ERO12_SCHPO
ID ERO12_SCHPO Reviewed; 567 AA.
AC Q9Y7P1;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=ERO1-like protein 2;
DE EC=1.8.4.-;
DE AltName: Full=Endoplasmic reticulum oxidoreductin-1-like protein B;
DE Flags: Precursor;
GN Name=ero12; ORFNames=SPCC1450.14c;
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; CU329672; CAB40181.2; -; Genomic_DNA.
DR PIR; T40996; T40996.
DR RefSeq; NP_588313.2; NM_001023303.3.
DR AlphaFoldDB; Q9Y7P1; -.
DR SMR; Q9Y7P1; -.
DR STRING; 4896.SPCC1450.14c.1; -.
DR iPTMnet; Q9Y7P1; -.
DR MaxQB; Q9Y7P1; -.
DR PaxDb; Q9Y7P1; -.
DR PRIDE; Q9Y7P1; -.
DR EnsemblFungi; SPCC1450.14c.1; SPCC1450.14c.1:pep; SPCC1450.14c.
DR GeneID; 2539325; -.
DR KEGG; spo:SPCC1450.14c; -.
DR PomBase; SPCC1450.14c; ero12.
DR VEuPathDB; FungiDB:SPCC1450.14c; -.
DR eggNOG; KOG2608; Eukaryota.
DR HOGENOM; CLU_023061_1_0_1; -.
DR InParanoid; Q9Y7P1; -.
DR OMA; RDYCVPD; -.
DR PhylomeDB; Q9Y7P1; -.
DR PRO; PR:Q9Y7P1; -.
DR Proteomes; UP000002485; Chromosome III.
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; IGI:PomBase.
DR GO; GO:0016972; F:thiol oxidase activity; IGI:PomBase.
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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..567
FT /note="ERO1-like protein 2"
FT /id="PRO_0000008427"
FT ACT_SITE 389
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT ACT_SITE 392
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 190
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT BINDING 201
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT BINDING 258
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT BINDING 261
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT BINDING 290
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 88..386
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT DISULFID 98..103
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT DISULFID 154..325
FT /evidence="ECO:0000250|UniProtKB:Q03103"
FT DISULFID 389..392
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q03103"
SQ SEQUENCE 567 AA; 65436 MW; 3C11DE7D58DEB52F CRC64;
MKIAKGLVGL LILYKNVCQV LCKSGSSVKS GSPWSIKNDG KSIIHDTLNS SYSDIENLNS
RVSPLLFDLT EKSDYMRFYR LNLFNKECRY NLDDNVACGS SACNVLVTDE QDVPEVWSSK
SLGKLEGFMP ELSRQIVETD RSVMEHVDKI SQSCLLERLD DEAHQYCYVD NELDSGCVYV
SLLENPERFT GYSGPHSTRI WEMIYNQCLP DSSAPTIDFP ALFMQGPLAP PPKPQEQLLK
ERMDAWTLEQ RVFYRVLSGM HSSISTHLCH GYLNQRNGVW GPNLQCFQEK VLNYPERLEN
LYFAYALMQR AIDKLYGHLD SLTFCHDSVL QDSEVRQKIA GLVSLIHNSP KMFDETMLFA
GDPSISTALK EDFREHFKTV SALMDCVGCE RCRLWGKIQT NGFGTALKIL FEVSNIEDEV
TNFDSRSFSL RLRRSEIVAL INTFDRLSRS INFVDDFKQI YSEQHKPASF KRRVLRRIKQ
LLFSVTPVAL HPFLQKTSSI LVDLYFDFKA EWDNVMLGFR YVFASYLRFP RLFKFVLFSQ
ESPFLNWTSH HLQRYIPKNW FPEVASV
