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Q03103

- ERO1_YEAST

UniProt

Q03103 - ERO1_YEAST

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Protein

Endoplasmic oxidoreductin-1

Gene
ERO1, YML130C, YM4987.05C
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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

FAD.1 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei187 – 1871FAD
Binding sitei189 – 1891FAD
Binding sitei200 – 2001FAD
Binding sitei228 – 2281FAD
Binding sitei231 – 2311FAD
Binding sitei260 – 2601FAD
Active sitei352 – 3521Nucleophile
Active sitei355 – 3551

GO - Molecular functioni

  1. oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor Source: InterPro
  2. protein disulfide isomerase activity Source: SGD
  3. thiol oxidase activity Source: SGD

GO - Biological processi

  1. oxidation-reduction process Source: SGD
  2. protein folding Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16234.
YEAST:G3O-32708-MONOMER.

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
ProteomesiUP000002311: Chromosome XIII

Organism-specific databases

CYGDiYML130c.
SGDiS000004599. ERO1.

Subcellular locationi

Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side 3 Publications

GO - Cellular componenti

  1. endoplasmic reticulum Source: SGD
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi90 – 901C → A: No effect. 2 Publications
Mutagenesisi100 – 1001C → A: Impairs the capture of mixed-disulfide with PDI1 thereby blocking its function. Loss of activity; when associated with A-105. 2 Publications
Mutagenesisi105 – 1051C → A: Loss of activity. 2 Publications
Mutagenesisi143 – 1431C → A: No effect; when associated with A-166. 1 Publication
Mutagenesisi150 – 1501C → A: Loss of regulatory disulfide bond and strongly increased activity towards PDI; when associated with A-295. 1 Publication
Mutagenesisi166 – 1661C → A: No effect; when associated with A-143. 1 Publication
Mutagenesisi208 – 2081C → A: No effect. 1 Publication
Mutagenesisi229 – 2291G → S in ERO1-1; induces defective folding of disulfide proteins. 1 Publication
Mutagenesisi231 – 2311H → Y in ERO1-2; induces defective folding of disulfide proteins. 1 Publication
Mutagenesisi295 – 2951C → A: Loss of regulatory disulfide bond and strongly increased activity towards PDI; when associated with A-150. 1 Publication
Mutagenesisi349 – 3491C → A: Does not affect activity but increases by twofold the amount of protein found in mixed disulfide with PDI1 or MPD2. 1 Publication
Mutagenesisi352 – 3521C → A: Loss of activity. Prevents its reoxidation thereby blocking its function. 2 Publications
Mutagenesisi355 – 3551C → A: Loss of activity. Prevents its reoxidation thereby blocking its function. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818 Reviewed predictionAdd
BLAST
Chaini19 – 563545Endoplasmic oxidoreductin-1PRO_0000008429Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi21 – 211N-linked (GlcNAc...) Reviewed prediction
Glycosylationi35 – 351N-linked (GlcNAc...) Reviewed prediction
Glycosylationi53 – 531N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi90 ↔ 3492 Publications
Disulfide bondi100 ↔ 105Redox-active2 Publications
Glycosylationi130 – 1301N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi143 ↔ 1662 Publications
Disulfide bondi150 ↔ 2952 Publications
Glycosylationi342 – 3421N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi352 ↔ 355Redox-active2 Publications
Glycosylationi425 – 4251N-linked (GlcNAc...) Reviewed prediction
Glycosylationi458 – 4581N-linked (GlcNAc...) Reviewed prediction
Glycosylationi468 – 4681N-linked (GlcNAc...) Reviewed prediction
Glycosylationi491 – 4911N-linked (GlcNAc...) Reviewed prediction

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.
PaxDbiQ03103.
PeptideAtlasiQ03103.

Expressioni

Inductioni

By unfolded protein response (UPR).3 Publications

Gene expression databases

GenevestigatoriQ03103.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi35075. 45 interactions.
DIPiDIP-4515N.
IntActiQ03103. 11 interactions.
MINTiMINT-503775.
STRINGi4932.YML130C.

Structurei

Secondary structure

1
563
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi56 – 7318
Turni77 – 793
Beta strandi80 – 867
Beta strandi91 – 933
Beta strandi95 – 984
Turni102 – 1054
Beta strandi109 – 1113
Helixi113 – 1153
Helixi118 – 1203
Helixi122 – 1254
Turni130 – 1323
Beta strandi133 – 1353
Beta strandi137 – 1393
Helixi141 – 1433
Helixi146 – 1494
Turni152 – 1543
Beta strandi159 – 1613
Helixi165 – 1684
Beta strandi176 – 1805
Turni181 – 1833
Helixi193 – 20513
Helixi216 – 24025
Beta strandi241 – 2433
Turni245 – 2473
Helixi254 – 2607
Turni261 – 2633
Helixi265 – 28521
Helixi286 – 2883
Helixi297 – 31115
Helixi316 – 3194
Turni325 – 3273
Helixi330 – 34617
Helixi347 – 3493
Helixi353 – 37624
Helixi381 – 3899
Helixi393 – 42432

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RP4X-ray2.20A56-424[»]
1RQ1X-ray2.80A56-424[»]
3M31X-ray1.85A56-424[»]
3NVJX-ray3.20A56-424[»]
ProteinModelPortaliQ03103.
SMRiQ03103. Positions 55-424.

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.

Keywords - Domaini

Redox-active center, Signal

Phylogenomic databases

eggNOGiCOG5061.
GeneTreeiENSGT00390000007753.
HOGENOMiHOG000158050.
OMAiCDRCRLW.
OrthoDBiEOG7SV15N.

