ID   NTE1_ASPOR              Reviewed;        1538 AA.
AC   Q2UDH2;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   22-FEB-2023, 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=AO090012000173;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE60393.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP007161; BAE60393.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q2UDH2; -.
DR   SMR; Q2UDH2; -.
DR   STRING; 510516.Q2UDH2; -.
DR   VEuPathDB; FungiDB:AO090012000173; -.
DR   OrthoDB; 5303733at2759; -.
DR   Proteomes; UP000006564; Chromosome 4.
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; 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.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Membrane; Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN           1..1538
FT                   /note="Lysophospholipase nte1"
FT                   /id="PRO_0000295312"
FT   TOPO_DOM        1..74
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        96..117
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        139..1538
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          1235..1399
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          242..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          302..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          529..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1517..1538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1239..1244
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1266..1270
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1386..1388
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        302..322
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1268
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1386
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   BINDING         692..811
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="1"
FT   BINDING         856..976
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="2"
SQ   SEQUENCE   1538 AA;  169603 MW;  F4CE23D63EA35DD7 CRC64;
     MATDGGPLAA SSASLDSSLS PLHASPSPSS TYTASSLALS APAIAASFSV ASTFSNSLIP
     PPPLPPPTPS TMAGWFGWVF SFFFQVIPSV LYWVITFATI TLPTWLFTLF SMSLTFTMNF
     TTLLLIALAI VSTISWFIRY RFLNMYSRLP SEPQRKEPHL DLFPDVQEGD SKPGLANYLD
     EFLSAIKVFG YLERPVFHEL TRTMQTRKLI AGETLMLEEE KGFCLVVDGL VQIFVKSMRD
     GKPNVDEGSN HMGAESSDED DHRVDGKQGY QLLTEVKNGA SMSSLFSILS LFTEDIQLRA
     SEGSSSSASS VGPSTNARVS DSFPASPHGL EDSPRSNFVR DHGDSVAHIS NSNGELLPSV
     PPLNLGESHA MPIQEPYPKP RSQPGKRRRK SVHPDIVARA MVDTTIAIIP ASAFRRLTRV
     YPRATAHIVQ VILTRLQRVT FATAHSYLGL NNDVLGIEKQ MTKFTTQDLP NEMRGAALDR
     LKDKFIKERD RLGPEEIIKG IALHNPFAGR RRRSSSFLRK EAVLHAKMAA QSKRPVSMAS
     PEDISGDRES AGPSPGDLLS TIQLSRFGPR YEHLAPKLLS PLTDKENPPF MAPVMHSSPF
     HRKKDAVDED ALFRESILDC IMNGIGLTSS TRDVLRKSSH TSGDISPKLL SYDSRRQKAV
     FTNNAFGFID PYDSSADGET ESMMSMSMTS AGGTSPIVNL REELRNDIEI VYFPQGSVLV
     EQGERHPGLY YVIDGFLDVG IPVSDKGEDL VGGSRPVYGQ PPEEFFPTLK RTTTSSSRVS
     GVTSATNDTK RKRQSRKSLY LIKPGGIQGY VGSVASYRSY TDVVAKTDVY VGFLPRSSLE
     RIAERYPIAL LTLAKRLTSL LPRLLLHIDF ALEWVQVSAG QVIYHQGDES DAIYLVLNGR
     LRSVLEGTDG KITVVGEYGQ GESVGELEVM TESTRPATLH AIRDTELAKF PRSLFNSLAQ
     EHPGITIQVS KLIAQRMRDL VELPMPEKGG EHANVGSVKT AASVVNLRTV GILPVTAGVP
     VVEFGHRLQN ALHQIGVTNG VTSLNQAAIL NHLGRHAFSK MGKLKLSQYL ADLEEKYGMV
     LYIADTNVNS PWTQTCITQA DCILLVGLAE SSPSIGEYER FLLGMKTTAR KELVLLHSER
     YCPPGLTRQW LKNRMWINGG HHHIQMGFRL TPEPSHPQAK RLGAVLKQRV QVIQAEIQKY
     TSRRIRQTPL YSAQTPFKGD FHRLARRLCG RSVGLVLGGG GARGIAQVGV IKALEEAGIP
     IDIIGGTSIG SFIGALYARD ADVVPMYGRA KKFAGRMASM WRFMLDLTYP TTSYTTGHEF
     NRGIFKTFGD SQIEDFWLEY YCNTTNISKS RPEFHSSGYT WRYVRASMSL AGLIPPICDE
     GSMLLDGGYI DNLTVTHMKG LGADVIFAVD VGSIDDNTPQ GYGDSLSGFW TVLNRWNPFS
     ACPNPPTLSE IQARLAYVSS IDNLERAKNT PGCLYMRPPI DPYGTLEFGK FDEIYQVGYA
     YGKQYLEKLR SEGSLPLPEE TEEKKKLQRT LAPRRASI
//