ID   NTE1_ASPCL              Reviewed;        1528 AA.
AC   A1C9L6;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   24-JAN-2024, entry version 86.
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=ACLA_055880;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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=EAW13540.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; DS027048; EAW13540.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001274966.1; XM_001274965.1.
DR   AlphaFoldDB; A1C9L6; -.
DR   SMR; A1C9L6; -.
DR   STRING; 344612.A1C9L6; -.
DR   EnsemblFungi; EAW13540; EAW13540; ACLA_055880.
DR   GeneID; 4707103; -.
DR   KEGG; act:ACLA_055880; -.
DR   eggNOG; KOG2968; Eukaryota.
DR   OrthoDB; 5303733at2759; -.
DR   Proteomes; UP000006701; 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..1528
FT                   /note="Lysophospholipase nte1"
FT                   /id="PRO_0000295309"
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..1528
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          1225..1389
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          238..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          761..785
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1507..1528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1229..1234
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1256..1260
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1376..1378
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        372..388
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1507..1521
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1258
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1376
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   BINDING         686..805
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   1528 AA;  168937 MW;  D5982DE223A05DD9 CRC64;
     MADGNLLGSS TSLTALLPTP SSASLSASLS SSSLPVSPFL APAPTTAITA SIASLSAQPP
     PPLPATPATM AGWIGWVFSF FFQFIPSVLY SVITFTTITL PTWLFTLFSM SLTFTMNFTT
     LLLILLAVVS TLGWFVRYRF LNMYSRLPPE PQRKEPQIDL FPDVQGGDSK PGLANYLDEF
     LSAIKVFGYL ERPVFHELTR TMQTRKLIAG ETLMLEEEKG FCLVVDGLVQ IFVKSTRDGK
     SGSDDELHHL GAESSDEEHH IDGKQGYQLL TEVKNGASMS SLFSILSLFT EDIQVWDSQS
     STSSSSSIAM RAARVPDSTP NSPRGGMDSP TPIFRDVPDP VSLVNENGDL PLVPPLHLEE
     SPIPPTNHAH DRRQHDHRKH HGRKHRKSVH PDIVARAMVD TTIAIIPASA FRRLTRVYPR
     ATAHIVQVIL TRLQRVTFAT AHSYLGLSNE VLGIEKQMTK FTTYDLPNNM RGTALDRLKD
     KFIKERDRLG TEEVTKGIAL HNPSAGRRRR SSSFMRKDAV LHAKMMSPKR AATVITSDNS
     YDHDSAGVSP GDLLSTIQQS RFGPRYEQPT PRLRSPLAEK ENSHFRLPAM QARNAFHRKE
     SLDEDALFRE CILDCIMKAI GLTSSTGEVL RKSSHSGEAS PKLLSYDSRR QKAVFSNNAF
     GFIDPYEGSG DGETESMMSM SVTSAGGTSP VTSLREELRN DIEIVYFPQG SVLVEQGERH
     PGLYYVIDGF LDVGMPVVDK GEDLVGVSKP ATAREPFPTL KRTTTASSIK PSATAANDPR
     RRKQSRKSLY LIKPGGIQGY VGAVASYRSY TDVVAKTDVY VGFLPRASLE RIAERYPIAL
     LTLAKRLTSL LPRLLLHIDF ALEWVQVNAG QVIYHQGDES DAIYLVLNGR LRSVLESADN
     KLTVIGEYGQ GESVGELEVM TESTRPATLH AIRDTELAKF PRSLFNSLAQ EHPGITIQVS
     KLIAQRMRDL VERPVTEKGA ERSSAGGVQT ATSTLNLRTV GILPVTAGVP VVEFGNRLLH
     ALHQIGVVNG VTSLNQSAIL NHLGRHAFSK MGKLKLAQYL ADLEEKYGMV LYIADTNVNS
     PWTQTCITQA DCILLVGLAE SSPSIGEYER FLLGMKTTAR KELVLLHSER YCPPGLTRRW
     LKNRVWINGG HHHIQMAFRL TAEPSHPETK RFGTVLKQRV QVLQAEIQKY TSRRIRQTPL
     YSAQTPFKGD FHRLARRLCG RAVGLVLGGG GARGIAHVGV IKALEEAGIP VDIIGGTSIG
     SFIGALYARD ADVVPMYGRA KKFAGRMGSM WRFALDLTYP TISYTTGHEF NRGIFKTFGD
     SQIEDFWLEF YCNTTNISKS RQEYHSSGYV WRYVRASMSL AGLIPPICDE GSMLLDGGYI
     DNLTVDHMKG LGADVIFAVD VGSIDDNTPQ GYGDSLSGFW VAFNRWNPFS SCPNPPTLSE
     IQARLAYVSS IDNLERAKIT PGCLYMRPPI DAYGTLEFGK FDEIYQVGYK FGKQFLEKLK
     NEGSLPLPEE TEEEKKLLRT MAPRRASI
//