ERO1_KLULA
ID ERO1_KLULA Reviewed; 561 AA.
AC Q8NIP5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Endoplasmic reticulum oxidoreductin-1;
DE EC=1.8.4.-;
DE Flags: Precursor;
GN Name=ERO1; OrderedLocusNames=KLLA0D10241g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RA Lodi T.;
RT "Cloning and characterization of ERO1 gene of Kluyveromyces lactis.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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}.
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DR EMBL; AJ489319; CAD33524.1; -; Genomic_DNA.
DR EMBL; CR382124; CAH00613.1; -; Genomic_DNA.
DR RefSeq; XP_453517.1; XM_453517.1.
DR AlphaFoldDB; Q8NIP5; -.
DR SMR; Q8NIP5; -.
DR STRING; 28985.XP_453517.1; -.
DR PRIDE; Q8NIP5; -.
DR EnsemblFungi; CAH00613; CAH00613; KLLA0_D10241g.
DR GeneID; 2893596; -.
DR KEGG; kla:KLLA0_D10241g; -.
DR eggNOG; KOG2608; Eukaryota.
DR HOGENOM; CLU_023061_1_0_1; -.
DR InParanoid; Q8NIP5; -.
DR OMA; RDYCVPD; -.
DR Proteomes; UP000000598; Chromosome D.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR GO; GO:0016972; F:thiol oxidase activity; IEA:EnsemblFungi.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; IEA:EnsemblFungi.
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..561
FT /note="Endoplasmic reticulum oxidoreductin-1"
FT /id="PRO_0000008425"
FT ACT_SITE 352
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT ACT_SITE 355
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT BINDING 187
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT BINDING 189
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT BINDING 200
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT BINDING 228
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT BINDING 231
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT BINDING 260
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..349
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT DISULFID 105..110
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT DISULFID 145..166
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT DISULFID 152..295
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT DISULFID 352..355
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
SQ SEQUENCE 561 AA; 64954 MW; 6DE6C6D85987C628 CRC64;
MVKVLQLCFL SAISLVQALN STVDQKDEAK VDINTVFDND STNFCRMDKT EAIGATCDVT
FHEINEVNNN IRPQLLSLVQ SDFFKYFKLD LYKECPFWSD NNGYCVNRAC AVDVVEDWDS
LPEYWQPEIL GNIENATTDI TDDECSFLDE LCDKPRFEAE KDIEYCDTND FNSQHSVLVD
LTANPERFTG YGGEQSSQIW SSIYKENCFS LGDENQCLAK DAFYRLISGL HASIGTHLSN
EHLNTETGKW EPNLELFMTR VGNFPDRVSN IYFNFAVVAK ALWKIRPYMN ELGFCNAYNE
DVKGMIDGVV SQLNSKVFNE DLLFHDEVSG QLKDDFRIRF KNVTKIMDCV QCDRCRLWGK
VQTTGYATSL KILFEMDNDD DVARQHVVDK LTKYELIALF NTFDRLSKSV EAVNRFEEMY
NYQLKSPGEK LASFFQLDNF FKVLNDKFNS ANHSSQEKES VSNVEKKVNE FNDLKMPEKK
KETHTEVREQ ASGVFKEAWD VEWKNFKQAL RFIVTSYTDL PSTVSKYTVL KLNKLWNKFI
GVPNYLEEGE ELEYPSYNYE E
