ERO1B_MOUSE
ID ERO1B_MOUSE Reviewed; 467 AA.
AC Q8R2E9; Q14DN0;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=ERO1-like protein beta;
DE Short=ERO1-L-beta;
DE EC=1.8.4.-;
DE AltName: Full=Endoplasmic reticulum oxidoreductase beta {ECO:0000250|UniProtKB:Q86YB8};
DE AltName: Full=Endoplasmic reticulum oxidoreductin-1-like protein B;
DE AltName: Full=Oxidoreductin-1-L-beta;
DE Flags: Precursor;
GN Name=Ero1b {ECO:0000250|UniProtKB:Q86YB8}; Synonyms=Ero1lb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=FVB/N; TISSUE=Intestine, and Liver;
RA Li B., Abplanalp W.A., Kim P.S.;
RT "Cloning of the two forms of Ero1, alpha and beta and their regulation in
RT cultured thyrocytes.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY, AND DIMERIZATION.
RX PubMed=16012172; DOI=10.1074/jbc.m505023200;
RA Dias-Gunasekara S., Gubbens J., van Lith M., Dunne C., Williams J.A.,
RA Kataky R., Scoones D., Lapthorn A., Bulleid N.J., Benham A.M.;
RT "Tissue-specific expression and dimerization of the endoplasmic reticulum
RT oxidoreductase Ero1beta.";
RL J. Biol. Chem. 280:33066-33075(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF CYS-396.
RX PubMed=20308425; DOI=10.1083/jcb.200911086;
RA Zito E., Chin K.T., Blais J., Harding H.P., Ron D.;
RT "ERO1-beta, a pancreas-specific disulfide oxidase, promotes insulin
RT biogenesis and glucose homeostasis.";
RL J. Cell Biol. 188:821-832(2010).
CC -!- FUNCTION: Oxidoreductase involved in disulfide bond formation in the
CC endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme
CC catalyzing protein disulfide formation, in order to allow P4HB to
CC sustain additional rounds of disulfide formation. Other protein
CC disulfide isomerase family members can also be reoxidized, but at lower
CC rates compared to P4HB, including PDIA2, PDIA3, PDIA4, PDIA6 and
CC NXNDC12. Following P4HB reoxidation, passes its electrons to molecular
CC oxygen via FAD, leading to the production of reactive oxygen species
CC (ROS) in the cell (By similarity). Involved in oxidative proinsulin
CC folding in pancreatic cells, hence required for glucose homeostasis in
CC vivo. {ECO:0000250, ECO:0000269|PubMed:20308425}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q86YB8};
CC -!- ACTIVITY REGULATION: Glutathione may be required to regulate its
CC activity in the endoplasmic reticulum. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Heterodimer with
CC ERO1A; disulfide-linked (By similarity). Also detected as monomer.
CC Homodimers may be somewhat less active than monomers. The abundance of
CC monomers and homodimers may be tissue-specific. Interacts with P4HB (By
CC similarity). Interacts with ERP44 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Lumenal side {ECO:0000250}.
CC Note=The association with ERP44 may be essential for its retention in
CC the endoplasmic reticulum. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in stomach and pancreas
CC (mostly in the islets of Langerhans) (at protein level).
CC {ECO:0000269|PubMed:16012172, ECO:0000269|PubMed:20308425}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: The Cys-90/Cys-95 and Cys-393/Cys-396 disulfide bonds constitute
CC the redox-active center. The Cys-90/Cys-95 disulfide bond may accept
CC electron from P4HB and funnel them to the active site disulfide Cys-
CC 393/Cys-396 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EROs family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF489856; AAL96670.1; -; mRNA.
DR EMBL; AK041951; BAC31108.1; -; mRNA.
DR EMBL; BC058721; AAH58721.1; -; mRNA.
DR EMBL; BC112426; AAI12427.1; -; mRNA.
DR EMBL; BC145888; AAI45889.1; -; mRNA.
DR EMBL; BC145890; AAI45891.1; -; mRNA.
DR CCDS; CCDS36594.1; -.
DR RefSeq; NP_080460.2; NM_026184.2.
DR AlphaFoldDB; Q8R2E9; -.
DR SMR; Q8R2E9; -.
DR STRING; 10090.ENSMUSP00000071864; -.
DR GlyConnect; 2305; 1 N-Linked glycan (1 site).
DR GlyGen; Q8R2E9; 4 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q8R2E9; -.
