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Q03103

- ERO1_YEAST

UniProt

Q03103 - ERO1_YEAST

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Protein

Endoplasmic oxidoreductin-1

Gene

ERO1

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

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei187 – 1871FAD1 Publication
Binding sitei189 – 1891FAD1 Publication
Binding sitei200 – 2001FAD1 Publication
Binding sitei228 – 2281FAD1 Publication
Binding sitei231 – 2311FAD1 Publication
Binding sitei260 – 2601FAD1 Publication
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 3 Publications; Peripheral membrane protein 3 Publications; Lumenal side 3 Publications

GO - Cellular componenti

  1. endoplasmic reticulum Source: SGD
  2. membrane Source: UniProtKB-KW
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 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 563545Endoplasmic oxidoreductin-1PRO_0000008429Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi21 – 211N-linked (GlcNAc...)Sequence Analysis
Glycosylationi35 – 351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi53 – 531N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi90 ↔ 349
Disulfide bondi100 ↔ 105Redox-active
Glycosylationi130 – 1301N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi143 ↔ 166
Disulfide bondi150 ↔ 295
Glycosylationi342 – 3421N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi352 ↔ 355Redox-active
Glycosylationi425 – 4251N-linked (GlcNAc...)Sequence Analysis
Glycosylationi458 – 4581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi468 – 4681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi491 – 4911N-linked (GlcNAc...)Sequence Analysis

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).2 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 – 7318Combined sources
Turni77 – 793Combined sources
Beta strandi80 – 867Combined sources
Beta strandi91 – 933Combined sources
Beta strandi95 – 984Combined sources
Turni102 – 1054Combined sources
Beta strandi109 – 1113Combined sources
Helixi113 – 1153Combined sources
Helixi118 – 1203Combined sources
Helixi122 – 1254Combined sources
Turni130 – 1323Combined sources
Beta strandi133 – 1353Combined sources
Beta strandi137 – 1393Combined sources
Helixi141 – 1433Combined sources
Helixi146 – 1494Combined sources
Turni152 – 1543Combined sources
Beta strandi159 – 1613Combined sources
Helixi165 – 1684Combined sources
Beta strandi176 – 1805Combined sources
Turni181 – 1833Combined sources
Helixi193 – 20513Combined sources
Helixi216 – 24025Combined sources
Beta strandi241 – 2433Combined sources
Turni245 – 2473Combined sources
Helixi254 – 2607Combined sources
Turni261 – 2633Combined sources
Helixi265 – 28521Combined sources
Helixi286 – 2883Combined sources
Helixi297 – 31115Combined sources
Helixi316 – 3194Combined sources
Turni325 – 3273Combined sources
Helixi330 – 34617Combined sources
Helixi347 – 3493Combined sources
Helixi353 – 37624Combined sources
Helixi381 – 3899Combined sources
Helixi393 – 42432Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
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

eggNOGiCOG5061.
GeneTreeiENSGT00390000007753.
HOGENOMiHOG000158050.
InParanoidiQ03103.
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

        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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti555 – 5551P → L in AAT93069. (PubMed:17322287)Curated

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 .
PIRi S58198.
RefSeqi NP_013576.1. NM_001182493.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi Q03103.
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.
  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: November 26, 2014
This is version 122 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