ERO1_CAEEL
ID ERO1_CAEEL Reviewed; 478 AA.
AC Q7YTU4; Q95Q33;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Endoplasmic reticulum oxidoreductin-1;
DE EC=1.8.4.-;
DE Flags: Precursor;
GN Name=ero-1; ORFNames=Y105E8B.8;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Oxidoreductase involved in disulfide bond formation in the
CC endoplasmic reticulum. Efficiently reoxidizes pdi-1, the enzyme
CC catalyzing protein disulfide formation, in order to allow pdi-1 to
CC sustain additional rounds of disulfide formation. Following pdi
CC reoxidation, passes its electrons to molecular oxygen via FAD, leading
CC to the production of reactive oxygen species (ROS) in the cell (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 {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Lumenal side {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q7YTU4-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q7YTU4-2; Sequence=VSP_036006;
CC -!- SIMILARITY: Belongs to the EROs family. {ECO:0000305}.
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DR EMBL; AL132877; CAC70110.4; -; Genomic_DNA.
DR EMBL; AL132877; CAD92388.2; -; Genomic_DNA.
DR RefSeq; NP_001021704.1; NM_001026533.5.
DR RefSeq; NP_001021705.2; NM_001026534.3.
DR AlphaFoldDB; Q7YTU4; -.
DR SMR; Q7YTU4; -.
DR BioGRID; 38710; 1.
DR DIP; DIP-26357N; -.
DR IntAct; Q7YTU4; 1.
DR STRING; 6239.Y105E8B.8c; -.
DR EPD; Q7YTU4; -.
DR PeptideAtlas; Q7YTU4; -.
DR PRIDE; Q7YTU4; -.
DR EnsemblMetazoa; Y105E8B.8a.1; Y105E8B.8a.1; WBGene00001334. [Q7YTU4-1]
DR EnsemblMetazoa; Y105E8B.8b.1; Y105E8B.8b.1; WBGene00001334. [Q7YTU4-2]
DR UCSC; Y105E8B.8b; c. elegans. [Q7YTU4-1]
DR WormBase; Y105E8B.8a; CE33847; WBGene00001334; ero-1. [Q7YTU4-1]
DR WormBase; Y105E8B.8b; CE42762; WBGene00001334; ero-1. [Q7YTU4-2]
DR eggNOG; KOG2608; Eukaryota.
DR HOGENOM; CLU_023061_2_2_1; -.
DR InParanoid; Q7YTU4; -.
DR PhylomeDB; Q7YTU4; -.
DR PRO; PR:Q7YTU4; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001334; Expressed in adult organism and 4 other tissues.
DR ExpressionAtlas; Q7YTU4; baseline and differential.
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; IMP:WormBase.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:ParkinsonsUK-UCL.
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 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..478
FT /note="Endoplasmic reticulum oxidoreductin-1"
FT /id="PRO_0000008420"
FT REGION 117..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 188
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 190
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 201
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 283
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 295
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..41
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 30..39
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 79..384
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 88..93
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 209..230
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 387..390
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT VAR_SEQ 1..139
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_036006"
SQ SEQUENCE 478 AA; 55154 MW; 1AFDDF7976154ADE CRC64;
MREPLLQLIV LSLIIIVVNT QFESGRLCFC KGFEAVEPCD CSKPQTIDKL NNHRIYEKVQ
KLLKKDFFRF YKVNMDKTCP FWADDRQCGT NQCGIAFCDD EVPAGLRRRN AVNMEAAAVK
EEEDDDAEKC ADAGNNIDPM DRTLHDDEKR QLDAMDHHDD GLEDKFCEIE DDESDGMHYV
DLSKNPERYT GYAGKSPQRV WKSIYEENCF KPDPKFDKNF LTNPSNFGMC LEKRVFYRLI
SGLHSAITIS IAAYNYKPPP PSLGQFGSQM GTWFRNTEMF AGRFGTKWSW EGPQRLRNVY
FIYLLELRAL LKAAPYLQNE LFYTGNDVED AETRKAVEDL LEEIRAYPNH FDESEMFTGV
ESHARALREE FRSHFVNISR IMDCVECDKC RLWGKVQTHG MGTALKILFS DLPHSHYKQD
SSKFQLTRNE VVALLQSFGR YSSSILEVDN FREDMYPGES VMNTAADGPP RKSNKIDL
