ERO1_NEUCR
ID ERO1_NEUCR Reviewed; 668 AA.
AC Q7SEY9;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Endoplasmic reticulum oxidoreductin-1;
DE EC=1.8.4.-;
DE Flags: Precursor;
GN Name=ero-1; ORFNames=NCU02074;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; CM002236; EAA35365.1; -; Genomic_DNA.
DR RefSeq; XP_964601.1; XM_959508.2.
DR AlphaFoldDB; Q7SEY9; -.
DR SMR; Q7SEY9; -.
DR STRING; 5141.EFNCRP00000001083; -.
DR PRIDE; Q7SEY9; -.
DR EnsemblFungi; EAA35365; EAA35365; NCU02074.
DR GeneID; 3880741; -.
DR KEGG; ncr:NCU02074; -.
DR VEuPathDB; FungiDB:NCU02074; -.
DR HOGENOM; CLU_023061_1_0_1; -.
DR InParanoid; Q7SEY9; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..668
FT /note="Endoplasmic reticulum oxidoreductin-1"
FT /id="PRO_0000008426"
FT REGION 116..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 416
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT ACT_SITE 419
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT BINDING 186
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT BINDING 188
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT BINDING 199
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT BINDING 282
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT BINDING 285
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT BINDING 314
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 79..413
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT DISULFID 89..94
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT DISULFID 150..352
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT DISULFID 416..419
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
SQ SEQUENCE 668 AA; 75607 MW; D5E410D19A20C3E3 CRC64;
MKPASRLFYL SLFALWSPEA QCKSDESCAI SPKAIVSDAC ASYSTLEQLN RDIKPALEDL
TRTTDFFSHY RLNLFNKECP FWNDENGMCG NIACAVETLD NEEDIPEVWR AKELGKLEGP
RAKHPGKSVQ KEEPKRPLQG KLGEDVGESC VVEYDDECDD RDYCVPDDEG ASSKGDYVSL
LRNPERFTGY AGDGAKQVWD AIYRENCFQK SSFPKSASLG DTYSVPKNPA AQDFRAVMQA
AGRQHMLEQQ REQNPLVPFV TKTGLESEDE CLEKRVFYKI VSGMHASIST HLCWDFLNQT
TGQWQPNLSC YINRLHKFPE RISNLYFNYA LLTRAVAKLG PYLSSHEEYT FCTGDPAQDA
DTRAKVLAVT SKAANTVPGP VFDESIMFKN GEGPSLKEDF RNRFRNISRL MDCVGCDKCR
LWGKLQTAGY GTALKVLFEF ANNDTSATSS ETDEIPFKLK RTELVALFNT YARLSSSLDA
IQKFRAMVEE SEEGQQPQSH EQIEGSENSG AHHIPDRAKK PRHVIVPTPD AADHAEASDT
NTATTAVDEA KAAGVTPAPK VEHQQQVEVD NNDDDDDDDE FHEFQRQPQQ PDTDPNFVYK
KRTLKDDFEN EFRAVFAAFK LVIRSYLNLP ALIYEITITE LKRFWQFYVG LPVMPRTWEF
RRPSLDEL
