ARE2_YEAST
ID ARE2_YEAST Reviewed; 642 AA.
AC P53629; D6W1J4; Q12673;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Sterol O-acyltransferase 2;
DE EC=2.3.1.- {ECO:0000269|PubMed:10672016};
DE AltName: Full=Sterol-ester synthase 2;
GN Name=ARE2 {ECO:0000303|PubMed:8650549}; Synonyms=SAT1;
GN OrderedLocusNames=YNR019W; ORFNames=N3206;
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], AND FUNCTION.
RX PubMed=8650549; DOI=10.1126/science.272.5266.1353;
RA Yang H., Bard M., Bruner D.A., Gleeson A., Deckelbaum R.J., Aljinovic G.,
RA Pohl T.M., Rothstein R., Sturley S.L.;
RT "Sterol esterification in yeast: a two-gene process.";
RL Science 272:1353-1356(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / SNY243;
RX PubMed=8798656; DOI=10.1074/jbc.271.39.24157;
RA Yu C., Kennedy N.J., Chang C.C.Y., Rothblatt J.A.;
RT "Molecular cloning and characterization of two isoforms of Saccharomyces
RT cerevisiae acyl-CoA:sterol acyltransferase.";
RL J. Biol. Chem. 271:24157-24163(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=10672016; DOI=10.1046/j.1432-1327.2000.01103.x;
RA Zweytick D., Leitner E., Kohlwein S.D., Yu C., Rothblatt J., Daum G.;
RT "Contribution of Are1p and Are2p to steryl ester synthesis in the yeast
RT Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 267:1075-1082(2000).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175 AND SER-176, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [11]
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).
CC -!- FUNCTION: Sterol O-acyltransferase that catalyzes the formation of
CC stery esters. {ECO:0000269|PubMed:10672016,
CC ECO:0000269|PubMed:8650549}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + ergosterol = CoA + ergosteryl ester;
CC Xref=Rhea:RHEA:33483, ChEBI:CHEBI:16933, ChEBI:CHEBI:52320,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:58342;
CC Evidence={ECO:0000269|PubMed:10672016};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33484;
CC Evidence={ECO:0000269|PubMed:10672016};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + zymosterol = CoA + zymosterol ester;
CC Xref=Rhea:RHEA:41476, ChEBI:CHEBI:18252, ChEBI:CHEBI:52322,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:58342;
CC Evidence={ECO:0000269|PubMed:10672016};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41477;
CC Evidence={ECO:0000269|PubMed:10672016};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10672016}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- MISCELLANEOUS: Present with 279 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC Sterol o-acyltransferase subfamily. {ECO:0000305}.
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DR EMBL; U51790; AAB02203.1; -; Genomic_DNA.
DR EMBL; U55383; AAC49441.1; -; Genomic_DNA.
DR EMBL; Z71634; CAA96298.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10560.1; -; Genomic_DNA.
DR PIR; S63350; S63350.
DR RefSeq; NP_014416.1; NM_001183196.1.
DR AlphaFoldDB; P53629; -.
DR SMR; P53629; -.
DR BioGRID; 35844; 153.
DR DIP; DIP-4050N; -.
DR IntAct; P53629; 8.
DR MINT; P53629; -.
DR STRING; 4932.YNR019W; -.
DR SwissLipids; SLP:000000707; -.
DR SwissLipids; SLP:000000708; -.
DR iPTMnet; P53629; -.
DR MaxQB; P53629; -.
DR PaxDb; P53629; -.
DR PRIDE; P53629; -.
DR EnsemblFungi; YNR019W_mRNA; YNR019W; YNR019W.
DR GeneID; 855753; -.
DR KEGG; sce:YNR019W; -.
DR SGD; S000005302; ARE2.
DR VEuPathDB; FungiDB:YNR019W; -.
DR eggNOG; KOG0380; Eukaryota.
DR GeneTree; ENSGT00950000183081; -.
DR HOGENOM; CLU_018190_2_1_1; -.
DR InParanoid; P53629; -.
DR OMA; FYLIFEC; -.
DR BioCyc; MetaCyc:YNR019W-MON; -.
DR BioCyc; YEAST:YNR019W-MON; -.
DR BRENDA; 2.3.1.26; 984.
DR PRO; PR:P53629; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53629; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0034737; F:ergosterol O-acyltransferase activity; IMP:SGD.
DR GO; GO:0008374; F:O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0008204; P:ergosterol metabolic process; IMP:SGD.
DR InterPro; IPR004299; MBOAT_fam.
DR InterPro; IPR014371; Oat_ACAT_DAG_ARE.
DR PANTHER; PTHR10408; PTHR10408; 1.
DR Pfam; PF03062; MBOAT; 1.
DR PIRSF; PIRSF000439; Oat_ACAT_DAG_ARE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..642
FT /note="Sterol O-acyltransferase 2"
FT /id="PRO_0000207651"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 567..587
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 622..642
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 174..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 523..529
FT /note="FYXDWWN motif"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT ACT_SITE 579
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 80
FT /note="G -> D (in Ref. 2; AAC49441)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="G -> E (in Ref. 2; AAC49441)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="I -> L (in Ref. 2; AAC49441)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="F -> S (in Ref. 2; AAC49441)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 642 AA; 74023 MW; 035FC4ED9C7CD830 CRC64;
MDKKKDLLEN EQFLRIQKLN AADAGKRQSI TVDDEGELYG LDTSGNSPAN EHTATTITQN
HSVVASNGDV AFIPGTATEG NTEIVTEEVI ETDDNMFKTH VKTLSSKEKA RYRQGSSNFI
SYFDDMSFEH RPSILDGSVN EPFKTKFVGP TLEKEIRRRE KELMAMRKNL HHRKSSPDAV
DSVGKNDGAA PTTVPTAATS ETVVTVETTI ISSNFSGLYV AFWMAIAFGA VKALIDYYYQ
HNGSFKDSEI LKFMTTNLFT VASVDLLMYL STYFVVGIQY LCKWGVLKWG TTGWIFTSIY
EFLFVIFYMY LTENILKLHW LSKIFLFLHS LVLLMKMHSF AFYNGYLWGI KEELQFSKSA
LAKYKDSIND PKVIGALEKS CEFCSFELSS QSLSDQTQKF PNNISAKSFF WFTMFPTLIY
QIEYPRTKEI RWSYVLEKIC AIFGTIFLMM IDAQILMYPV AMRALAVRNS EWTGILDRLL
KWVGLLVDIV PGFIVMYILD FYLIWDAILN CVAELTRFGD RYFYGDWWNC VSWADFSRIW
NIPVHKFLLR HVYHSSMSSF KLNKSQATLM TFFLSSVVHE LAMYVIFKKL RFYLFFFQML
QMPLVALTNT KFMRNRTIIG NVIFWLGICM GPSVMCTLYL TF
