NTE1_MAGO7
ID NTE1_MAGO7 Reviewed; 1503 AA.
AC A4QVZ8; G4N5L8;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 91.
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; ORFNames=MGG_06143;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(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}.
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DR EMBL; CM001233; EHA52211.1; -; Genomic_DNA.
DR RefSeq; XP_003712018.1; XM_003711970.1.
DR AlphaFoldDB; A4QVZ8; -.
DR SMR; A4QVZ8; -.
DR STRING; 318829.MGG_06143T0; -.
DR EnsemblFungi; MGG_06143T0; MGG_06143T0; MGG_06143.
DR GeneID; 2684255; -.
DR KEGG; mgr:MGG_06143; -.
DR VEuPathDB; FungiDB:MGG_06143; -.
DR eggNOG; KOG2968; Eukaryota.
DR HOGENOM; CLU_000960_1_1_1; -.
DR InParanoid; A4QVZ8; -.
DR OMA; FTMNFTT; -.
DR OrthoDB; 253518at2759; -.
DR Proteomes; UP000009058; Chromosome 3.
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; -; 3.
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; 1.
DR Pfam; PF01734; Patatin; 1.
DR SMART; SM00100; cNMP; 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..1503
FT /note="Lysophospholipase NTE1"
FT /id="PRO_0000295324"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..71
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..1503
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 1200..1364
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 252..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1204..1209
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1231..1235
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1351..1353
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 262..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1233
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1351
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT BINDING 658..777
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="1"
FT BINDING 821..941
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="2"
SQ SEQUENCE 1503 AA; 165037 MW; 3CC03B000E44724B CRC64;
MDSSTAALAT ASAKLDAVAQ QGSSSWIGFF ANIILGIISL VYSILYSVLK LTTFSIPSLL
YTLFSTSLTV TMNATTLMLI IVLVFSLVSW FVRYRYLNMY SRLPPEPQRK EPDVDLFPDT
HPGGSKPGLS NYLDEFLSAI KIFGYLERPV FHELTRSMQT RKLIAGETFN LEEEKGFCMV
VDGLVEIFVK SARTGQHPVG ESCSIDSDGS DEHEEYQAGN QRYQLLTEVH NGAPMSSLFS
IMSLFTEDIK LRHGGDEGGE PTSATETYTS SRYGLGNDFS DQRESTVSVP TTPQLERSSS
HGPTLHDGDA NPSMGGRVPA SIPPMSLDPP LQSRPKRPTT SRHATTSVHP DIIARATVDT
TIAIIPASAF RRLIQIYPKY TAHIVHVILS RFQRVTLATA YNYLGLTSEV LHIEKSMIDN
ATCQLPNFLR GDALTRLKEK FNHERERIGE KDCTKGIALH NSSTGRRRKS TASLRKEAAL
QAITHGQRPS SVTASPPLQP RESGNKHTSN SGDLLMNIQL SRNGGRRSTS NMDPLTRQST
LLGSLETEVV SPLSQRTSNP FETRRHAHIS LNKRETRDED GLFRESILEC MFKAIGLTAN
GTGAREPDSA DASPRLTSYD QIRRGGYSSH NAFGFIDPYG GSVDGDADSI TSGGTGPGLP
VNPHALAHDM RDEVEIVFFP SGSVLVEQGE RNPGLYYVVD GFLDVCMSAA DESSGDILKA
SKNESSLNIG PGNQQGSAGR DRFMDANLGQ SSSRKRASNV RRNVALIKPG GLAGYVGSIS
SHRSFIDVVA KTDVYVGFLP RQSLERIVDR YPIVLLTMAK RLTNLLPKLI LHIDFALEWL
QVNAGEVIFH GGEESEAIYI VLNGRLRLVE DRQEGGVDVR GEFGQGESIG ELEVLTESAR
SGTLHAIRNT ELVKFPRTLF NSLAQEHPNI TIKISKIIAS RMRKVVDDPS TFVGKEGALK
ASLNKSSSTL NLRTVAILPV TSGVPVVEFG NRLMGALTQV GTPNGATSLS QSAILNHLGR
HAFNKMGKLK LSQYLADLEE KYGLVMYVAD TNVNSPWTQT CITQADCILL VGLAEGSPEI
GEYERFMLGM KSTARKVLVL LHADRYAEPG LTRSWLRNRM WINGGHHHVQ MAFRTQSVPI
NPTAKRTGPS LKERVQILQA EIQKYTSRKV RHSPFYSPDA PFKGDFHRLA RRLCGKSVGL
VLGGGGARGL AHIGIIRAME ESGIPIDIVG GTSIGSFVGA LYARHADVVP IFGLSKKFAG
RMASVWRFAL DLTYPSASYT TGHEFNRGIF KTFGKAQIED FWLEFYCNTT NISKSRQEIH
TSGYAWRYVR ASMSLAGLLP PLCDEGSMLL DGGYIDNLTV SHMKSLGVDI IFAVDVGSLD
DDVPQAYGDT LSGLWAFVNR WNPLSSTPNP PTLAEIQARL AYVSSVDALE RAKMTPGCVY
MRPPIDEYGT LEFGRFDEIV QVGYKYGLEF LQKLRDEGAL PVVEETEAKK ALRRTMAPRR
ASI