Family and domain databases

InterProiIPR007266. Ero1.
[Graphical view]
PANTHERiPTHR12613. PTHR12613. 1 hit.
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

MRLRTAIATL CLTAFTSATS NNSYIATDQT QNAFNDTHFC KVDRNDHVSP    50
SCNVTFNELN AINENIRDDL SALLKSDFFK YFRLDLYKQC SFWDANDGLC 100
LNRACSVDVV EDWDTLPEYW QPEILGSFNN DTMKEADDSD DECKFLDQLC 150
QTSKKPVDIE DTINYCDVND FNGKNAVLID LTANPERFTG YGGKQAGQIW 200
STIYQDNCFT IGETGESLAK DAFYRLVSGF HASIGTHLSK EYLNTKTGKW 250
EPNLDLFMAR IGNFPDRVTN MYFNYAVVAK ALWKIQPYLP EFSFCDLVNK 300
EIKNKMDNVI SQLDTKIFNE DLVFANDLSL TLKDEFRSRF KNVTKIMDCV 350
QCDRCRLWGK IQTTGYATAL KILFEINDAD EFTKQHIVGK LTKYELIALL 400
QTFGRLSESI ESVNMFEKMY GKRLNGSENR LSSFFQNNFF NILKEAGKSI 450
RYTIENINST KEGKKKTNNS QSHVFDDLKM PKAEIVPRPS NGTVNKWKKA 500
WNTEVNNVLE AFRFIYRSYL DLPRNIWELS LMKVYKFWNK FIGVADYVSE 550
ETREPISYKL DIQ 563
Length:563
Mass (Da):65,033
Last modified:November 1, 1997 - v1
Checksum:i928CE700AE6137EF
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti555 – 5551P → L in AAT93069. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
Z50178 Genomic DNA. Translation: CAA90553.1 .
AY693050 Genomic DNA. Translation: AAT93069.1 .
BK006946 Genomic DNA. Translation: DAA09769.1 .
PIRi S58198.
RefSeqi NP_013576.1. NM_001182493.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1RP4 X-ray 2.20 A 56-424 [» ]
1RQ1 X-ray 2.80 A 56-424 [» ]
3M31 X-ray 1.85 A 56-424 [» ]
3NVJ X-ray 3.20 A 56-424 [» ]
ProteinModelPortali Q03103.
SMRi Q03103. Positions 55-424.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 35075. 45 interactions.
DIPi DIP-4515N.
IntActi Q03103. 11 interactions.
MINTi MINT-503775.
STRINGi 4932.YML130C.

Proteomic databases

MaxQBi Q03103.
PaxDbi Q03103.
PeptideAtlasi Q03103.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YML130C ; YML130C ; YML130C .
GeneIDi 854909.
KEGGi sce:YML130C.

Organism-specific databases

CYGDi YML130c.
SGDi S000004599. ERO1.

Phylogenomic databases

eggNOGi COG5061.
GeneTreei ENSGT00390000007753.
HOGENOMi HOG000158050.
OMAi CDRCRLW.
OrthoDBi EOG7SV15N.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-16234.
YEAST:G3O-32708-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q03103.
NextBioi 977902.

Gene expression databases

Genevestigatori Q03103.

Family and domain databases

InterProi IPR007266. Ero1.
[Graphical view ]
PANTHERi PTHR12613. PTHR12613. 1 hit.
Pfami PF04137. ERO1. 1 hit.
[Graphical view ]
PIRSFi PIRSF017205. ERO1. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum."
    Frand A.R., Kaiser C.A.
    Mol. Cell 1:161-170(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, INDUCTION.
  5. "Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum."
    Pollard M.G., Travers K.J., Weissman J.S.
    Mol. Cell 1:171-182(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, INDUCTION, MUTAGENESIS OF HIS-231.
  6. "Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum."
    Frand A.R., Kaiser C.A.
    Mol. Cell 4:469-477(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DIRECT OXIDATION OF PDI1 AND MPD2.
  7. "Biochemical basis of oxidative protein folding in the endoplasmic reticulum."
    Tu B.P., Ho-Schleyer S.C., Travers K.J., Weissman J.S.
    Science 290:1571-1574(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR.
  8. "Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum."
    Frand A.R., Kaiser C.A.
    Mol. Biol. Cell 11:2833-2843(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-90; CYS-100; CYS-105; CYS-208; CYS-349; CYS-352 AND CYS-355.
  9. "The C-terminal domain of yeast Ero1p mediates membrane localization and is essential for function."
    Pagani M., Pilati S., Bertoli G., Valsasina B., Sitia R.
    FEBS Lett. 508:117-120(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DOMAIN.
  10. "The FAD- and O(2)-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum."
    Tu B.P., Weissman J.S.
    Mol. Cell 10:983-994(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Oxidative protein folding in eukaryotes: mechanisms and consequences."
    Tu B.P., Weissman J.S.
    J. Cell Biol. 164:341-346(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  12. "Modulation of cellular disulfide-bond formation and the ER redox environment by feedback regulation of Ero1."
    Sevier C.S., Qu H., Heldman N., Gross E., Fass D., Kaiser C.A.
    Cell 129:333-344(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, DISULFIDE BONDS, MUTAGENESIS OF CYS-90; CYS-100; CYS-105; CYS-143; CYS-150; CYS-166; CYS-295; CYS-352 AND CYS-355.
  13. "Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell."
    Gross E., Kastner D.B., Kaiser C.A., Fass D.
    Cell 117:601-610(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 56-424 IN COMPLEX WITH FAD, POTENTIAL HOMODIMERIZATION, DISULFIDE BONDS, MUTAGENESIS OF GLY-229.

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: June 11, 2014
This is version 119 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

External Data

Dasty 3

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