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Protein

ERO1-like protein alpha

Gene

Ero1a

Organism
Rattus norvegicus (Rat)
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 similarity).By similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei186 – 1861FADBy similarity
Binding sitei188 – 1881FADBy similarity
Binding sitei199 – 1991FADBy similarity
Binding sitei248 – 2481FADBy similarity
Binding sitei251 – 2511FADBy similarity
Binding sitei283 – 2831FADBy similarity
Binding sitei296 – 2961FADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Apoptosis, Electron transport, Transport

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiR-RNO-264876. Insulin processing.
R-RNO-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 alphaImported
Endoplasmic reticulum oxidoreductin-1-like protein
Global ischemia-induced protein 11
Oxidoreductin-1-L-alpha
Gene namesi
Name:Ero1aImported
Synonyms:Ero1l, Giig11
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 15

Organism-specific databases

RGDi621713. Ero1a.

Subcellular locationi

GO - Cellular componenti

  • dendrite Source: RGD
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 464441ERO1-like protein alphaPRO_0000008417Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi35 ↔ 48By similarity
Disulfide bondi37 ↔ 46By similarity
Disulfide bondi85 ↔ 387By similarity
Disulfide bondi94 ↔ 130Alternate; alternateBy similarity
Disulfide bondi94 ↔ 99Redox-active; alternateBy similarity
Disulfide bondi99 ↔ 104AlternateBy similarity
Modified residuei106 – 1061PhosphoserineBy similarity
Modified residuei142 – 1421PhosphoserineBy similarity
Disulfide bondi207 ↔ 237By similarity
Glycosylationi276 – 2761N-linked (GlcNAc...)Sequence analysis
Glycosylationi380 – 3801N-linked (GlcNAc...)Sequence analysis
Disulfide bondi390 ↔ 393Redox-activeBy similarity

Post-translational modificationi

N-glycosylated.
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

PaxDbiQ8R4A1.
PRIDEiQ8R4A1.

PTM databases

iPTMnetiQ8R4A1.
UniCarbKBiQ8R4A1.

Expressioni

Inductioni

Stimulated by hypoxia; suggesting that it is regulated via the HIF-pathway. Increased expression in brain after global cerebral ischemia.2 Publications

Gene expression databases

ExpressionAtlasiQ8R4A1. baseline and differential.
GenevisibleiQ8R4A1. RN.

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

IntActiQ8R4A1. 2 interactions.
MINTiMINT-4570198.
STRINGi10116.ENSRNOP00000009404.

Structurei

3D structure databases

ProteinModelPortaliQ8R4A1.
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.
InParanoidiQ8R4A1.
KOiK10950.
PhylomeDBiQ8R4A1.
TreeFamiTF314471.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8R4A1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGRGWGLLVG LLGVVWLLRS GQGEEQQQET AAQRCFCQVS GYLDDCTCDV
60 70 80 90 100
ETIDKFNNYR LFPRLQKLLE SDYFRYYKVN LRKPCPFWND INQCGRRDCA
110 120 130 140 150
VKPCHSDEVP DGIKSASYKY SKEANLLEEC EQAERLGAVD ESLSEETQKA
160 170 180 190 200
VLQWTKHDDS SDSFCEVDDI QSPDAEYVDL LLNPERYTGY KGPDAWRIWS
210 220 230 240 250
VIYEENCFKP QTIQRPLASG QGKHKENTFY SWLEGLCVEK RAFYRLISGL
260 270 280 290 300
HASINVHLSA RYLLQDNWLE KKWGHNVTEF QQRFDGVLTE GEGPRRLKNL
310 320 330 340 350
YFLYLIELRA LSKVLPFFER PDFQLFTGNK VQDVENKELL LEILHEVKSF
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):54,018
Last modified:June 1, 2002 - v1
Checksum:i1B71741A9C413772
GO
Isoform 2 (identifier: Q8R4A1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     15-122: VWLLRSGQGE...IKSASYKYSK → FQ

