Reviewed, UniProtKB/Swiss-Prot Q12284 (ERV2_YEAST)

Names and origin

Protein names

Recommended name:
    FAD-linked sulfhydryl oxidase ERV2
    EC=1.8.3.2

Gene names

Name:	ERV2
Ordered Locus Names:	YPR037C
ORF Names:	YP3085.03C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	196 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.3 Ref.4
Catalytic activity	4 R'C(R)SH + O2 = 2 R'C(R)S-S(R)CR' + 2 H2O.
Cofactor	FAD.
Subunit structure	Homodimer. Interacts with the substrate protein PDI1, forming transient intermolecular disulfide bridges. Ref.3 Ref.4
Subcellular location	Endoplasmic reticulum membrane; Single-pass type III membrane protein; Lumenal side. Ref.3 Ref.4
Miscellaneous	Present with 259 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Contains 1 ERV/ALR sulfhydryl oxidase domain.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Signal-anchor Transmembrane
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW protein thiol-disulfide exchange Ref.4 Inferred from genetic interaction. Source: SGD
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW microsome Ref.3 Inferred from direct assay. Source: SGD
Molecular function	thiol oxidase activity Ref.3 Inferred from direct assay. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 196

196

FAD-linked sulfhydryl oxidase ERV2

PRO_0000001188

Regions

Topological domain

1 – 12

12

Cytoplasmic Potential

Transmembrane

13 – 35

23

Signal-anchor for type II/III membrane protein Potential

Topological domain

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

Amino acid modifications

Disulfide bond

121 ↔ 124

Redox-active Potential

Disulfide bond

150 ↔ 167

Ref.6

Disulfide bond

176 ↔ 178

Ref.6

Experimental info

Mutagenesis

121

1

C → A: Loss of function. Ref.4

Mutagenesis

124

1

C → A: Loss of function. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

196

Helix Strand Turn

Details...

Helix

75 – 94

20

Helix

102 – 118

17

Helix

122 – 134

13

Helix

142 – 159

18

Helix

170 – 173

4

Sequences

	Sequence		Length	Mass (Da)
	Q12284-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 7FEE76B5F01D3D65	FASTA	196	22,141
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"Functional comparison of the yeast scERV1 and scERV2 genes." Stein G., Lisowsky T. Yeast 14:171-180(1998) [PubMed: 9483805] [Abstract] Cited for: CHARACTERIZATION.
[3]	"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: 11313344] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, FAD-BINDING, SUBUNIT.
[4]	"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: 11584268] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, FAD-BINDING, MUTAGENESIS OF CYS-121 AND CYS-124, SUBUNIT, INTERACTION WITH PDI1.
[5]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"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: 11740506] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 71-187, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Z71255 Genomic DNA. Translation: CAA94987.1.
Z68111 Genomic DNA. Translation: CAA92143.1.

PIR

S61060.

RefSeq

NP_015362.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JR8	X-ray	1.50	A/B	71-187	[»]
1JRA	X-ray	2.00	A/B/C/D	71-187	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:3906N.

IntAct

Q12284. 2 interactions.

Proteomic databases

PeptideAtlas

Q12284.

Genome annotation databases

Ensembl

YPR037C. Saccharomyces cerevisiae. [Contig view]

GeneID

856152.

GenomeReviews

Gene locus YPR037C in contig U00094_GR.

KEGG

sce:YPR037C.

NMPDR

fig|4932.3.peg.6498.

Organism-specific databases

CYGD

YPR037c.

SGD

S000006241. ERV2.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

Q12284.

OMA

Q12284. FHTLLAR.

Enzyme and pathway databases

BRENDA

1.8.3.2. 250.

Gene expression databases

ArrayExpress

Q12284.

GermOnline

YPR037C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR017905. ERV/ALR_sulphydryl_oxidase.
IPR006863. Evr1_Alr.
[Graphical view]

Gene3D

G3DSA:1.20.120.310. Evr1_Alr. 1 hit.

Pfam

PF04777. Evr1_Alr. 1 hit.
[Graphical view]

PROSITE

PS51324. ERV_ALR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

981280.

Entry information

Entry name

ERV2_YEAST

Accession

Primary (citable) accession number: Q12284

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)