NTE1_YEAST
ID NTE1_YEAST Reviewed; 1679 AA.
AC Q04958; D6VZB4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Lysophospholipase NTE1;
DE EC=3.1.1.5 {ECO:0000269|PubMed:15044461};
DE AltName: Full=Intracellular phospholipase B;
DE AltName: Full=Neuropathy target esterase homolog;
GN Name=NTE1; OrderedLocusNames=YML059C; ORFNames=YM9958.03C;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 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 [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ACTIVITY REGULATION,
RP AND MUTAGENESIS OF SER-1406.
RX PubMed=15044461; DOI=10.1074/jbc.m400830200;
RA Zaccheo O., Dinsdale D., Meacock P.A., Glynn P.;
RT "Neuropathy target esterase and its yeast homologue degrade
RT phosphatidylcholine to glycerophosphocholine in living cells.";
RL J. Biol. Chem. 279:24024-24033(2004).
RN [6]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=15611060; DOI=10.1074/jbc.m413999200;
RA Fernandez-Murray J.P., McMaster C.R.;
RT "Nte1p-mediated deacylation of phosphatidylcholine functionally interacts
RT with Sec14p.";
RL J. Biol. Chem. 280:8544-8552(2005).
RN [7]
RP FUNCTION.
RX PubMed=16777854; DOI=10.1074/jbc.m603548200;
RA Gaspar M.L., Aregullin M.A., Jesch S.A., Henry S.A.;
RT "Inositol induces a profound alteration in the pattern and rate of
RT synthesis and turnover of membrane lipids in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 281:22773-22785(2006).
RN [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634 AND THR-803, AND
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.
RX PubMed=19841481; DOI=10.1074/jbc.m109.063958;
RA Fernandez-Murray J.P., Gaspard G.J., Jesch S.A., McMaster C.R.;
RT "NTE1-encoded phosphatidylcholine phospholipase B regulates transcription
RT of phospholipid biosynthetic genes.";
RL J. Biol. Chem. 284:36034-36046(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300; SER-312; SER-632;
RP SER-634; SER-653; SER-661; SER-670; SER-680 AND SER-739, AND IDENTIFICATION
RP 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 [13]
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).
CC -!- FUNCTION: Intracellular phospholipase B that catalyzes the double
CC deacylation of phosphatidylcholine (PC) to glycerophosphocholine
CC (GroPCho). Plays an important role in membrane lipid homeostasis.
CC Responsible for the rapid PC turnover in response to inositol, elevated
CC temperatures, or when choline is present in the growth medium
CC (PubMed:15044461, PubMed:15611060, PubMed:16777854). NTE1 activity
CC impacts the repressing transcriptional activity of OPI1, the main
CC regulator of phospholipid synthesis gene transcription
CC (PubMed:19841481). {ECO:0000269|PubMed:15044461,
CC ECO:0000269|PubMed:15611060, ECO:0000269|PubMed:16777854,
CC ECO:0000269|PubMed:19841481}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC Evidence={ECO:0000269|PubMed:15044461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC Evidence={ECO:0000305|PubMed:15044461};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + 2 H2O = 2 a
CC carboxylate + 2 H(+) + sn-glycerol 3-phosphocholine;
CC Xref=Rhea:RHEA:32907, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:29067, ChEBI:CHEBI:57643;
CC Evidence={ECO:0000269|PubMed:15044461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32908;
CC Evidence={ECO:0000305|PubMed:15044461};
CC -!- ACTIVITY REGULATION: Positively regulated by SEC14. Inhibited by
CC organophosphorus esters in the order phenyl saligenin phosphate (PSP) >
CC phenyldipentyl phosphinate (PDPP) = diisopropyl fluorophosphate (DFP) >
CC and paraoxon (PXN). {ECO:0000269|PubMed:15044461,
CC ECO:0000269|PubMed:15611060}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15044461}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15044461}. Lipid droplet
CC {ECO:0000269|PubMed:24868093}.
CC -!- MISCELLANEOUS: Present with 521 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NTE family. {ECO:0000305}.
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DR EMBL; Z46729; CAA86716.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09838.1; -; Genomic_DNA.
DR PIR; S49802; S49802.
DR RefSeq; NP_013652.1; NM_001182418.1.
DR AlphaFoldDB; Q04958; -.
DR SMR; Q04958; -.
DR BioGRID; 35107; 86.
DR DIP; DIP-5949N; -.
DR IntAct; Q04958; 16.
DR MINT; Q04958; -.
DR STRING; 4932.YML059C; -.
DR SwissLipids; SLP:000000073; -.
DR iPTMnet; Q04958; -.
DR MaxQB; Q04958; -.
DR PaxDb; Q04958; -.
DR PRIDE; Q04958; -.
DR TopDownProteomics; Q04958; -.
DR EnsemblFungi; YML059C_mRNA; YML059C; YML059C.
DR GeneID; 854943; -.
DR KEGG; sce:YML059C; -.
DR SGD; S000004524; NTE1.
DR VEuPathDB; FungiDB:YML059C; -.
DR eggNOG; KOG2968; Eukaryota.
DR GeneTree; ENSGT00940000168388; -.
DR HOGENOM; CLU_000960_1_1_1; -.
DR InParanoid; Q04958; -.
DR OMA; FTMNFTT; -.
DR BioCyc; MetaCyc:G3O-32654-MON; -.
DR BioCyc; YEAST:G3O-32654-MON; -.
