ID   NTE1_DEBHA              Reviewed;        1544 AA.
AC   Q6BQK9;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 94.
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=DEHA2E04400g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382137; CAG87737.2; -; Genomic_DNA.
DR   RefSeq; XP_459511.2; XM_459511.1.
DR   AlphaFoldDB; Q6BQK9; -.
DR   SMR; Q6BQK9; -.
DR   STRING; 4959.XP_459511.2; -.
DR   EnsemblFungi; CAG87737; CAG87737; DEHA2E04400g.
DR   GeneID; 2902795; -.
DR   KEGG; dha:DEHA2E04400g; -.
DR   VEuPathDB; FungiDB:DEHA2E04400g; -.
DR   eggNOG; KOG2968; Eukaryota.
DR   HOGENOM; CLU_000960_1_1_1; -.
DR   InParanoid; Q6BQK9; -.
DR   OMA; FTMNFTT; -.
DR   OrthoDB; 253518at2759; -.
DR   Proteomes; UP000000599; Chromosome E.
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:0046486; P:glycerolipid metabolic process; IEA:UniProt.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00038; CAP_ED; 1.
DR   Gene3D; 2.60.120.10; -; 2.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR002641; PNPLA_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Pfam; PF01734; Patatin; 1.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF51206; SSF51206; 2.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
DR   PROSITE; PS51635; PNPLA; 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..1544
FT                   /note="Lysophospholipase NTE1"
FT                   /id="PRO_0000295319"
FT   TOPO_DOM        1..37
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        59..76
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        98..1544
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          1237..1401
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          265..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          424..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1241..1246
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1268..1272
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1388..1390
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        267..312
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        424..533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..552
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1270
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1388
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   BINDING         681..811
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="1"
FT   BINDING         807..960
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="2"
SQ   SEQUENCE   1544 AA;  173122 MW;  B83771ADE5D86F30 CRC64;
     MSTIEIVSTV AEYTEIHSPV SSKFLLPSAR DSSSSISLFS AIFWFWSWLF FKIMNIFLYY
     IPNIIVNLFS VNFQITLSLS SIVITLTGII SFCFLIVRYK YLTRYSKTTK STDKPKSSNK
     NIDLVGSIKK NKRGDSKSTS NYLDEFLSAI KVFGYLERPV FHELTRNMTT QKLSSEEILY
     LDEKLGFSIV VEGTIQVYTK VNSVNSSTTS NSDDNELNFE KDDLLTIGDQ CYQLLNEVKS
     GSPLSSLMST LDLFKPVDPD TMSNRLFSPF ELDSNPASNP LSPDNTGSKS FDPLSSGNFN
     DTSLSSSDRN YPNIVARPKP IEDSNNLNTA TIAIIPYSAF QKVQSKYPKA TSHIVTMVIT
     RLYKITMNTI HSYLGLTREI IRSEIQLNES EGAKDSLPSY LYDGVIEKFY GDKNNETLLN
     KTAESPSVSI NKTSSSSSSL PKKSTTSLRP LNRNQSSRYV VLDSRSKSTH PGDLLSSVPL
     SRRSDYYQTH TTIQPDPEEV RSQSRTKMTS PVLPKRQISS NGGPTLKGHS SSTTKFENIR
     DRTFSDEREE TEETSLRIAI IENIFKILGI NEVSNMIGSM SDLNSRSSSV NSSVVGLPSL
     MNNGNESKYP NGIFDFNTGK VRYDSISSFP TSLNKGANNN LKFYDTVNQS QLKDMDHEND
     KSSQVDINNL MFKRKSIPIQ SFESNFYDVK NEFSKHLNIK YFGPNTTLVE QESFNSGLYY
     VIDGTLDVFY KPASKESENL TPMNKKKLYT VKSGGLAGYL SSIIGVRSLV SISTPGDKGV
     IVAHIPKNEF SKLLDKFYFL QLPVASKLKS LLSSQILTID YALEWCHIPA GDVLCSQGDL
     ANGFHIVLSG RFRVVRYNNN KSSEVNPDDN TDIHDYNNNL IDESLSYKSR KKKDDITILG
     EYGHGETIGE VEVLTASRRT NSLIAVRDSE TARIPRTLFE MLSLRNPSIM VKVSRIVANK
     MAKKDNIGIP STISSNVPLI VTNTDSHISN DYKTITILPT VSGLPVRDFA DKLVSALKNI
     GRNVIALDQA STLTHLGRHA FDERLAQLKL SGYFAYLEEE YQTIVYVCDT PLKSNWTSTC
     ISQGDCILLL ADADDDDVAT NIGEYERLLM KLKTTARTDL CLIHADKYVE PGSTSVWLKN
     RIWVQGHHHI QMEIARDNSV QQGQKTSIIK NIAAKISSRT NTNIKSRLEN VKTKAILSLN
     KFNNRLSRRT HSYKTVQAHK NDFLRLARIL SNESVGLVLG GGGSRGISHV GVVMALEKHG
     IPIDLIGGTS IGSFVGGLYA KDYNIVSIYG RAKRFAKRVS SWWRMVLDLT YPVTSYITGY
     EFNRGIWKIF GSSEIEDFWI RYFCNSTNIT NSTMDIHESG FSWRFIRASM SLAGLLPPIT
     YGGSMLLDGG YLDNLPVMEM KKKGAKYIIA VDVGSVDDRT PMNYGDTLSG FWVLFNRWNP
     FSRHPNVPNM MDIQLRLAYV ASVNALELAK KTPGVIYLRP PIDDYATLDF AKFDEIYHVG
     MAYADNLLTR WEQTGKIPPI AGMIDRSRIR NGEERKSLYR RSSI