AYR1_YEAST
ID AYR1_YEAST Reviewed; 297 AA.
AC P40471; D6VVG3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=NADPH-dependent 1-acyldihydroxyacetone phosphate reductase {ECO:0000303|PubMed:10617610};
DE Short=ADR;
DE EC=1.1.1.101 {ECO:0000269|PubMed:1512203};
DE AltName: Full=1-acyl DHAP reductase;
DE AltName: Full=Acyl/alkyl DHAP reductase;
DE AltName: Full=Acylglycerone-phosphate reductase;
DE AltName: Full=Triacylglycerol lipase AYR1 {ECO:0000303|PubMed:24187129};
DE Short=TAG lipase;
DE EC=3.1.1.3 {ECO:0000269|PubMed:24187129};
GN Name=AYR1 {ECO:0000303|PubMed:10617610};
GN Synonyms=GBG1 {ECO:0000303|PubMed:23956635}; OrderedLocusNames=YIL124W;
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=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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 PROTEIN SEQUENCE OF 32-41; 63-79; 127-134; 224-235; 240-252 AND 261-273,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (JUN-2005) to UniProtKB.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=1512203; DOI=10.1128/jb.174.17.5702-5710.1992;
RA Racenis P.V., Lai J.L., Das A.K., Mullick P.C., Hajra A.K., Greenberg M.L.;
RT "The acyl dihydroxyacetone phosphate pathway enzymes for glycerolipid
RT biosynthesis are present in the yeast Saccharomyces cerevisiae.";
RL J. Bacteriol. 174:5702-5710(1992).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=10515935; DOI=10.1128/jb.181.20.6441-6448.1999;
RA Athenstaedt K., Zweytick D., Jandrositz A., Kohlwein S.D., Daum G.;
RT "Identification and characterization of major lipid particle proteins of
RT the yeast Saccharomyces cerevisiae.";
RL J. Bacteriol. 181:6441-6448(1999).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=10617610; DOI=10.1074/jbc.275.1.235;
RA Athenstaedt K., Daum G.;
RT "1-acyldihydroxyacetone-phosphate reductase (Ayr1p) of the yeast
RT Saccharomyces cerevisiae encoded by the open reading frame YIL124w is a
RT major component of lipid particles.";
RL J. Biol. Chem. 275:235-240(2000).
RN [7]
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 [8]
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 [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16407407; DOI=10.1091/mbc.e05-08-0740;
RA Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N.,
RA Schoenfisch B., Guiard B., Pfanner N., Meisinger C.;
RT "Proteomic analysis of the yeast mitochondrial outer membrane reveals
RT accumulation of a subclass of preproteins.";
RL Mol. Biol. Cell 17:1436-1450(2006).
RN [10]
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 [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=23956635; DOI=10.4489/myco.2010.38.2.0102;
RA Ahn K.W., Kim S.W., Kang H.G., Kim K.H., Park Y.H., Choi W.J., Park H.M.;
RT "Deletion of GBG1/AYR1 alters cell wall biogenesis in Saccharomyces
RT cerevisiae.";
RL Mycobiology 38:102-107(2010).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=21820081; DOI=10.1016/j.bbalip.2011.07.015;
RA Grillitsch K., Connerth M., Kofeler H., Arrey T.N., Rietschel B.,
RA Wagner B., Karas M., Daum G.;
RT "Lipid particles/droplets of the yeast Saccharomyces cerevisiae revisited:
RT lipidome meets proteome.";
RL Biochim. Biophys. Acta 1811:1165-1176(2011).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION
RP BY MASS SPECTROMETRY, AND MUTAGENESIS OF SER-18.
RX PubMed=24187129; DOI=10.1074/jbc.m113.509927;
RA Ploier B., Scharwey M., Koch B., Schmidt C., Schatte J., Rechberger G.,
RA Kollroser M., Hermetter A., Daum G.;
RT "Screening for hydrolytic enzymes reveals Ayr1p as a novel triacylglycerol
RT lipase in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 288:36061-36072(2013).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=24868093; DOI=10.1194/jlr.m050229;
RA Currie E., Guo X., Christiano R., Chitraju C., Kory N., Harrison K.,
RA Haas J., Walther T.C., Farese R.V. Jr.;
RT "High-confidence proteomic analysis of yeast lipid droplets identifies
RT additional droplet proteins and reveals connections to dolichol synthesis
RT and sterol acetylation.";
RL J. Lipid Res. 55:1465-1477(2014).
RN [15]
RP FUNCTION.
