ID   NTE1_YARLI              Reviewed;        1427 AA.
AC   Q6CF18;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=YALI0B11044g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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; CR382128; CAG82990.1; -; Genomic_DNA.
DR   RefSeq; XP_500744.1; XM_500744.1.
DR   AlphaFoldDB; Q6CF18; -.
DR   SMR; Q6CF18; -.
DR   STRING; 4952.CAG82990; -.
DR   EnsemblFungi; CAG82990; CAG82990; YALI0_B11044g.
DR   GeneID; 2906874; -.
DR   KEGG; yli:YALI0B11044g; -.
DR   VEuPathDB; FungiDB:YALI0_B11044g; -.
DR   HOGENOM; CLU_000960_1_1_1; -.
DR   InParanoid; Q6CF18; -.
DR   OMA; FTMNFTT; -.
DR   Proteomes; UP000001300; Chromosome B.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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:0004622; F:lysophospholipase activity; IBA:GO_Central.
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   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; 2.
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   3: Inferred from homology;
KW   Endoplasmic reticulum; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Membrane; Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN           1..1427
FT                   /note="Lysophospholipase NTE1"
FT                   /id="PRO_0000295332"
FT   TOPO_DOM        1..60
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        82..96
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        118..1427
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          1124..1288
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          281..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          787..807
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1128..1133
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1155..1159
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1275..1277
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        281..301
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1157
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1275
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   BINDING         615..735
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="1"
FT   BINDING         731..870
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="2"
SQ   SEQUENCE   1427 AA;  158153 MW;  7A0F25C6577907B7 CRC64;
     MDSLHVSSTS VLVDVVEAVE TATSLVVDTA EAVATEQATP TAVISNALAR SAYAAHTSLS
     YLAWAFGLWF LRLIGWVCYG IPTYVLGLLG RTINISLQFS SLLLILIALV TVVVAVVRYK
     YLTVYSRLPQ EQPRQEPEID MYDESDNEDE KTGFANYFDE FLSAVKIFGY LERPVFHELT
     RHMQTWKLSA DEMVPLDDEQ GFSVVVEGTV QVFAKQSSFV QNPTSVPDSR KEDSIMFNGE
     RYTLLSEIKN GAPLTSLFNI LSLFTDDLQL HKNFDSAVNS PMTSASDVPN MSLSSDGSDD
     LQKGEPQFGE PRLSEKPAAK LSVTVRAATD STIAIIPAAA FRRITKKFPQ ATAHIVQVIL
     TRFQRVTFQT GHHYFGLTPE IFQTEVNLNS HARNELPGYL REGAVKKLNQ VYDASQMGGR
     PKKYTVTLNK KNKGKGSRRQ RFSVQLNNQG HLNSQSRMVS LDSLEAVGDH MNPGDLLTNV
     PLSRQGRPVF ELSSVKHKAS IQNLSFSGND DENEDTALRT ALVEAIFKVL GIDRDSIQSS
     IMAVKTMSNT ASPMFTGATT GGSSGSLGEE LRSRRTGQDS LGASHFGVGL PSERSQNSFY
     ARSETSTSSV DEDSLMAAPF DTIRNDVAQY MDVVLFKKDS LLIKQDDPTP GLYYLIDGVL
     EVGYTDHHKI YHDLYTVQPG GVGGYIGSIL GHRSFADLRA RTDVYAGFLP RAAIERMSDK
     YPMVHLTMAK SLTKVLSRLL LHLDFAMEWV QVRAGQKIYK EGQEADAIYI VLNGRVRSVA
     ETKGDSGIVG GESGDAKDGK SHRKNLTSIG EYGKGESVGE LEVLTLTRRP STLVAIRDAE
     LAKIPRALFE SLALHYPSIT FEISRIVASR VRTLMEDSAP IPRRMHTFDM AAHHDSYLTI
     AVVPISQDVD VSEFGRRLYN GMQAVGREAC HLNHASVLNH MGRHAFNPLG KLKLSGFLDD
     IEDRYQTVLY VADTPPGSSW THTCISQADC VLLVADARSE PDIGEYERVL VKMRTTARTE
     MVLIHPERYV PPGLTSAWLK PRVWVHTHHH VQMDLPRHEA DVLASIRKMK RTGTLANLKN
     KVQTIQEEFR SMYRPKANIY STSSANKDDF NRLARILSGQ AIGLVLGGGG ARGISHIGII
     KALEDSGIPI DFVGGTSIGS FIGGLYAKEY DLVPIYGRAK KFSGRVSSLW RMALDLTYPA
     TSYTTGHEFN RGIWKAFGDS RIEDFWLRYF TNTTNITHSR MEIHTSGYAW RYIRASMSLA
     GLLPPLTDNG SMLLDGGYVD NLPVSEMKAQ GASVVFAVDV GSIDDTTPMN YGDSLSGAWV
     MWNRWNPFGR HPNVPNLAEI QARLAYVSSV GALEKAKHTP GVIYMRPPID DFATLDFAKF
     LDIYRVGNKY GHKFLTELRE DGKFPAIPGM ENVKTKHKRT IARRNSI