ID   NTE1_PICST              Reviewed;        1546 AA.
AC   A3LYZ4;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 80.
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=PICST_33358;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(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}.
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DR   EMBL; CP000501; ABN68251.2; -; Genomic_DNA.
DR   RefSeq; XP_001386280.2; XM_001386243.1.
DR   AlphaFoldDB; A3LYZ4; -.
DR   SMR; A3LYZ4; -.
DR   STRING; 4924.XP_001386280.2; -.
DR   EnsemblFungi; ABN68251; ABN68251; PICST_33358.
DR   GeneID; 4840528; -.
DR   KEGG; pic:PICST_33358; -.
DR   eggNOG; KOG2968; Eukaryota.
DR   HOGENOM; CLU_000960_1_1_1; -.
DR   InParanoid; A3LYZ4; -.
DR   OMA; FTMNFTT; -.
DR   OrthoDB; 253518at2759; -.
DR   Proteomes; UP000002258; Chromosome 7.
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; -; 2.
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; 1.
DR   SUPFAM; SSF51206; SSF51206; 2.
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..1546
FT                   /note="Lysophospholipase NTE1"
FT                   /id="PRO_0000295329"
FT   TOPO_DOM        1..45
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        67..81
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        103..1546
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          1239..1403
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1243..1248
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1270..1274
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1390..1392
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1272
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1390
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   BINDING         689..820
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="1"
FT   BINDING         816..965
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="2"
SQ   SEQUENCE   1546 AA;  171904 MW;  844221F7DC95189F CRC64;
     MKDSTEALNS IAFAVDTTLS SILPSSLAPP SAPPATSSFL KSIWYAFWWL WSMVVFKIMN
     IILLYIPSKI MNALSINFEI TLNLSSILVA LSAIITVCFL VVRYKYLTGY SKDTSDRKTK
     GKVNPSASNI NLKNQSLDYV DQKKGHRRTT NYLDEFLSAI KVFGYLEKSV FHELTKNMTT
     QKLSHDEILY LDEKLGFSIV VEGVMQVYTR ITENSNVSGG FDPDDDNELN YEKDDVLIIG
     NQRYQLLNEV KSGAPLSSLV SVLDLLKPVD SEDSTSDMLH SFNISDDDNI SKIPEISPIS
     LPFQGIHAGA KDDSVPPSPI IRPSKTKQLY PEIVARPKSR PHKEHTGHHL HHVHHSGATI
     AIIPYSAFQR VQSKYPKATS HIVTMVLARL YKVTFNTIHD YLGLTKEIME SEVKLNTTSS
     VRGANLPGYL FDGLLDKIYG ANGINEASLS RKSDFQRASS VNLNKQKTTL CDAKSSRYVL
     LDSRLKSTHP GDLLSSVPLS RRSDYYQTHS HPLSADDPLV RSAFPSSKTL SSLSSPTSNL
     KRASSNLKFE NIRDRSFSDD REETEETSLR IAVVESIFKI LGISEKSTAM RNLSSFNSGR
     SSVSSSIVGL SNLMSADDKF DTNAARVRFD SYNGFSSTAT SISRSSTPIK FYNTINQNQL
     HNHHMGDSVS GINISTLSRQ HQANRNSSPT EFNFANVKSD FAKCLEIKSY GPNTTIVEQG
     SFNSGLYYVI DGSLDVLYRP SNHGEPSSNR EDNLKKLYSV KSGGVAGYLS SVVGFRSLVT
     IRTSKKRGVI VAHISKSDYS KLMDRYYFLQ LPVATKLKKL LSPQILTIDY ALEWCHIPAG
     GVLCSQGDLA NGFHIVLSGR FRVVRNKSDR YQGNTSDDDI LGFSDTSMDC SPSSDINNED
     LEVLGEYGHG ESIGEVEVLT ASRRTNSLIA VRDSETARIP RTLFEMLSLS NPSIMVKVSR
     IVASKVVYKD VLDQSSRNST LIPSSTASHI SNDYKTITIL PTVSGLPVRE FADKLVSALK
     AIGRNVIALD QASTLTHLGR HAFDERLAQL KLSGYFAYLE EEYETIVYIC DTPLKSNWTS
     TCISQGDCIL LLADAEDDVV ATGIGDYERL LINLKTMART DLCLLHPEKY VEPGSTSIWL
     KNRIWVQGHH HIEMEIIRKK DENSVKKRPN IISELASKIG SKTNPSIKST LEDVRLKAIS
     SFVKLNTSFV HSDRYKAVQP HKNDFLRLAR ILSNEAVGLV LGGGGSRGIS HVGIVTALER
     HGIPVDLIGG TSIGSLVGGL YAKDYNIVSI YGRAKKFSKR VASLWRSVFD LTYPVTSYIT
     GYEFNRGIWK IFGFTEIEDF WIRYFCNTTN ITNSTMDIHE SGYSWRFIRA SMSLAGLLPP
     IAFQGCMLLD GGYLDNLPVS EMKKKGAKYI IAVDVGSADD RTPMNYGDTL SGFWVLFNRW
     NPFSKHPNVP NMMDIQMRLA YVASVNALEA AKKTNGVIYL RPPIDNYATL DFAKFDEIYH
     VGLNYADKLF SSWSKNGKLP AIAGMVDKAK IKSGDDKKVL YRRNSI