ID   NTE1_EMENI              Reviewed;        1527 AA.
AC   Q5BAE9; C8VPA5;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   24-JAN-2024, entry version 108.
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=AN2481;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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=CBF86943.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAA63799.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AACD01000041; EAA63799.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001307; CBF86943.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_660085.1; XM_654993.1.
DR   AlphaFoldDB; Q5BAE9; -.
DR   SMR; Q5BAE9; -.
DR   STRING; 227321.Q5BAE9; -.
DR   GeneID; 2875190; -.
DR   KEGG; ani:AN2481.2; -.
DR   VEuPathDB; FungiDB:AN2481; -.
DR   eggNOG; KOG2968; Eukaryota.
DR   HOGENOM; CLU_000960_1_1_1; -.
DR   InParanoid; Q5BAE9; -.
DR   OrthoDB; 5303733at2759; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; 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; 2.
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..1527
FT                   /note="Lysophospholipase nte1"
FT                   /id="PRO_0000295320"
FT   TOPO_DOM        1..73
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        95..116
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        138..1527
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          1224..1388
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          299..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          567..596
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          765..785
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1504..1527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1228..1233
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1255..1259
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1375..1377
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        299..315
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..596
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1257
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1375
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   BINDING         682..809
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="1"
FT   BINDING         846..966
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="2"
SQ   SEQUENCE   1527 AA;  168413 MW;  27E5289D1C9A881A CRC64;
     MADSGASVPS PDLPDLDSLH ASLSLPDIPS VAATSLSTSL PAISAKVSGF PSFSSHLPPP
     PLLSPPTPTT MVGWIGWVFS LVFQTIPSVL YWVITFSTIT LPTWLFTLFS MSLTFTMNFT
     TLLLIVLGLV STVSWFIRYR FLNMYSRLPP EPQRKEPQLD LFPDVQEGDS KPGLANYLDE
     FLSAIKVFGY LERPVFHELT RTMQTRKLIA GETLQLEEEK GFCLVVDGLV QIFVKSMRSG
     KHGLNGEVIE GSSDEDDQAR DGKQGYQLLT EVKNGASMSS LFSILSLFTE DIRLRASEGS
     SSSMSSVQPS PARTTPAPFL DSPGEMLNGS PMVLPRDSEV DSSAINGEAE PLPPVPPLHL
     GESRASSYHP NGQSTASERV RGNRRKSVHP DIVARAMVDT TIAIIPASAF RRLTRLYPRA
     TAHIVQVILT RLQRVTFATA HSYLGLTNEV LGIEKQMTKF TTYDLPNDIR GAALDRLKDK
     FLKEKDRLGS EEVTRGIALH NPYAGRRRRS MSFVRKEAAL KAKMPLPKRP NSLINPERPF
     HGYDTAGVSP GDLLSTIQLS RFGPRHDQFA TTPRLHSPLT EKERSPLRRS SLQRKDSVDE
     DALFRESILD CIMKGIGLTP SSHNALRKGS HSGELSPKLV SYDSRRQKAV FSNNAFGFID
     AYEGSGDGDT ESMMSMSVTS AGGTSPIVYL REDLLNDIEI VYFPKGAVLV EQGERHPGLY
     YVIDGFLDVG VQVNEKGDDL VGASRPGHAQ PDEELFPTLK RTQTATSRGA TAAAPINESK
     RKKPSRKSLY MIKPGGMQGY VGAMASYRSY TDVVAKTDVY VGFLPRASLE RLAERYPIAL
     LTLAKRLTGL LPRLLLHIDF ALEWVQVNAG QVIYHQGDES DAIYITLNGR LRSVHEGKGG
     KMTVVGEHGQ GESVGELEVM TESTRPATLH AIRDTELAKF PRSLFNSLAQ EHTGITIQVS
     KLIAQRMRDL VENPMTEQGE PGNTGSVKTA TSTLNLRTVG ILPITTGVPV VEFGNRLLSA
     LQQIGVTDGV TSLNQAAILN HLGRHAFSRM GKLKLSQYLA DLEEKYGMVL YIADTNVNSP
     WTQTCISQAD CILLVGLAES SPNVGEYERF LLGMKTTARK ELVLLHADRY CPPGLTRKWL
     KNRVWINGGH HHIQMAFRLT AEPSHPQTKR LGTVLKQRVQ ILQAEIQKYT SRRIRQTPIY
     SAQTPFKGDF HRLARRLCGR AVGLVLGGGG ARGIAHVGVI KALEEAGIPV DIVGGTSIGA
     FIGGLYARDA DVVPMYGRAK KFAGRMGSIW RFALDLTYPS VSYTTGHEFN RGIFKTFGDS
     QIEDFWLEFY CNTTNISRSR AEYHSSGYVW RYVRASMSLA GLLPPICDEG SMLLDGGYID
     NLTVAHMKTL GADVIFAIDV GSIDDNTPQG YGDSLSGMWS VINRWNPFSS IPNPPTLSEI
     QARLAYVSSI DNLERAKNIP GCLYMRPPID RYGTLEFGNF DEIYQVGYAY GKEYLQKLKS
     QGSLPLPEEN EEKKKLQRTL APRRASI
//