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UniProtKB/Swiss-Prot entry Q12284


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ERV2_YEAST
Primary accession number Q12284
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on November 1, 1997 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 74)
Name and origin of the protein
Protein name FAD-linked sulfhydryl oxidase ERV2
Synonym EC 1.8.3.2
Gene name
Name: ERV2
OrderedLocusNames: YPR037C
ORFNames: YP3085.03C
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169875 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[2]
CHARACTERIZATION.
DOI=10.1002/(SICI)1097-0061(19980130)14:2<171::AID-YEA209>3.0.CO;2-U; PubMed=9483805 [NCBI, ExPASy, EBI, Israel, Japan]
Stein G., Lisowsky T.;
"Functional comparison of the yeast scERV1 and scERV2 genes.";
Yeast 14:171-180(1998).
[3]
FUNCTION, SUBCELLULAR LOCATION, FAD-BINDING, AND SUBUNIT.
DOI=10.1074/jbc.M100134200; PubMed=11313344 [NCBI, ExPASy, EBI, Israel, Japan]
Gerber J., Muehlenhoff U., Hofhaus G., Lill R., Lisowsky T.;
"Yeast ERV2p is the first microsomal FAD-linked sulfhydryl oxidase of the Erv1p/Alrp protein family.";
J. Biol. Chem. 276:23486-23491(2001).
[4]
FUNCTION, SUBCELLULAR LOCATION, FAD-BINDING, MUTAGENESIS OF CYS-121 AND CYS-124, SUBUNIT, AND INTERACTION WITH PDI1.
DOI=10.1038/ncb1001-874; PubMed=11584268 [NCBI, ExPASy, EBI, Israel, Japan]
Sevier C.S., Cuozzo J.W., Vala A., Aaslund F., Kaiser C.A.;
"A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation.";
Nat. Cell Biol. 3:874-882(2001).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[6]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 71-187, AND DISULFIDE BONDS.
DOI=10.1038/nsb740; PubMed=11740506 [NCBI, ExPASy, EBI, Israel, Japan]
Gross E., Sevier C.S., Vala A., Kaiser C.A., Fass D.;
"A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p.";
Nat. Struct. Biol. 9:61-67(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z71255; CAA94987.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z68111; CAA92143.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S61060; S61060.
RefSeq NP_015362.1; -.
3D structure databases
PDB
1JR8; X-ray; 1.50 A; A/B=71-187.[ExPASy / RCSB / EBI]
1JRA; X-ray; 2.00 A; A/B/C/D=71-187.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1JR8; -.
1JRA; -.
ModBase Q12284.
Protein-protein interaction databases
DIP DIP:3906N; -.
IntAct Q12284; -.
Organism-specific databases
CYGD YPR037c; -.
SGD S000006241; ERV2.
Yeast-GFP YPR037C.
Gene expression databases
ArrayExpress Q12284; -.
GermOnline YPR037C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005792; Cellular component: microsome (inferred from direct assay from SGD).
GO:0016972; Molecular function: thiol oxidase activity (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
GO:0006467; Biological process: protein thiol-disulfide exchange (inferred from genetic interaction from SGD).
QuickGo view.
Family and domain databases
InterPro IPR006863; Evr1_Alr.
Graphical view of domain structure.
Gene3D G3DSA:1.20.120.310; Evr1_Alr; 1.
Pfam PF04777; Evr1_Alr; 1.
Pfam graphical view of domain structure.
PROSITE PS51324; ERV_ALR; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q12284.
Proteomic databases
PeptideAtlas Q12284; -.
Genome annotation databases
Ensembl YPR037C; Saccharomyces cerevisiae. [Contig view]
GeneID 856152; -.
GenomeReviews U00094_GR; YPR037C.
KEGG sce:YPR037C; -.
NMPDR fig|4932.3.peg.6498; -.
Phylogenomic databases
HOGENOM Q12284; -.
Other
LinkHub Q12284; -.
NextBio 981280; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Oxidoreductase; Signal-anchor; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   196  196     FAD-linked sulfhydryl oxidase ERV2. PRO_0000001188
TOPO_DOM   1    12  12     Cytoplasmic (Potential). 
TRANSMEM   13    35  23     Signal-anchor for type II/III membrane protein (Potential). 
TOPO_DOM   36   196  161     Lumenal (Potential). 
DOMAIN   72   174  103     ERV/ALR sulfhydryl oxidase. 
REGION   78    86  9     FAD-binding. 
REGION   153   174  22     FAD-binding. 
DISULFID   121   124        Redox-active (Potential). 
DISULFID   150   167         
DISULFID   176   178         
MUTAGEN   121   121        C->A: Loss of function. 
MUTAGEN   124   124        C->A: Loss of function. 
HELIX   75    94  20      
HELIX   102   118  17      
HELIX   122   134  13      
HELIX   142   159  18      
HELIX   170   173  4      
Sequence information
Length: 196 AA [This is the length of the unprocessed precursor] Molecular weight: 22141 Da [This is the MW of the unprocessed precursor] CRC64: 7FEE76B5F01D3D65 [This is a checksum on the sequence]
        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 

Q12284 in FASTA format

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