ERO1_ARATH
ID ERO1_ARATH Reviewed; 469 AA.
AC Q9C7S7;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Endoplasmic reticulum oxidoreductin-1;
DE EC=1.8.4.-;
DE Flags: Precursor;
GN Name=AERO1; Synonyms=ERO1; OrderedLocusNames=At1g72280; ORFNames=T9N14.18;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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 -!- PTM: N-glycosylated. {ECO:0000269|PubMed:13678526}.
CC -!- SIMILARITY: Belongs to the EROs family. {ECO:0000305}.
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DR EMBL; AC067754; AAG51798.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35298.1; -; Genomic_DNA.
DR EMBL; BT008774; AAP68213.1; -; mRNA.
DR PIR; E96746; E96746.
DR RefSeq; NP_177372.1; NM_105887.4.
DR AlphaFoldDB; Q9C7S7; -.
DR SMR; Q9C7S7; -.
DR BioGRID; 28780; 1.
DR STRING; 3702.AT1G72280.1; -.
DR PaxDb; Q9C7S7; -.
DR PRIDE; Q9C7S7; -.
DR ProteomicsDB; 220641; -.
DR EnsemblPlants; AT1G72280.1; AT1G72280.1; AT1G72280.
DR GeneID; 843560; -.
DR Gramene; AT1G72280.1; AT1G72280.1; AT1G72280.
DR KEGG; ath:AT1G72280; -.
DR Araport; AT1G72280; -.
DR TAIR; locus:2207031; AT1G72280.
DR eggNOG; KOG2608; Eukaryota.
DR HOGENOM; CLU_023061_2_1_1; -.
DR InParanoid; Q9C7S7; -.
DR OMA; RDYCVPD; -.
DR OrthoDB; 1181226at2759; -.
DR PhylomeDB; Q9C7S7; -.
DR PRO; PR:Q9C7S7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C7S7; baseline and differential.
DR Genevisible; Q9C7S7; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
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; IDA:TAIR.
DR GO; GO:0016972; F:thiol oxidase activity; IEA:InterPro.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0051604; P:protein maturation; IEA:EnsemblPlants.
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..36
FT /evidence="ECO:0000255"
FT CHAIN 37..469
FT /note="Endoplasmic reticulum oxidoreductin-1"
FT /id="PRO_0000008422"
FT BINDING 201
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 203
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 214
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 242
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 245
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 275
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 282
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 52..71
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 54..69
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 108..372
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 117..122
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 222..231
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 375..378
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
SQ SEQUENCE 469 AA; 53830 MW; BA26B590F84BD8D4 CRC64;
MGKGAIKEEE SEKKRKTWRW PLATLVVVFL AVAVSSRTNS NVGFFFSDRN SCSCSLQKTG
KYKGMIEDCC CDYETVDNLN TEVLNPLLQD LVTTPFFRYY KVKLWCDCPF WPDDGMCRLR
DCSVCECPEN EFPEPFKKPF VPGLPSDDLK CQEGKPQGAV DRTIDNRAFR GWVETKNPWT
HDDDTDSGEM SYVNLQLNPE RYTGYTGPSA RRIWDSIYSE NCPKYSSGET CPEKKVLYKL
ISGLHSSISM HIAADYLLDE SRNQWGQNIE LMYDRILRHP DRVRNMYFTY LFVLRAVTKA
TAYLEQAEYD TGNHAEDLKT QSLIKQLLYS PKLQTACPVP FDEAKLWQGQ SGPELKQQIQ
KQFRNISALM DCVGCEKCRL WGKLQVQGLG TALKILFSVG NQDIGDQTLQ LQRNEVIALV
NLLNRLSESV KMVHDMSPDV ERLMEDQIAK VSAKPARLRR IWDLAVSFW
