ID   NTE1_PICGU              Reviewed;        1438 AA.
AC   A5DHA3;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   03-AUG-2022, entry version 75.
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; ORFNames=PGUG_02654;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; CH408157; EDK38556.2; -; Genomic_DNA.
DR   RefSeq; XP_001484925.1; XM_001484875.1.
DR   AlphaFoldDB; A5DHA3; -.
DR   SMR; A5DHA3; -.
DR   STRING; 4929.XP_001484925.1; -.
DR   EnsemblFungi; EDK38556; EDK38556; PGUG_02654.
DR   GeneID; 5127010; -.
DR   KEGG; pgu:PGUG_02654; -.
DR   VEuPathDB; FungiDB:PGUG_02654; -.
DR   eggNOG; KOG2968; Eukaryota.
DR   HOGENOM; CLU_000960_1_1_1; -.
DR   InParanoid; A5DHA3; -.
DR   OMA; FTMNFTT; -.
DR   OrthoDB; 253518at2759; -.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
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; 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; IPR002641; PNPLA_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF01734; Patatin; 1.
DR   SUPFAM; SSF51206; SSF51206; 3.
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..1438
FT                   /note="Lysophospholipase NTE1"
FT                   /id="PRO_0000295328"
FT   TOPO_DOM        1..25
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        47..64
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        86..1438
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          1131..1295
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          432..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1135..1140
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1162..1166
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1282..1284
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1164
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1282
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   BINDING         590..720
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="1"
FT   BINDING         707..856
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="2"
SQ   SEQUENCE   1438 AA;  160000 MW;  4961090B281985BB CRC64;
     MDSDTSSADF HSTETLVSTP KYSYGVLINV ILLVSWTCFR VVNWFLVTLP SILLGMLSKT
     FQITLSLSSI LMFVVAVTAI CFLVVRYKYL TRYSRNSAAK EPAKKSFDID DLSKKKKSSS
     KTSSNYLDQF LSAIQVFGYL EGPVFHELTR NMTTQKVLPN EVLYLDESLG FSIVVEGTMQ
     VYTKVTNLSN SSLNAEDDGL DLRYENDDVL CIGNDKYQLL NEVKSGAPLS SLMSTLDLFT
     SNEVPLSPTK FGSYSLTAVT PLELSPNNTG GNSPPPSLAP EIVARPKGTT STTLAIIPYT
     AFQRLHKKYP KATSHIVTMV LTRLYKVSMN TIYNYLGLSK DILDCERNLN AETNERLPSY
     LSKGIIEKFH KTEESASVEG SPTLPRRSTV NLRALTRQAS SSRYVVLASR SKSTHPGDLL
     SSVPLSRRSD YYETQTIPNE SEDSPTIQRS SLRRRASHST SLRKSNSVLE DIRVRGFSNE
     REETEETSLR TAIVEQIFTH LGISEDDPTV MNINPTSASS SASSSIVGIS KLNYGSLDSI
     NSPRVDPMTS IRSSLASNGN KVYQTINQHT KEADVLQEKP KKVVLPGSRG DDSDFVAVKD
     EFARAIQMKY IQPGKTIIEQ DSFHTGIFYV IDGSLDVIQE SNGKSKKIYT VKAGGITGYL
     NCLIGMKSLV SVKASEDSSA IVAHIPSHMY SKLIDKFYFL QLPIARRLKR LLSKQFLTID
     YALEWCHISA GDILSKEGEP ANGFHIVLSG RFRVVKFKTP FKPVASKAGH DTYDYNDNLI
     DESNKKYTSN DVEILGEYGH GESIGEVEVL TASLRKNTLI AVRDSETARI PRALFELLSL
     QNPSIMVKVS RIVANRLSKK DSEEILDKPL AMTSSDSPYI SSNFKTITIL PTVSQLPVRE
     FADKLVQALK AIGRNVIALD QASTLTHLGK HAFDERLAEL KLSGYFAYLE EKYETIVYVC
     DTPVKSNWTS TCISQGDCIL LLADADDEDT AESIGSYERL LIKLKTTART DLCLIHPEKY
     VTPGSTSIWL KNRVWVQGHH HIQMEISPTQ TTSVMKPKIP IISELAKKIK DRANPNIKLK
     LEEVKGKALA SFVKLNNKIN AHGRMSFNGV SVHKNDFLRL ARILSNEAVG LVLGGGGSRG
     ISHVGVVIAL EKHGIPIDLV GGTSIGSFVG GLYAMDYNTV SIYGRAKKFA KRVSSFWRIL
     TDLTYPVTSY MTGYEFNRGI WKIFGFTEIE DFWLRYFCNS TNITNSTMDI HETGYSWRFI
     RASMSLAGLL PPITYNGSML LDGGYLDNLP VSEMKKKGAK YIIAVDVGSV DDRTPMNYGD
     TLSGFWVLLN RWNPFSKHPD VPNMMDIQLR LAYVASVNAL EISKKTPGVM YLRPPIENYA
     TLDFAKYDEI YRVGYVYADE LFTSWKSSGK LPDIAGMGDK VRKDMSGEHV SLSRRNSI