ID   ERV2_YEAST              Reviewed;         196 AA.
AC   Q12284;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   16-JUN-2009, entry version 79.
DE   RecName: Full=FAD-linked sulfhydryl oxidase ERV2;
DE            EC=1.8.3.2;
GN   Name=ERV2; OrderedLocusNames=YPR037C; ORFNames=YP3085.03C;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313271; PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
RA   Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
RA   Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
RA   Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
RA   Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
RA   Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
RA   Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
RA   Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
RA   Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
RA   Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
RA   Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
RA   Zollner A., Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [2]
RP   CHARACTERIZATION.
RX   MEDLINE=98144799; PubMed=9483805;
RX   DOI=10.1002/(SICI)1097-0061(19980130)14:2<171::AID-YEA209>3.0.CO;2-U;
RA   Stein G., Lisowsky T.;
RT   "Functional comparison of the yeast scERV1 and scERV2 genes.";
RL   Yeast 14:171-180(1998).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, FAD-BINDING, AND SUBUNIT.
RX   PubMed=11313344; DOI=10.1074/jbc.M100134200;
RA   Gerber J., Muehlenhoff U., Hofhaus G., Lill R., Lisowsky T.;
RT   "Yeast ERV2p is the first microsomal FAD-linked sulfhydryl oxidase of
RT   the Erv1p/Alrp protein family.";
RL   J. Biol. Chem. 276:23486-23491(2001).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, FAD-BINDING, MUTAGENESIS OF CYS-121
RP   AND CYS-124, SUBUNIT, AND INTERACTION WITH PDI1.
RX   PubMed=11584268; DOI=10.1038/ncb1001-874;
RA   Sevier C.S., Cuozzo J.W., Vala A., Aaslund F., Kaiser C.A.;
RT   "A flavoprotein oxidase defines a new endoplasmic reticulum pathway
RT   for biosynthetic disulphide bond formation.";
RL   Nat. Cell Biol. 3:874-882(2001).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 71-187, AND DISULFIDE BONDS.
RX   MEDLINE=21624659; PubMed=11740506; DOI=10.1038/nsb740;
RA   Gross E., Sevier C.S., Vala A., Kaiser C.A., Fass D.;
RT   "A new FAD-binding fold and intersubunit disulfide shuttle in the
RT   thiol oxidase Erv2p.";
RL   Nat. Struct. Biol. 9:61-67(2002).
CC   -!- FUNCTION: FAD-dependent sulfhydryl oxidase that catalyzes
CC       disulfide bond formation in the endoplasmic reticulum lumen in
CC       parallel to ERO1.
CC   -!- CATALYTIC ACTIVITY: 4 R'C(R)SH + O(2) = 2 R'C(R)S-S(R)CR' + 2
CC       H(2)O.
CC   -!- COFACTOR: FAD.
CC   -!- SUBUNIT: Homodimer. Interacts with the substrate protein PDI1,
CC       forming transient intermolecular disulfide bridges.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       type III membrane protein; Lumenal side.
CC   -!- MISCELLANEOUS: Present with 259 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Contains 1 ERV/ALR sulfhydryl oxidase domain.
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DR   EMBL; Z71255; CAA94987.1; -; Genomic_DNA.
DR   EMBL; Z68111; CAA92143.1; -; Genomic_DNA.
DR   PIR; S61060; S61060.
DR   RefSeq; NP_015362.1; -.
DR   PDB; 1JR8; X-ray; 1.50 A; A/B=71-187.
DR   PDB; 1JRA; X-ray; 2.00 A; A/B/C/D=71-187.
DR   PDBsum; 1JR8; -.
DR   PDBsum; 1JRA; -.
DR   DIP; DIP:3906N; -.
DR   IntAct; Q12284; 2.
DR   PeptideAtlas; Q12284; -.
DR   Ensembl; YPR037C; Saccharomyces cerevisiae.
DR   GeneID; 856152; -.
DR   GenomeReviews; U00094_GR; YPR037C.
DR   KEGG; sce:YPR037C; -.
DR   NMPDR; fig|4932.3.peg.6498; -.
DR   CYGD; YPR037c; -.
DR   SGD; S000006241; ERV2.
DR   HOGENOM; Q12284; -.
DR   OMA; Q12284; FHTLLAR.
DR   BRENDA; 1.8.3.2; 250.
DR   NextBio; 981280; -.
DR   ArrayExpress; Q12284; -.
DR   GermOnline; YPR037C; Saccharomyces cerevisiae.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005792; C:microsome; IDA:SGD.
DR   GO; GO:0016972; F:thiol oxidase activity; IDA:SGD.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006467; P:protein thiol-disulfide exchange; IGI:SGD.
DR   InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR   InterPro; IPR006863; Evr1_Alr.
DR   Gene3D; G3DSA:1.20.120.310; Evr1_Alr; 1.
DR   Pfam; PF04777; Evr1_Alr; 1.
DR   PROSITE; PS51324; ERV_ALR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Disulfide bond;
KW   Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Oxidoreductase;
KW   Signal-anchor; Transmembrane.
FT   CHAIN         1    196       FAD-linked sulfhydryl oxidase ERV2.
FT                                /FTId=PRO_0000001188.
FT   TOPO_DOM      1     12       Cytoplasmic (Potential).
FT   TRANSMEM     13     35       Signal-anchor for type II/III membrane
FT                                protein (Potential).
FT   TOPO_DOM     36    196       Lumenal (Potential).
FT   DOMAIN       72    174       ERV/ALR sulfhydryl oxidase.
FT   REGION       78     86       FAD-binding.
FT   REGION      153    174       FAD-binding.
FT   DISULFID    121    124       Redox-active (Potential).
FT   DISULFID    150    167
FT   DISULFID    176    178
FT   MUTAGEN     121    121       C->A: Loss of function.
FT   MUTAGEN     124    124       C->A: Loss of function.
FT   HELIX        75     94
FT   HELIX       102    118
FT   HELIX       122    134
FT   HELIX       142    159
FT   HELIX       170    173
SQ   SEQUENCE   196 AA;  22141 MW;  7FEE76B5F01D3D65 CRC64;
     MKQIVKRSHA IRIVAALGII GLWMFFSSNE LSIATPGLIK AKSGIDEVQG AAAEKNDARL
     KEIEKQTIMP LMGDDKVKKE VGRASWKYFH TLLARFPDEP TPEEREKLHT FIGLYAELYP
     CGECSYHFVK LIEKYPVQTS SRTAAAMWGC HIHNKVNEYL KKDIYDCATI LEDYDCGCSD
     SDGKRVSLEK EAKQHG
//