ID   NTE1_PHANO              Reviewed;        1512 AA.
AC   Q0UJ42;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   24-JAN-2024, entry version 84.
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=SNOG_08222;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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=EAT84498.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH445336; EAT84498.2; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001798544.1; XM_001798492.1.
DR   AlphaFoldDB; Q0UJ42; -.
DR   SMR; Q0UJ42; -.
DR   STRING; 321614.Q0UJ42; -.
DR   GeneID; 5975442; -.
DR   KEGG; pno:SNOG_08222; -.
DR   VEuPathDB; FungiDB:JI435_082220; -.
DR   eggNOG; KOG2968; Eukaryota.
DR   InParanoid; Q0UJ42; -.
DR   OMA; SSGYVWR; -.
DR   OrthoDB; 5303733at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
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:0046486; P:glycerolipid metabolic process; IEA:UniProt.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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; 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.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Membrane; Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN           1..1512
FT                   /note="Lysophospholipase NTE1"
FT                   /id="PRO_0000295327"
FT   TOPO_DOM        1..48
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        70..83
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        105..1512
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          1209..1373
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          204..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          534..556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          740..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1213..1218
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1240..1244
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1360..1362
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        268..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..551
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1242
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1360
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   BINDING         669..793
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="1"
FT   BINDING         830..950
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="2"
SQ   SEQUENCE   1512 AA;  166935 MW;  330CE41E31FC0E28 CRC64;
     MAAPDAMTSL VKSSVALLSS AHESLPTSLA AMKTAETAPS STFGILGRVI LSILSVLPTL
     LFWVSYTLPT WLFTLFSMSL TFTMNFTTLM LVLVFVVSTI SYFVRYRYLT MYARLPPEPQ
     REEPQVEVFP ESQEGDSKRG LSNYLDEFLS AIKVFGYLER PVFHELTRTM QTRRLAAGET
     ILLEEEKGFC LVVDGLVQIF VKSNREESDS DEDDGELQGE SGGGSAQAHR QGYQLLTEVK
     NGAPMSSLFS ILSLFTEDVK LRHDEDSGPS SSTPMSPQHR PSMTRNSSFN MDDSRPETPI
     EAQEATIRRR RTSALASPTA GGRLSNVPPL SLDTDGFNDN FKHSKQRRSP SRSTKPKSAH
     PDIVARATVD TTIAIIPATA FRRLTRIYPK ATAHIVQVIL TRLQRVTLAT SHAYLSLTNE
     VLRTEKLMNK YTTYDLPGFL RDAPLERLKE KFTKETERLG SDEGMKGIAL HNPGAGRRRR
     TSVSIRSSTA AQARLAAARG TSIGSNVEAI SRLTSPEQGM RNDRISAGDL LTNTQMSRGT
     GRSGRSSFSQ PYQHDVRRDA RTPLDASGFN PFASPSMRPN LHRQESIDEA TVFRESVLGC
     MFKAIGLTSP ENPVPRPAAS VEQSPRLVSF DAKRQKAIFT SAFGFMDPYE ASRDGDADSV
     ASASNLSTLS ASGNGNLLEE VVNDVEIVFF PKDAVLVEQG ERNPGLYYVI DGFLDVSVAV
     EEDSSESNVL GTLPTGPAVT EDDLFGPPLQ PTATNTSLRN GENSKKKRSR KSLFMTRPGG
     LAGYLGTVSS NRSFVDVTAK TDVYVGFLPR ASIERIVERY PVVLLTMAKR LTTLLPRLIQ
     HIDFALEWVQ VNAGQVIYNQ GEESDAIYIV LNGRLRAIKD AENGKVTVIG EYGQGDSVGE
     LEVLTETARP GSLHAIRDTE LAKFPKTLFN SLALEHPGIT IKISKIIASR MRALVDDPLH
     EQSKERSNKA TRTNVSSTVN LRTVAILPVT AGIPVVDFAS RLMNALNQIG VPRGVVSLNQ
     AAILNHLGRH AFNRMGKLKL SQYLADLEEK YGMVLYVADT PVKSPWTQTC ISQADCILLV
     GLAESSPNIG EYERFLLTTK TTARKELVLL HAERYCPSGL TRKWLRNWPW INGSHHHMQM
     SFRATAEPVH QTGRRLGNAI KQRVQVIQAE IQKYTSKRVR QTPLYSADTP FKGDFHRLAR
     RLCGKSVGLV LGGGGARGIS QIGIIRALEE AGIPIDIVGG TSIGSFIGAL YAWDADVVPM
     YGRAKKFSGR MGSMWRFALD LTYPSASYTT GHEFNRGIFK TFGNSQIEDF WLEFYCNTTN
     ISKSRSEIHT SGYVWRYVRA SMSLAGLLPP LCDNGSMLLD GGYIDNLTVA HMKSLGADVI
     FAIDVGSLDE DTPQAFGDSL SGFWATFNRW NPFSTHANPP TLSEIQSRLA YVSSIDALER
     AKNTPGCRYM RPPIDPYGTL DFAKFEEIYE VGYKYGKGFL AQLREQGVLP VTEETEKEKN
     LRRTMAPRRA SI
//