ID   NTE1_CHAGB              Reviewed;        1521 AA.
AC   Q2H0D3;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 77.
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=CHGG_04763;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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=EAQ88144.1; Type=Frameshift; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH408032; EAQ88144.1; ALT_FRAME; Genomic_DNA.
DR   RefSeq; XP_001223977.1; XM_001223976.1.
DR   AlphaFoldDB; Q2H0D3; -.
DR   SMR; Q2H0D3; -.
DR   STRING; 38033.XP_001223977.1; -.
DR   EnsemblFungi; EAQ88144; EAQ88144; CHGG_04763.
DR   GeneID; 4392000; -.
DR   eggNOG; KOG2968; Eukaryota.
DR   HOGENOM; CLU_000960_1_1_1; -.
DR   InParanoid; Q2H0D3; -.
DR   OrthoDB; 253518at2759; -.
DR   Proteomes; UP000001056; Unassembled WGS sequence.
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; IEA:UniProtKB-EC.
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; 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; 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.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Membrane; Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN           1..1521
FT                   /note="Lysophospholipase NTE1"
FT                   /id="PRO_0000295316"
FT   TOPO_DOM        1..50
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        72..96
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        118..1521
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          1217..1381
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          280..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          315..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          738..768
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1221..1226
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1248..1252
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1368..1370
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        315..335
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        738..759
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1250
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1368
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         837..957
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="2"
SQ   SEQUENCE   1521 AA;  167339 MW;  4120EA5A39BDAFF2 CRC64;
     MDVVNSTARA AVTSATAVTA VTGTGDRHPN PLSSAVAAAS DVANAHGSSS WLGLFARVVL
     WLLQFVSMVL YYAIKLATIS VPTLLYTLFS TSLTVTMNAT TLMLIVAAMI GAISWVVRYR
     YLNMYSRLPP EPQRKEPDVD LFPDTHEEGI KSGLSNYFDE FLSAIKIFGY LERPVFHELT
     RSMQTRKLIA GESFNLEEEK GFCLVVDGLV EIFVKSSSYN RRYPHGPYFS PNSEAPSSDD
     EHPAPGQQRY QLLTEVRNGA PMSSLFSIMS LFTEDVPLRH ADEDNSEPGT TTHSGLFPNY
     PASADFRKSR VRMDSVPNTP QMDASASSSA NNLPGQLDRG LPHVPPISLD GTGFSKPQRP
     VPKRSNTTSA HPDIIARATV DTTVAIIPAS AFRRLIKIYP KATAHIVHVI LSRFQRVTLA
     TAYNYLGLTN EVLQIERQML KYTTQQLPNH LRGDALDRLK EKFKREVERM GEEDDVSKGI
     ALHNARAGRR RRSTATLRKE AALQAFSKQR NISSMSGSSL AIPNAGDLVT HLQQSRGGGN
     RAQSVAFTDG PSPHLDVERE AVSPLAQRTF DPFVTPRSIH VALEKRETLD EDNLFRESIL
     ECMFRSIGLT GSGGSNKDAD SNQASPRLIS FDQRRQKALY TNHAFGFMDG LDGSADGDTE
     SITSAGLSLP ASPNPQFLAQ EMRDEMEIVF FPKGSVLVEQ GERNPGLYYV VDGFLDICTQ
     EDAAASDVVH PTSRTSLHAM DSAQSIRSPQ RSPQPFAESM RSGNKVDDAE IKSKPNRRSV
     ALIKPGGLAG YVGTISSYRS FIEVVAKTDV YVGFLPLTSI ERIVDRYPIV LLTMAKRLTN
     LLPRLILHID FALEWLQVNA GQVIFHEGDE SEAIYIVLNG RLRLVEDRKD GGMNVKAEYG
     QGESIGELEV LTETSRSGTL HAIRDTELVK FPRTLFNSLA QEHPNITIKI SKIIASRMRA
     LIDDPSTMLG IKDSSGRSSI NKSSTTLNLR TVAVLPVSAG VPVVEFSNRL LSALTEVGAP
     NGATSLNSAA VLNHLGKHAF NRMGKLKLSQ YLADLEEKYG LVIYVADTNV NAPWTQTCVA
     QADCVLMVGL ADGSPEIGEY ERFMLGMKST ARKILVLLHQ ERYSNSGLTR KWLKNRVWIN
     GGHFHVQMTY SPNAVPIHPP AKPSGPTLRE RVQILQAEIQ KYTSRKVRHS PFYSPDAPFK
     GDFHRLARRL CGKSVGLVLG GGGARGIAQI GIIRAMQEAG IPIDIVGGTS IGAFIGALYA
     RHADFVPIVN AAKKFSGRMA SMWRFALDLT YPSASYTTGH EFNRGIFKAF GNTQIEDFWL
     DYYCNTTNIS KSRAEFHTSG YAWWYVRASM SLAGLLLPLC DEGSMLLDGG YVDNLTVSHM
     KSLGSDVIFA VDVGALDDNT PQAFGDSLSG MWAFFNRWNP FSSVANPPTL AEIQARLAYV
     SSVDALERAK TLPGCIYMRP PIEEYGTLDF GKFMEIYGVG YKYGQEFLAK LRERGGVLPI
     GEEMGGKKGL RRTMAPRRAS I