ID PLPL6_MOUSE Reviewed; 1355 AA.
AC Q3TRM4; Q7TQD6; Q9R114;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 27-MAR-2024, entry version 139.
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:0000269|PubMed:18086666, ECO:0000305|PubMed:16963094};
GN Name=Pnpla6; Synonyms=Nte;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ;
RX PubMed=10640712; DOI=10.1016/s0925-4773(99)00239-7;
RA Moser M., Stempfl T., Li Y., Glynn P., Buttner R., Kretzschmar D.;
RT "Cloning and expression of the murine sws/NTE gene.";
RL Mech. Dev. 90:279-282(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Bone;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=12640454; DOI=10.1038/ng1131;
RA Winrow C.J., Hemming M.L., Allen D.M., Quistad G.B., Casida J.E.,
RA Barlow C.;
RT "Loss of neuropathy target esterase in mice links organophosphate exposure
RT to hyperactivity.";
RL Nat. Genet. 33:477-485(2003).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16963094; DOI=10.1016/j.taap.2006.08.002;
RA Read D.J., Langford L., Barbour H.R., Forshaw P.J., Glynn P.;
RT "Phospholipase B activity and organophosphorus compound toxicity in
RT cultured neural cells.";
RL Toxicol. Appl. Pharmacol. 219:190-195(2007).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18086666; DOI=10.1074/jbc.m709598200;
RA Kienesberger P.C., Lass A., Preiss-Landl K., Wolinski H., Kohlwein S.D.,
RA Zimmermann R., Zechner R.;
RT "Identification of an insulin-regulated lysophospholipase with homology to
RT neuropathy target esterase.";
RL J. Biol. Chem. 283:5908-5917(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Phospholipase B that deacylates intracellular
CC phosphatidylcholine (PtdCho), generating glycerophosphocholine
CC (GroPtdCho) (PubMed:18086666) (Probable). This deacylation occurs at
CC both sn-2 and sn-1 positions of PtdCho. Catalyzes the hydrolysis of
CC several naturally occurring membrane-associated lipids. Hydrolyzes
CC lysophospholipids and monoacylglycerols, preferring the 1-acyl to the
CC 2-acyl isomer. Does not catalyze hydrolysis of di- or triacylglycerols
CC or fatty acid amides (By similarity). {ECO:0000250|UniProtKB:Q8IY17,
CC ECO:0000269|PubMed:18086666, ECO:0000305|PubMed:16963094}.
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:0000269|PubMed:18086666, ECO:0000305|PubMed:16963094};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC Evidence={ECO:0000269|PubMed:18086666};
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:0000269|PubMed:18086666};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000269|PubMed:18086666};
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:0000269|PubMed:18086666};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49093;
CC Evidence={ECO:0000269|PubMed:18086666};
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 -!- 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:0000269|PubMed:16963094}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:18086666};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16963094}; Single-pass type III membrane protein
CC {ECO:0000305|PubMed:16963094}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q3TRM4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TRM4-2; Sequence=VSP_026390;
CC Name=3;
CC IsoId=Q3TRM4-3; Sequence=VSP_026390, VSP_026391;
CC Name=4;
CC IsoId=Q3TRM4-4; Sequence=VSP_026392, VSP_026393;
CC -!- TISSUE SPECIFICITY: Expressed in brain, testes and kidney (at protein
CC level) (PubMed:12640454). Expressed ubiquitously in brain of young mice
CC (PubMed:10640712). Reaching adulthood, there is a most prominent
CC expression in Purkinje cells, granule cells and pyramidal neurons of
CC the hippocampus and some large neurons in the medulla oblongata,
CC nucleus dentatus and pons (PubMed:10640712).
CC {ECO:0000269|PubMed:10640712, ECO:0000269|PubMed:12640454}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryonic respiratory system,
CC different epithelial structures and strongly in the spinal ganglia,
CC during the development. {ECO:0000269|PubMed:10640712}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Embryonically lethal. At 9 dpc, embryos are
CC smaller, and their development is delayed (PubMed:12640454). At 10-11
CC dpc, the development is arrested with signs of resorption
CC (PubMed:12640454). Heterozygous mice have lower catalytic activity
CC towards the synthetic compound phenyl valerate in the brain and show
CC increased motor activity (PubMed:12640454).
CC {ECO:0000269|PubMed:12640454}.
