LPL1_YEAST
ID LPL1_YEAST Reviewed; 450 AA.
AC Q08448; D6W2C2; O00022;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Lipid droplet phospholipase 1 {ECO:0000303|PubMed:25014274};
DE EC=3.1.-.- {ECO:0000269|PubMed:25014274};
DE EC=3.1.1.4 {ECO:0000269|PubMed:25014274};
GN Name=LPL1 {ECO:0000303|PubMed:25014274}; OrderedLocusNames=YOR059C;
GN ORFNames=YOR29-10;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9133743;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<379::aid-yea85>3.0.co;2-g;
RA Valens M., Bohn C., Daignan-Fornier B., Dang V.-D., Bolotin-Fukuhara M.;
RT "The sequence of a 54.7 kb fragment of yeast chromosome XV reveals the
RT presence of two tRNAs and 24 new open reading frames.";
RL Yeast 13:379-390(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 [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 INDUCTION.
RX PubMed=19073890; DOI=10.1091/mbc.e08-02-0140;
RA Metzger M.B., Michaelis S.;
RT "Analysis of quality control substrates in distinct cellular compartments
RT reveals a unique role for Rpn4p in tolerating misfolded membrane
RT proteins.";
RL Mol. Biol. Cell 20:1006-1019(2009).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, DOMAIN, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF GLY-88; SER-90
RP AND GLY-92.
RX PubMed=25014274; DOI=10.1016/j.bbalip.2014.06.013;
RA Selvaraju K., Rajakumar S., Nachiappan V.;
RT "Identification of a phospholipase B encoded by the LPL1 gene in
RT Saccharomyces cerevisiae.";
RL Biochim. Biophys. Acta 1842:1383-1392(2014).
CC -!- FUNCTION: Phospholipase involved in maintaining the lipid droplet
CC morphology (PubMed:25014274). Has phospholipase activity with broad
CC substrate specificity, acting on glycerophospholipids
CC phosphatidylethanolamine (PE), phosphatidic acid (PA),
CC phosphatidycholine (PC) and phosphatidylserine (PS), primarily at sn-2
CC position (PubMed:25014274). It can later remove fatty acids from the
CC sn-1 position of the produced lysophospholipids such as
CC lysophosphatidylethanolamine (LPE) (PubMed:25014274). Shows also
CC activity toward phosphatidylglycerol, but, in contrast to what was
CC observed with the other phospholipids tested, prefers the sn-1 position
CC (PubMed:25014274). {ECO:0000269|PubMed:25014274}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + H2O = a 1-
CC acyl-sn-glycero-3-phosphoethanolamine + a fatty acid + H(+);
CC Xref=Rhea:RHEA:44604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:64381, ChEBI:CHEBI:64612;
CC Evidence={ECO:0000269|PubMed:25014274};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44605;
CC Evidence={ECO:0000269|PubMed:25014274};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + H2O = a fatty acid
CC + H(+) + sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:32967,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:64381, ChEBI:CHEBI:143890;
CC Evidence={ECO:0000269|PubMed:25014274};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32968;
CC Evidence={ECO:0000269|PubMed:25014274};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1-acyl-sn-
CC glycero-3-phosphate + a fatty acid + H(+); Xref=Rhea:RHEA:44420,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57970, ChEBI:CHEBI:58608;
CC Evidence={ECO:0000269|PubMed:25014274};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44421;
CC Evidence={ECO:0000269|PubMed:25014274};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000269|PubMed:25014274};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000269|PubMed:25014274};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H2O = a 1-acyl-
CC sn-glycero-3-phospho-L-serine + a fatty acid + H(+);
CC Xref=Rhea:RHEA:44672, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:57262, ChEBI:CHEBI:64379;
CC Evidence={ECO:0000269|PubMed:25014274};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44673;
CC Evidence={ECO:0000269|PubMed:25014274};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoglycerol + H2O = a 2-acyl-sn-
CC glycero-3-phosphoglycerol + a fatty acid + H(+);
CC Xref=Rhea:RHEA:62032, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:145393, ChEBI:CHEBI:145394;
CC Evidence={ECO:0000269|PubMed:25014274};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62033;
CC Evidence={ECO:0000269|PubMed:25014274};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-(9Z-octadecenoyl)-2-acyl-sn-glycero-3-phosphocholine + H2O
CC = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + a fatty acid +
CC H(+); Xref=Rhea:RHEA:62036, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28610, ChEBI:CHEBI:28868, ChEBI:CHEBI:78421;
CC Evidence={ECO:0000269|PubMed:25014274};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62037;
CC Evidence={ECO:0000269|PubMed:25014274};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-(9Z-octadecenoyl)-2-acyl-sn-glycero-3-phosphoglycerol +
CC H2O = (9Z)-octadecenoate + a 2-acyl-sn-glycero-3-phosphoglycerol +
CC H(+); Xref=Rhea:RHEA:62044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:145392, ChEBI:CHEBI:145393;
CC Evidence={ECO:0000269|PubMed:25014274};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62045;
CC Evidence={ECO:0000269|PubMed:25014274};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-aryl-1,2-dihexadecanoyl-sn-glycero-3-phosphoethanolamine
CC + H2O = an N-aryl-1-hexadecanoyl-sn-glycero-3-phosphoethanolamine +
CC H(+) + hexadecanoate; Xref=Rhea:RHEA:62048, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:145395,
CC ChEBI:CHEBI:145396; Evidence={ECO:0000269|PubMed:25014274};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62049;
CC Evidence={ECO:0000269|PubMed:25014274};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-(9Z-octadecenoyl)-2-acyl-sn-glycero-3-phosphate + H2O = 1-
CC (9Z-octadecenoyl)-sn-glycero-3-phosphate + a fatty acid + H(+);
CC Xref=Rhea:RHEA:62052, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:74544, ChEBI:CHEBI:145397;
CC Evidence={ECO:0000269|PubMed:25014274};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62053;
CC Evidence={ECO:0000269|PubMed:25014274};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphoethanolamine + H2O = 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:62100, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:73004, ChEBI:CHEBI:73005;
CC Evidence={ECO:0000269|PubMed:25014274};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62101;
CC Evidence={ECO:0000269|PubMed:25014274};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.86 mM for phosphatidylethanolamine (PE)
CC {ECO:0000269|PubMed:25014274};
CC KM=0.97 mM for phosphatidic acid (PA) {ECO:0000269|PubMed:25014274};
CC KM=1.12 mM for phosphatidylglycerol (PG)
CC {ECO:0000269|PubMed:25014274};
CC KM=0.83 mM for phosphatidycholine (PC) {ECO:0000269|PubMed:25014274};
CC KM=0.92 mM for phosphatidylserine (PS) {ECO:0000269|PubMed:25014274};
CC Vmax=4.55 umol/min/mg enzyme toward phosphatidylethanolamine (PE)
CC {ECO:0000269|PubMed:25014274};
CC Vmax=4.05 umol/min/mg enzyme toward phosphatidic acid (PA)
CC {ECO:0000269|PubMed:25014274};
CC Vmax=3.25 umol/min/mg enzyme toward phosphatidylglycerol (PG)
CC {ECO:0000269|PubMed:25014274};
CC Vmax=1.65 umol/min/mg enzyme toward phosphatidycholine (PC)
CC {ECO:0000269|PubMed:25014274};
CC Vmax=1.05 umol/min/mg enzyme toward phosphatidylserine (PS)
CC {ECO:0000269|PubMed:25014274};
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:10515935,
CC ECO:0000269|PubMed:25014274}. Membrane {ECO:0000255}; Single-pass
CC membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is up-regulated by the transcription factor RPN4.
CC {ECO:0000269|PubMed:19073890}.
CC -!- DISRUPTION PHENOTYPE: Leads to an altered morphology of lipid droplets
CC with a smaller size. {ECO:0000269|PubMed:25014274}.
