ID   NTE1_CANGA              Reviewed;        1728 AA.
AC   Q6FKJ1;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   RecName: Full=Lysophospholipase NTE1;
DE            EC=3.1.1.5;
DE   AltName: Full=Intracellular phospholipase B;
DE   AltName: Full=Neuropathy target esterase homolog;
GN   Name=NTE1; OrderedLocusNames=CAGL0L11154g;
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS
RC   138;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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 (By
CC       similarity). {ECO:0000250}.
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   -!- ACTIVITY REGULATION: Inhibited by organophosphorus esters.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NTE family. {ECO:0000305}.
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DR   EMBL; CR380958; CAG62227.1; -; Genomic_DNA.
DR   RefSeq; XP_449253.1; XM_449253.1.
DR   AlphaFoldDB; Q6FKJ1; -.
DR   SMR; Q6FKJ1; -.
DR   STRING; 284593.Q6FKJ1; -.
DR   EnsemblFungi; CAGL0L11154g-T; CAGL0L11154g-T-p1; CAGL0L11154g.
DR   GeneID; 2891028; -.
DR   KEGG; cgr:CAGL0L11154g; -.
DR   CGD; CAL0135996; CAGL0L11154g.
DR   VEuPathDB; FungiDB:CAGL0L11154g; -.
DR   eggNOG; KOG2968; Eukaryota.
DR   HOGENOM; CLU_000960_1_1_1; -.
DR   InParanoid; Q6FKJ1; -.
DR   OMA; SSGYVWR; -.
DR   Proteomes; UP000002428; Chromosome L.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0034638; P:phosphatidylcholine catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0071071; P:regulation of phospholipid biosynthetic process; IEA:EnsemblFungi.
DR   CDD; cd00038; CAP_ED; 2.
DR   CDD; cd07227; Pat_Fungal_NTE1; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR001423; LysoPLipase_patatin_CS.
DR   InterPro; IPR002641; PNPLA_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR14226:SF29; NEUROPATHY TARGET ESTERASE SWS; 1.
DR   PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF01734; Patatin; 1.
DR   SMART; SM00100; cNMP; 2.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 4.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
DR   PROSITE; PS51635; PNPLA; 1.
DR   PROSITE; PS01237; UPF0028; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Membrane; Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN           1..1728
FT                   /note="Lysophospholipase NTE1"
FT                   /id="PRO_0000295315"
FT   TOPO_DOM        1..44
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        66..97
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        119..1728
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          1422..1586
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          141..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          285..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          454..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          596..660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          687..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1034..1055
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1426..1431
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1453..1457
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1573..1575
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        149..166
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..308
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..343
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..363
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        598..634
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        687..714
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        727..756
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1455
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1573
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   BINDING         854..987
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="1"
FT   BINDING         983..1121
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="2"
SQ   SEQUENCE   1728 AA;  193367 MW;  88C134F24072720A CRC64;
     MDSSSIAHES DIVSTERNIL PERFISNKQQ GNYLEDGSGD GNGKAAEHWL LAAIFNFFWV
     ISYFISGSTH IAFRSSWYIV SLLLLKFPKW IIVEANHIHL TIPFSVLVVT LAIIFYVSYE
     FLKGRLLSEY KNLTSDLNTD SLNSKNSKSS RLLHHDSKDS NTTRRRRYSS GKLLSSALHE
     SHSGINGGDD GDDTFLSSYL DQFLSAIRIF GYLEKPVFHD LTKNMKTQKL DEGEILLLDN
     SVGFAIVVEG TLDIYHEVEE KGNMNDIDGD FMVDDNQSIY SILKRKKKKY STSRHGQYNN
     NSDPGHYNGH NVNGDDEDDD DGILQMRSSS RNQNIPSFDA IESSSSDEES DINDGDSESQ
     SESDDESTGF IRLKDGLGKF QLLNTVKAGN PVSSLVNILN LFTSANDNVT SPSRTGRMDS
     NYTNPVERPT SKLSTSIEES AMRLELGKYS LSPTEASYRS TSNPSNNFSK DNDPLSKSIS
     GPDAVTTPSL PPLNNRAFVI PKVVARAATD CTIAIIPPQA FAKLKAKYPR SASHIIQMIL
     TKLYHVTFQT AHKYLGLTQE IAYTELLLNR TVSYDLPNYL KEIVIDRFKD KGKDMNLQKG
     FQSPTSSRLT SNFNGNSNNQ RTNSRNSQAL MSTRDLRKTR PELSQQSSMI HSPTPITGSR
     HVVLESRDKY NPGDLLSNVP LSRINLASPS SRGFDYSSMK KESSPQSSVN SRKRSTTGER
     PRLLKRPSIY NNQSSSRSDA LKGNNSNNKD INFTSFSAQE ETEDSVVRMA LVEAMLTYLG
     VNKTNMSILP GIYDGAPSEP HSHRASEISL VSSYTSSAAP QTTIRILPKE YAIVSTRKQK
     QSSKKRRKYK EEISPTLDYE YAKNEFAQAI ELQYFKQGTV IVEQDTRGKG LYYVVSGKID
     VTTSTVSDHE IFNSTRDKKK KKSKTLFTIE SGGIAGYLSS LVSYKSFVTL IAKTDVYVGF
     LPYQTLEKLC DKYFLIYLRI AESLTSLLTP RMLKLDHALE WLHLNASDTL FNQGDPANGI
     YVILNGRLRQ LRNPELEENS TDYPNDGEEK DSSRDSTIVM GELGQGESFG EVEVLTAMDR
     ISSMVAVRDT ELARIPRSLF ELLAIEHPSI MIRVSRLVAK KILGQGQANM ALPKIGSGSN
     LRHDLNLTIP PSSSSSIHTH SYGNDNSNQM NNANFRTITI LPITSGLPVE SFAMKLVHAF
     KQVGRTTIGL NQRTTLSHLG RHAFDKLAKL KESGYFAELE ELYQTVVYIA DTPVKSSWTK
     TCIAQADCVI LLARADDSPE IGEYERLLLK SKTTSRTELV LLHNERSVEP GMTQRWLRSR
     SWVHNHYHIQ FAMDSLVNSS NVKDTGGNIG ALNLVDKFIQ TELGRKTQYN ISKLLPESIK
     MTVENFSSRF MKRKRQYYTP VHRHKDDFLR LARILSGQAI GLVLGGGGAR GLSHLGILQA
     LEERGIPIDM IGGTSIGSFV GGLYAKDYDL VPIFGRIKKF AGRISSIWRM LSDFTWPVTS
     YTTGHEFNRG IWKSFGDTRI EDFWVQYFCN STNITESVQE IHSYGYAWRY VRASMSLAGL
     LPPIEDNGSM LLDGGYVDNL PVLEMKARGC NTIFAVDVGS VDDRTPMKYG DSLNGFWIIL
     NRWNPFSKHP NIPTMAEIQV RLGYVSSVNA LEKAKRTPGV IYVRPPIENY ATLDFGKFEE
     IYKVGADFGK VFLQALAEEG KMPYIPGSNA DLVGDVETGF FLHRRNSI
//