ATF2_YEAST
ID ATF2_YEAST Reviewed; 535 AA.
AC P53296; D6VUW1; E9P955;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Alcohol O-acetyltransferase 2 {ECO:0000303|PubMed:10103065};
DE Short=AATase 2 {ECO:0000303|PubMed:10103065};
DE EC=2.3.1.84 {ECO:0000269|PubMed:10103065};
DE AltName: Full=Acetyl-CoA:pregnenolone acetyltransferase {ECO:0000303|PubMed:10103065};
DE Short=APAT {ECO:0000303|PubMed:10103065};
GN Name=ATF2 {ECO:0000303|PubMed:10103065}; OrderedLocusNames=YGR177C;
GN ORFNames=G7135;
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=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP PROTEIN SEQUENCE OF 130-139 AND 145-160, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION PHENOTYPE.
RX PubMed=10103065; DOI=10.1046/j.1432-1327.1999.00282.x;
RA Cauet G., Degryse E., Ledoux C., Spagnoli R., Achstetter T.;
RT "Pregnenolone esterification in Saccharomyces cerevisiae. A potential
RT detoxification mechanism.";
RL Eur. J. Biochem. 261:317-324(1999).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12957907; DOI=10.1128/aem.69.9.5228-5237.2003;
RA Verstrepen K.J., Van Laere S.D., Vanderhaegen B.M., Derdelinckx G.,
RA Dufour J.P., Pretorius I.S., Winderickx J., Thevelein J.M., Delvaux F.R.;
RT "Expression levels of the yeast alcohol acetyltransferase genes ATF1, Lg-
RT ATF1, and ATF2 control the formation of a broad range of volatile esters.";
RL Appl. Environ. Microbiol. 69:5228-5237(2003).
RN [6]
RP FUNCTION.
RX PubMed=12937998; DOI=10.1007/s10295-003-0070-0;
RA Horton C.E., Huang K.X., Bennett G.N., Rudolph F.B.;
RT "Heterologous expression of the Saccharomyces cerevisiae alcohol
RT acetyltransferase genes in Clostridium acetobutylicum and Escherichia coli
RT for the production of isoamyl acetate.";
RL J. Ind. Microbiol. Biotechnol. 30:427-432(2003).
RN [7]
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 [8]
RP FUNCTION.
RX PubMed=16845703; DOI=10.1002/yea.1382;
RA Lilly M., Bauer F.F., Lambrechts M.G., Swiegers J.H., Cozzolino D.,
RA Pretorius I.S.;
RT "The effect of increased yeast alcohol acetyltransferase and esterase
RT activity on the flavour profiles of wine and distillates.";
RL Yeast 23:641-659(2006).
RN [9]
RP FUNCTION.
RX PubMed=17891501; DOI=10.1007/s00449-007-0159-3;
RA Singh R., Vadlani P.V., Harrison M.L., Bennett G.N., San K.Y.;
RT "Aerobic production of isoamyl acetate by overexpression of the yeast
RT alcohol acetyl-transferases AFT1 and AFT2 in Escherichia coli and using
RT low-cost fermentation ingredients.";
RL Bioprocess Biosyst. Eng. 31:299-306(2008).
RN [10]
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=25093817; DOI=10.1371/journal.pone.0104141;
RA Lin J.L., Wheeldon I.;
RT "Dual N- and C-terminal helices are required for endoplasmic reticulum and
RT lipid droplet association of alcohol acetyltransferases in Saccharomyces
RT cerevisiae.";
RL PLoS ONE 9:E104141-E104141(2014).
CC -!- FUNCTION: Can use acetyl-CoA to synthesize acetate esters from various
CC alcohols, producing ethyl acetate, isoamyl acetate, isobutyl acetate,
CC butyl acetate, hexyl acetate, heptyl acetate and octyl acetate
CC (PubMed:12957907, PubMed:12937998, PubMed:16845703, PubMed:17891501).
CC ATF2 seems to play only a minor role in the acetate ester synthesis,
CC compared to ATF1 (PubMed:12957907). Plays an active role in the
CC detoxification hydroxysteroids and possibly certain phytochemicals, in
CC association with the efflux pumps PDR5 and SNQ2 (PubMed:10103065).
CC {ECO:0000269|PubMed:10103065, ECO:0000269|PubMed:12937998,
CC ECO:0000269|PubMed:12957907, ECO:0000269|PubMed:16845703,
CC ECO:0000269|PubMed:17891501}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + an aliphatic alcohol = an acetyl ester + CoA;
CC Xref=Rhea:RHEA:17229, ChEBI:CHEBI:2571, ChEBI:CHEBI:47622,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.84;
CC Evidence={ECO:0000269|PubMed:10103065};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.52 uM for pregnenolone {ECO:0000269|PubMed:10103065};
CC KM=1.1 uM for acetyl-CoA {ECO:0000269|PubMed:10103065};
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:25093817}.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:25093817};
CC Peripheral membrane protein {ECO:0000269|PubMed:25093817}.
