Q9V3A6 (ERO1L_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ero1-like protein
EC=1.8.4.-

Alternative name(s):
Endoplasmic oxidoreductin-1-like protein

Gene names

Name:	Ero1L
ORF Names:	CG1333

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	483 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly Pdi isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on Pdi to transfer oxidizing equivalent. Does not oxidize all Pdi related proteins, suggesting that it can discriminate between Pdi and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently of glutathione. May be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress By similarity.
Cofactor	FAD By similarity.
Subunit structure	May function both as a monomer and a homodimer By similarity.
Subcellular location	Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side By similarity.
Sequence similarities	Belongs to the EROs family.
Sequence caution	The sequence AAF09172.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Endoplasmic reticulum Membrane
Domain	Redox-active center Signal
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	chaperone mediated protein folding requiring cofactor Inferred from sequence or structural similarity. Source: UniProtKB electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW protein thiol-disulfide exchange Inferred from electronic annotation. Source: InterPro transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 29	29	Potential
	Chain	30 – 483	454	Ero1-like protein		PRO_0000008421
Sites
	Binding site	206	1	FAD By similarity
	Binding site	208	1	FAD By similarity
	Binding site	219	1	FAD By similarity
	Binding site	262	1	FAD By similarity
	Binding site	265	1	FAD By similarity
	Binding site	301	1	FAD By similarity
Amino acid modifications
	Glycosylation	232	1	N-linked (GlcNAc...) Potential
	Glycosylation	395	1	N-linked (GlcNAc...) Potential
	Disulfide bond	94 ↔ 402		By similarity
	Disulfide bond	103 ↔ 108		Redox-active By similarity
	Disulfide bond	405 ↔ 408		Redox-active By similarity
Experimental info
	Sequence conflict	58	1	D → Y in AAF09172. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9V3A6 [UniParc]. Last modified July 5, 2004. Version 2. Checksum: 38C9F37B233A3E93	FASTA	483	55,660
	10 20 30 40 50 60 MTTRTVQRNL WASAAVVLVL LLLWTDTTGG YFAAIDETET SKNCFCELEG SINDCSCDVD 70 80 90 100 110 120 TVDHFNNMKI YPRLQSLLVK NFFRFYKVNL RQECPFWPDD SRCAMRFCQV ENCEEQAIPQ 130 140 150 160 170 180 GIKDKGEHKE KAAFKYTREA QVGGSACSDG EDFDSSLGFL DTSISDQAHR EFELWAKHDE 190 200 210 220 230 240 AEEDFCIVDD HEEGSQYVDL LLNPERYTGY KGESAHRIWK SIYLENCFGG NNETANKFSN 250 260 270 280 290 300 YVPHLDLRNV CLEQRAFYRI ISGLHSSINI HLCSKYLLSE SKDFLDPQGI WGPNVKEFKR 310 320 330 340 350 360 RFSPETTSGE GPHWLRNLYF IYLIELRALA KAAPYLRRED YYTGIAEEDD EVKLAINDML 370 380 390 400 410 420 SVIENFQSHF DENALFSNGI ASIKFKHDYK EKFRNISRIM SCVGCDKCKL WGKLQTQGLG 430 440 450 460 470 480 TALKILYSEK LNLATESGLW DKPHIEADPI FRLSRTEIVA LFNAFGRLSN SIYEMENFRC VLR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum." Cabibbo A., Pagani M., Fabbri M., Rocchi M., Farmery M.R., Bulleid N.J., Sitia R. J. Biol. Chem. 275:4827-4833(2000) [PubMed: 10671517] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF125280 mRNA. Translation: AAF09172.1. Different initiation. AE014296 Genomic DNA. Translation: AAF47851.2. BT021422 mRNA. Translation: AAX33570.1.
RefSeq	NP_647865.2. NM_139608.3.
UniGene	Dm.7704.
3D structure databases
ProteinModelPortal	Q9V3A6.
SMR	Q9V3A6. Positions 43-483.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9V3A6.
Proteomic databases
PRIDE	Q9V3A6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0073217; FBpp0073073; FBgn0261274.
GeneID	38500.
KEGG	dme:Dmel_CG1333.
Organism-specific databases
CTD	30001.
FlyBase	FBgn0261274. Ero1L.
Phylogenomic databases
GeneTree	EMGT00050000006143.
InParanoid	Q9V3A6.
OMA	ISIHIAA.
OrthoDB	EOG4FQZ6W.
PhylomeDB	Q9V3A6.
Gene expression databases
Bgee	Q9V3A6.
GermOnline	CG1333. Drosophila melanogaster.
Family and domain databases
InterPro	IPR007266. ER_oxidoreductin-1. [Graphical view]
PANTHER	PTHR12613. ERO1. 1 hit.
Pfam	PF04137. ERO1. 1 hit. [Graphical view]
PIRSF	PIRSF017205. ERO1. 1 hit.
SUPFAM	SSF110019. ERO1. 1 hit.
ProtoNet	Search...
Other
NextBio	808960.

Entry information

Entry name

ERO1L_DROME

Accession

Primary (citable) accession number: Q9V3A6
Secondary accession number(s): Q5BI02, Q7KNC7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	July 5, 2004
Last modified:	January 25, 2012
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project