Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

ERO1-like protein alpha

Gene

ERO1A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins. Involved in the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thereby playing a role in retrotranslocation of the toxin. Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1.7 Publications

Cofactori

FAD2 Publications

Activity 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 the active site Cys-94 and Cys-131, and between Cys-99 and Cys-104. Glutathione may be required to regulate its activity in the endoplasmic reticulum.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei187FADCombined sources1 Publication1
Binding sitei189FADCombined sources1 Publication1
Binding sitei200FADCombined sources1 Publication1
Binding sitei252FADCombined sources1 Publication1
Binding sitei255FADCombined sources1 Publication1
Binding sitei287FADCombined sources1 Publication1
Binding sitei300FADCombined sources1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processApoptosis, Electron transport, Transport
LigandFAD, Flavoprotein

Enzyme and pathway databases

ReactomeiR-HSA-264876 Insulin processing
R-HSA-3299685 Detoxification of Reactive Oxygen Species

Names & Taxonomyi

Protein namesi
Recommended name:
ERO1-like protein alpha (EC:1.8.4.-)
Short name:
ERO1-L
Short name:
ERO1-L-alpha
Alternative name(s):
Endoplasmic oxidoreductin-1-like protein
Endoplasmic reticulum oxidoreductase alphaImported
Oxidoreductin-1-L-alpha
Gene namesi
Name:ERO1AImported
Synonyms:ERO1L
ORF Names:UNQ434/PRO865
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

EuPathDBiHostDB:ENSG00000197930.12
HGNCiHGNC:13280 ERO1A
MIMi615435 gene
neXtProtiNX_Q96HE7

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi85C → A: Alters protein folding and stability. Loss of regulatory disulfide bond formation and increased activity towards P4HB; when associated with A-131. 2 Publications1
Mutagenesisi85C → S: Induces a decrease in activity. 2 Publications1
Mutagenesisi94C → S: Induces a decrease in activity towards thioredoxin. Loss of activity towards thioredoxin and loss of regulatory disulfide bond formation; when associated with A-99. 2 Publications1
Mutagenesisi99C → A: Acts as a weak dominant-negative mutant. Loss of activity towards thioredoxin. Loss of regulatory disulfide bond formation; when associated with A-94. 2 Publications1
Mutagenesisi104C → A: No effect. Strongly increased activity towards P4HB and UPR induction, but no broad oxidative injury; when associated with A-131. 3 Publications1
Mutagenesisi104C → S: No effect. 3 Publications1
Mutagenesisi131C → A: Loss of regulatory disulfide bond formation and increased activity towards P4HB. Loss of regulatory disulfide bond formation and strongly increased activity towards P4HB; when associated with A-85. Loss of regulatory disulfide bond formation, strongly increased activity towards P4HB and UPR induction, but no broad oxidative injury; when associated with A-104. 4 Publications1
Mutagenesisi166C → A: No effect. 2 Publications1
Mutagenesisi208C → A or S: No effect. 2 Publications1
Mutagenesisi241C → A or S: No effect. 2 Publications1
Mutagenesisi280N → A: No effect on activity. 1 Publication1
Mutagenesisi384N → A: No effect on activity. 1 Publication1
Mutagenesisi391C → A: Alters protein folding. Prevents formation of regulatory disulfide bond and down-regulation of activity. Decreases association with P4HB. 3 Publications1
Mutagenesisi394C → A: Retains activity towards P4HB. Does not act as a dominant negative mutant. Induces defects in folding. Remains associated with P4HB. 5 Publications1
Mutagenesisi395F → D: Increased catalytical activity. 1 Publication1
Mutagenesisi397C → A: Acts as a dominant negative mutant; does not induce defects in folding; remains associated with P4HB. 3 Publications1

Organism-specific databases

DisGeNETi30001
OpenTargetsiENSG00000197930
PharmGKBiPA27862

Chemistry databases

ChEMBLiCHEMBL1671609

Polymorphism and mutation databases

BioMutaiERO1L
DMDMi50400608

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 231 PublicationAdd BLAST23
ChainiPRO_000000841524 – 468ERO1-like protein alphaAdd BLAST445

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi35 ↔ 48Combined sources1 Publication
Disulfide bondi37 ↔ 46Combined sources1 Publication
Disulfide bondi85 ↔ 391Combined sources1 Publication
Disulfide bondi94 ↔ 131AlternateCombined sources1 Publication
Disulfide bondi94 ↔ 99Redox-active; alternate2 Publications
Disulfide bondi99 ↔ 104AlternateCurated
Modified residuei106PhosphoserineCombined sources1
Modified residuei143PhosphoserineCombined sources1
Disulfide bondi208 ↔ 241Combined sources1 Publication
Glycosylationi280N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi384N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi394 ↔ 397Redox-activeCombined sources1 Publication

