ID   NTE1_ASPNC              Reviewed;        1531 AA.
AC   A2R350;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 84.
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=An14g03050;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAK46542.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AM270320; CAK46542.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; A2R350; -.
DR   SMR; A2R350; -.
DR   PaxDb; A2R350; -.
DR   EnsemblFungi; CAK46542; CAK46542; An14g03050.
DR   Proteomes; UP000006706; Chromosome 1R.
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; 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.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Membrane; Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN           1..1531
FT                   /note="Lysophospholipase nte1"
FT                   /id="PRO_0000295311"
FT   TOPO_DOM        1..72
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        94..115
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        137..1531
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          1228..1392
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          242..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          303..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          766..789
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1510..1531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1232..1237
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1259..1263
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1379..1381
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        330..345
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1261
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1379
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   BINDING         689..809
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="1"
FT   BINDING         849..969
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="2"
SQ   SEQUENCE   1531 AA;  169000 MW;  2145CB24C8D6CE79 CRC64;
     MATGDGIIAA PPSLESSSLD PLHVLPASSS TAARSLATSI PALTASFSVV SGFSSHLPPP
     PVTPPAPSTM VGWIGWIFSF IFQVIPSVLY WIVTFTTITL PTWLFTLFSM SLTFTMNFTT
     LLLIALAVVS TISWFIRYRF LNMYSRLPPE PQRKEPQLDL FPDVPDSDTK PGLANYLDEF
     LSAIKVFGYL ERPVFHELTR TMQTRKLIAG ETLLLEEEKG FCLVVDGLVQ IFVKSMRDRK
     SGSDEELNRM AGESSDEDDH RPDGRQGYQL LTEVKNGASM SSLFSILSLF TEDVQLRYAD
     SSASSASSIG PGLAIGPDSF PASPREMDDS PHVYQGDRLD PASHRNSTAE DLPAVPPLNL
     GESQVPPAHS ARSESRKYSG KTRRKSVHPD IVARAMVDTT IAIIPASAFR RLTRVYPKAT
     AHIVQVILTR LQRVTFATAH SYLGLNNEVL GIEKQMTKFT TYDLPNELRG SALDRLKDKF
     IKERDRLGQE EVTKGIALHN PYGGRRPRSS SFRRKEAALQ AKMVASKRPV SMVAQDSALS
     DRENSGVSPG DLLSTIQLSR FGPRYEHLAP RLLSPLTEKE HSPLRSPSPM IPGRASPFHR
     KESLDEDALF RESILECIMK GIGLTGSTND FLRKSSHPSG DVSPKLLSYD SRRQKAVFSN
     NAFGFIDPYE GSADGESESM MSMSVTSAGG TSPIVNLREE LRNDIEIVYF PQGSVLVEQG
     ERHPGLYYVV DGFLDVGIPV DDKEEDLVGS SRPAHEELFP MLRRTNTSSS RVSGSAAAAN
     DPRRKKQSRR SLYLIKPGGI QGYVGAVASY RSYTDVVAKT DVYVGFLPRA SLERIAERYP
     LALLTLAKRL TSLLPRLLLH IDFALEWVQV SAGQVIYHQG DESDAIYLAL NGRLRSVHEG
     PNGKMTVVGE YGQGESVGEL EVMTESTRPA TLHAIRDTEL AKFPRTLFNS LAQEHPGITI
     QVSKLIAQRM RDLVETPLAE KGGEPGVSGT VKTAKSTLNL RTVGILPVTA GVPVVEFGNR
     LLQALHQIGV TNGATSLNQA AILNHLGRHA FSKMGKLKLS QYLADLEEKY GMVLYIADTS
     VNSPWTQTCI TQADCILLVG LAESTPSIGE YERFLLGMKT TARKELVLLH GERYCPPGLT
     RQWLKNRVWI NGGHHHVQMA FRLTAEPSHP QTKRFGTVLK QRVQVIQAEI QKYTSRRIRQ
     SPLYSAQTPF KGDFHRLARR LCGRSVGLVL GGGGARGIAQ VGVIKALEEA GIPIDVIGGT
     SIGSFIGALY ARDADVVPMY GRAKKFAGRM GSIWRFALDL TYPTVSYTTG HEFNRGIFKT
     FGDSQIEDFW LEFYCNTTNI SRSRAEYHSS GYTWRYVRAS MSLAGLIPPI CDEGSMLLDG
     GYIDNLTVDH MKGLGADVIF AVDVGSIDDN TPQVYGDSLS GFWAVVNRWN PFSSCPNPPT
     LSEIQARLAY VSSIENLERA KNTPGCLYMR PPIDPYGTLD FAKFDEIYQL GYAYGKNYLE
     KLKREGSLPL PEETEEKKKL QRTLAPRRAS I