ENV9_YEAST
ID ENV9_YEAST Reviewed; 330 AA.
AC Q08651; D6W2U8;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Probable oxidoreductase ENV9;
DE EC=1.1.1.-;
DE AltName: Full=Late endosome and vacuole interface protein 9;
GN Name=ENV9; OrderedLocusNames=YOR246C;
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 [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9153759;
RX DOI=10.1002/(sici)1097-0061(199704)13:5<483::aid-yea105>3.0.co;2-u;
RA Poirey R., Jauniaux J.-C.;
RT "Sequencing analysis of a 36.8 kb fragment of yeast chromosome XV reveals
RT 26 open reading frames including SEC63, CDC31, SUG2, GCD1, RBL2, PNT1, PAC1
RT and VPH1.";
RL Yeast 13:483-487(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
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 [6]
RP FUNCTION IN REPLICATION OF BMV.
RX PubMed=14671320; DOI=10.1073/pnas.2536857100;
RA Kushner D.B., Lindenbach B.D., Grdzelishvili V.Z., Noueiry A.O., Paul S.M.,
RA Ahlquist P.;
RT "Systematic, genome-wide identification of host genes affecting replication
RT of a positive-strand RNA virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:15764-15769(2003).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX PubMed=19756047; DOI=10.1038/msb.2009.64;
RA Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT new roles for protein glycosylation in eukaryotes.";
RL Mol. Syst. Biol. 5:308-308(2009).
RN [8]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=21912603; DOI=10.1371/journal.pone.0023696;
RA Ricarte F., Menjivar R., Chhun S., Soreta T., Oliveira L., Hsueh T.,
RA Serranilla M., Gharakhanian E.;
RT "A genome-wide immunodetection screen in S. cerevisiae uncovers novel genes
RT involved in lysosomal vacuole function and morphology.";
RL PLoS ONE 6:E23696-E23696(2011).
CC -!- FUNCTION: Probable dehydrogenase required for replication of Brome
CC mosaic virus. Involved in vacuolar processing and morphology.
CC {ECO:0000269|PubMed:14671320, ECO:0000269|PubMed:21912603}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:14562095}.
CC Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
CC -!- DISRUPTION PHENOTYPE: Exhibits lumenal vesicles within vacuoles
CC suggestive of vacuole fusion/fission defects. Leads to internal
CC accumulation of precursor CPY. {ECO:0000269|PubMed:21912603}.
CC -!- MISCELLANEOUS: Present with 892 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z75154; CAA99467.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11014.1; -; Genomic_DNA.
DR PIR; S67139; S67139.
DR RefSeq; NP_014889.3; NM_001183665.3.
DR AlphaFoldDB; Q08651; -.
DR SMR; Q08651; -.
DR BioGRID; 34637; 176.
DR DIP; DIP-5387N; -.
DR STRING; 4932.YOR246C; -.
DR iPTMnet; Q08651; -.
DR MaxQB; Q08651; -.
DR PaxDb; Q08651; -.
DR PRIDE; Q08651; -.
DR EnsemblFungi; YOR246C_mRNA; YOR246C; YOR246C.
DR GeneID; 854420; -.
DR KEGG; sce:YOR246C; -.
DR SGD; S000005772; ENV9.
DR VEuPathDB; FungiDB:YOR246C; -.
DR eggNOG; KOG1208; Eukaryota.
DR GeneTree; ENSGT00940000168183; -.
DR HOGENOM; CLU_010194_44_6_1; -.
DR InParanoid; Q08651; -.
DR OMA; DGHEAQW; -.
DR BioCyc; YEAST:G3O-33739-MON; -.
DR Reactome; R-SCE-5365859; RA biosynthesis pathway.
DR PRO; PR:Q08651; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08651; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005773; C:vacuole; IEA:GOC.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006624; P:vacuolar protein processing; IMP:SGD.
DR GO; GO:0007033; P:vacuole organization; IMP:SGD.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 2.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Lipid droplet; Membrane; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..330
FT /note="Probable oxidoreductase ENV9"
FT /id="PRO_0000245256"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 202
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 47..53
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 330 AA; 37485 MW; 7556FC07BB4F6F0D CRC64;
MLDPRILPYY DPAVERKIAV VTGGNTGIGW YTVLHLYLHG FVVYICGRNS HKISKAIQEI
LAEAKKRCHE DDDGSSPGAG PGPSIQRLGS LHYIHLDLTD LKCVERAALK ILKLEDHIDV
LVNNAGIMAV PLEMTKDGFE VQLQTNYISH FIFTMRLLPL LRHCRGRIIS LSSIGHHLEF
MYWKLSKTWD YKPNMLFTWF RYAMSKTALI QCTKMLAIKY PDVLCLSVHP GLVMNTNLFS
YWTRLPIVGI FFWLLFQVVG FFFGVSNEQG SLASLKCALD PNLSVEKDNG KYFTTGGKES
KSSYVSNNVD EAASTWIWTV HQLRDRGFDI
