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Q8R180

- ERO1A_MOUSE

UniProt

Q8R180 - ERO1A_MOUSE

Protein

ERO1-like protein alpha

Gene

Ero1l

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (24 Mar 2009)
      Previous versions | rss
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    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

    FAD.By 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

    1. oxidoreductase activity Source: MGI
    2. oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor Source: InterPro
    3. protein disulfide isomerase activity Source: InterPro
    4. protein disulfide oxidoreductase activity Source: MGI

    GO - Biological processi

    1. 4-hydroxyproline metabolic process Source: MGI
    2. brown fat cell differentiation Source: MGI
    3. cell redox homeostasis Source: MGI
    4. chaperone mediated protein folding requiring cofactor Source: Ensembl
    5. endoplasmic reticulum unfolded protein response Source: MGI
    6. extracellular matrix organization Source: MGI
    7. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: UniProtKB
    8. protein folding Source: MGI
    9. protein maturation by protein folding Source: MGI
    10. release of sequestered calcium ion into cytosol Source: UniProtKB
    11. response to endoplasmic reticulum stress Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Apoptosis, Electron transport, Transport

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    ReactomeiREACT_189141. Detoxification of Reactive Oxygen Species.
    REACT_207837. Insulin processing.

    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 oxidoreductin-1-like protein
    Oxidoreductin-1-L-alpha
    Gene namesi
    Name:Ero1l
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:1354385. Ero1l.

    Subcellular locationi

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

    GO - Cellular componenti

    1. integral component of endoplasmic reticulum membrane Source: MGI

    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_0000008416Add
    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; alternate
    Disulfide bondi94 ↔ 99Redox-active; alternateBy similarity
    Disulfide bondi99 ↔ 104AlternateBy 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.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

    MaxQBiQ8R180.
    PaxDbiQ8R180.
    PRIDEiQ8R180.

    PTM databases

    PhosphoSiteiQ8R180.

    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

    ArrayExpressiQ8R180.
    BgeeiQ8R180.
    CleanExiMM_ERO1L.
    GenevestigatoriQ8R180.

    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 interaction.
    MINTiMINT-4094692.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8R180.
    SMRiQ8R180. Positions 34-461.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the EROs family.Curated

    Keywords - Domaini

    Redox-active center, Signal

    Phylogenomic databases

    eggNOGiCOG5061.
    GeneTreeiENSGT00390000007753.
    HOGENOMiHOG000012778.
    HOVERGENiHBG051507.
    InParanoidiQ8R180.
    KOiK10950.
    OMAiEADDIHS.
    OrthoDBiEOG7PP579.
    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

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    MGRAWGLLVG LLGVVWLLRL GHGEERRPET AAQRCFCQVS GYLDDCTCDV    50
    ETIDKFNNYR LFPRLQKLLE SDYFRYYKVN LKKPCPFWND INQCGRRDCA 100
    VKPCHSDEVP DGIKSASYKY SEEANRIEEC EQAERLGAVD ESLSEETQKA 150
    VLQWTKHDDS SDSFCEIDDI QSPDAEYVDL LLNPERYTGY KGPDAWRIWS 200
    VIYEENCFKP QTIQRPLASG RGKSKENTFY NWLEGLCVEK RAFYRLISGL 250
    HASINVHLSA RYLLQDTWLE KKWGHNVTEF QQRFDGILTE GEGPRRLRNL 300
    YFLYLIELRA LSKVLPFFER PDFQLFTGNK VQDAENKALL LEILHEIKSF 350
    PLHFDENSFF AGDKNEAHKL KEDFRLHFRN ISRIMDCVGC FKCRLWGKLQ 400
    TQGLGTALKI LFSEKLIANM PESGPSYEFQ LTRQEIVSLF NAFGRISTSV 450
    RELENFRHLL QNVH 464
    Length:464
    Mass (Da):54,084
    Last modified:March 24, 2009 - v2
    Checksum:iFED19B00E1FBD2A1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti130 – 1301C → G in AAH25102. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF144695 mRNA. Translation: AAF20364.1 .
    BC025102 mRNA. Translation: AAH25102.1 .
    AK009667 mRNA. Translation: BAB26428.1 .
    CCDSi CCDS36893.1.
    RefSeqi NP_056589.1. NM_015774.3.
    UniGenei Mm.387108.

    3D structure databases

    ProteinModelPortali Q8R180.
    SMRi Q8R180. Positions 34-461.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8R180. 1 interaction.
    MINTi MINT-4094692.

    PTM databases

    PhosphoSitei Q8R180.

    Proteomic databases

    MaxQBi Q8R180.
    PaxDbi Q8R180.
    PRIDEi Q8R180.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000022378 ; ENSMUSP00000022378 ; ENSMUSG00000021831 .
    GeneIDi 50527.
    KEGGi mmu:50527.
    UCSCi uc007tgm.2. mouse.

    Organism-specific databases

    CTDi 30001.
    MGIi MGI:1354385. Ero1l.

    Phylogenomic databases

    eggNOGi COG5061.
    GeneTreei ENSGT00390000007753.
    HOGENOMi HOG000012778.
    HOVERGENi HBG051507.
    InParanoidi Q8R180.
    KOi K10950.
    OMAi EADDIHS.
    OrthoDBi EOG7PP579.
    PhylomeDBi Q8R180.
    TreeFami TF314471.

    Enzyme and pathway databases

    Reactomei REACT_189141. Detoxification of Reactive Oxygen Species.
    REACT_207837. Insulin processing.

    Miscellaneous databases

    ChiTaRSi ERO1L. mouse.
    NextBioi 307530.
    PROi Q8R180.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8R180.
    Bgeei Q8R180.
    CleanExi MM_ERO1L.
    Genevestigatori Q8R180.

    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

    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.
      , 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.

    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: October 1, 2014
    This is version 110 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

    External Data

    Dasty 3