ID NTE1_CRYNJ Reviewed; 1621 AA.
AC P0CP36; Q55U92; Q5KI53;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=CND04180;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW42828.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017344; AAW42828.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_570135.1; XM_570135.1.
DR AlphaFoldDB; P0CP36; -.
DR SMR; P0CP36; -.
DR STRING; 214684.P0CP36; -.
DR PaxDb; 214684-P0CP36; -.
DR EnsemblFungi; AAW42828; AAW42828; CND04180.
DR VEuPathDB; FungiDB:CND04180; -.
DR eggNOG; KOG2968; Eukaryota.
DR InParanoid; P0CP36; -.
DR OrthoDB; 5303733at2759; -.
DR Proteomes; UP000002149; Chromosome 4.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004622; F:lysophospholipase activity; IBA:GO_Central.
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 CDD; cd07227; Pat_Fungal_NTE1; 1.
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; IPR001423; LysoPLipase_patatin_CS.
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; 2.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 3.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 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..1621
FT /note="Lysophospholipase NTE1"
FT /id="PRO_0000295318"
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
//