DR PhosphoSitePlus; Q8R2E9; -.
DR EPD; Q8R2E9; -.
DR jPOST; Q8R2E9; -.
DR MaxQB; Q8R2E9; -.
DR PaxDb; Q8R2E9; -.
DR PRIDE; Q8R2E9; -.
DR ProteomicsDB; 275943; -.
DR Antibodypedia; 34698; 202 antibodies from 25 providers.
DR DNASU; 67475; -.
DR Ensembl; ENSMUST00000071973; ENSMUSP00000071864; ENSMUSG00000057069.
DR GeneID; 67475; -.
DR KEGG; mmu:67475; -.
DR UCSC; uc007plr.1; mouse.
DR CTD; 56605; -.
DR MGI; MGI:1914725; Ero1b.
DR VEuPathDB; HostDB:ENSMUSG00000057069; -.
DR eggNOG; KOG2608; Eukaryota.
DR GeneTree; ENSGT00390000007753; -.
DR HOGENOM; CLU_023061_2_2_1; -.
DR InParanoid; Q8R2E9; -.
DR OMA; RDYCVPD; -.
DR PhylomeDB; Q8R2E9; -.
DR TreeFam; TF314471; -.
DR Reactome; R-MMU-264876; Insulin processing.
DR BioGRID-ORCS; 67475; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Ero1lb; mouse.
DR PRO; PR:Q8R2E9; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8R2E9; protein.
DR Bgee; ENSMUSG00000057069; Expressed in islet of Langerhans and 233 other tissues.
DR ExpressionAtlas; Q8R2E9; baseline and differential.
DR Genevisible; Q8R2E9; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IDA:MGI.
DR GO; GO:0016972; F:thiol oxidase activity; ISO:MGI.
DR GO; GO:0045454; P:cell redox homeostasis; IGI:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IGI:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR GO; GO:0030070; P:insulin processing; IMP:MGI.
DR GO; GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; IGI:MGI.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; ISO:MGI.
DR GO; GO:0022417; P:protein maturation by protein folding; IMP:MGI.
DR InterPro; IPR007266; Ero1.
DR InterPro; IPR037192; ERO1-like_sf.
DR PANTHER; PTHR12613; PTHR12613; 1.
DR Pfam; PF04137; ERO1; 1.
DR PIRSF; PIRSF017205; ERO1; 1.
DR SUPFAM; SSF110019; SSF110019; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Electron transport; Endoplasmic reticulum; FAD;
KW Flavoprotein; Glycoprotein; Membrane; Oxidoreductase; Redox-active center;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..467
FT /note="ERO1-like protein beta"
FT /id="PRO_0000008419"
FT BINDING 186
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 188
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 199
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 251
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 254
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 286
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 299
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 81..390
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 90..130
FT /note="Alternate"
FT /evidence="ECO:0000250|UniProtKB:Q86YB8"
FT DISULFID 90..95
FT /note="Redox-active; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 100..262
FT /evidence="ECO:0000250|UniProtKB:Q86YB8"
FT DISULFID 207..240
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 393..396
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT MUTAGEN 396
FT /note="C->A: Complete loss of disulfide oxidase activity in
FT vitro."
FT /evidence="ECO:0000269|PubMed:20308425"
SQ SEQUENCE 467 AA; 53518 MW; 442E7D6CB42A2446 CRC64;
MSPGFRRAVT GQGAAAAVQL LVTLSFLSSL VKTQVTGVLD DCLCDIDSID KFNTYKIFPK
IKKLQERDYF RYYKVNLKRP CPFWAEDGHC SIKDCHVEPC PESKIPVGIK AGRSNKYSQA
ANSTKELDDC EQANKLGAIN STLSNESKEA FIDWARYDDS QDHFCELDDE RSPAAQYVDL
LLNPERYTGY KGSSAWRVWN SIYEENCFKP RSVYRPLNPL APSRGEDDGE SFYTWLEGLC
LEKRVFYKLI SGLHASINLH LCANYLLEET WGKPSWGPNI KEFRRRFDPV ETKGEGPRRL
KNLYFLYLIE LRALSKVAPY FERSIVDLYT GNVEDDADTK TLLLSIFQDT KSFPMHFDEK
SMFAGDKKGA KSLKEEFRLH FKNISRIMDC VGCDKCRLWG KLQTQGLGTA LKILFSEKEI
QNLPENSPSK GFQLTRQEIV ALLNAFGRLS TSIRELQNFK ALLQHRR
