ID   NTE1_LODEL              Reviewed;        1443 AA.
AC   A5E708;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-MAY-2023, entry version 79.
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=LELG_05397;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC   NRRL YB-4239;
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: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; CH981532; EDK47216.1; -; Genomic_DNA.
DR   RefSeq; XP_001523551.1; XM_001523501.1.
DR   AlphaFoldDB; A5E708; -.
DR   SMR; A5E708; -.
DR   STRING; 379508.A5E708; -.
DR   GeneID; 5230489; -.
DR   KEGG; lel:LELG_05397; -.
DR   VEuPathDB; FungiDB:LELG_05397; -.
DR   eggNOG; KOG2968; Eukaryota.
DR   HOGENOM; CLU_000960_1_1_1; -.
DR   InParanoid; A5E708; -.
DR   OMA; SSGYVWR; -.
DR   OrthoDB; 5303733at2759; -.
DR   Proteomes; UP000001996; Unassembled WGS sequence.
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: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; 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; 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; 1.
DR   Pfam; PF01734; Patatin; 1.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 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..1443
FT                   /note="Lysophospholipase NTE1"
FT                   /id="PRO_0000295323"
FT   TOPO_DOM        1..59
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        81..1443
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          1136..1300
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          103..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          199..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1140..1145
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1167..1171
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1287..1289
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        103..119
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..233
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1169
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1287
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   BINDING         619..750
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="1"
FT   BINDING         746..871
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="2"
SQ   SEQUENCE   1443 AA;  161900 MW;  339E4C844D414585 CRC64;
     MEEELAIEDL PRLTGTVSLN NGLLHSIYNE TTVFKILRWS LVEIPKYILK LMSKNLEINL
     NVSSILIITL LIAAGILVIV RYKFLTGYSE DIKKGGSNAN TKALGQQSTN YPKSTSSGLF
     VEKSKDKKPS NYLDEFLMAI KVFGYLDKQV FHELTKSMTT QKLSRDEVMC LDEKIGFLIV
     VEGTAQVYTK VTKKSNRNKY DELGQNGRDE GEEADEDDEE EEKEVGDDGD DEMDVEAMRN
     RGNGTKNGKM HGLDTDNFEE NDDFLKLGEQ NYQLLNEVKS GAALSSLIST LDLFKPLKSE
     STLTPLDSMG SGVSLNLDYL DRAGARLKAL ENDSDADTRD STYPDIIVRP KKKKHSDTIT
     VAIIPQSAFE RVQMKYPKST SHIVTMVLTR LYKVTMTTIH NYLGLTGEIF KLEIELNKSC
     ELGLPRYLVD GLIERLSQGG SNERKQQAKH FRRSPLERTQ SRYVLLNSRV KSNNPGDLLS
     SVPISRDDPK LRVNKSSAPT LVDGSNRINF TDNIEETEEN SLRIAIIENI FKIVGINEAQ
     NLPHEQAPFR SLNSSANSSS IALNSPGYFS PNLPATTGRH HNVLKFSSND SLMNTISLSQ
     LKSQKTHSIS RGSTTQKQLY KRRNPITEMN IKDAFAKVME LKYIEPNTTV VQQNSVFCGL
     YYVINGSLEV HYKQAETYSK SATSKHVYTV GAGGIAGYMS CVVGFRSLVS IKTPKKTGAV
     VAYIAKNDYN QLLDKFYFLQ LPMATKLKSL LSKQVMTIDY ALEWCHIPAG NVLCSQGDLA
     NGFHVVLSGR FRVVRKEKRK GSNRDEVKVL GEYGHGESIG EVEVLTASRR SNSLIAVRDS
     ETARIPRTLF EILSFQNPSI MVKVSRLVAS KVLSSEKTLS QATHSFITSS SNESFISADY
     KTITILPTVS GLPVRDFADK LVHSLKAIGR NVIALDQALT LTHLGRHAFD ESLVRLKLSG
     YFAYLEEEYE TVVYICDTPV QSNWTSTCIS QGDCVLLLAD ADDQYTASSV GEYEQLLIKM
     KTTARTDLCL IHQEKFVVSG STSRWLKNRM WVQGHHHIQM YIERNNETIG PGKKSFINEM
     AAKFVQNKSL ISKFEEARSK ALSWRREEQL KDLTLGSHKS DFLRLARILS NEAVGLVLGG
     GGSRGISHVG VVTALERHGI PVDLIGGTSI GSFVGGLYAK DYNIVSIYGR AKKFSKRVSS
     VWRMIFDLTY PVTSYITGYE FNRGIWKVFG FTEIEDFWIK YFCNSTNITN STMDIHESGY
     AWRFIRASMS LAGLLPPIAF KGCMLLDGGY LDNLPVMEMK RRGAKHIFAV DVGSVDDRTP
     MDYGDTLSGF WVVFNKWNPF SKHPNVPNMM DIQLRLAYVA SVNALEEAKR TPGVYYLRPP
     IDNYATLDFG KFDEIYQVGL GYADKLFTEW ENKKQLPEIA GFVKRDGMQN GGERIKMYRR
     NTM
//