ARE1_YEAST
ID ARE1_YEAST Reviewed; 610 AA.
AC P25628; D6VR57;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Sterol O-acyltransferase 1;
DE EC=2.3.1.- {ECO:0000269|PubMed:10672016};
DE AltName: Full=Sterol-ester synthase 1;
GN Name=ARE1 {ECO:0000303|PubMed:10672016}; Synonyms=SAT2;
GN OrderedLocusNames=YCR048W; ORFNames=YCR48W;
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=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
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 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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, AND IDENTIFICATION BY
RP 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).
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 + lanosterol = CoA + lanosteryl ester;
CC Xref=Rhea:RHEA:33479, ChEBI:CHEBI:16521, ChEBI:CHEBI:52394,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:58342;
CC Evidence={ECO:0000269|PubMed:10672016};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33480;
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 -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC Sterol o-acyltransferase subfamily. {ECO:0000305}.
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DR EMBL; X59720; CAA42296.1; -; Genomic_DNA.
DR EMBL; AY692921; AAT92940.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07526.1; -; Genomic_DNA.
DR PIR; S19461; S19461.
DR RefSeq; NP_009978.1; NM_001178762.1.
DR AlphaFoldDB; P25628; -.
DR SMR; P25628; -.
DR BioGRID; 31030; 167.
DR DIP; DIP-4998N; -.
DR IntAct; P25628; 6.
DR MINT; P25628; -.
DR STRING; 4932.YCR048W; -.
DR SwissLipids; SLP:000000706; -.
DR SwissLipids; SLP:000000709; -.
DR iPTMnet; P25628; -.
DR MaxQB; P25628; -.
DR PaxDb; P25628; -.
DR PRIDE; P25628; -.
DR TopDownProteomics; P25628; -.
DR EnsemblFungi; YCR048W_mRNA; YCR048W; YCR048W.
DR GeneID; 850415; -.
DR KEGG; sce:YCR048W; -.
DR SGD; S000000644; ARE1.
DR VEuPathDB; FungiDB:YCR048W; -.
DR eggNOG; KOG0380; Eukaryota.
DR GeneTree; ENSGT00950000183081; -.
DR HOGENOM; CLU_018190_2_1_1; -.
DR InParanoid; P25628; -.
DR OMA; ITEHWIM; -.
DR BioCyc; MetaCyc:YCR048W-MON; -.
DR BioCyc; YEAST:YCR048W-MON; -.
DR PRO; PR:P25628; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25628; 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; IGI:SGD.
DR GO; GO:0034738; F:lanosterol O-acyltransferase activity; IMP:SGD.
DR GO; GO:0008374; F:O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0008204; P:ergosterol metabolic process; IBA:GO_Central.
DR GO; GO:0016125; P:sterol 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..610
FT /note="Sterol O-acyltransferase 1"
FT /id="PRO_0000207648"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 535..555
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 590..610
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 41..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 491..497
FT /note="FYXDWWN motif"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT COMPBIAS 41..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 547
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 610 AA; 71613 MW; FF72EFB9238B2205 CRC64;
MTETKDLLQD EEFLKIRRLN SAEANKRHSV TYDNVILPQE SMEVSPRSST TSLVEPVEST
EGVESTEAER VAGKQEQEEE YPVDAHMQKY LSHLKSKSRS RFHRKDASKY VSFFGDVSFD
PRPTLLDSAI NVPFQTTFKG PVLEKQLKNL QLTKTKTKAT VKTTVKTTEK TDKADAPPGE
KLESNFSGIY VFAWMFLGWI AIRCCTDYYA SYGSAWNKLE IVQYMTTDLF TIAMLDLAMF
LCTFFVVFVH WLVKKRIINW KWTGFVAVSI FELAFIPVTF PIYVYYFDFN WVTRIFLFLH
SVVFVMKSHS FAFYNGYLWD IKQELEYSSK QLQKYKESLS PETREILQKS CDFCLFELNY
QTKDNDFPNN ISCSNFFMFC LFPVLVYQIN YPRTSRIRWR YVLEKVCAII GTIFLMMVTA
QFFMHPVAMR CIQFHNTPTF GGWIPATQEW FHLLFDMIPG FTVLYMLTFY MIWDALLNCV
AELTRFADRY FYGDWWNCVS FEEFSRIWNV PVHKFLLRHV YHSSMGALHL SKSQATLFTF
FLSAVFHEMA MFAIFRRVRG YLFMFQLSQF VWTALSNTKF LRARPQLSNV VFSFGVCSGP
SIIMTLYLTL
