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
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 (By similarity). Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1.By similarity2 Publications

Cofactori

FADBy similarity

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 the active site Cys-94 and Cys-130, and between Cys-99 and Cys-104. Glutathione may be required to regulate its activity in the endoplasmic reticulum (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei186FADBy similarity1
Binding sitei188FADBy similarity1
Binding sitei199FADBy similarity1
Binding sitei248FADBy similarity1
Binding sitei251FADBy similarity1
Binding sitei283FADBy similarity1
Binding sitei296FADBy similarity1

GO - Molecular functioni

GO - Biological processi

  • 4-hydroxyproline metabolic process Source: MGI
  • animal organ senescence Source: Ensembl
  • brown fat cell differentiation Source: MGI
  • cell redox homeostasis Source: MGI
  • cellular protein modification process Source: GO_Central
  • cellular response to hypoxia Source: Ensembl
  • chaperone mediated protein folding requiring cofactor Source: MGI
  • endoplasmic reticulum unfolded protein response Source: MGI
  • extracellular matrix organization Source: MGI
  • intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: UniProtKB
  • oxidation-reduction process Source: MGI
  • protein folding Source: MGI
  • protein folding in endoplasmic reticulum Source: GO_Central
  • protein maturation by protein folding Source: MGI
  • release of sequestered calcium ion into cytosol Source: UniProtKB
  • response to endoplasmic reticulum stress Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Apoptosis, Electron transport, Transport

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiR-MMU-264876. Insulin processing.
R-MMU-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 reticulum oxidoreductase alphaBy similarity
Endoplasmic reticulum oxidoreductin-1-like protein
Oxidoreductin-1-L-alpha
Gene namesi
Name:Ero1aBy similarity
Synonyms:Ero1l
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1354385. Ero1l.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000000841624 – 464ERO1-like protein alphaAdd BLAST441

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi35 ↔ 48By similarity
Disulfide bondi37 ↔ 46By similarity
Disulfide bondi85 ↔ 387By similarity
Disulfide bondi94 ↔ 130AlternateBy similarity
Disulfide bondi94 ↔ 99Redox-active; alternateBy similarity
Disulfide bondi99 ↔ 104AlternateBy similarity
Modified residuei106PhosphoserineBy similarity1
Modified residuei142PhosphoserineBy similarity1
Disulfide bondi207 ↔ 237By similarity
Glycosylationi276N-linked (GlcNAc...)Sequence analysis1
Glycosylationi380N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi390 ↔ 393Redox-activeBy similarity

Post-translational modificationi

N-glycosylated.By similarity
The Cys-94/Cys-99 and Cys-390/Cys-393 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-390/Cys-393. The regulatory Cys-99/Cys-104 disulfide bond stabilizes the other regulatory bond Cys-94/Cys-130 (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ8R180.
MaxQBiQ8R180.
PaxDbiQ8R180.
PRIDEiQ8R180.

PTM databases

iPTMnetiQ8R180.
PhosphoSitePlusiQ8R180.
SwissPalmiQ8R180.

Expressioni

Tissue specificityi

Widely expressed (at protein level).1 Publication

Inductioni

Stimulated by hypoxia; suggesting that it is regulated via the HIF-pathway. By ER stress in a DDIT3/CHOP-dependent manner.2 Publications

Gene expression databases

BgeeiENSMUSG00000021831.
CleanExiMM_ERO1L.
ExpressionAtlasiQ8R180. baseline and differential.
GenevisibleiQ8R180. MM.

Interactioni

Subunit structurei

Predominantly monomer. May function both as a monomer and a homodimer. Interacts with PDILT (By similarity).By similarity

Protein-protein interaction databases

IntActiQ8R180. 1 interactor.
MINTiMINT-4094692.
STRINGi10090.ENSMUSP00000022378.

Structurei

3D structure databases

ProteinModelPortaliQ8R180.
ModBaseiSearch...
MobiDBiSearch...

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.
InParanoidiQ8R180.
KOiK10950.
OMAiFCEVDDI.
OrthoDBiEOG091G04ZQ.
PhylomeDBiQ8R180.
TreeFamiTF314471.

