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Q8R180 (ERO1A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ERO1-like protein alpha

Short name=ERO1-L
Short name=ERO1-L-alpha
EC=1.8.4.-
Alternative name(s):
Endoplasmic reticulum oxidoreductin-1-like protein
Oxidoreductin-1-L-alpha
Gene names
Name:Ero1l
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length464 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.6

Cofactor

FAD By similarity.

Enzyme regulation

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.

Subunit structure

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

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side By similarity. Note: The association with ERP44 is essential for its retention in the endoplasmic reticulum By similarity.

Tissue specificity

Widely expressed (at protein level). Ref.6

Induction

Stimulated by hypoxia; suggesting that it is regulated via the HIF-pathway. By ER stress in a DDIT3/CHOP-dependent manner. Ref.4 Ref.5

Post-translational modification

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.

Sequence similarities

Belongs to the EROs family.

Ontologies

Keywords
   Biological processApoptosis
Electron transport
Transport
   Cellular componentEndoplasmic reticulum
Membrane
   DomainRedox-active center
Signal
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process4-hydroxyproline metabolic process

Inferred from genetic interaction PubMed 22981861. Source: MGI

brown fat cell differentiation

Inferred from direct assay PubMed 18492766. Source: MGI

cell redox homeostasis

Inferred from genetic interaction PubMed 23589496. Source: MGI

chaperone mediated protein folding requiring cofactor

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum unfolded protein response

Inferred from direct assay PubMed 15601821. Source: MGI

extracellular matrix organization

Inferred from genetic interaction PubMed 22981861. Source: MGI

intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress

Inferred from mutant phenotype Ref.5. Source: UniProtKB

protein folding

Inferred from direct assay PubMed 15601821. Source: MGI

protein maturation by protein folding

Inferred from genetic interaction PubMed 22981861. Source: MGI

release of sequestered calcium ion into cytosol

Inferred from mutant phenotype Ref.5. Source: UniProtKB

response to endoplasmic reticulum stress

Inferred from direct assay Ref.5. Source: UniProtKB

   Cellular_componentintegral component of endoplasmic reticulum membrane

Inferred from sequence orthology Ref.1. Source: MGI

   Molecular_functionoxidoreductase activity

Inferred from direct assay PubMed 15601821. Source: MGI

oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor

Inferred from electronic annotation. Source: InterPro

protein disulfide isomerase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 464441ERO1-like protein alpha
PRO_0000008416

Sites

Binding site1861FAD By similarity
Binding site1881FAD By similarity
Binding site1991FAD By similarity
Binding site2481FAD By similarity
Binding site2511FAD By similarity
Binding site2831FAD By similarity
Binding site2961FAD By similarity

Amino acid modifications

Modified residue1421Phosphoserine By similarity
Glycosylation2761N-linked (GlcNAc...) Potential
Glycosylation3801N-linked (GlcNAc...) Potential
Disulfide bond35 ↔ 48 By similarity
Disulfide bond37 ↔ 46 By similarity
Disulfide bond85 ↔ 387 By similarity
Disulfide bond94 ↔ 130Alternate; alternate
Disulfide bond94 ↔ 99Redox-active; alternate By similarity
Disulfide bond99 ↔ 104Alternate By similarity
Disulfide bond207 ↔ 237 By similarity
Disulfide bond390 ↔ 393Redox-active By similarity

Experimental info

Sequence conflict1301C → G in AAH25102. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8R180 [UniParc].

Last modified March 24, 2009. Version 2.
Checksum: FED19B00E1FBD2A1

FASTA46454,084
        10         20         30         40         50         60 
MGRAWGLLVG LLGVVWLLRL GHGEERRPET AAQRCFCQVS GYLDDCTCDV ETIDKFNNYR 

        70         80         90        100        110        120 
LFPRLQKLLE SDYFRYYKVN LKKPCPFWND INQCGRRDCA VKPCHSDEVP DGIKSASYKY 

       130        140        150        160        170        180 
SEEANRIEEC EQAERLGAVD ESLSEETQKA VLQWTKHDDS SDSFCEIDDI QSPDAEYVDL 

       190        200        210        220        230        240 
LLNPERYTGY KGPDAWRIWS VIYEENCFKP QTIQRPLASG RGKSKENTFY NWLEGLCVEK 

       250        260        270        280        290        300 
RAFYRLISGL HASINVHLSA RYLLQDTWLE KKWGHNVTEF QQRFDGILTE GEGPRRLRNL 

       310        320        330        340        350        360 
YFLYLIELRA LSKVLPFFER PDFQLFTGNK VQDAENKALL LEILHEIKSF PLHFDENSFF 

       370        380        390        400        410        420 
AGDKNEAHKL KEDFRLHFRN ISRIMDCVGC FKCRLWGKLQ TQGLGTALKI LFSEKLIANM 

       430        440        450        460 
PESGPSYEFQ LTRQEIVSLF NAFGRISTSV RELENFRHLL QNVH 

« Hide

References

« Hide 'large scale' references
[1]"ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum."
Cabibbo A., Pagani M., Fabbri M., Rocchi M., Farmery M.R., Bulleid N.J., Sitia R.
J. Biol. Chem. 275:4827-4833(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary tumor.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 232-464.
Strain: C57BL/6J.
Tissue: Tongue.
[4]"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: INDUCTION.
[5]"Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis."
Li G., Mongillo M., Chin K.T., Harding H., Ron D., Marks A.R., Tabas I.
J. Cell Biol. 186:783-792(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[6]"ERO1-beta, a pancreas-specific disulfide oxidase, promotes insulin biogenesis and glucose homeostasis."
Zito E., Chin K.T., Blais J., Harding H.P., Ron D.
J. Cell Biol. 188:821-832(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF144695 mRNA. Translation: AAF20364.1.
BC025102 mRNA. Translation: AAH25102.1.
AK009667 mRNA. Translation: BAB26428.1.
RefSeqNP_056589.1. NM_015774.3.
UniGeneMm.387108.

3D structure databases

ProteinModelPortalQ8R180.
SMRQ8R180. Positions 34-461.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8R180. 1 interaction.
MINTMINT-4094692.

PTM databases

PhosphoSiteQ8R180.

Proteomic databases

PaxDbQ8R180.
PRIDEQ8R180.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022378; ENSMUSP00000022378; ENSMUSG00000021831.
GeneID50527.
KEGGmmu:50527.
UCSCuc007tgm.2. mouse.

Organism-specific databases

CTD30001.
MGIMGI:1354385. Ero1l.

Phylogenomic databases

eggNOGCOG5061.
GeneTreeENSGT00390000007753.
HOGENOMHOG000012778.
HOVERGENHBG051507.
InParanoidQ8R180.
KOK10950.
OMAQVENCEE.
OrthoDBEOG7PP579.
PhylomeDBQ8R180.
TreeFamTF314471.

Gene expression databases

ArrayExpressQ8R180.
BgeeQ8R180.
CleanExMM_ERO1L.
GenevestigatorQ8R180.

Family and domain databases

InterProIPR007266. Ero1.
[Graphical view]
PANTHERPTHR12613:SF0. PTHR12613:SF0. 1 hit.
PfamPF04137. ERO1. 1 hit.
[Graphical view]
PIRSFPIRSF017205. ERO1. 1 hit.
ProtoNetSearch...

Other

ChiTaRSERO1L. mouse.
NextBio307530.
PROQ8R180.
SOURCESearch...

Entry information

Entry nameERO1A_MOUSE
AccessionPrimary (citable) accession number: Q8R180
Secondary accession number(s): Q9CV47, Q9QY03
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: March 24, 2009
Last modified: April 16, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot