ID   NTE1_NEUCR              Reviewed;        1515 AA.
AC   Q7S8J1;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 106.
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=NCU08276;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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}.
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DR   EMBL; CM002239; EAA32668.3; -; Genomic_DNA.
DR   RefSeq; XP_961904.3; XM_956811.3.
DR   AlphaFoldDB; Q7S8J1; -.
DR   SMR; Q7S8J1; -.
DR   STRING; 5141.EFNCRP00000008431; -.
DR   EnsemblFungi; EAA32668; EAA32668; NCU08276.
DR   GeneID; 3878043; -.
DR   KEGG; ncr:NCU08276; -.
DR   VEuPathDB; FungiDB:NCU08276; -.
DR   HOGENOM; CLU_000960_1_1_1; -.
DR   InParanoid; Q7S8J1; -.
DR   Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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; IBA:GO_Central.
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; IPR001423; LysoPLipase_patatin_CS.
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; 2.
DR   SUPFAM; SSF51206; SSF51206; 3.
DR   SUPFAM; SSF52151; SSF52151; 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..1515
FT                   /note="Lysophospholipase nte1"
FT                   /id="PRO_0000295326"
FT   TOPO_DOM        1..59
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        81..102
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        124..1515
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          1212..1376
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          278..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          519..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          617..639
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1216..1221
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1243..1247
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1363..1365
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        539..554
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..580
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1245
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1363
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   BINDING         670..789
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="1"
FT   BINDING         835..955
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="2"
SQ   SEQUENCE   1515 AA;  167560 MW;  BB4572D40BEB6275 CRC64;
     MESLSNLGNA MSSVLSETTS TTATAILADP TEALSSVVAL ASDAVSKATS DVVPEHTPTS
     WFTIILWLLH RISSVLYFVI KLTTITTPTF LFNIFSTSLT VTMNATTLVL IMLFMMAGVT
     WVVRYRYLNM YSRLPPEPQR KEPAVDLFPE TQEEGVKSGL ASYFDEFLSA IKIFGYLERP
     VFHELTRSMQ TRKLIAGETL NLEEEQGFCL VVDGMVEIFV KSARDGRRSS SGPSFESDDE
     EGFAPGRQRY QLLTEVRNGA PMSSLFSIMS LFTEDIQMHD TDDDDSPDPT PSAPGTAMPG
     YPMNANFQQS NDTLPSIPGT PLSDNHVMQR GMASAESLTM SPLAHDSSRI PSLSLVNTRP
     AVPRRPVPKR LNTTSAHPDI IARATVDTTI AIIPASAFRR LIKIYPKATA HIVHVILSRF
     QRVTLATAYN YLGLSGEVLQ MERNILKHTV RQLPNHLRGD ALDRLKEKFK RERERIGEKE
     VEKGIALHNA HAARRRRSAA SLRKEVALQA YSKRRQSIVT ATPAFGTRRE RPSPDMPSPG
     DLLTNTQQLK SGPASQLDLA RDATSPRPQR NLSPFSTPRN AHVSLDTREA LDEDDMFRES
     VLECMFRAIG LTGNGSVNPD STQASPRFVP TDQRRSRGGP GHTAFGFMDA FDPFDNDTES
     VTSCGFSSSS PVPNPQLLAH DMKDEVEIVF FPKGSVLVEQ GERNPGLYYV IDGFLDICVP
     GDDSSHDLLQ SSAKVDHGHD SATGADAFGA NSSRFPEPNM NNNFGAEQKK GKQGRRSVAL
     IKPGGLAGYV GTISSYRSFI DVVARTDVCV GFLPLASIDR IVDRYPIVML TMAKRLTELL
     PRLLLHIDFA LEWVQVNSGQ VLFREGDESE AIYLVLNGRL RLVEDQKDGG MNVKAEFGQG
     ESIGELEVLT ESARTGTLHA IRETELVKFP RTLFNSLAQE HPNITIKISK IIAARMRAFI
     DDPSRMGLKD NVVRSYKSSS TLNLRTVAIL PVTAGVPVVE FGNRLMNALS QVGPPNGATC
     LNQAAILNHL GKLAFNRMGK LKLSQYLADL EEKYGLVVYV ADTNVNTPWT QTCITQADCL
     LFVGLADSSP EIGEYERFML GMKSTARKIL VLVHQERYSN PGLTRQWLKN RMWINGGHFH
     VQMAYTSNTV PIHPPTKRFG PSLKQRVQIL QAEIQKYTSR KVRHVPFYSP DAPFKGDFHR
     LARRLCGKSV GLVLGGGGAR GIAHVGIIRA MEEAGIPIDM VGGTSIGAFI GGLYARHADV
     VPIFGLAKKF AGRMASMWRF AFDLTYPSAS YTTGHEFNRG IFKTFGKTQI EDFWLEYYCN
     TTNISKSRVE FHTSGYAWRY IRASMSLAGL LPPLCDEGSM LLDGGYIDNL TVSRMKSLGS
     DVIFAVDVGS LDDNTPQAFG DSLSGVWAFF NRWNPFSSVP NPPTLAEIQA RLAYVSSVGE
     LERAKTMPGC IYMRPPIDDY GTLDFGKFDE IYGVGYKYGQ EFLQKLREQG VLPLVEETEA
     KKALRRTMAP RRASI