ID   NTE1_CRYNB              Reviewed;        1621 AA.
AC   P0CP37; Q55U92; Q5KI53;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 49.
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=CNBD2140;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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; AAEY01000019; EAL21520.1; -; Genomic_DNA.
DR   RefSeq; XP_776167.1; XM_771074.1.
DR   AlphaFoldDB; P0CP37; -.
DR   SMR; P0CP37; -.
DR   PRIDE; P0CP37; -.
DR   EnsemblFungi; AAW42828; AAW42828; CND04180.
DR   EnsemblFungi; EAL21520; EAL21520; CNBD2140.
DR   GeneID; 4935603; -.
DR   KEGG; cnb:CNBD2140; -.
DR   VEuPathDB; FungiDB:CNBD2140; -.
DR   HOGENOM; CLU_000960_1_1_1; -.
DR   Proteomes; UP000001435; Chromosome 4.
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:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR   CDD; cd00038; CAP_ED; 2.
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; IPR001423; LysoPLipase_patatin_CS.
DR   InterPro; IPR002641; PNPLA_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Pfam; PF00027; cNMP_binding; 1.
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; Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN           1..1621
FT                   /note="Lysophospholipase NTE1"
FT                   /id="PRO_0000410176"
FT   TOPO_DOM        1..12
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        34..59
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        81..1621
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          1316..1480
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          188..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          648..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          711..735
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          772..791
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          839..870
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1320..1325
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1347..1351
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1467..1469
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        304..326
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..375
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        545..560
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        772..786
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1349
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1467
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   BINDING         788..907
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="1"
FT   BINDING         951..1070
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="2"
SQ   SEQUENCE   1621 AA;  178011 MW;  0F00F6E602754505 CRC64;
     MSSIPTPPDA NGNPLIALAV AVIYAILYVL QGVKYGVSLL TIGIPSCIVR MLQYSLTISL
     GFPHLLALFA GALLALFFLI RYRYLTRYAQ LKESALPPPS PPALASRLLP LDGDGLGLPD
     SRSQTSSFHN YLDDFLSAIR IFGYLEKPVF HELSRHLQTR RLAAGDTLEI GGGEFWCVVE
     GKVQVFAPDA SSQGTPTPSS DTNSPTRPSF NGYHLLNEVS TGGTLSSLFS ILSLFTEDIK
     LSWKSSADDE GEEEQIFEGA PEQSSAKLRV RRANSDVSQL GPDSIGVRAM DPTPLPESID
     SHGDSSVPQR RRERSSSIDA AGETVREREG IFASASLPIS STEPPSPRRS QSLRSSPRLN
     SATNLLSSQS EHLRSSVPRK AGIEIGSKAL KGTIARATED TTLAVIPAAA FRKLTRKFPK
     ASGTIVQVVL ERFSRVTFMT AHKYLGLTRE ILQTESSLNL LVTHPLPRSF YTGGGMQALR
     ARFQPEALAK ESVHYDSLKS SPNARVSSKD YFNYVPASPT VKAPSLPAMT PKPLSPIIHK
     SSLGQTATTT VKNEPLNGGS SPLDETRDKV PSFGLSTAAA TNPDASFRHA SPFIRRTSAM
     RQQVAAGDLA MSVHNLPDES GQAYYRPTAI TPGLSKMDTW QRRYSSSWNL NDSPHTDGQP
     VDPQRDDESL LNESFDLKEA VLNSIAKSIG LYQEAESNSD MIARSSMAPS VSALSTPNSP
     MFPPNAGTPL QGSTRSRPPH FGNVLDLINA SSQNEGVIGG MLREAAFNSR PDDEASSISM
     SLHDSQGGAS GVDRKIMKDL ERHVEILFFK KGSVLVKEGE RSPGMYYVID GFLETSLPFR
     STSSNQENPN STPGSKHRQS SFGSSNERPF KTALGLDTSK GKELDDGSKK DEALFTVKPG
     GIAGYLSSLC CTDSYVDITA KTDCFVGFLP HHTLERIIER RPIVLLTLAK RLLSLLSPLV
     LHIDAALDWQ QLNAGQVLYE KGDKSTDFYI VINGRLRAFT EKNDNMHVLR EYGQNDSIGE
     LDVITAVDRS ETVHAIRDSE LVRIPAALFD AISIKHPETT VQFMRLIAGR VRRALGDEMN
     GRVPGLPTTD MNLKTVCVLG STRNVPVTQF AGKLKNALEE IGASTSYLDQ GIVMRHLGRH
     AFARIGKLKV AGWLADQEQH YRTVLYVADS PPASQWTLTC IRQADLVLVV SMGDDPSLGE
     YEKLLLATKT TARKELILLH DERTVAPGST RQWLSNRPWI QTHYHVELPG VVTPARPIPP
     VHDAAAIAAF KHLREQVETR IKKYRGLRPF TRPRRPPHMN DFARIARRLC GQQIGLVLGG
     GGARGISHIG MLQALEEFGI PIDAIGGCSI GSFVGGLYAR ETDLLETAGR TKQFSGRMGS
     MWRILSDVTY PFVSYTTGHE FNRGIYKAFY NTHIEDFWIP FFANSTNITH SRMEVHRTGY
     AWRYVRASMT LAGLLPPLSD NGNLLVDGGY MDNTPIQPLR ENGIRDIIVV DVGSVDDTSP
     RDYGDSVSGW WIFFNRFNPF YERRVLSMTE ISSRLTYVSS VKTLEGVKAT PGCHYIAMPV
     QQFDTLGGFK RFSEVMEIGL KAGRETLKKW KEEGKLPTGL VDEAKGSKAV QRGNRLRRMS
     I