PLPL7_MOUSE
ID PLPL7_MOUSE Reviewed; 1352 AA.
AC A2AJ88; A9YTK0; B0LS74; B0ZTC6; B9EJ75; Q3TD21; Q3UFP1; Q66JS2; Q6P3F9;
AC Q8BTY7; Q8R064; Q8R3C5;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Patatin-like phospholipase domain-containing protein 7;
DE EC=3.1.1.- {ECO:0000269|PubMed:18086666, ECO:0000269|PubMed:22326266, ECO:0000269|PubMed:28887301};
DE EC=3.1.1.5 {ECO:0000269|PubMed:18086666, ECO:0000269|PubMed:28887301};
DE AltName: Full=Neuropathy target esterase-related esterase;
DE Short=NRE;
DE Short=NTE-related esterase;
GN Name=Pnpla7;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 801-1352 (ISOFORM 2).
RC STRAIN=129, and FVB/N; TISSUE=Limb, and Mammary tumor;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-1352 (ISOFORMS 1; 2 AND 3), FUNCTION,
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RC STRAIN=Kunming; TISSUE=Brain;
RX PubMed=22326266; DOI=10.1016/j.gene.2012.01.064;
RA Chang P.A., Wang Z.X., Long D.X., Qin W.Z., Wei C.Y., Wu Y.J.;
RT "Identification of two novel splicing variants of murine NTE-related
RT esterase.";
RL Gene 497:164-171(2012).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1280, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP AND TOPOLOGY.
RX PubMed=28887301; DOI=10.1074/jbc.m117.792978;
RA Heier C., Kien B., Huang F., Eichmann T.O., Xie H., Zechner R., Chang P.A.;
RT "The phospholipase PNPLA7 functions as a lysophosphatidylcholine hydrolase
RT and interacts with lipid droplets through its catalytic domain.";
RL J. Biol. Chem. 292:19087-19098(2017).
CC -!- FUNCTION: Lysophospholipase which preferentially deacylates unsaturated
CC lysophosphatidylcholine (C18:1), generating glycerophosphocholine
CC (PubMed:18086666, PubMed:28887301). Can also deacylate, to a lesser
CC extent, lysophosphatidylethanolamine (C18:1), lysophosphatidyl-L-serine
CC (C18:1) and lysophosphatidic acid (C16:0) (PubMed:22326266,
CC PubMed:18086666, PubMed:28887301). {ECO:0000269|PubMed:18086666,
CC ECO:0000269|PubMed:22326266, ECO:0000269|PubMed:28887301}.
CC -!- FUNCTION: [Isoform 2]: Lysophospholipase.
CC {ECO:0000269|PubMed:22326266}.
CC -!- FUNCTION: [Isoform 3]: Lacks lysophospholipase activity.
CC {ECO:0000269|PubMed:22326266}.
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:0000269|PubMed:28887301};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC Evidence={ECO:0000269|PubMed:18086666, ECO:0000269|PubMed:28887301};
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:0000269|PubMed:28887301};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40808;
CC Evidence={ECO:0000269|PubMed:28887301};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O =
CC (9Z)-octadecenoate + H(+) + sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:40895, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:74971, ChEBI:CHEBI:143890;
CC Evidence={ECO:0000269|PubMed:28887301};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40896;
CC Evidence={ECO:0000269|PubMed:28887301};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O =
CC (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine;
CC Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617;
CC Evidence={ECO:0000269|PubMed:28887301};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500;
CC Evidence={ECO:0000269|PubMed:28887301};
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 -!- ACTIVITY REGULATION: cAMP does not regulate lysophospholipase activity
CC in vitro (PubMed:18086666, PubMed:28887301). Slightly inhibited by
CC organophosphorus (OP) compounds such as mipafox, which is likely why
CC mice are less sensitive to distal axonophathy induced by OPs compared
CC to humans (PubMed:18086666). {ECO:0000269|PubMed:18086666,
CC ECO:0000269|PubMed:28887301}.