Post-translational modificationi

N-glycosylated.3 Publications
The Cys-94/Cys-99 and Cys-394/Cys-397 disulfide bonds constitute the redox-active center. The Cys-94/Cys-99 disulfide bond may accept electron from P4HB and funnel them to the active site disulfide Cys-394/Cys-397 (By similarity). The regulatory Cys-99/Cys-104 disulfide bond stabilizes the other regulatory bond Cys-94/Cys-131 (PubMed:23027870).By similarity1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ96HE7
MaxQBiQ96HE7
PaxDbiQ96HE7
PeptideAtlasiQ96HE7
PRIDEiQ96HE7
ProteomicsDBi76737

PTM databases

GlyConnecti1225
iPTMnetiQ96HE7
PhosphoSitePlusiQ96HE7
SwissPalmiQ96HE7

Expressioni

Tissue specificityi

Widely expressed at low level. Expressed at high level in upper digestive tract. Highly expressed in esophagus. Weakly expressed in stomach and duodenum.1 Publication

Inductioni

Stimulated by hypoxia; suggesting that it is regulated via the HIF-pathway.1 Publication

Gene expression databases

BgeeiENSG00000197930 Expressed in 218 organ(s), highest expression level in esophagus squamous epithelium
CleanExiHS_ERO1L
ExpressionAtlasiQ96HE7 baseline and differential
GenevisibleiQ96HE7 HS

Organism-specific databases

HPAiCAB034294
HPA026653
HPA030053

Interactioni

Subunit structurei

Predominantly monomer. May function both as a monomer and a homodimer. Interacts with PDILT.3 Publications

Binary interactionsi

Protein-protein interaction databases

BioGridi119025, 27 interactors
IntActiQ96HE7, 12 interactors
MINTiQ96HE7
STRINGi9606.ENSP00000379042

Chemistry databases

BindingDBiQ96HE7

Structurei

Secondary structure

1468
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ96HE7
SMRiQ96HE7
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96HE7

Family & Domainsi

Sequence similaritiesi

Belongs to the EROs family.Curated

Keywords - Domaini

Redox-active center, Signal

Phylogenomic databases

eggNOGiKOG2608 Eukaryota
COG5061 LUCA
GeneTreeiENSGT00390000007753
HOGENOMiHOG000012778
HOVERGENiHBG051507
InParanoidiQ96HE7
KOiK10950
OMAiMDCVGCL
OrthoDBiEOG091G04ZQ
PhylomeDBiQ96HE7
TreeFamiTF314471

Family and domain databases

InterProiView protein in InterPro
IPR007266 Ero1
IPR037192 ERO1-like_sf
PANTHERiPTHR12613 PTHR12613, 1 hit
PfamiView protein in Pfam
PF04137 ERO1, 1 hit
PIRSFiPIRSF017205 ERO1, 1 hit
SUPFAMiSSF110019 SSF110019, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

Q96HE7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGRGWGFLFG LLGAVWLLSS GHGEEQPPET AAQRCFCQVS GYLDDCTCDV
60 70 80 90 100
ETIDRFNNYR LFPRLQKLLE SDYFRYYKVN LKRPCPFWND ISQCGRRDCA
110 120 130 140 150
VKPCQSDEVP DGIKSASYKY SEEANNLIEE CEQAERLGAV DESLSEETQK
160 170 180 190 200
AVLQWTKHDD SSDNFCEADD IQSPEAEYVD LLLNPERYTG YKGPDAWKIW
210 220 230 240 250
NVIYEENCFK PQTIKRPLNP LASGQGTSEE NTFYSWLEGL CVEKRAFYRL
260 270 280 290 300
ISGLHASINV HLSARYLLQE TWLEKKWGHN ITEFQQRFDG ILTEGEGPRR
310 320 330 340 350
LKNLYFLYLI ELRALSKVLP FFERPDFQLF TGNKIQDEEN KMLLLEILHE
360 370 380 390 400
IKSFPLHFDE NSFFAGDKKE AHKLKEDFRL HFRNISRIMD CVGCFKCRLW
410 420 430 440 450
GKLQTQGLGT ALKILFSEKL IANMPESGPS YEFHLTRQEI VSLFNAFGRI
460
STSVKELENF RNLLQNIH
Length:468
Mass (Da):54,393
Last modified:July 19, 2004 - v2
Checksum:i92ECE6531C9CCA33
GO

Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V5B3G3V5B3_HUMAN
ERO1-like protein alpha
ERO1A
169Annotation score:
G3V3E6G3V3E6_HUMAN
ERO1-like protein alpha
ERO1A
257Annotation score:
G3V503G3V503_HUMAN
ERO1-like protein alpha
ERO1A
125Annotation score:
G3V2H0G3V2H0_HUMAN
ERO1-like protein alpha
ERO1A
75Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti456E → K in AAH08674 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF081886 mRNA Translation: AAF35260.1
AF123887 mRNA Translation: AAF06104.1
AY358463 mRNA Translation: AAQ88828.1
AK292839 mRNA Translation: BAF85528.1
AL133453 Genomic DNA No translation available.
BC008674 mRNA Translation: AAH08674.1
BC012941 mRNA Translation: AAH12941.1
CCDSiCCDS9709.1
RefSeqiNP_055399.1, NM_014584.2
UniGeneiHs.525339
Hs.592304

Genome annotation databases

EnsembliENST00000395686; ENSP00000379042; ENSG00000197930
GeneIDi30001
KEGGihsa:30001
UCSCiuc001wzv.4 human

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF081886 mRNA Translation: AAF35260.1
AF123887 mRNA Translation: AAF06104.1
AY358463 mRNA Translation: AAQ88828.1
AK292839 mRNA Translation: BAF85528.1
AL133453 Genomic DNA No translation available.
BC008674 mRNA Translation: AAH08674.1
BC012941 mRNA Translation: AAH12941.1
CCDSiCCDS9709.1
RefSeqiNP_055399.1, NM_014584.2
UniGeneiHs.525339
Hs.592304

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AHQX-ray2.35A22-468[»]
3AHRX-ray3.07A22-468[»]
ProteinModelPortaliQ96HE7
SMRiQ96HE7
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119025, 27 interactors
IntActiQ96HE7, 12 interactors
MINTiQ96HE7
STRINGi9606.ENSP00000379042

Chemistry databases

BindingDBiQ96HE7
ChEMBLiCHEMBL1671609

PTM databases

GlyConnecti1225
iPTMnetiQ96HE7
PhosphoSitePlusiQ96HE7
SwissPalmiQ96HE7

Polymorphism and mutation databases

BioMutaiERO1L
DMDMi50400608

Proteomic databases

EPDiQ96HE7
MaxQBiQ96HE7
PaxDbiQ96HE7
PeptideAtlasiQ96HE7
PRIDEiQ96HE7
ProteomicsDBi76737

Protocols and materials databases

DNASUi30001
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000395686; ENSP00000379042; ENSG00000197930
GeneIDi30001
KEGGihsa:30001
UCSCiuc001wzv.4 human

Organism-specific databases

CTDi30001
DisGeNETi30001
EuPathDBiHostDB:ENSG00000197930.12
GeneCardsiERO1A
HGNCiHGNC:13280 ERO1A
HPAiCAB034294
HPA026653
HPA030053
MIMi615435 gene
neXtProtiNX_Q96HE7
OpenTargetsiENSG00000197930
PharmGKBiPA27862
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2608 Eukaryota
COG5061 LUCA
GeneTreeiENSGT00390000007753
HOGENOMiHOG000012778
HOVERGENiHBG051507
InParanoidiQ96HE7
KOiK10950
OMAiMDCVGCL
OrthoDBiEOG091G04ZQ
PhylomeDBiQ96HE7
TreeFamiTF314471

Enzyme and pathway databases

ReactomeiR-HSA-264876 Insulin processing
R-HSA-3299685 Detoxification of Reactive Oxygen Species

Miscellaneous databases

ChiTaRSiERO1A human
EvolutionaryTraceiQ96HE7
GeneWikiiERO1L
GenomeRNAii30001
PROiPR:Q96HE7
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000197930 Expressed in 218 organ(s), highest expression level in esophagus squamous epithelium
CleanExiHS_ERO1L
ExpressionAtlasiQ96HE7 baseline and differential
GenevisibleiQ96HE7 HS

Family and domain databases

InterProiView protein in InterPro
IPR007266 Ero1
IPR037192 ERO1-like_sf
PANTHERiPTHR12613 PTHR12613, 1 hit
PfamiView protein in Pfam
PF04137 ERO1, 1 hit
PIRSFiPIRSF017205 ERO1, 1 hit
SUPFAMiSSF110019 SSF110019, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiERO1A_HUMAN
AccessioniPrimary (citable) accession number: Q96HE7
Secondary accession number(s): A8K9X4
, A8MYW1, Q7LD45, Q9P1Q9, Q9UKV6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: October 10, 2018
This is version 161 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again