DR Reactome; R-SCE-6814848; Glycerophospholipid catabolism.
DR PRO; PR:Q04958; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04958; protein.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0004622; F:lysophospholipase activity; IDA:SGD.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; IMP:SGD.
DR GO; GO:0071071; P:regulation of phospholipid biosynthetic process; IMP:SGD.
DR CDD; cd00038; CAP_ED; 2.
DR Gene3D; 2.60.120.10; -; 3.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR001423; LysoPLipase_patatin_CS.
DR InterPro; IPR002641; PNPLA_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF01734; Patatin; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; SSF51206; 3.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
DR PROSITE; PS51635; PNPLA; 1.
DR PROSITE; PS01237; UPF0028; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Hydrolase; Lipid degradation; Lipid droplet;
KW Lipid metabolism; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1679
FT /note="Lysophospholipase NTE1"
FT /id="PRO_0000172528"
FT TOPO_DOM 1..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..103
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..1679
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT DOMAIN 1373..1537
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1377..1382
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1404..1408
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1524..1526
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 261..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..295
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1406
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1524
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT BINDING 803..947
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="1"
FT BINDING 943..1074
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="2"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 739
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 803
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 1406
FT /note="S->A: Loss of esterase activity."
FT /evidence="ECO:0000269|PubMed:15044461"
SQ SEQUENCE 1679 AA; 187133 MW; 550FFCD4ACAF8E25 CRC64;
MRSMNCTTNN TNNTGQNTKN SLGSSFNSSN YTSYRFQTCL TDQIISEAQT WSLSSLFNFS
WVVSYFVMGA SRMIFRYGWY LATLSLLRIP KWIFFKLHHV QFTLSFWLIL FALAVIVFVT
YTIMKERILS QYKRLTPEFL PLENTGKSGS SANINAASTQ SANAPPAIGS STTGASSIID
SKKHSLKDGN ENETFLSSYL DQFLSAIKIF GYLEKPVFHD LTKNMKTQKM DEGEILLLDS
TIGFAIVVEG TLQLYHEVDH SDKDHGDETD HSDTDGLDDQ DRDEEDEEED DDIDNYDTKS
CSSNLIDEED ESVGYIHLKN GLGNFQLLNT VKPGNPLTSL VSILNLFTHS MSSYGNSNFP
SELSSPIDTT VSVNNMFCSS EQNFSNTDSM TNSTNSFPTF PSSMPKLVAR AATDCTIGII
PPQSFAKLTA KYPRSASHII QMVLTKLYHV TFQTAHDYLG LTKEIMDIEV LLNKSIVYEL
PYYLKEAVIR KFKTVDKSSG SADLEPKPKN SNASSKLKKP PKAKPSDGII QSLKIANANA
NTSSNSLSLK PEFTHHPSSR HVVLGSRDQF NPGDLLSNVP LSRTMDILSP NPIHNNNRNK
SNGINTSTSN QHKRSSRSSS NNASVHSKKF SSLSPELRNA QLSTSPLSLD NTSVHDHIHP
SPVHLKGRVS PRPNLLPTTS FSAAQEETED SALRMALVEA MLTYLGVNKS NMSVSSSSIA
NMSSLNSPQL NEMYSRRPSN ASFLMSPHCT PSDISVASSF ASPQTQPTML RILPKEYTIS
NKRHNKSKSQ DKKKPRAYKE ELTPNLDFED VKKDFAQGIQ LKFFKKGTTI VEQNARGKGL
FYIISGKVNV TTNSSSSVVS SMSKPEQVSA QSSHKGENPH HTQHLLYSVG SGGIVGYLSS
LIGYKSFVNI VAKSDVYVGF LSSATLERLF DKYFLIYLRI SDSLTKLLSS RLLKLDHALE
WVHLRASETL FSQGDSANGI YVVLNGRLRQ LQQQSLSNSN TSSEEVETQN IILGELAQGE
SFGEVEVLTA MNRYSTIVAV RDSELARIPR TLFELLALEH PSIMIRVSRL VAKKIVGDRT
VPALTGDPLS IKENDFTSLI PPTKASYSSS LSHKPQNITS GTITFRTITI LPITSGLPVE
AFAMKLVQAF KQVGRTTIGL NQRTTLTHLG RHAFDRLSKL KQSGYFAELE EMYQTVVYIS
DTPVKSNWTR TCIAQGDCIL LLADARSPSA EIGEYEKLLL NSKTTARTEL ILLHPERYVE
PGLTHKWLRY RPWVHSHHHI QFSLTGTTLM NEGKMHVLNN GALALMDKLI QTEFSRKTQQ
NISKLLPDSI KNTVENFSSR FMKSKRQYYT PVHRHKNDFL RLARILSGQA IGLVLGGGGA
RGISHLGVIQ AIEEQGIPVD VIGGTSIGSF VGGLYAKDYD LVPIYGRVKK FAGRISSIWR
MLTDLTWPVT SYTTGHEFNR GIWKTFGDTR IEDFWIQYYC NSTNITDSVQ EIHSFGYAWR
YIRASMSLAG LLPPLEENGS MLLDGGYVDN LPVTEMRARG CQTIFAVDVG SADDRTPMEY
GDSLNGFWII FNRWNPFSSH PNIPNMAEIQ VRLGYVASVN ALEKAKNTPG VVYVRPPIEE
YATLDFSKFE EIYHVGVDYG RIFLQGLIDD DKMPYIPGSQ ETTLNSQVPE FLLHRRNSI
