ERV2_YEAST
ID ERV2_YEAST Reviewed; 196 AA.
AC Q12284; D6W448;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=FAD-linked sulfhydryl oxidase ERV2;
DE EC=1.8.3.2 {ECO:0000269|PubMed:11313344};
GN Name=ERV2; OrderedLocusNames=YPR037C; ORFNames=YP3085.03C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX 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., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., 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., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP CHARACTERIZATION.
RX 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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, FAD-BINDING, SUBUNIT, AND CATALYTIC
RP ACTIVITY.
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 the
RT Erv1p/Alrp protein family.";
RL J. Biol. Chem. 276:23486-23491(2001).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, FAD-BINDING, MUTAGENESIS OF CYS-121 AND
RP 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 for
RT biosynthetic disulphide bond formation.";
RL Nat. Cell Biol. 3:874-882(2001).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8] {ECO:0007744|PDB:1JR8, ECO:0007744|PDB:1JRA}
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 71-187 IN COMPLEX WITH FAD,
RP COFACTOR, AND DISULFIDE BONDS.
RX 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 thiol
RT oxidase Erv2p.";
RL Nat. Struct. Biol. 9:61-67(2002).
CC -!- FUNCTION: FAD-dependent sulfhydryl oxidase that catalyzes disulfide
CC bond formation in the endoplasmic reticulum lumen in parallel to ERO1.
CC {ECO:0000255|PROSITE-ProRule:PRU00654, ECO:0000269|PubMed:11313344,
CC ECO:0000269|PubMed:11584268}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR';
CC Xref=Rhea:RHEA:17357, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:16520, ChEBI:CHEBI:17412; EC=1.8.3.2;
CC Evidence={ECO:0000269|PubMed:11313344};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00654,
CC ECO:0000269|PubMed:11313344, ECO:0000269|PubMed:11584268,
CC ECO:0000269|PubMed:11740506};
CC -!- SUBUNIT: Homodimer. Interacts with the substrate protein PDI1, forming
CC transient intermolecular disulfide bridges.
CC {ECO:0000269|PubMed:11313344, ECO:0000269|PubMed:11584268}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11313344, ECO:0000269|PubMed:11584268}; Single-pass
CC type III membrane protein {ECO:0000269|PubMed:11313344,
CC ECO:0000269|PubMed:11584268}; Lumenal side
CC {ECO:0000269|PubMed:11313344, ECO:0000269|PubMed:11584268}.
CC -!- MISCELLANEOUS: Present with 259 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z71255; CAA94987.1; -; Genomic_DNA.
DR EMBL; Z68111; CAA92143.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11464.1; -; Genomic_DNA.
DR PIR; S61060; S61060.
DR RefSeq; NP_015362.1; NM_001184134.1.
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 AlphaFoldDB; Q12284; -.
DR SMR; Q12284; -.
DR BioGRID; 36216; 53.
DR DIP; DIP-3906N; -.
DR IntAct; Q12284; 1.
DR MINT; Q12284; -.
DR STRING; 4932.YPR037C; -.
DR iPTMnet; Q12284; -.
DR MaxQB; Q12284; -.
DR PaxDb; Q12284; -.
DR PRIDE; Q12284; -.
DR EnsemblFungi; YPR037C_mRNA; YPR037C; YPR037C.
DR GeneID; 856152; -.
DR KEGG; sce:YPR037C; -.
DR SGD; S000006241; ERV2.
DR VEuPathDB; FungiDB:YPR037C; -.
DR eggNOG; KOG3355; Eukaryota.
DR HOGENOM; CLU_070631_2_2_1; -.
DR InParanoid; Q12284; -.
DR OMA; PEYDCST; -.
DR BioCyc; YEAST:G3O-34195-MON; -.
DR BRENDA; 1.8.3.2; 984.
DR ChiTaRS; ERV2; yeast.
DR EvolutionaryTrace; Q12284; -.
DR PRO; PR:Q12284; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12284; protein.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0016971; F:flavin-linked sulfhydryl oxidase activity; IBA:GO_Central.
DR GO; GO:0016972; F:thiol oxidase activity; IDA:SGD.
DR Gene3D; 1.20.120.310; -; 1.
DR InterPro; IPR039799; ALR/ERV.
DR InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR PANTHER; PTHR12645; PTHR12645; 1.
DR Pfam; PF04777; Evr1_Alr; 1.
DR SUPFAM; SSF69000; SSF69000; 1.
DR PROSITE; PS51324; ERV_ALR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Endoplasmic reticulum; FAD; Flavoprotein;
KW Membrane; Oxidoreductase; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..196
FT /note="FAD-linked sulfhydryl oxidase ERV2"
FT /id="PRO_0000001188"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..35
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..196
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 72..174
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT BINDING 78
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11740506,
FT ECO:0007744|PDB:1JR8, ECO:0007744|PDB:1JRA"
FT BINDING 83
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11740506,
FT ECO:0007744|PDB:1JR8, ECO:0007744|PDB:1JRA"
FT BINDING 86
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11740506,
FT ECO:0007744|PDB:1JR8, ECO:0007744|PDB:1JRA"
FT BINDING 127
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11740506,
FT ECO:0007744|PDB:1JR8, ECO:0007744|PDB:1JRA"
FT BINDING 150
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11740506,
FT ECO:0007744|PDB:1JR8, ECO:0007744|PDB:1JRA"
FT BINDING 153
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11740506,
FT ECO:0007744|PDB:1JR8, ECO:0007744|PDB:1JRA"
FT BINDING 157
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11740506,
FT ECO:0007744|PDB:1JR8, ECO:0007744|PDB:1JRA"
FT BINDING 162
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11740506,
FT ECO:0007744|PDB:1JR8, ECO:0007744|PDB:1JRA"
FT BINDING 174
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11740506,
FT ECO:0007744|PDB:1JR8, ECO:0007744|PDB:1JRA"
FT DISULFID 121..124
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT DISULFID 150..167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654,
FT ECO:0000269|PubMed:11740506"
FT DISULFID 176..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654,
FT ECO:0000269|PubMed:11740506"
FT MUTAGEN 121
FT /note="C->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:11584268"
FT MUTAGEN 124
FT /note="C->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:11584268"
FT HELIX 75..94
FT /evidence="ECO:0007829|PDB:1JR8"
FT HELIX 102..118
FT /evidence="ECO:0007829|PDB:1JR8"
FT HELIX 122..134
FT /evidence="ECO:0007829|PDB:1JR8"
FT HELIX 142..159
FT /evidence="ECO:0007829|PDB:1JR8"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:1JR8"
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
