ID   NTE1_NEOFI              Reviewed;        1523 AA.
AC   A1D9Y2;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   24-JAN-2024, entry version 90.
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=NFIA_030460;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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=EAW20613.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS027693; EAW20613.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001262510.1; XM_001262509.1.
DR   AlphaFoldDB; A1D9Y2; -.
DR   SMR; A1D9Y2; -.
DR   STRING; 331117.A1D9Y2; -.
DR   EnsemblFungi; EAW20613; EAW20613; NFIA_030460.
DR   GeneID; 4588979; -.
DR   KEGG; nfi:NFIA_030460; -.
DR   VEuPathDB; FungiDB:NFIA_030460; -.
DR   eggNOG; KOG2968; Eukaryota.
DR   OrthoDB; 5303733at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 3.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR001423; LysoPLipase_patatin_CS.
DR   InterPro; IPR002641; PNPLA_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR14226:SF29; NEUROPATHY TARGET ESTERASE SWS; 1.
DR   PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF01734; Patatin; 1.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 3.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 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..1523
FT                   /note="Lysophospholipase nte1"
FT                   /id="PRO_0000295325"
FT   TOPO_DOM        1..66
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        88..109
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        131..1523
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          1220..1384
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          309..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          524..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1502..1523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1224..1229
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1251..1255
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1371..1373
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        328..343
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..384
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1253
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1371
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   BINDING         681..800
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="1"
FT   BINDING         841..961
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="2"
SQ   SEQUENCE   1523 AA;  168447 MW;  95665818D567EF4B CRC64;
     MADGVTLVDS TGLHSFSSSP SLSTSSSSLT AVALSLATSA SAVTASYSIS HLPPPPLPPV
     PTTMAGWIGW VFSFFFQVIP SVLYWVITFS TITLPTWLFT LFSMSLTFTM NFTTLLLIVL
     AMVSTISWFI RYRFLNMYSR LPPEPQRKEP QVDLFPDVQE GDSKPGLANY LDEFLSAIKV
     FGYLERPVFH ELTRTMQTRK LIAGETLMLE EEKGFCLVVD GLVQIFVKSM RDGKSDTDEE
     LHHLGAESSD EEHHIDGKQG YQLLTEVKNG ASMSSLFSIL SLFTEDIQLR ENESSGSSSS
     SIALRAARVP NSIPTSPRGV MDSPSLGFQD HSDDTSNMIT NGDLPSVPPL HLGESHTPPS
     GDQHHQQHHE SRKHSSRKRR KSVHPDIVAR AMVDTTIAII PASAFRRLTR VYPRATAHIV
     QVILTRLQRV TFATAHSYLG LSNEVLGIEK QMTKFTTYDL PNNMRGAALD RLKDKFIKER
     DRLGSEEVTK GIALHNPSAG RRRRSSSFLR KDAALQVKMM TPRRAATVVT PESAPAEHDT
     YGVSPGDLLS TIQSSRFGPR YEQPPAKLQS PLAEKENTHF RLPAMQARHT FRRQDTMDED
     ALFRECILDC IMKGIGLTSS TRDALRKSSH SGDASPKLLS YDSRRQKAIF TNNAFGFIDP
     YEGSGDGETE SLMSMSVTSA GGTSPVINLR EELRNDIEIV YFPKGSVLVE QGERHPGLYY
     VIDGFLDVGV PIVEKGEDLV GVSKPAASKE SFPTLKRTTT ANSIGAGGTA ANDSRRRKQS
     RKSLYLIKPG GIQGYVGAVA SYRSYTDVVA KTDVYVGFLP RASLERIAER YPIALLTLAK
     RLTSILPRLL LHIDFALEWL QVNAGQVIYH QGDESDAIYL VLNGRLRSVL ESPGNKLAVI
     GEYGQGESVG ELEVMTESTR PATLHAIRDT ELAKFPRSLF NSLAQEHPGI TIQVSKLIAQ
     RMRDLVERPV TEKGVERSNA GGVQTATSTV NLRTVGILPV TAGVPVVEFG NRLLHALHQV
     GVTNGVTSLN QAAILNHLGR HAFSKMGKLK LSQYLADLEE KYGMVLYIAD TNVSSPWTQT
     CITQADCILL VGLAESSPSI GEYERFLLGM KTTARKELVL LHSERYCPPG LTRRWLKNRV
     WINGGHHHIQ MAFRLTAEPS HPETKRFGTV LKQRVQVLQA EIQKYTSRRI RQTPLYSAQS
     PFKGDFHRLA RRLCGRAVGL VLGGGGARGI AHVGVIKALE EAGIPVDIIG GTSIGSFIGA
     LYARDADVVP MYGRAKKFAG RMGSMWRFAL DLTYPTVSYT TGHEFNRGIF KTFGDSQIED
     FWLEFYCNTT NISKSRPEYH SSGYVWRYVR ASMSLAGLIP PICDEGSMLL DGGYIDNLTV
     DHMKGLGADV IFAVDVGSID DNTPQVYGDS LSGFWSVFNR WNPFSSCPNP PTLSEIQARL
     AYVSSIDNLE RAKNIPGCLY MRPPIDGYGT LEFGKFDEIY QVGYAFGKQF LEKLKTEGSL
     PLPEETEEKK KLQRTMAPRR ASI
//