ERO1_ASHGO
ID ERO1_ASHGO Reviewed; 546 AA.
AC Q75BB5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Endoplasmic reticulum oxidoreductin-1;
DE EC=1.8.4.-;
DE Flags: Precursor;
GN Name=ERO1; OrderedLocusNames=ADL348W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 193.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Essential oxidoreductase that oxidizes proteins in the
CC endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing
CC directly PDI1 isomerase through a direct disulfide exchange. Does not
CC act as a direct oxidant of folding substrate, but relies on PDI1 to
CC transfer oxidizing equivalent. Does not oxidize all pdi related
CC proteins, suggesting that it can discriminate between PDI1 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:Q03103};
CC -!- SUBUNIT: May function both as a monomer and a homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Lumenal side {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; AE016817; AAS51571.2; -; Genomic_DNA.
DR RefSeq; NP_983747.2; NM_209100.2.
DR AlphaFoldDB; Q75BB5; -.
DR SMR; Q75BB5; -.
DR STRING; 33169.AAS51571; -.
DR EnsemblFungi; AAS51571; AAS51571; AGOS_ADL348W.
DR GeneID; 4619882; -.
DR KEGG; ago:AGOS_ADL348W; -.
DR eggNOG; KOG2608; Eukaryota.
DR HOGENOM; CLU_023061_1_0_1; -.
DR InParanoid; Q75BB5; -.
DR OMA; RDYCVPD; -.
DR Proteomes; UP000000591; Chromosome IV.
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:EnsemblFungi.
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 3: Inferred from homology;
KW Disulfide bond; Electron transport; Endoplasmic reticulum; FAD;
KW Flavoprotein; Glycoprotein; Membrane; Oxidoreductase; Redox-active center;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..546
FT /note="Endoplasmic reticulum oxidoreductin-1"
FT /id="PRO_0000008424"
FT ACT_SITE 347
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT ACT_SITE 350
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT BINDING 182
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT BINDING 184
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT BINDING 195
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT BINDING 223
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT BINDING 226
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT BINDING 255
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 84..344
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT DISULFID 94..99
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT DISULFID 137..161
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT DISULFID 144..290
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT DISULFID 347..350
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
SQ SEQUENCE 546 AA; 62527 MW; DBE5486F211903C9 CRC64;
MQLNKLMLGF MLCASALADD GQQAAEPHTS ANFCKIDKDQ QVGSTCDITF HELNEINEQI
RPQLARLVKT DFFRYFKLDL YKECPFWSDN NGYCVNRACA VDVVDDWESV PDIWQPEVLG
GLDEDSVKSE GGESDECSFL NELCGRRREF ARPEPLSIDY CDVTDFTNKD SVLVDLVANP
ERFTGYGGEQ SAQIWSAIYK ENCFTLGEQG FCLAKDVFYR LISGLHASIA THLSNDYLDT
KTGKWGPNLE LFMARVGNHP DRVANIYFNF AVVAKALWKI QPYLERVEFC NVYDTNVKDM
ISNVVSRLDS RVFNEDLLFQ DDISMRMKDD FRRRFKNVTK IMDCVHCDRC RMWGKVQTTG
YATSLKILFE MDAGDEKARQ RVVDKLTKYE LIGLFNTFDR ISKSVNAINN FERMYHSQME
TNTSSIAAFF QNNFFRLGFT ETEDQETSNA TADMPLPEDS ASDNEPYFAD LKIPARRSKK
QTKEESTSAL QQELQGVYHA LQFIWNSYVN LPRNLLILVL DVANTWFNNF IGVPTQINIL
GDDASD
