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Q12284 (ERV2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
FAD-linked sulfhydryl oxidase ERV2

EC=1.8.3.2
Gene names
Name:ERV2
Ordered Locus Names:YPR037C
ORF Names:YP3085.03C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length196 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation in the endoplasmic reticulum lumen in parallel to ERO1. Ref.4 Ref.5

Catalytic activity

2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2.

Cofactor

FAD.

Subunit structure

Homodimer. Interacts with the substrate protein PDI1, forming transient intermolecular disulfide bridges. Ref.4 Ref.5

Subcellular location

Endoplasmic reticulum membrane; Single-pass type III membrane protein; Lumenal side Ref.4 Ref.5.

Miscellaneous

Present with 259 molecules/cell in log phase SD medium.

Sequence similarities

Contains 1 ERV/ALR sulfhydryl oxidase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 196196FAD-linked sulfhydryl oxidase ERV2
PRO_0000001188

Regions

Topological domain1 – 1212Cytoplasmic Potential
Transmembrane13 – 3523Helical; Signal-anchor; Potential
Topological domain36 – 196161Lumenal Potential
Domain72 – 174103ERV/ALR sulfhydryl oxidase
Region78 – 869FAD-binding
Region153 – 17422FAD-binding

Amino acid modifications

Disulfide bond121 ↔ 124Redox-active Potential
Disulfide bond150 ↔ 167 Ref.8
Disulfide bond176 ↔ 178 Ref.8

Experimental info

Mutagenesis1211C → A: Loss of function. Ref.5
Mutagenesis1241C → A: Loss of function. Ref.5

Secondary structure

........... 196
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q12284 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 7FEE76B5F01D3D65

FASTA19622,141
        10         20         30         40         50         60 
MKQIVKRSHA IRIVAALGII GLWMFFSSNE LSIATPGLIK AKSGIDEVQG AAAEKNDARL 

        70         80         90        100        110        120 
KEIEKQTIMP LMGDDKVKKE VGRASWKYFH TLLARFPDEP TPEEREKLHT FIGLYAELYP 

       130        140        150        160        170        180 
CGECSYHFVK LIEKYPVQTS SRTAAAMWGC HIHNKVNEYL KKDIYDCATI LEDYDCGCSD 

       190 
SDGKRVSLEK EAKQHG 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Functional comparison of the yeast scERV1 and scERV2 genes."
Stein G., Lisowsky T.
Yeast 14:171-180(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[4]"Yeast ERV2p is the first microsomal FAD-linked sulfhydryl oxidase of the Erv1p/Alrp protein family."
Gerber J., Muehlenhoff U., Hofhaus G., Lill R., Lisowsky T.
J. Biol. Chem. 276:23486-23491(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, FAD-BINDING, SUBUNIT.
[5]"A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation."
Sevier C.S., Cuozzo J.W., Vala A., Aaslund F., Kaiser C.A.
Nat. Cell Biol. 3:874-882(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, FAD-BINDING, MUTAGENESIS OF CYS-121 AND CYS-124, SUBUNIT, INTERACTION WITH PDI1.
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p."
Gross E., Sevier C.S., Vala A., Kaiser C.A., Fass D.
Nat. Struct. Biol. 9:61-67(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 71-187, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z71255 Genomic DNA. Translation: CAA94987.1.
Z68111 Genomic DNA. Translation: CAA92143.1.
BK006949 Genomic DNA. Translation: DAA11464.1.
PIRS61060.
RefSeqNP_015362.1. NM_001184134.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JR8X-ray1.50A/B71-187[»]
1JRAX-ray2.00A/B/C/D71-187[»]
ProteinModelPortalQ12284.
SMRQ12284. Positions 74-179.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36216. 18 interactions.
DIPDIP-3906N.
IntActQ12284. 1 interaction.
MINTMINT-560963.
STRING4932.YPR037C.

Proteomic databases

MaxQBQ12284.
PaxDbQ12284.
PeptideAtlasQ12284.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPR037C; YPR037C; YPR037C.
GeneID856152.
KEGGsce:YPR037C.

Organism-specific databases

CYGDYPR037c.
SGDS000006241. ERV2.

Phylogenomic databases

eggNOGCOG5054.
HOGENOMHOG000180458.
KOK17891.
OMAGRASWKY.
OrthoDBEOG7WDNCT.

Enzyme and pathway databases

BioCycYEAST:G3O-34195-MONOMER.

Gene expression databases

GenevestigatorQ12284.

Family and domain databases

Gene3D1.20.120.310. 1 hit.
InterProIPR017905. ERV/ALR_sulphydryl_oxidase.
[Graphical view]
PfamPF04777. Evr1_Alr. 1 hit.
[Graphical view]
SUPFAMSSF69000. SSF69000. 1 hit.
PROSITEPS51324. ERV_ALR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ12284.
NextBio981280.

Entry information

Entry nameERV2_YEAST
AccessionPrimary (citable) accession number: Q12284
Secondary accession number(s): D6W448
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: May 14, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XVI

Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references