PLPL6_PONAB
ID PLPL6_PONAB Reviewed; 1365 AA.
AC Q5RDS0;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Patatin-like phospholipase domain-containing protein 6 {ECO:0000305};
DE AltName: Full=Neuropathy target esterase;
DE EC=3.1.1.5 {ECO:0000250|UniProtKB:Q8IY17};
GN Name=PNPLA6; Synonyms=NTE;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phospholipase B that deacylates intracellular
CC phosphatidylcholine (PtdCho), generating glycerophosphocholine
CC (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of
CC PtdCho. Catalyzes the hydrolysis of several naturally occurring
CC membrane-associated lipids. Hydrolyzes lysophospholipids and
CC monoacylglycerols, preferring the 1-acyl to the 2-acyl isomer. Does not
CC catalyze hydrolysis of di- or triacylglycerols or fatty acid amides.
CC {ECO:0000250|UniProtKB:Q8IY17}.
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 Evidence={ECO:0000250|UniProtKB:Q3TRM4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC Evidence={ECO:0000250|UniProtKB:Q3TRM4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:72998;
CC Evidence={ECO:0000250|UniProtKB:Q3TRM4,
CC ECO:0000250|UniProtKB:Q8IY17};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000250|UniProtKB:Q3TRM4,
CC ECO:0000250|UniProtKB:Q8IY17};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-
CC octadecenoate + H(+) + sn-glycerol 3-phosphocholine;
CC Xref=Rhea:RHEA:40807, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:28610, ChEBI:CHEBI:30823;
CC Evidence={ECO:0000250|UniProtKB:Q8IY17};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40808;
CC Evidence={ECO:0000250|UniProtKB:Q8IY17};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoylglycerol + H2O = glycerol + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:39959, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:69081; Evidence={ECO:0000250|UniProtKB:Q8IY17};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39960;
CC Evidence={ECO:0000250|UniProtKB:Q8IY17};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hexadecanoylglycerol + H2O = glycerol + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:39963, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:75455; Evidence={ECO:0000250|UniProtKB:Q8IY17};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39964;
CC Evidence={ECO:0000250|UniProtKB:Q8IY17};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75342; Evidence={ECO:0000250|UniProtKB:Q8IY17};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488;
CC Evidence={ECO:0000250|UniProtKB:Q8IY17};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:38491, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:73990; Evidence={ECO:0000250|UniProtKB:Q8IY17};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492;
CC Evidence={ECO:0000250|UniProtKB:Q8IY17};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+);
CC Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392;
CC Evidence={ECO:0000250|UniProtKB:Q8IY17};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133;
CC Evidence={ECO:0000250|UniProtKB:Q8IY17};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphate + H2O = H(+) +
CC hexadecanoate + sn-glycerol 3-phosphate; Xref=Rhea:RHEA:49092,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57518, ChEBI:CHEBI:57597;
CC Evidence={ECO:0000250|UniProtKB:Q3TRM4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49093;
CC Evidence={ECO:0000250|UniProtKB:Q3TRM4};
CC -!- ACTIVITY REGULATION: Inhibited by a series a OPs such as mipafox (MPX),
CC phenyl saligenin phosphate (PSP), phenyl dipentyl phosphinate (PDPP),
CC diisopropyl fluorophosphate and paraoxon.
CC {ECO:0000250|UniProtKB:Q8IY17}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8IY17}; Single-pass type III membrane protein
CC {ECO:0000250|UniProtKB:Q8IY17}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q8IY17}.
CC -!- SIMILARITY: Belongs to the NTE family. {ECO:0000305}.
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DR EMBL; CR857832; CAH90087.1; -; mRNA.
DR RefSeq; NP_001124999.1; NM_001131527.1.
DR AlphaFoldDB; Q5RDS0; -.
DR SMR; Q5RDS0; -.
DR STRING; 9601.ENSPPYP00000010625; -.
DR GeneID; 100453292; -.
DR KEGG; pon:100453292; -.
DR CTD; 10908; -.
DR eggNOG; KOG2968; Eukaryota.
DR InParanoid; Q5RDS0; -.
DR OrthoDB; 253518at2759; -.
DR Proteomes; UP000001595; Unplaced.
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; ISS:UniProtKB.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 3.
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; 3.
DR Pfam; PF01734; Patatin; 1.
