ID NTE1_ENCCU Reviewed; 905 AA. AC Q8SVN8; DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 22-FEB-2023, 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=ECU05_0070; OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite). OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae; OC Encephalitozoon. OX NCBI_TaxID=284813; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GB-M1; RX PubMed=11719806; DOI=10.1038/35106579; RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F., RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P., RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J., RA Vivares C.P.; RT "Genome sequence and gene compaction of the eukaryote parasite RT Encephalitozoon cuniculi."; RL Nature 414:450-453(2001). 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}. 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; AL590445; CAD26524.1; -; Genomic_DNA. DR RefSeq; NP_597347.1; NM_001041213.1. DR AlphaFoldDB; Q8SVN8; -. DR SMR; Q8SVN8; -. DR STRING; 284813.Q8SVN8; -. DR GeneID; 859011; -. DR KEGG; ecu:ECU05_0070; -. DR VEuPathDB; MicrosporidiaDB:ECU05_0070; -. DR HOGENOM; CLU_000960_1_3_1; -. DR InParanoid; Q8SVN8; -. DR OMA; WRIFRIN; -. DR OrthoDB; 5303733at2759; -. DR Proteomes; UP000000819; Chromosome V. 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:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro. DR CDD; cd07225; Pat_PNPLA6_PNPLA7; 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; PF01734; Patatin; 1. 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..905 FT /note="Lysophospholipase NTE1" FT /id="PRO_0000295321" FT TRANSMEM 1..21 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 22..905 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT DOMAIN 610..774 FT /note="PNPLA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161" FT MOTIF 614..619 FT /note="GXGXXG" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161" FT MOTIF 641..645 FT /note="GXSXG" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161" FT MOTIF 761..763 FT /note="DGA/G" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161" FT ACT_SITE 643 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161" FT ACT_SITE 761 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161" FT BINDING 198..319 FT /ligand="a nucleoside 3',5'-cyclic phosphate" FT /ligand_id="ChEBI:CHEBI:58464" FT /ligand_label="1" FT BINDING 310..428 FT /ligand="a nucleoside 3',5'-cyclic phosphate" FT /ligand_id="ChEBI:CHEBI:58464" FT /ligand_label="2" SQ SEQUENCE 905 AA; 103088 MW; 94B9D7775EA8E92C CRC64; MVSLSLLIAI IVVTGLLAGF RHYGSSRCRT VPFKIKSRSI EKTASTRLLG MSLEDAMKRY PLFNFYPGQS IREILSSWER VTYGNGETIA APGFILQGLV EIWYREHLVC VKEKGSFLNG SMELLGYSTR GTKKARGSVE VLLIDASLVR DNIWYILFSM LRKSCIEIAC RYFELESKLV EKETMKIKDD GQGHLDLFLS FLNEKLLLNL DDGKEILRRD IEARLIGRGE TIKDSEESMD YIMYVVSGEI LVLAGESAFV FGKGSVFGYF SLFFDLYSSI KIQAREDSSV LLCSSSVLLK FGLDEKKFDH SMLLDIDESL HIIDESAEWM RLLPGDMIAQ KGDASKEIFY IGAGSVKSAS RESSSGTVIG GKECIFGESW NESSIATRIT DVVRIPSLLV DYFLERDKSF FKKYTKRLFE SGNKANGKIV SIIPVGQYKD IESFSRKLKS AIGASSLLLS RRDVVEILAR RAFDTTEEVR FMDYLTKMSR RYEIILIYVE NEYSRLLRYL LNFSDVLLAV GTTFADIPEY NVYCRIEFVK IYEERRASDE RSVKKSKKIN HGPRYLESRK ESFGQYDRVH HVLFPSKTML FCSKDFQRLA RSLLGKRIGL VLGGGGARGL AHIGVIQALE EEGIPIDCVG GTSMGAFIGA LYAKECNNYH VFKQAKRFSR KMSNIWILLL DLTYPICSMF SGHAFNRSLH SIFGDGLIQD LWLEYFCITT NIVSYEEEVH RNGMVWRYVR ASMGLCGYLP PICDNKKLLV DGGYLNNVPA DVMMGMQVEK IITVDVGTVL ENDHFDYGDT LSGFTILFNK FFGNKKFVTM EEIQYRLAYI STERKMKELE ANGNIIMLRP DLGKYRTMDF KKFDEIVACG YQSTKNAIAK WKQEGTYDVL FFSLKKQTPK RRYSV //