NTE1_CANGA
ID NTE1_CANGA Reviewed; 1728 AA.
AC Q6FKJ1;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=CAGL0L11154g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380958; CAG62227.1; -; Genomic_DNA.
DR RefSeq; XP_449253.1; XM_449253.1.
DR AlphaFoldDB; Q6FKJ1; -.
DR SMR; Q6FKJ1; -.
DR STRING; 5478.XP_449253.1; -.
DR PRIDE; Q6FKJ1; -.
DR EnsemblFungi; CAG62227; CAG62227; CAGL0L11154g.
DR GeneID; 2891028; -.
DR KEGG; cgr:CAGL0L11154g; -.
DR CGD; CAL0135996; CAGL0L11154g.
DR VEuPathDB; FungiDB:CAGL0L11154g; -.
DR eggNOG; KOG2968; Eukaryota.
DR HOGENOM; CLU_000960_1_1_1; -.
DR InParanoid; Q6FKJ1; -.
DR OMA; DFWLQYY; -.
DR Proteomes; UP000002428; Chromosome L.
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:0034638; P:phosphatidylcholine catabolic process; IEA:EnsemblFungi.
DR GO; GO:0071071; P:regulation of phospholipid biosynthetic process; IEA:EnsemblFungi.
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; 2.
DR Pfam; PF01734; Patatin; 1.
DR SMART; SM00100; cNMP; 2.
DR SUPFAM; SSF51206; SSF51206; 4.
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; Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..1728
FT /note="Lysophospholipase NTE1"
FT /id="PRO_0000295315"
FT TOPO_DOM 1..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..97
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..1728
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 1422..1586
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 141..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1426..1431
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1453..1457
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1573..1575
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 149..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..363
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1455
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1573
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT BINDING 854..987
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="1"
FT BINDING 983..1121
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="2"
SQ SEQUENCE 1728 AA; 193367 MW; 88C134F24072720A CRC64;
MDSSSIAHES DIVSTERNIL PERFISNKQQ GNYLEDGSGD GNGKAAEHWL LAAIFNFFWV
ISYFISGSTH IAFRSSWYIV SLLLLKFPKW IIVEANHIHL TIPFSVLVVT LAIIFYVSYE
FLKGRLLSEY KNLTSDLNTD SLNSKNSKSS RLLHHDSKDS NTTRRRRYSS GKLLSSALHE
SHSGINGGDD GDDTFLSSYL DQFLSAIRIF GYLEKPVFHD LTKNMKTQKL DEGEILLLDN
SVGFAIVVEG TLDIYHEVEE KGNMNDIDGD FMVDDNQSIY SILKRKKKKY STSRHGQYNN
NSDPGHYNGH NVNGDDEDDD DGILQMRSSS RNQNIPSFDA IESSSSDEES DINDGDSESQ
SESDDESTGF IRLKDGLGKF QLLNTVKAGN PVSSLVNILN LFTSANDNVT SPSRTGRMDS
NYTNPVERPT SKLSTSIEES AMRLELGKYS LSPTEASYRS TSNPSNNFSK DNDPLSKSIS
GPDAVTTPSL PPLNNRAFVI PKVVARAATD CTIAIIPPQA FAKLKAKYPR SASHIIQMIL
TKLYHVTFQT AHKYLGLTQE IAYTELLLNR TVSYDLPNYL KEIVIDRFKD KGKDMNLQKG
FQSPTSSRLT SNFNGNSNNQ RTNSRNSQAL MSTRDLRKTR PELSQQSSMI HSPTPITGSR
HVVLESRDKY NPGDLLSNVP LSRINLASPS SRGFDYSSMK KESSPQSSVN SRKRSTTGER
PRLLKRPSIY NNQSSSRSDA LKGNNSNNKD INFTSFSAQE ETEDSVVRMA LVEAMLTYLG
VNKTNMSILP GIYDGAPSEP HSHRASEISL VSSYTSSAAP QTTIRILPKE YAIVSTRKQK
QSSKKRRKYK EEISPTLDYE YAKNEFAQAI ELQYFKQGTV IVEQDTRGKG LYYVVSGKID
VTTSTVSDHE IFNSTRDKKK KKSKTLFTIE SGGIAGYLSS LVSYKSFVTL IAKTDVYVGF
LPYQTLEKLC DKYFLIYLRI AESLTSLLTP RMLKLDHALE WLHLNASDTL FNQGDPANGI
YVILNGRLRQ LRNPELEENS TDYPNDGEEK DSSRDSTIVM GELGQGESFG EVEVLTAMDR
ISSMVAVRDT ELARIPRSLF ELLAIEHPSI MIRVSRLVAK KILGQGQANM ALPKIGSGSN
LRHDLNLTIP PSSSSSIHTH SYGNDNSNQM NNANFRTITI LPITSGLPVE SFAMKLVHAF
KQVGRTTIGL NQRTTLSHLG RHAFDKLAKL KESGYFAELE ELYQTVVYIA DTPVKSSWTK
TCIAQADCVI LLARADDSPE IGEYERLLLK SKTTSRTELV LLHNERSVEP GMTQRWLRSR
SWVHNHYHIQ FAMDSLVNSS NVKDTGGNIG ALNLVDKFIQ TELGRKTQYN ISKLLPESIK
MTVENFSSRF MKRKRQYYTP VHRHKDDFLR LARILSGQAI GLVLGGGGAR GLSHLGILQA
LEERGIPIDM IGGTSIGSFV GGLYAKDYDL VPIFGRIKKF AGRISSIWRM LSDFTWPVTS
YTTGHEFNRG IWKSFGDTRI EDFWVQYFCN STNITESVQE IHSYGYAWRY VRASMSLAGL
LPPIEDNGSM LLDGGYVDNL PVLEMKARGC NTIFAVDVGS VDDRTPMKYG DSLNGFWIIL
NRWNPFSKHP NIPTMAEIQV RLGYVSSVNA LEKAKRTPGV IYVRPPIENY ATLDFGKFEE
IYKVGADFGK VFLQALAEEG KMPYIPGSNA DLVGDVETGF FLHRRNSI