DR SMART; SM00100; cNMP; 3.
DR SUPFAM; SSF51206; SSF51206; 3.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 3.
DR PROSITE; PS51635; PNPLA; 1.
DR PROSITE; PS01237; UPF0028; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1365
FT /note="Patatin-like phospholipase domain-containing protein
FT 6"
FT /id="PRO_0000292201"
FT TOPO_DOM 1..50
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..1365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 971..1137
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 343..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1296..1365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 975..980
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1002..1006
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1124..1126
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 356..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..391
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1004
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1124
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT BINDING 186..313
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="1"
FT BINDING 502..624
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="2"
FT BINDING 620..740
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="3"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY17"
FT MOD_RES 352
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY17"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY17"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY17"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY17"
FT MOD_RES 455
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY17"
FT CARBOHYD 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1365 AA; 149750 MW; A700733C7A74EB39 CRC64;
MGTSSHGLAT NSSGAKVAER DGFQDVPAPG EGAAGRICGA QPVPFVPQVL GVMIGAGVAV
VVTAVLILLV VRRLRVPKTP APDGPRYRFR KRDKVLFYGR KIMRKVSQST SSLVDTSVSA
TSRPRMKKKL KMLNIAKKIL RIQKETPTLQ RKEPPPAVLE ADLTEGDLAN SHLPSEVLYM
FKNVRVLGHF EKPLFLELCR HMVFQRLGQG DYVFRPGQPD ASIYVVQDGL LELCLPGPDG
KECVVKEVVP GDSVNSLLSI LDVITGHQHP QRTVSARAAR DSTVLRLPVE AFSAVFAKYP
ESLVRVVQII MVRLQRVTFL ALHNYLGLTN ELFSHEIQPL RLFPSPGLPT RTSPVRGSKR
MVSTSATDEP RETPGRPPDP TGAPLPGPTG DPVKPTSLET PSAPLLSRCV SMPGDISGLQ
GGPRSDFDMA YERGRISVSL QEGASGGSLA APARTPTQEP REQPAGACEY SYCEDESATG
GCPFGPYQGR QTSSIFEAAK RELAKLMRIE DPSLLNSRVL LHHAKAGTII ARQGDQDVSL
HFVLWGCLHV YQHMIDKAED VCLFVAQPGE LVGQLAVLTG EPLIFTLRAQ RDCTFLRISK
SDFYEIMRAQ PSVVLSAAHT VAARMSPFVR QMDFAIDWTA VEAGRALYRQ GDRSDCTYIV
LNGRLRSVIQ RGSGKKELVG EYGRGDLIGV VEALTRQPRA TTVHAVRDTE LAKLPEGTLG
HIKRRHPQVV TRLIHLLSQK ILGNLQQLQG PFPGSGLGVP PHSELTNPAS NLATVAVLPV
CAEVPMVAFT LELQHALQAI GPTLLLNSDI IRARLGASAL DSIQEFRLSG WLAQQEDAHR
IVLYQTDASL TPWTVRCLRQ ADCILIVGLG DQEPTLGQLE QMLENTAVRA LKQLVLLHRE
EGAGPTRTVE WLNMRSWCSG HPHLRCPRRL FSRRSPAKLH ELYEKVFSRR ADRHSDFSRL
ARVLTGNTIA LVLGGGGARG CSHIGVLKAL EEAGVPVDLV GGTSIGSFIG ALYAEERSAS
RTKQRAREWA KSMTSVLEPV LDLTYPVTSM FTGSAFNRSI HRVFQDKQIE DLWLPYFNVT
TDITASAMRV HKDGSLWRYV RASMTLSGYL PPLCDPKDGH LLMDGGYINN LPADIARSMG
AKTVIAIDVG SQDETDLSTY GDSLSGWWLL WKRLNPWADK VKVPDMAEIQ SRLAYVSCVR
QLEVVKSSSY CEYLRPPIDC FKTMDFGKFD QVYDVGYQYG KAVFGGWSRG NVIEKMLTDR
RSTDLNESRR ADVLAYPSSG FTDLAEIVSR IEPPTSYVSD GCADGEESDC LTEYEEDAGP
DCSRDEGGSP EGASPSTASE MEEEKSILRQ RRCLPQEPPG SATDA