CC Note=Traffics to lipid droplets during the stationary phase
CC (PubMed:25093817). {ECO:0000269|PubMed:25093817}.
CC -!- DOMAIN: Segments of the N- and C-terminal domains (residues 19-36 and
CC 515-532, respectively) are predicted to be amphipathic helices and are
CC essential for endoplasmic reticulum membrane association
CC (PubMed:25093817). {ECO:0000269|PubMed:25093817}.
CC -!- DISRUPTION PHENOTYPE: Results in an 18% decrease in isoamyl acetate
CC formation and causes a 13% reduction of ethyl acetate formation
CC (PubMed:12957907). Leads to the complete elimination of acetyl-
CC CoA:pregnenolone acetyltransferase activity and consequently abolishes
CC the esterification of pregnenolone and increases the toxicity of
CC pregnenolone (PubMed:10103065). {ECO:0000269|PubMed:10103065,
CC ECO:0000269|PubMed:12957907}.
CC -!- MISCELLANEOUS: Present with 3000 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ATF1 alcohol acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; Z72961; CAA97203.1; -; Genomic_DNA.
DR EMBL; AY723818; AAU09735.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08272.1; -; Genomic_DNA.
DR PIR; S64491; S64491.
DR RefSeq; NP_011693.1; NM_001181306.1.
DR AlphaFoldDB; P53296; -.
DR BioGRID; 33429; 62.
DR DIP; DIP-5544N; -.
DR IntAct; P53296; 6.
DR MINT; P53296; -.
DR STRING; 4932.YGR177C; -.
DR iPTMnet; P53296; -.
DR MaxQB; P53296; -.
DR PaxDb; P53296; -.
DR PRIDE; P53296; -.
DR EnsemblFungi; YGR177C_mRNA; YGR177C; YGR177C.
DR GeneID; 853088; -.
DR KEGG; sce:YGR177C; -.
DR SGD; S000003409; ATF2.
DR VEuPathDB; FungiDB:YGR177C; -.
DR eggNOG; ENOG502QTAU; Eukaryota.
DR GeneTree; ENSGT00940000176620; -.
DR HOGENOM; CLU_043707_0_0_1; -.
DR InParanoid; P53296; -.
DR OMA; HLENYFA; -.
DR BioCyc; MetaCyc:YGR177C-MON; -.
DR BioCyc; YEAST:YGR177C-MON; -.
DR BRENDA; 2.3.1.84; 984.
DR PRO; PR:P53296; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53296; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0004026; F:alcohol O-acetyltransferase activity; IDA:SGD.
DR GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:1901089; P:acetate ester metabolic process involved in fermentation; IGI:SGD.
DR GO; GO:0009636; P:response to toxic substance; IMP:SGD.
DR GO; GO:0008202; P:steroid metabolic process; IMP:SGD.
DR GO; GO:0034209; P:sterol acetylation; IMP:SGD.
DR InterPro; IPR010828; Atf2/Sli1-like.
DR Pfam; PF07247; AATase; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Direct protein sequencing; Endoplasmic reticulum;
KW Lipid droplet; Membrane; Reference proteome; Transferase.
FT CHAIN 1..535
FT /note="Alcohol O-acetyltransferase 2"
FT /id="PRO_0000064721"
FT REGION 19..36
FT /note="Membrane association"
FT /evidence="ECO:0000269|PubMed:25093817"
FT REGION 515..532
FT /note="Membrane association"
FT /evidence="ECO:0000269|PubMed:25093817"
FT ACT_SITE 189
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P40353"
FT ACT_SITE 193
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P40353"
FT CONFLICT 179
FT /note="T -> A (in Ref. 3; AAU09735)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 61898 MW; D615241A7DF1ECD5 CRC64;
MEDIEGYEPH ITQELIDRGH ARRMGHLENY FAVLSRQKMY SNFTVYAELN KGVNKRQLML
VLKVLLQKYS TLAHTIIPKH YPHHEAYYSS EEYLSKPFPQ HDFIKVISHL EFDDLIMNNQ
PEYREVMEKI SEQFKKDDFK VTNRLIELIS PVIIPLGNPK RPNWRLICLP GKDTDGFETW
KNFVYVTNHC GSDGVSGSNF FKDLALLFCK IEEKGFDYDE EFIEDQVIID YDRDYTEISK
LPKPITDRID YKPALTSLPK FFLTTFIYEH CNFKTSSEST LTARYSPSSN ANASYNYLLH
FSTKQVEQIR AQIKKNVHDG CTLTPFIQAC FLVALYRLDK LFTKSLLEYG FDVAIPSNAR
RFLPNDEELR DSYKYGSNVG GSHYAYLISS FDIPEGDNDK FWSLVEYYYD RFLESYDNGD
HLIGLGVLQL DFIVENKNID SLLANSYLHQ QRGGAIISNT GLVSQDTTKP YYVRDLIFSQ
SAGALRFAFG LNVCSTNVNG MNMDMSVVQG TLRDRGEWES FCKLFYQTIG EFASL
