ERO1L_DROME
ID ERO1L_DROME Reviewed; 483 AA.
AC Q9V3A6; E2QCT2; Q5BI02; Q7KNC7;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Ero1-like protein;
DE EC=1.8.4.-;
DE AltName: Full=Endoplasmic reticulum oxidoreductin-1-like protein;
DE Flags: Precursor;
GN Name=Ero1L; ORFNames=CG1333;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10671517; DOI=10.1074/jbc.275.7.4827;
RA Cabibbo A., Pagani M., Fabbri M., Rocchi M., Farmery M.R., Bulleid N.J.,
RA Sitia R.;
RT "ERO1-L, a human protein that favors disulfide bond formation in the
RT endoplasmic reticulum.";
RL J. Biol. Chem. 275:4827-4833(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the EROs family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF09172.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF125280; AAF09172.1; ALT_INIT; mRNA.
DR EMBL; AE014296; AAN11590.1; -; Genomic_DNA.
DR EMBL; BT021422; AAX33570.1; -; mRNA.
DR RefSeq; NP_647865.2; NM_139608.4.
DR AlphaFoldDB; Q9V3A6; -.
DR SMR; Q9V3A6; -.
DR BioGRID; 63978; 4.
DR STRING; 7227.FBpp0073073; -.
DR GlyGen; Q9V3A6; 2 sites.
DR PaxDb; Q9V3A6; -.
DR PRIDE; Q9V3A6; -.
DR DNASU; 38500; -.
DR EnsemblMetazoa; FBtr0073217; FBpp0073073; FBgn0261274.
DR GeneID; 38500; -.
DR KEGG; dme:Dmel_CG1333; -.
DR CTD; 38500; -.
DR FlyBase; FBgn0261274; Ero1L.
DR VEuPathDB; VectorBase:FBgn0261274; -.
DR eggNOG; KOG2608; Eukaryota.
DR GeneTree; ENSGT00390000007753; -.
DR HOGENOM; CLU_023061_2_2_1; -.
DR InParanoid; Q9V3A6; -.
DR OMA; RDYCVPD; -.
DR OrthoDB; 1181226at2759; -.
DR PhylomeDB; Q9V3A6; -.
DR BioGRID-ORCS; 38500; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 38500; -.
DR PRO; PR:Q9V3A6; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0261274; Expressed in saliva-secreting gland and 27 other tissues.
DR Genevisible; Q9V3A6; DM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; ISS:UniProtKB.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0016972; F:thiol oxidase activity; IMP:FlyBase.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; ISS:UniProtKB.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; IMP:FlyBase.
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 2: Evidence at transcript 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..29
FT /evidence="ECO:0000255"
FT CHAIN 30..483
FT /note="Ero1-like protein"
FT /id="PRO_0000008421"
FT BINDING 206
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 208
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 219
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 262
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 265
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 301
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..57
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 46..55
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 94..402
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 103..108
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 227..251
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 405..408
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT CONFLICT 58
FT /note="D -> Y (in Ref. 1; AAF09172)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 483 AA; 55660 MW; 38C9F37B233A3E93 CRC64;
MTTRTVQRNL WASAAVVLVL LLLWTDTTGG YFAAIDETET SKNCFCELEG SINDCSCDVD
TVDHFNNMKI YPRLQSLLVK NFFRFYKVNL RQECPFWPDD SRCAMRFCQV ENCEEQAIPQ
GIKDKGEHKE KAAFKYTREA QVGGSACSDG EDFDSSLGFL DTSISDQAHR EFELWAKHDE
AEEDFCIVDD HEEGSQYVDL LLNPERYTGY KGESAHRIWK SIYLENCFGG NNETANKFSN
YVPHLDLRNV CLEQRAFYRI ISGLHSSINI HLCSKYLLSE SKDFLDPQGI WGPNVKEFKR
RFSPETTSGE GPHWLRNLYF IYLIELRALA KAAPYLRRED YYTGIAEEDD EVKLAINDML
SVIENFQSHF DENALFSNGI ASIKFKHDYK EKFRNISRIM SCVGCDKCKL WGKLQTQGLG
TALKILYSEK LNLATESGLW DKPHIEADPI FRLSRTEIVA LFNAFGRLSN SIYEMENFRC
VLR
