NTE1_ENCCU
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 03-AUG-2022, entry version 99.
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}.
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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; 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: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 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 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
