ID   NTE1_KLULA              Reviewed;        1441 AA.
AC   Q6CWC2;
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=KLLA0B05225g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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:0000305};
CC       Single-pass type I membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the NTE family. {ECO:0000305}.
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DR   EMBL; CR382122; CAH02160.1; -; Genomic_DNA.
DR   RefSeq; XP_451767.1; XM_451767.1.
DR   AlphaFoldDB; Q6CWC2; -.
DR   SMR; Q6CWC2; -.
DR   STRING; 28985.XP_451767.1; -.
DR   EnsemblFungi; CAH02160; CAH02160; KLLA0_B05225g.
DR   GeneID; 2896879; -.
DR   KEGG; kla:KLLA0_B05225g; -.
DR   eggNOG; KOG2968; Eukaryota.
DR   HOGENOM; CLU_000960_1_1_1; -.
DR   InParanoid; Q6CWC2; -.
DR   OMA; FTMNFTT; -.
DR   Proteomes; UP000000598; Chromosome B.
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; 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   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   3: Inferred from homology;
KW   Endoplasmic reticulum; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Membrane; Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN           1..1441
FT                   /note="Lysophospholipase NTE1"
FT                   /id="PRO_0000295322"
FT   TOPO_DOM        1..22
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        44..1441
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          1137..1301
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          154..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          376..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          551..585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1141..1146
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1168..1172
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1288..1290
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        396..419
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..445
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..573
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1170
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1288
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   BINDING         592..718
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="1"
FT   BINDING         707..836
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="2"
SQ   SEQUENCE   1441 AA;  162157 MW;  B882F8E0F9533C00 CRC64;
     MWLTSYVLPR LKNILLLQFH ITLPLNYLVL LLLSTVIITY LFLRTRILSN YSQLKDDVSD
     ENNINRKDYM DASSASFLLN REKHKGFTSY LDEFLSAIKI FGYLEKPVFH ELTKSMKTEK
     LQEGEIVLLD DSVGFTIVVE GTLEILHKMD NRHSNPSGDA AANATAFEPP SNDDGYLING
     EKFQLLNIVK TGNPLSSLVS IMKLFSNRST HLNEGTHPST TNNTPGPGSP NLTGEINSFL
     DSTLPAKFGS ADSANGNHPI SPMELESTFD NLSEASENDR SAKIPDIIAR AASDCTIAII
     PSSSFQRLLV KYPRSASHII QMILTKLYRV TFKTAHTYLG LTNEIIFTEF QSINKDNLKL
     PEYFRRSIIS YFTNRQDDTG SSASTIQKRP QLHRRDSNNS LNYGSRHVVL NSRDQYNPGD
     LLSNVPLPRL NPQQRNDLSN TNSSSTLSRA DYRPIILNNF SSSQFEETEV SSWRLALVEI
     IFQQLGITKD TIEPPISDDF SLHDHSLDEK GLVRRSSYSS FTSLSSSIAT HSSNHLVTFL
     PRESQQFSRL NRTGGKMASH SKRLNGSSRS NSRTDRSESF DHFRNENLGG DNQFSDFESV
     KEDFSKCIKI LKFEEGETIL CQNSNPQGIY YLVSGEVDVI SETKDGNTDE SYERTLYTAT
     EGYILGYLSS ILGCKSLVTL KVSKGPAYLG LIPYNDLERL CDKYFMIYLK LSEILTNSLS
     PNLLRLDYFL EWIQLDSSET LFNQGDPANG VYLVLNGRLR QLFYEDADSD IVTQMAELSK
     GESFGEVEVL TAIHRLNTVV AIRDTELARI PRTLFEFLAV EHPSIMIHVS RMVAKKAMLM
     NFKSGIGFSG SQPITKLIGD ETAMQKRYDF NLNIKSNKSS KKNELISNTV NYKTLTLLPI
     TEGLPVEEFA YKLINALRQC GKTTIGLNQR TTLSHLGRHA FNKLSKLKQS GYFAELEELY
     EIVVYIADTP VSSSWTQTCI SQGDCILLLA DATCDPKIGE FERLLLKSKT TARTDLILLH
     PERYVVPGST SKWLKNRMWI QSHHHIQFTP MEKVAEPDPI PNIKPLSQLV EKFKENTKKT
     QENFVKFLPD SIKTTVETLS GKYIDPKPNP KFYTSVDPIK NDFLRLARTL SGQAVGLVLG
     GGGARGLSHL GIIKALEEQG IPIDIIGGTS IGSFVGGLYA MDYDLVPIYG RVKKFAGRVG
     SLWRMLSDLT WPVTSYTTGH EFNRGIWKSF RDYRIEDFWI SYYCNSTNIT ESVQEIHSSG
     FAWRYIRASM SLAGLLPPIV DNGNMLLDGG YVDNLPVTEM TQRGCKIVFA VDVGSVDDRT
     PMSYGDSLNG FWIVLNRWNP FSKHPNIPNM AEIQMRLGYV ASVNALERAK STPGVVYIRP
     PIENYATLDF GKFEEIYQVG YAYGHDFLQH LQEKNELPPI AGTTTSAYAD KENMLQRRNS
     I