DNA. Translation: CAA90553.1.
AY693050 Genomic DNA. Translation: AAT93069.1.
BK006946 Genomic DNA. Translation: DAA09769.1.
PIRiS58198.
RefSeqiNP_013576.1. NM_001182493.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RP4X-ray2.20A56-424[»]
1RQ1X-ray2.80A56-424[»]
3M31X-ray1.85A56-424[»]
3NVJX-ray3.20A56-424[»]
ProteinModelPortaliQ03103.
SMRiQ03103.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35075. 46 interactors.
DIPiDIP-4515N.
IntActiQ03103. 11 interactors.
MINTiMINT-503775.

Proteomic databases

MaxQBiQ03103.
PRIDEiQ03103.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYML130C; YML130C; YML130C.
GeneIDi854909.
KEGGisce:YML130C.

Organism-specific databases

EuPathDBiFungiDB:YML130C.
SGDiS000004599. ERO1.

Phylogenomic databases

GeneTreeiENSGT00390000007753.
HOGENOMiHOG000158050.
InParanoidiQ03103.
OMAiTHICAEY.
OrthoDBiEOG092C1KNC.

Enzyme and pathway databases

BioCyciMetaCyc:G3O-32708-MONOMER.
YEAST:G3O-32708-MONOMER.
ReactomeiR-SCE-3299685. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

EvolutionaryTraceiQ03103.
PROiQ03103.

Family and domain databases

InterProiIPR007266. Ero1.
[Graphical view]
PANTHERiPTHR12613. PTHR12613. 2 hits.
PfamiPF04137. ERO1. 1 hit.
[Graphical view]
PIRSFiPIRSF017205. ERO1. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiERO1_YEAST
AccessioniPrimary (citable) accession number: Q03103
Secondary accession number(s): D6W0F5, E9P913
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.