Show »
Length:358
Mass (Da):41,592
Checksum:iCFE237DB53C6F65A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41G → A in AAL61547 (PubMed:12694393).Curated
Sequence conflicti4 – 41G → A in AAL61548 (PubMed:12694393).Curated
Sequence conflicti20 – 223SGQ → LGH in AAL61547 (PubMed:12694393).Curated
Sequence conflicti26 – 283QQQ → RRP in AAL61547 (PubMed:12694393).Curated
Sequence conflicti365 – 3651N → H in AAL61547 (PubMed:12694393).Curated
Sequence conflicti365 – 3651N → H in AAL61548 (PubMed:12694393).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei15 – 122108VWLLR…YKYSK → FQ in isoform 2. 1 PublicationVSP_011023Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY071924 mRNA. Translation: AAL61547.1.
AY071925 mRNA. Translation: AAL61548.1.
AF489855 mRNA. Translation: AAL96669.1.
RefSeqiNP_612537.1. NM_138528.1.
UniGeneiRn.64648.

Genome annotation databases

EnsembliENSRNOT00000009404; ENSRNOP00000009404; ENSRNOG00000006462. [Q8R4A1-1]
GeneIDi171562.
KEGGirno:171562.
UCSCiRGD:621713. rat. [Q8R4A1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY071924 mRNA. Translation: AAL61547.1.
AY071925 mRNA. Translation: AAL61548.1.
AF489855 mRNA. Translation: AAL96669.1.
RefSeqiNP_612537.1. NM_138528.1.
UniGeneiRn.64648.

3D structure databases

ProteinModelPortaliQ8R4A1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8R4A1. 2 interactions.
MINTiMINT-4570198.
STRINGi10116.ENSRNOP00000009404.

PTM databases

iPTMnetiQ8R4A1.
UniCarbKBiQ8R4A1.

Proteomic databases

PaxDbiQ8R4A1.
PRIDEiQ8R4A1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000009404; ENSRNOP00000009404; ENSRNOG00000006462. [Q8R4A1-1]
GeneIDi171562.
KEGGirno:171562.
UCSCiRGD:621713. rat. [Q8R4A1-1]

Organism-specific databases

CTDi30001.
RGDi621713. Ero1a.

Phylogenomic databases

eggNOGiKOG2608. Eukaryota.
COG5061. LUCA.
GeneTreeiENSGT00390000007753.
HOGENOMiHOG000012778.
HOVERGENiHBG051507.
InParanoidiQ8R4A1.
KOiK10950.
PhylomeDBiQ8R4A1.
TreeFamiTF314471.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ8R4A1.

Gene expression databases

ExpressionAtlasiQ8R4A1. baseline and differential.
GenevisibleiQ8R4A1. RN.

Family and domain databases

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

Publicationsi

  1. "Ero1-L, an ischemia-inducible gene from rat brain with homology to global ischemia-induced gene 11 (Giig11), is localized to neuronal dendrites by a dispersed identifier (ID) element-dependent mechanism."
    Chen D., Jin K., Kawaguchi K., Nakayama M., Zhou X., Xiong Z., Zhou A., Mao X.O., Greenberg D.A., Graham S.H., Simon R.P.
    J. Neurochem. 85:670-679(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, INDUCTION.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. "Cloning of the two forms of Ero1, alpha and beta and their regulation in cultured thyrocytes."
    Li B., Abplanalp W.A., Kim P.S.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Thyroid.
  3. "The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-Lalpha."
    Gess B., Hofbauer K.H., Wenger R.H., Lohaus C., Meyer H.E., Kurtz A.
    Eur. J. Biochem. 270:2228-2235(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION.

Entry informationi

Entry nameiERO1A_RAT
AccessioniPrimary (citable) accession number: Q8R4A1
Secondary accession number(s): Q8VH29, Q8VH30
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: June 1, 2002
Last modified: June 8, 2016
This is version 100 of the entry and version 1 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. 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.