ID   NTE1_ASPFU              Reviewed;        1522 AA.
AC   Q4WA15;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=AFUA_4G03000;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(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; AAHF01000016; EAL84448.1; -; Genomic_DNA.
DR   RefSeq; XP_746486.1; XM_741393.1.
DR   AlphaFoldDB; Q4WA15; -.
DR   SMR; Q4WA15; -.
DR   STRING; 746128.CADAFUBP00009732; -.
DR   EnsemblFungi; EAL84448; EAL84448; AFUA_4G03000.
DR   GeneID; 3503855; -.
DR   KEGG; afm:AFUA_4G03000; -.
DR   VEuPathDB; FungiDB:Afu4g03000; -.
DR   eggNOG; KOG2968; Eukaryota.
DR   HOGENOM; CLU_000960_1_1_1; -.
DR   InParanoid; Q4WA15; -.
DR   OMA; FTMNFTT; -.
DR   OrthoDB; 253518at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
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: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; 2.
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..1522
FT                   /note="Lysophospholipase nte1"
FT                   /id="PRO_0000295310"
FT   TOPO_DOM        1..65
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        87..108
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        130..1522
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          1219..1383
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          308..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          523..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          757..776
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1501..1522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1223..1228
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1250..1254
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1370..1372
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        8..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..342
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..383
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1252
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1370
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   BINDING         680..800
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="1"
FT   BINDING         840..960
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="2"
SQ   SEQUENCE   1522 AA;  168262 MW;  4EB5CC71B03724B3 CRC64;
     MADGVTQVDS TGLHSFSPSP SLSSSSSLPA VALSLAVSAS AVTASYSISH LPPPPLPPVP
     TTMAGWIGWV FSFFFQVIPS VLYWIITFST ITLPTWLFTL FSMSLTFTMN FTTLLLIVLA
     VVSTISWFIR YRFLNMYSRL PPEPQRKEPQ VDLFPDVQEG DSKPGLANYL DEFLSAIKVF
     GYLERPVFHE LTRTMQTRKL IAGETLMLEE EKGFCLVVDG LVQIFVKSMR DGKSDTDEEL
     HHLGAESSDE EHHIDGKQGY QLLTEVKNGA SMSSLFSILS LFTEDIQLRE NESSGSSSSS
     IALRAARVPN SIPTSPRGVM DSPSLGFQDH SDDTSNMITN GELPSVPPLH LGESRTPPSG
     DQHHQQHHES RKHSSRKRRK SVHPDIVARA MVDTTIAIIP ASAFRRLTRV YPRATAHIVQ
     VILTRLQRVT FATAHSYLGL SNEVLGIEKQ MTKFTTYDLP NNMRGAALDR LKDKFIKERD
     RLGSEEVTKG IALHNPSAGR RRRSSSFLRK DAALQAKLMT PRRAATVVTP ESAPAEHDTY
     GVSPGDLLST IQSSRFGPRY EQPPAKLQTP LAEKENTHFR LPAMQARHTF RRQDTMDEDG
     LFRECILDCI MKGIGLTSST RDALRKSNHS GEASPKLLSY DSRRQKAIFT NNAFGFIDPY
     EGSGDGETES LMSMSVTSAG GTSPVINLRE ELRNDIEIVY FPKGSVLVEQ GERHPGLYYV
     IDGFLDVGVP IVDKGEDLVG VSKPAASKGS FPTLKRTTTA NSVGAGGTAA NDSRRRKQSR
     KSLYLIKPGG IQGYVGAVAS YRSYTDVVAK TDVYVGFLPR ASLERIAERY PIALLTLAKR
     LTSILPRLLL HIDFALEWVQ VNAGQVIYRQ GDESDAIYLV LNGRLRSVLE SPGNKLAVVG
     EYGQGESVGE LEVMTESTRP ATLHAIRDTE LAKFPRSLFN SLAQEHPGIT IQVSKLIAQR
     MRDLVERPVT EKGVERSNAG SVQTATSTVN LRTVGILPVT AGVPVVEFGN RLLHALHQVG
     VTNGVTSLNQ AAILNHLGRH AFSKMGKLKL SQYLADLEEK YGMVLYIADT NVSSPWTQTC
     ITQADCILLV GLAESSPSIG EYERFLLGMK TTARKELVLL HAERYCPPGL TRRWLKNRVW
     INGGHHHIQM AFRLTAEPTH PETKRFGTVL KQRVQVLQAE IQKYTSRRIR QTPLYSAQSP
     FKGDFHRLAR RLCGRAVGLV LGGGGARGIA HVGVIKALEE AGIPVDIIGG TSIGSFIGAL
     YARDADVVPM YGRAKKFAGR MGSMWRFALD LTYPTVSYTT GHEFNRGIFK TFGDSQIEDF
     WLEFYCNTTN ISKSRPEYHS SGYVWRYVRA SMSLAGLIPP ICDEGSMLLD GGYIDNLTVD
     HMKGLGADVI FAVDVGSIDD NTPQVYGDSL SGFWSVFNRW NPFSSCPNPP TLSEIQARLA
     YVSSIDNLER AKNIPGCLYM RPPIDGYGTL EFGKFDEIYQ VGYAFGKQFL EKLKSEGSLP
     LPEETEEKKK LQRTLAPRRA SI