CC -!- MISCELLANEOUS: Present with 1210 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the putative lipase ROG1 family. {ECO:0000305}.
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DR EMBL; Z70678; CAA94544.1; -; Genomic_DNA.
DR EMBL; Z74967; CAA99252.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10838.1; -; Genomic_DNA.
DR PIR; S66942; S66942.
DR RefSeq; NP_014702.1; NM_001183478.1.
DR AlphaFoldDB; Q08448; -.
DR BioGRID; 34458; 74.
DR DIP; DIP-4169N; -.
DR IntAct; Q08448; 6.
DR STRING; 4932.YOR059C; -.
DR SwissLipids; SLP:000001976; -.
DR ESTHER; yeast-yo059; Duf_676.
DR MaxQB; Q08448; -.
DR PaxDb; Q08448; -.
DR PRIDE; Q08448; -.
DR EnsemblFungi; YOR059C_mRNA; YOR059C; YOR059C.
DR GeneID; 854225; -.
DR KEGG; sce:YOR059C; -.
DR SGD; S000005585; LPL1.
DR VEuPathDB; FungiDB:YOR059C; -.
DR eggNOG; KOG4372; Eukaryota.
DR HOGENOM; CLU_027968_2_0_1; -.
DR InParanoid; Q08448; -.
DR OMA; SGREMFI; -.
DR BioCyc; YEAST:G3O-33599-MON; -.
DR PRO; PR:Q08448; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08448; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0004622; F:lysophospholipase activity; IDA:SGD.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR GO; GO:0044255; P:cellular lipid metabolic process; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0055088; P:lipid homeostasis; IMP:SGD.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR007751; DUF676_lipase-like.
DR InterPro; IPR044294; Lipase-like.
DR PANTHER; PTHR12482; PTHR12482; 2.
DR Pfam; PF05057; DUF676; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Lipid degradation; Lipid droplet; Lipid metabolism; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..450
FT /note="Lipid droplet phospholipase 1"
FT /id="PRO_0000237649"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 88..92
FT /note="Lipase-specific GXSXG motif"
FT /evidence="ECO:0000269|PubMed:25014274"
FT ACT_SITE 90
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT MUTAGEN 88
FT /note="G->A: Completely abolishes the phospholipase
FT activity; when associated with A-90 and A-92."
FT /evidence="ECO:0000269|PubMed:25014274"
FT MUTAGEN 90
FT /note="S->A: Partially abolishes the phospholipase activity
FT towards PS and PA. Completely abolishes the phospholipase
FT activity; when associated with A-88 and A-92."
FT /evidence="ECO:0000269|PubMed:25014274"
FT MUTAGEN 92
FT /note="G->A: Completely abolishes the phospholipase
FT activity; when associated with A-88 and A-90."
FT /evidence="ECO:0000269|PubMed:25014274"
SQ SEQUENCE 450 AA; 51106 MW; E04CCDA6FCE96AAD CRC64;
MTSDKHLFVL IHGLWGNYTH MESMRTILST TLKKEDVNDD MIYFLPKQNA MFKTFDGIEI
IGYRTLIEVC EFIRDYKDGK ITKLSVMGYS QGGLVARFMI GKMLTEFKEL FEDIEPQLFI
TMATPHLGVE FYNPTGIAYK SALYSALRTL GSTILGKSGR EMFIANSSNN ILVKLSQGEY
LEALSLFKWR IAFANVKNDR TVAFYTAFIT DCDPFIDFDN KLKYTFEEKI PGSGYKGILP
KIVDLNALNV NSHAPTKPTK TYKKWGRTIL IILVATFLIL PIALVMNGLG TAYSYIVTCK
YRKMLSNGIL HNEVRGKLGL TEQLKGYVTD AYGSIINSAL DMDANYEASN SNLVNEEELP
WKEFIQKYTT INDGVWKSKF KKLPFDENRK VILRNLNKLK WIRVPIYIKA VNAHGVIVAR
RGMDENTAAT GIACIEFTAQ LLAYLMHKSN
