LOA1_YEAST
ID LOA1_YEAST Reviewed; 300 AA.
AC Q06508; D6W4D7;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Lysophosphatidic acid:oleoyl-CoA acyltransferase 1 {ECO:0000305};
DE Short=LPAAT;
DE Short=Lysophosphatidic acid acyltransferase;
DE EC=2.3.1.51 {ECO:0000269|PubMed:22090344};
DE AltName: Full=Vacuolar protein sorting-associated protein 66;
GN Name=LOA1 {ECO:0000303|PubMed:22090344};
GN Synonyms=VPS66 {ECO:0000303|PubMed:12134085}; OrderedLocusNames=YPR139C;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 FUNCTION.
RX PubMed=12134085; DOI=10.1091/mbc.02-01-0005;
RA Bonangelino C.J., Chavez E.M., Bonifacino J.S.;
RT "Genomic screen for vacuolar protein sorting genes in Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 13:2486-2501(2002).
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 SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=22090344; DOI=10.1091/mbc.e11-07-0650;
RA Ayciriex S., Le Guedard M., Camougrand N., Velours G., Schoene M.,
RA Leone S., Wattelet-Boyer V., Dupuy J.W., Shevchenko A., Schmitter J.M.,
RA Lessire R., Bessoule J.J., Testet E.;
RT "YPR139c/LOA1 encodes a novel lysophosphatidic acid acyltransferase
RT associated with lipid droplets and involved in TAG homeostasis.";
RL Mol. Biol. Cell 23:233-246(2012).
CC -!- FUNCTION: Acyl-CoA-dependent lysophosphatidic acid acyltransferase with
CC preference for oleoyl-CoA. Involved in triacylglyceride homeostasis and
CC lipid droplet formation. Involved in vacuolar protein sorting.
CC {ECO:0000269|PubMed:12134085, ECO:0000269|PubMed:22090344}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000269|PubMed:22090344};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC Evidence={ECO:0000305|PubMed:22090344};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate
CC = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:33187, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:57518, ChEBI:CHEBI:64839;
CC Evidence={ECO:0000269|PubMed:22090344};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188;
CC Evidence={ECO:0000305|PubMed:22090344};
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:21820081,
CC ECO:0000269|PubMed:22090344}. Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:22090344}; Single-pass membrane protein
CC {ECO:0000255}. Note=Lipid droplets consist of a surface phospholipid
CC monolayer and a hydrophobic interior. The latter makes embedding of
CC proteins containing transmembrane segments difficult, and these may
CC instead adopt a hairpin or monotonic conformation when associated with
CC lipid droplet membranes. Always localizes to lipid droplets,
CC irrespective of whether cells are grown on glucose or oleate.
CC {ECO:0000269|PubMed:21820081}.
CC -!- MISCELLANEOUS: Present with 6630 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
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DR EMBL; U40829; AAB68279.1; -; Genomic_DNA.
DR EMBL; AY693235; AAT93254.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11553.1; -; Genomic_DNA.
DR PIR; S69028; S69028.
DR RefSeq; NP_015465.1; NM_001184236.1.
DR AlphaFoldDB; Q06508; -.
DR SMR; Q06508; -.
DR BioGRID; 36308; 29.
DR IntAct; Q06508; 4.
DR MINT; Q06508; -.
DR STRING; 4932.YPR139C; -.
DR SwissLipids; SLP:000000079; -.
DR MaxQB; Q06508; -.
DR PaxDb; Q06508; -.
DR PRIDE; Q06508; -.
DR EnsemblFungi; YPR139C_mRNA; YPR139C; YPR139C.
DR GeneID; 856261; -.
DR KEGG; sce:YPR139C; -.
DR SGD; S000006343; LOA1.
DR VEuPathDB; FungiDB:YPR139C; -.
DR eggNOG; ENOG502RYF8; Eukaryota.
DR HOGENOM; CLU_048121_1_0_1; -.
DR InParanoid; Q06508; -.
DR OMA; NWRDKGT; -.
DR BioCyc; MetaCyc:G3O-34274-MON; -.
DR BioCyc; YEAST:G3O-34274-MON; -.
DR BRENDA; 2.3.1.51; 984.
DR PRO; PR:Q06508; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06508; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IDA:SGD.
DR GO; GO:0035356; P:cellular triglyceride homeostasis; IMP:SGD.
DR GO; GO:0034389; P:lipid droplet organization; IMP:SGD.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006623; P:protein targeting to vacuole; HMP:SGD.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Lipid droplet; Lipid metabolism; Membrane;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..300
FT /note="Lysophosphatidic acid:oleoyl-CoA acyltransferase 1"
FT /id="PRO_0000065908"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 101..106
FT /note="HXXXXD motif"
SQ SEQUENCE 300 AA; 33816 MW; D04AAB2CCF051D23 CRC64;
MEKYTNWRDN GTGIAPFLPN TIRKPSKVMT ACLLGILGVK TIIMLPLIML YLLTGQNNLL
GLILKFTFSW KEEITVQGIK KRDVRKSKHY PQKGKLYICN CTSPLDAFSV VLLAQGPVTL
LVPSNDIVYK VSIREFINFI LAGGLDIKLY GHEVAELSQL GNTVNFMFAE GTSCNGKSVL
PFSITGKKLK EFIDPSITTM NPAMAKTKKF ELQTIQIKTN KTAITTLPIS NMEYLSRFLN
KGINVKCKIN EPQVLSDNLE ELRVALNGGD KYKLVSRKLD VESKRNFVKE YISDQRKKRK
