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 10-APR-2019, entry version 89. 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., RA Weissenbach J., 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, CC elevated temperatures, or when choline is present in the growth CC medium (By 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 CC {ECO:0000305}; 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 ProteinModelPortal; Q8SVN8; -. DR SMR; Q8SVN8; -. DR GeneID; 859011; -. DR KEGG; ecu:ECU05_0070; -. DR EuPathDB; MicrosporidiaDB:ECU05_0070; -. DR eggNOG; KOG2968; Eukaryota. DR eggNOG; COG0664; LUCA. DR eggNOG; COG1752; LUCA. DR HOGENOM; HOG000113869; -. DR InParanoid; Q8SVN8; -. DR KO; K14676; -. DR OrthoDB; 253518at2759; -. DR Proteomes; UP000000819; Chromosome V. 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:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro. 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; PF01734; Patatin; 1. 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 Complete proteome; Endoplasmic reticulum; Hydrolase; KW Lipid degradation; Lipid metabolism; Membrane; Reference proteome; KW Repeat; Transmembrane; Transmembrane helix. FT CHAIN 1 905 Lysophospholipase NTE1. FT /FTId=PRO_0000295321. FT TRANSMEM 1 21 Helical. {ECO:0000255}. FT TOPO_DOM 22 905 Cytoplasmic. {ECO:0000250}. FT DOMAIN 610 774 PNPLA. {ECO:0000255|PROSITE- FT ProRule:PRU01161}. FT NP_BIND 198 319 cNMP 1. FT NP_BIND 310 428 cNMP 2. FT MOTIF 614 619 GXGXXG. {ECO:0000255|PROSITE- FT ProRule:PRU01161}. FT MOTIF 641 645 GXSXG. {ECO:0000255|PROSITE- FT ProRule:PRU01161}. FT MOTIF 761 763 DGA/G. {ECO:0000255|PROSITE- FT ProRule:PRU01161}. FT ACT_SITE 643 643 Nucleophile. {ECO:0000255|PROSITE- FT ProRule:PRU01161}. FT ACT_SITE 761 761 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU01161}. 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 //