ERO2_ARATH
ID ERO2_ARATH Reviewed; 472 AA.
AC Q7X9I4; Q9ZV11;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Endoplasmic reticulum oxidoreductin-2;
DE EC=1.8.4.-;
DE Flags: Precursor;
GN Name=AERO2; Synonyms=ERO2; OrderedLocusNames=At2g38960; ORFNames=T7F6.13;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RC TISSUE=Cultured root;
RX PubMed=13678526; DOI=10.1089/152308603768295122;
RA Dixon D.P., Van Lith M., Edwards R., Benham A.;
RT "Cloning and initial characterization of the Arabidopsis thaliana
RT endoplasmic reticulum oxidoreductins.";
RL Antioxid. Redox Signal. 5:389-396(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
CC -!- FUNCTION: Essential oxidoreductase that oxidizes proteins in the
CC endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing
CC directly PDI isomerase through a direct disulfide exchange. Does not
CC act as a direct oxidant of folding substrate, but relies on PDI to
CC transfer oxidizing equivalent. Does not oxidize all PDI related
CC proteins, suggesting that it can discriminate between PDI and related
CC proteins. Its reoxidation probably involves electron transfer to
CC molecular oxygen via FAD. Acts independently of glutathione. May be
CC responsible for a significant proportion of reactive oxygen species
CC (ROS) in the cell, thereby being a source of oxidative stress (By
CC similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q96HE7};
CC -!- SUBUNIT: May function both as a monomer and a homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:13678526}; Peripheral membrane protein
CC {ECO:0000269|PubMed:13678526}; Lumenal side
CC {ECO:0000269|PubMed:13678526}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q7X9I4-1; Sequence=Displayed;
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:13678526}.
CC -!- SIMILARITY: Belongs to the EROs family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC79609.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ551466; CAD83855.1; -; mRNA.
DR EMBL; AC005770; AAC79609.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC09618.1; -; Genomic_DNA.
DR PIR; E84811; E84811.
DR RefSeq; NP_181430.2; NM_129454.4. [Q7X9I4-1]
DR AlphaFoldDB; Q7X9I4; -.
DR SMR; Q7X9I4; -.
DR STRING; 3702.AT2G38960.3; -.
DR PaxDb; Q7X9I4; -.
DR ProteomicsDB; 220699; -. [Q7X9I4-1]
DR EnsemblPlants; AT2G38960.1; AT2G38960.1; AT2G38960. [Q7X9I4-1]
DR GeneID; 818481; -.
DR Gramene; AT2G38960.1; AT2G38960.1; AT2G38960. [Q7X9I4-1]
DR KEGG; ath:AT2G38960; -.
DR Araport; AT2G38960; -.
DR eggNOG; KOG2608; Eukaryota.
DR HOGENOM; CLU_023061_2_1_1; -.
DR InParanoid; Q7X9I4; -.
DR PhylomeDB; Q7X9I4; -.
DR PRO; PR:Q7X9I4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q7X9I4; baseline and differential.
DR Genevisible; Q7X9I4; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0016972; F:thiol oxidase activity; IEA:InterPro.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; IBA:GO_Central.
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 Alternative splicing; Disulfide bond; Electron transport;
KW Endoplasmic reticulum; FAD; Flavoprotein; Glycoprotein; Membrane;
KW Oxidoreductase; Redox-active center; Reference proteome; Signal; Transport.
FT SIGNAL 1..37
FT /evidence="ECO:0000255"
FT CHAIN 38..472
FT /note="Endoplasmic reticulum oxidoreductin-2"
FT /id="PRO_0000008423"
FT BINDING 200
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 202
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 213
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 241
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 244
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 274
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 281
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 55..74
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 57..72
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 111..371
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 120..125
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 221..230
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 374..377
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
SQ SEQUENCE 472 AA; 53449 MW; DC947F5293788B6B CRC64;
MAETDVGSVK GKEKGSGKRW ILLIGAIAAV LLAVVVAVFL NTQNSSISEF TGKICNCRQA
EQQKYIGIVE DCCCDYETVN RLNTEVLNPL LQDLVKTPFY RYFKVKLWCD CPFWPDDGMC
RLRDCSVCEC PESEFPEVFK KPLSQYNPVC QEGKPQATVD RTLDTRAFRG WTVTDNPWTS
DDETDNDEMT YVNLRLNPER YTGYIGPSAR RIWEAIYSEN CPKHTSEGSC QEEKILYKLV
SGLHSSISVH IASDYLLDEA TNLWGQNLTL LYDRVLRYPD RVQNLYFTFL FVLRAVTKAE
DYLGEAEYET GNVIEDLKTK SLVKQVVSDP KTKAACPVPF DEAKLWKGQR GPELKQQLEK
QFRNISAIMD CVGCEKCRLW GKLQILGLGT ALKILFTVNG EDNLRHNLEL QRNEVIALMN
LLHRLSESVK YVHDMSPAAE RIAGGHASSG NSFWQRIVTS IAQSKAVSGK RS
