NTE1_USTMA
ID NTE1_USTMA Reviewed; 1883 AA.
AC Q4PF83; A0A0D1EAB5;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=UMAG_01230;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003141; KIS71330.1; -; Genomic_DNA.
DR RefSeq; XP_011387164.1; XM_011388862.1.
DR AlphaFoldDB; Q4PF83; -.
DR SMR; Q4PF83; -.
DR STRING; 5270.UM01230P0; -.
DR EnsemblFungi; KIS71330; KIS71330; UMAG_01230.
DR GeneID; 23562320; -.
DR KEGG; uma:UMAG_01230; -.
DR VEuPathDB; FungiDB:UMAG_01230; -.
DR eggNOG; KOG2968; Eukaryota.
DR HOGENOM; CLU_000960_1_1_1; -.
DR InParanoid; Q4PF83; -.
DR OMA; HTAHKYL; -.
DR OrthoDB; 253518at2759; -.
DR Proteomes; UP000000561; Chromosome 2.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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; IBA:GO_Central.
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; 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; 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..1883
FT /note="Lysophospholipase NTE1"
FT /id="PRO_0000295331"
FT TOPO_DOM 1..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..103
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..1883
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 1544..1708
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 284..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1084..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1852..1883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1548..1553
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1575..1579
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1695..1697
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 298..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..957
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..981
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1069
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1861..1876
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1577
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1695
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT BINDING 863..1158
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="1"
FT BINDING 1166..1285
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="2"
SQ SEQUENCE 1883 AA; 203826 MW; AF91BC38E34B0FF5 CRC64;
MSQVPVASPA SWSSVASAAA AAVSAATSAS SSLAASVDEP AATTATAATA SYADERNPLI
ALFDGLLRVV LASLNLIRIL ATFSTITVPS LVYAILHYSL TLQLNFPSLA LLFLTSLISA
FIWLRYRHLN KYERLREVPI TRDEGFNLNP DVASPGGDND RGSFHNYLDD FLQAIRIFGF
LEKPVFHELA RHLQTRRLVA GDSLSLDTDF SFYIVIDGHV QVYAPLPSAT ASAVGQDSVE
DEDDSGYQLL NEVESGGTLS SLFTILSLFT EDVKLSFDDH DDPHLAPPHP AYPAMDRLNN
SSAANHLGRG NNATAPTSPY SSAFNPPSQT AAQLQLNAAA LRNVPAAIST EGAVERLGGS
AAVRSTSKSS HARTASSGTA SATVQDGDTS TIMDPLEQND DGVTSSLYHA PDLQMPPAQA
AAPFSHFAPS YHPSPAGTPI SSLPGSTHSP YFRGRATSIH ALHEAAGGPN TPGSILSAMS
SSAHGHYHPQ ADYLPRQGAG TVARATVDTT LAVIPAEAFK RLTKKFPNAA AHIVQVILAR
LSRVTFHTAH KYLGLTKEVM RTEKSINDLA CFPLPSEFYE KGGMDKLRHR FLPQPNSKRE
TTVDDDYFRD FQEWTSISQR SSTPVPGSKD DTKDAATSSP PKVRIASDLP SLTTSSKQSN
QKPTSSRISA ARTPWGHPDP PLKTPTARNM VGPGDLLSMA SLSQDGWYTT GFDMHSAQPT
PRAKPRSVSK LEPFHGPLPH PVDDSTDGTS PLSGASPIPI RKGSSTMYHQ GEAIGTDRPF
ANIGLPHFDI KNEVMDCIAK SIGLAQAAHS PLAPSYQASP HINAQDSLLQ RSVFKSAFGS
LSMLDAAMAE EESSITGTNS SMAGHGHSGF HPSDFENEVE IKFFPAGSTL VKAGESRAGL
FYVIDGFLDV LLPAEANELE EEDRLKPNMN HKSAKTDASS GSSRQNRPGS HRKDSSSASL
RAGLLDERNL READVSLPQR RGTEADRISS NGDGNSGSVH RPAMREGSSS STSYGTPAGL
RKKPTESAKV GNALDGTGGA GSSSRRKPSH VSSGSGATTM PRHPDATNSN MAFTAKQPVL
HPSLHQQQPL RGKPSQQSSQ RSKDGKRSIF TVGRGGIAGY LSSLLGTASY VDITAKTDVY
VGFLPAHALE RIMERRPIVL LTLCKRLLSL LPPLILHIDS SLDWQQVNAG QVIYREDDPS
DSFFIVINGR LRAITEKTNG IEVHNEYGQG DSVGELDVIT NSRRRTTLHA IRDSELAKMP
STLFNAISVR HPAITIQISR IIARRVRTEL VRSKQEGAAL GAPIPGLPDL GRNNLNLKTV
AIVPVTRQVP VIDFAAKLQT AFDDTIGGRA IFLDQSSVMG VLGRHAFSRM GKLKLAGWLA
DLEQKYRLVV YVVDTPVSSA WSQTSIRQAD CVLMVGFGDE PAMGEYERLL MSVKTTARKE
LVLLHPERSV PPGSTREWLK NRPWVHAHHH VEMPGLTGSH AGAAISTGGD PKAVKALRNL
KQKLETSLQR YRKTMTPLSA SGRPHHASDF ARLARRLCGM SIGLVLGGGG ARGCAHLGVI
RALEERGIPI DMVGGTSIGS LVGGLYAREA EMVSTFGRAK RFAGRMASLW RFASDLTYPV
VSYTTGHEFN RGVFKAIQET HIEDMWIPFF CNTTNITWSR MEVHTSGYAW RYIRGSMTLA
GLIPPLVDEG NMLVDGGYVD NLPVTVMLAM GARSVFAVDV GSIDDTSPRA YGDTLSGWWV
LLNRWNPWSD ASKIPSIPDI QGRLTYVSSV KTLEEAKKVK GCFYMRMPVE EFGTLAFGRF
DMIYEKGYKA AVELLDGWDA EGKLPSGTER EDFEDDWEDG DEYEEYEVYT DDESGVGGGV
RKIRKKRRRT RRKAGISARR NSI