RX PubMed=26162625; DOI=10.15252/embj.201490315;
RA Shpilka T., Welter E., Borovsky N., Amar N., Mari M., Reggiori F.,
RA Elazar Z.;
RT "Lipid droplets and their component triglycerides and steryl esters
RT regulate autophagosome biogenesis.";
RL EMBO J. 34:2117-2131(2015).
RN [16]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=28916712; DOI=10.1083/jcb.201706043;
RA Krueger V., Becker T., Becker L., Montilla-Martinez M., Ellenrieder L.,
RA Voegtle F.N., Meyer H.E., Ryan M.T., Wiedemann N., Warscheid B.,
RA Pfanner N., Wagner R., Meisinger C.;
RT "Identification of new channels by systematic analysis of the mitochondrial
RT outer membrane.";
RL J. Cell Biol. 216:3485-3495(2017).
CC -!- FUNCTION: Can convert acyl and alkyl dihydroxyacetone-phosphate (DHAP)
CC into glycerolipids and ether lipids, respectively. Required for the
CC biosynthesis of phosphatidic acid via the DHAP pathway, where it
CC reduces 1-acyl DHAP to lysophosphatidic acid (LPA) (PubMed:1512203,
CC PubMed:10617610). Also has triacylglycerol (TAG) lipase activity.
CC Involved in the mobilization of the non-polar storage lipids
CC triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs
CC (PubMed:24187129). Required for spore germination (PubMed:10617610).
CC Plays a role in cell wall biogenesis, but this effect may be indirect
CC by affecting the activities of cell wall synthesis enzymes
CC (PubMed:23956635). Lipolysis of TAG by AYR1 is essential for
CC starvation-induced autophagy (PubMed:26162625). Forms an NADPH-
CC regulated cation-selective channel in the mitochondrial outer membrane
CC (PubMed:28916712). {ECO:0000269|PubMed:10617610,
CC ECO:0000269|PubMed:1512203, ECO:0000269|PubMed:23956635,
CC ECO:0000269|PubMed:24187129, ECO:0000269|PubMed:26162625,
CC ECO:0000269|PubMed:28916712}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acylglycerone 3-phosphate + H(+) + NADPH = a 1-acyl-sn-
CC glycero-3-phosphate + NADP(+); Xref=Rhea:RHEA:33375,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57534, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:57970, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:10617610};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33376;
CC Evidence={ECO:0000305|PubMed:10617610};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphate + NADP(+) = 1-
CC hexadecanoylglycerone 3-phosphate + H(+) + NADPH;
CC Xref=Rhea:RHEA:17341, ChEBI:CHEBI:15378, ChEBI:CHEBI:57518,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58303, ChEBI:CHEBI:58349;
CC EC=1.1.1.101; Evidence={ECO:0000269|PubMed:1512203};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC Evidence={ECO:0000269|PubMed:24187129};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000305|PubMed:24187129};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-
CC octadecenoate + di-(9Z)-octadecenoylglycerol + H(+);
CC Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945;
CC Evidence={ECO:0000269|PubMed:24187129};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC Evidence={ECO:0000305|PubMed:24187129};
CC -!- ACTIVITY REGULATION: Inhibited by divalent cations and N-
CC ethylmaleimide. Activity is reduced under anaerobic growth conditions.
CC {ECO:0000269|PubMed:1512203}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20 uM for NADPH {ECO:0000269|PubMed:1512203};
CC KM=15 uM for hexadecyl dihydroxyacetone-phosphate
CC {ECO:0000269|PubMed:1512203};
CC KM=3.5 mM for p-nitrophenylacetate {ECO:0000269|PubMed:24187129};
CC KM=1.52 mM for p-nitrophenylbutyrate {ECO:0000269|PubMed:24187129};
CC KM=61.21 uM for 1,2,3-tri-(9Z-octadecenoyl)-glycerol
CC {ECO:0000269|PubMed:24187129};
CC Vmax=3.8 nmol/min/mg enzyme for hexadecyl dihydroxyacetone-phosphate
CC {ECO:0000269|PubMed:1512203};
CC Vmax=18.5 umol/min/mg enzyme for p-nitrophenylacetate
CC {ECO:0000269|PubMed:24187129};
CC Vmax=14.06 umol/min/mg enzyme for p-nitrophenylbutyrate
CC {ECO:0000269|PubMed:24187129};
CC Vmax=10.93 pmol/h/mg enzyme for 1,2,3-tri-(9Z-octadecenoyl)-glycerol
CC {ECO:0000269|PubMed:24187129};
CC pH dependence:
CC Optimum pH is 6.7-7.2. {ECO:0000269|PubMed:1512203};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius. Thermostable for 10 min up
CC to 45 degrees Celsius. {ECO:0000269|PubMed:1512203};
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:10515935,
CC ECO:0000269|PubMed:10617610, ECO:0000269|PubMed:21820081,
CC ECO:0000269|PubMed:24868093}. Mitochondrion outer membrane
CC {ECO:0000269|PubMed:16407407, ECO:0000269|PubMed:28916712}. Endoplasmic
CC reticulum {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:28916712}.