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.

Q8R180-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRAWGLLVG LLGVVWLLRL GHGEERRPET AAQRCFCQVS GYLDDCTCDV
60 70 80 90 100
ETIDKFNNYR LFPRLQKLLE SDYFRYYKVN LKKPCPFWND INQCGRRDCA
110 120 130 140 150
VKPCHSDEVP DGIKSASYKY SEEANRIEEC EQAERLGAVD ESLSEETQKA
160 170 180 190 200
VLQWTKHDDS SDSFCEIDDI QSPDAEYVDL LLNPERYTGY KGPDAWRIWS
210 220 230 240 250
VIYEENCFKP QTIQRPLASG RGKSKENTFY NWLEGLCVEK RAFYRLISGL
260 270 280 290 300
HASINVHLSA RYLLQDTWLE KKWGHNVTEF QQRFDGILTE GEGPRRLRNL
310 320 330 340 350
YFLYLIELRA LSKVLPFFER PDFQLFTGNK VQDAENKALL LEILHEIKSF
360 370 380 390 400
PLHFDENSFF AGDKNEAHKL KEDFRLHFRN ISRIMDCVGC FKCRLWGKLQ
410 420 430 440 450
TQGLGTALKI LFSEKLIANM PESGPSYEFQ LTRQEIVSLF NAFGRISTSV
460
RELENFRHLL QNVH
Length:464
Mass (Da):54,084
Last modified:March 24, 2009 - v2
Checksum:iFED19B00E1FBD2A1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti130C → G in AAH25102 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF144695 mRNA. Translation: AAF20364.1.
BC025102 mRNA. Translation: AAH25102.1.
AK009667 mRNA. Translation: BAB26428.1.
CCDSiCCDS36893.1.
RefSeqiNP_056589.1. NM_015774.3.
UniGeneiMm.387108.

Genome annotation databases

EnsembliENSMUST00000022378; ENSMUSP00000022378; ENSMUSG00000021831.
GeneIDi50527.
KEGGimmu:50527.
UCSCiuc007tgm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF144695 mRNA. Translation: AAF20364.1.
BC025102 mRNA. Translation: AAH25102.1.
AK009667 mRNA. Translation: BAB26428.1.
CCDSiCCDS36893.1.
RefSeqiNP_056589.1. NM_015774.3.
UniGeneiMm.387108.

3D structure databases

ProteinModelPortaliQ8R180.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8R180. 1 interactor.
MINTiMINT-4094692.
STRINGi10090.ENSMUSP00000022378.

PTM databases

iPTMnetiQ8R180.
PhosphoSitePlusiQ8R180.
SwissPalmiQ8R180.

Proteomic databases

EPDiQ8R180.
MaxQBiQ8R180.
PaxDbiQ8R180.
PRIDEiQ8R180.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022378; ENSMUSP00000022378; ENSMUSG00000021831.
GeneIDi50527.
KEGGimmu:50527.
UCSCiuc007tgm.2. mouse.

Organism-specific databases

CTDi50527.
MGIiMGI:1354385. Ero1l.

Phylogenomic databases

eggNOGiKOG2608. Eukaryota.
COG5061. LUCA.
GeneTreeiENSGT00390000007753.
HOGENOMiHOG000012778.
HOVERGENiHBG051507.
InParanoidiQ8R180.
KOiK10950.
OMAiFCEVDDI.
OrthoDBiEOG091G04ZQ.
PhylomeDBiQ8R180.
TreeFamiTF314471.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiEro1l. mouse.
PROiQ8R180.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000021831.
CleanExiMM_ERO1L.
ExpressionAtlasiQ8R180. baseline and differential.
GenevisibleiQ8R180. MM.

Family and domain databases

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

Entry informationi

Entry nameiERO1A_MOUSE
AccessioniPrimary (citable) accession number: Q8R180
Secondary accession number(s): Q9CV47, Q9QY03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: March 24, 2009
Last modified: November 2, 2016
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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.