CC -!- MISCELLANEOUS: Specific chemical modification by some organophosphorus
CC (OP) compounds leads to distal axonopathy in humans and chicken
CC (Probable). The effects of these compounds in mice appear to be less
CC severe (Probable). Mice treated with 1 mg/kg/body weight of ethyl
CC octylphosphonofluoridate (EOPF) have elevated motor activity in the
CC long term (PubMed:12640454). Higher doses result in increased mortality
CC (PubMed:12640454). {ECO:0000269|PubMed:12640454,
CC ECO:0000305|PubMed:12640454}.
CC -!- SIMILARITY: Belongs to the NTE family. {ECO:0000305}.
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DR EMBL; AF173829; AAD51700.1; -; mRNA.
DR EMBL; AK162641; BAE37004.1; -; mRNA.
DR EMBL; AC170806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC054789; AAH54789.1; -; mRNA.
DR EMBL; BC056999; AAH56999.1; -; mRNA.
DR CCDS; CCDS40206.1; -. [Q3TRM4-3]
DR RefSeq; NP_001116290.2; NM_001122818.2.
DR RefSeq; NP_056616.2; NM_015801.2. [Q3TRM4-3]
DR RefSeq; XP_006508887.1; XM_006508824.3.
DR RefSeq; XP_006508888.2; XM_006508825.3.
DR RefSeq; XP_006508893.2; XM_006508830.3.
DR RefSeq; XP_017168379.1; XM_017312890.1.
DR AlphaFoldDB; Q3TRM4; -.
DR SMR; Q3TRM4; -.
DR BioGRID; 206099; 6.
DR STRING; 10090.ENSMUSP00000146680; -.
DR ChEMBL; CHEMBL3259506; -.
DR SwissLipids; SLP:000001979; -.
DR GlyConnect; 2555; 1 N-Linked glycan (1 site).
DR GlyCosmos; Q3TRM4; 1 site, 1 glycan.
DR GlyGen; Q3TRM4; 5 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (4 sites).
DR iPTMnet; Q3TRM4; -.
DR PhosphoSitePlus; Q3TRM4; -.
DR SwissPalm; Q3TRM4; -.
DR EPD; Q3TRM4; -.
DR jPOST; Q3TRM4; -.
DR MaxQB; Q3TRM4; -.
DR PaxDb; 10090-ENSMUSP00000106699; -.
DR PeptideAtlas; Q3TRM4; -.
DR ProteomicsDB; 289688; -. [Q3TRM4-1]
DR ProteomicsDB; 289689; -. [Q3TRM4-2]
DR ProteomicsDB; 289690; -. [Q3TRM4-3]
DR ProteomicsDB; 289691; -. [Q3TRM4-4]
DR Pumba; Q3TRM4; -.
DR Antibodypedia; 2222; 285 antibodies from 30 providers.
DR DNASU; 50767; -.
DR Ensembl; ENSMUST00000004681.14; ENSMUSP00000004681.8; ENSMUSG00000004565.16. [Q3TRM4-3]
DR Ensembl; ENSMUST00000111070.4; ENSMUSP00000106699.3; ENSMUSG00000004565.16. [Q3TRM4-3]
DR GeneID; 50767; -.
DR KEGG; mmu:50767; -.
DR UCSC; uc009krr.1; mouse. [Q3TRM4-3]
DR UCSC; uc009krs.1; mouse. [Q3TRM4-2]
DR UCSC; uc009krt.1; mouse. [Q3TRM4-4]
DR UCSC; uc009kru.1; mouse. [Q3TRM4-1]
DR AGR; MGI:1354723; -.
DR CTD; 10908; -.
DR MGI; MGI:1354723; Pnpla6.
DR VEuPathDB; HostDB:ENSMUSG00000004565; -.
DR eggNOG; KOG2968; Eukaryota.
DR GeneTree; ENSGT00940000159130; -.
DR HOGENOM; CLU_000960_1_0_1; -.
DR InParanoid; Q3TRM4; -.
DR OMA; CIEDLWI; -.
DR OrthoDB; 5303733at2759; -.
DR PhylomeDB; Q3TRM4; -.
DR TreeFam; TF300519; -.
DR Reactome; R-MMU-6814848; Glycerophospholipid catabolism.
DR BioGRID-ORCS; 50767; 6 hits in 79 CRISPR screens.
DR PRO; PR:Q3TRM4; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q3TRM4; Protein.
DR Bgee; ENSMUSG00000004565; Expressed in retinal neural layer and 259 other cell types or tissues.
DR ExpressionAtlas; Q3TRM4; baseline and differential.
DR Genevisible; Q3TRM4; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; ISS:MGI.
DR GO; GO:0004622; F:lysophospholipase activity; IDA:UniProtKB.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
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 CDD; cd07225; Pat_PNPLA6_PNPLA7; 1.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
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; IPR001423; LysoPLipase_patatin_CS.
