ERO11_SCHPO
ID ERO11_SCHPO Reviewed; 467 AA.
AC O74401;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=ERO1-like protein 1;
DE EC=1.8.4.-;
DE AltName: Full=Endoplasmic reticulum oxidoreductin-1-like protein A;
DE Flags: Precursor;
GN Name=ero11; ORFNames=SPBC4F6.16c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=15449306; DOI=10.1002/yea.1149;
RA Kettner K., Blomberg A., Roedel G.;
RT "Schizosaccharomyces pombe ER oxidoreductin-like proteins SpEro1a p and
RT SpEro1b p.";
RL Yeast 21:1035-1044(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.
CC {ECO:0000269|PubMed:15449306}.
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
CC {ECO:0000269|PubMed:15449306}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15449306}; Lumenal side
CC {ECO:0000269|PubMed:15449306}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15449306}.
CC -!- SIMILARITY: Belongs to the EROs family. {ECO:0000305}.
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DR EMBL; CU329671; CAA20736.1; -; Genomic_DNA.
DR PIR; T40513; T40513.
DR RefSeq; NP_596116.1; NM_001022033.2.
DR AlphaFoldDB; O74401; -.
DR SMR; O74401; -.
DR BioGRID; 277417; 7.
DR STRING; 4896.SPBC4F6.16c.1; -.
DR MaxQB; O74401; -.
DR PaxDb; O74401; -.
DR PRIDE; O74401; -.
DR EnsemblFungi; SPBC4F6.16c.1; SPBC4F6.16c.1:pep; SPBC4F6.16c.
DR PomBase; SPBC4F6.16c; ero11.
DR VEuPathDB; FungiDB:SPBC4F6.16c; -.
DR eggNOG; KOG2608; Eukaryota.
DR HOGENOM; CLU_023061_1_1_1; -.
DR InParanoid; O74401; -.
DR OMA; PDAWRIW; -.
DR PhylomeDB; O74401; -.
DR PRO; PR:O74401; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:PomBase.
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 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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..467
FT /note="ERO1-like protein 1"
FT /id="PRO_0000008428"
FT ACT_SITE 358
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT ACT_SITE 361
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT BINDING 147
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT BINDING 149
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT BINDING 160
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 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 68..355
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT DISULFID 78..83
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT DISULFID 114..296
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT DISULFID 358..361
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
SQ SEQUENCE 467 AA; 54626 MW; 49DB8E3B4DE5035E CRC64;
MIGITKLISI WNAIWNFLLL PEIIISQTDT SSTGIYQMQS KVRSLVPVLT ERSDYFSYYR
VNLYRSSCPL WENDNAMCSN QGCAVKSLNE IEIPKVWKKL SDFEPHSKKN DTKCNWKYNP
DLDYCYLDNS TSPDEYVYVS LVQNPERFTG YAGDHSAAIW RSIYEQNCFV VDDDDNPSEQ
PKSNALFRPN QIPLNLFTEN HDDTSLSPSV ACLEKRMFNR IISGFHASIS THVCQNYYDV
EEQRWTQNLD WWRAKVGSFP DRIENIFFNY ALLHQALVQI ATQMKNITSD SSFTFCPTDK
DVDWRTHTAF EQLVYHAYQD RHVINREQFF ADEEAKRFKD SFRKHFRDIS RIMDCVGCDK
CRLWGKVQIT GYGTALKLLL EPETQLSDLR PEEVVALVNT FDRISHSVEA TFWFSLKAKT
NDTLDAIKAL IYKTYRSPSK EILAFFIDQT WYLFYALFFI CNVPRVI