CC -!- INDUCTION: Expressed during vegetative growth with a maximum level of
CC transcription at G1 phase, after which it is decreased during the
CC remainder of the cell cycle. {ECO:0000269|PubMed:23956635}.
CC -!- DISRUPTION PHENOTYPE: Reduces the activities of beta-1,3-glucan
CC synthase and chitin synthase III, while increasing chitin synthase I
CC and II activities. Shows altered cell wall composition as well as
CC susceptibility towards cell wall inhibitors such as zymolyase,
CC calcofluor white, and nikkomycin Z. {ECO:0000269|PubMed:23956635}.
CC -!- MISCELLANEOUS: Present with 3671 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}.
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DR EMBL; Z46833; CAA86868.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08429.1; -; Genomic_DNA.
DR PIR; S49885; S49885.
DR RefSeq; NP_012142.3; NM_001179472.3.
DR AlphaFoldDB; P40471; -.
DR SMR; P40471; -.
DR BioGRID; 34867; 142.
DR DIP; DIP-4614N; -.
DR IntAct; P40471; 11.
DR MINT; P40471; -.
DR STRING; 4932.YIL124W; -.
DR SwissLipids; SLP:000000056; -.
DR TCDB; 1.A.115.1.1; the pore-forming nadph-dependent 1-acyldihydroxyacetone phosphate reductase (ayr1) family.
DR iPTMnet; P40471; -.
DR MaxQB; P40471; -.
DR PaxDb; P40471; -.
DR PRIDE; P40471; -.
DR DNASU; 854682; -.
DR EnsemblFungi; YIL124W_mRNA; YIL124W; YIL124W.
DR GeneID; 854682; -.
DR KEGG; sce:YIL124W; -.
DR SGD; S000001386; AYR1.
DR VEuPathDB; FungiDB:YIL124W; -.
DR eggNOG; KOG1209; Eukaryota.
DR GeneTree; ENSGT00940000154593; -.
DR HOGENOM; CLU_010194_2_9_1; -.
DR InParanoid; P40471; -.
DR OMA; TPIWAKA; -.
DR BioCyc; MetaCyc:YIL124W-MON; -.
DR BioCyc; YEAST:YIL124W-MON; -.
DR SABIO-RK; P40471; -.
DR PRO; PR:P40471; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40471; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0102566; F:1-acyl dihydroxyacetone phosphate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0000140; F:acylglycerone-phosphate reductase activity; IMP:SGD.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:SGD.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IMP:SGD.
DR GO; GO:0019433; P:triglyceride catabolic process; IGI:SGD.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; Hydrolase;
KW Lipid degradation; Lipid droplet; Lipid metabolism; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; NAD; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..297
FT /note="NADPH-dependent 1-acyldihydroxyacetone phosphate
FT reductase"
FT /id="PRO_0000054520"
FT MOTIF 16..20
FT /note="GXSXG"
FT /evidence="ECO:0000305|PubMed:24187129"
FT ACT_SITE 18
FT /note="Nucleophile; for lipase activity"
FT /evidence="ECO:0000305|PubMed:24187129"
FT ACT_SITE 157
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 13..21
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 63..65
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 157..161
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 190..192
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT MUTAGEN 18
FT /note="S->A: Completely abolishes lipase activity."
FT /evidence="ECO:0000269|PubMed:24187129"
SQ SEQUENCE 297 AA; 32814 MW; B614C0E0B1FB0CE0 CRC64;
MSELQSQPKK IAVVTGASGG IGYEVTKELA RNGYLVYACA RRLEPMAQLA IQFGNDSIKP
YKLDISKPEE IVTFSGFLRA NLPDGKLDLL YNNAGQSCTF PALDATDAAV EQCFKVNVFG
HINMCRELSE FLIKAKGTIV FTGSLAGVVS FPFGSIYSAS KAAIHQYARG LHLEMKPFNV
RVINAITGGV ATDIADKRPL PETSIYNFPE GREAFNSRKT MAKDNKPMPA DAYAKQLVKD
ILSTSDPVDV YRGTFANIMR FVMIFVPYWL LEKGLSKKFK LDKVNNALKS KQKNKDD