DR InterPro; IPR002641; PNPLA_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR PANTHER; PTHR14226:SF26; PATATIN-LIKE PHOSPHOLIPASE DOMAIN-CONTAINING PROTEIN 6; 1.
DR Pfam; PF00027; cNMP_binding; 3.
DR Pfam; PF01734; Patatin; 1.
DR SMART; SM00100; cNMP; 3.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 3.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 3.
DR PROSITE; PS51635; PNPLA; 1.
DR PROSITE; PS01237; UPF0028; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW Lipid degradation; Lipid metabolism; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..1355
FT /note="Patatin-like phospholipase domain-containing protein
FT 6"
FT /id="PRO_0000292200"
FT TOPO_DOM 1..43
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..1355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 961..1127
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 338..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1286..1355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 965..970
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 992..996
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1114..1116
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 349..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 994
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1114
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT BINDING 179..306
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="1"
FT BINDING 492..614
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="2"
FT BINDING 610..730
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="3"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY17"
FT MOD_RES 345
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY17"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY17"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY17"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY17"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..41
FT /note="MGTPSHELNTTSSGAEVIQKTLEEGLGRRICVAQPVPFVPQ -> MEAPLQT
FT GM (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10640712,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_026390"
FT VAR_SEQ 448
FT /note="R -> RTPTQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10640712"
FT /id="VSP_026391"
FT VAR_SEQ 1123..1169
FT /note="ADIARSMGAKTVIAIDVGSQDETDLSTYGDSLSGWWLLWKRLNPWAD -> G
FT KWLPTHICMDTYHQTHAHTDFCTCRLEGTGLYEWRSSRGHTQLCTEL (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026392"
FT VAR_SEQ 1170..1355
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026393"
FT CONFLICT 240
FT /note="E -> K (in Ref. 1; AAD51700)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1355 AA; 149537 MW; 813263C6A82083ED CRC64;
MGTPSHELNT TSSGAEVIQK TLEEGLGRRI CVAQPVPFVP QVLGVMIGAG VAVLVTAVLI
LLVVRRLRVQ KTPAPEGPRY RFRKRDKVLF YGRKIMRKVS QSTSSLVDTS VSTTSRPRMK
KKLKMLNIAK KILRIQKETP TLQRKEPPPS VLEADLTEGD LANSHLPSEV LYMLKNVRVL
GHFEKPLFLE LCRHMVFQRL GQGDYVFRPG QPDASIYVVQ DGLLELCLPG PDGKECVVKE
VVPGDSVNSL LSILDVITGH QHPQRTVSAR AARDSTVLRL PVEAFSAVFT KYPESLVRVV
QIIMVRLQRV TFLALHNYLG LTNELFSHEI QPLRLFPSPG LPTRTSPVRG SKRVVSTSGT
EDTSKETSGR PLDSIGAPLP GPAGDPVKPT SLEAPPAPLL SRCISMPVDI SGLQGGPRSD
FDMAYERGRI SVSLQEEASG GPQTASPREL REQPAGACEY SYCEDESATG GCPFGPYQGR
QTSSIFEAAK RELAKLMRIE DPSLLNSRVL LHHAKAGTII ARQGDQDVSL HFVLWGCLHV
YQRMIDKAEE VCLFVAQPGE LVGQLAVLTG EPLIFTLRAQ RDCTFLRISK SHFYEIMRAQ
PSVVLSAAHT VAARMSPFVR QMDFAIDWTA VEAGRALYRQ GDRSDCTYIV LNGRLRSVIQ
RGSGKKELVG EYGRGDLIGV VEALTRQPRA TTVHAVRDTE LAKLPEGTLG HIKRRYPQVV
TRLIHLLSQK ILGNLQQLQG PFPGSGLSVP QHSELTNPAS NLSTVAILPV CAEVPMMAFT
LELQHALQAI GPTLLLNSDV IRALLGASAL DSIQEFRLSG WLAQQEDAHR IVLYQTDTSL
TPWTVRCLRQ ADCILIVGLG DQEPTVGQLE QMLENTAVRA LKQLVLLHRE EGPGPTRTVE
WLNMRSWCSG HLHLRCPRRL 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
CEYLRPSIDC FKTMDFGKFD QIYDVGYQYG KAVFGGWTRG EVIEKMLTDR RSTDLNESRR
ADILAFPSSG FTDLAEIVSR IEPPTSYVSD GCADGEESDC LTEYEEDAGP DCSRDEGGSP
EGASPSTASE VEEEKSTLRQ RRFLPQETPS SVADA
//