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:18086666, ECO:0000269|PubMed:28887301}; Single-pass
CC type III membrane protein {ECO:0000269|PubMed:28887301}. Lipid droplet
CC {ECO:0000269|PubMed:18086666, ECO:0000269|PubMed:28887301}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22326266}; Single-pass type III membrane protein
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22326266}; Single-pass type III membrane protein
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22326266}; Single-pass type III membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A2AJ88-1; Sequence=Displayed;
CC Name=2; Synonyms=mNREV1 {ECO:0000303|PubMed:22326266};
CC IsoId=A2AJ88-2; Sequence=VSP_026506, VSP_026507;
CC Name=3; Synonyms=mNREV2 {ECO:0000303|PubMed:22326266};
CC IsoId=A2AJ88-3; Sequence=VSP_053967, VSP_053968;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed in white and brown adipose
CC tissue, cardiac muscle, skeletal muscle, and testis.
CC {ECO:0000269|PubMed:18086666, ECO:0000269|PubMed:22326266}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in white adipose tissue,
CC cardiac muscle, skeletal muscle, and testis.
CC {ECO:0000269|PubMed:22326266}.
CC -!- TISSUE SPECIFICITY: [Isoform 3]: Expressed in white adipose tissue,
CC cardiac muscle, skeletal muscle, and testis.
CC {ECO:0000269|PubMed:22326266}.
CC -!- INDUCTION: By nutritional conditions (PubMed:22326266,
CC PubMed:18086666). Expression of isoform 3 is switched to the expression
CC of isoform 2 during fasting (PubMed:22326266).
CC {ECO:0000269|PubMed:18086666, ECO:0000269|PubMed:22326266}.
CC -!- INDUCTION: [Isoform 1]: Expression levels are not affected by fasting.
CC {ECO:0000269|PubMed:22326266}.
CC -!- INDUCTION: [Isoform 2]: In white adipose tissue, cardiac muscle,
CC skeletal muscle, and testis, expression levels are down-regulated under
CC well-fed conditions and are up-regulated during fasting.
CC {ECO:0000269|PubMed:22326266}.
CC -!- INDUCTION: [Isoform 3]: In white adipose tissue, cardiac muscle,
CC skeletal muscle, and testis, expression levels are up-regulated under
CC well-fed conditions and are down-regulated during fasting.
CC {ECO:0000269|PubMed:22326266}.
CC -!- DOMAIN: The 3 cNMP binding domains are required for localization to the
CC endoplasmic reticulum (PubMed:28887301). The cNMP binding domain 3 is
CC involved in the binding to lipid droplets (PubMed:28887301).
CC {ECO:0000269|PubMed:28887301}.
CC -!- SIMILARITY: Belongs to the NTE family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-27 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27342.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH27342.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=AAI41366.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI41367.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC40302.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE28519.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE41783.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK088362; BAC40302.1; ALT_INIT; mRNA.
DR EMBL; AK148380; BAE28519.1; ALT_INIT; mRNA.
DR EMBL; AK170417; BAE41783.1; ALT_INIT; mRNA.
DR EMBL; AL732585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025621; AAH25621.1; -; mRNA.
DR EMBL; BC027342; AAH27342.1; ALT_SEQ; mRNA.
DR EMBL; BC064003; AAH64003.1; -; mRNA.
DR EMBL; BC080793; AAH80793.1; -; mRNA.
DR EMBL; BC141365; AAI41366.1; ALT_INIT; mRNA.
DR EMBL; BC141366; AAI41367.1; ALT_INIT; mRNA.
DR EMBL; EU293208; ABX89593.1; -; mRNA.
DR EMBL; EU368675; ABY82074.1; -; mRNA.
DR EMBL; EU402948; ABY89725.2; -; mRNA.
DR CCDS; CCDS50522.1; -. [A2AJ88-1]
DR RefSeq; NP_666363.3; NM_146251.4. [A2AJ88-1]
DR RefSeq; XP_017173518.1; XM_017318029.1.
DR RefSeq; XP_017173519.1; XM_017318030.1. [A2AJ88-2]
DR AlphaFoldDB; A2AJ88; -.
DR SMR; A2AJ88; -.
DR BioGRID; 232300; 5.
DR STRING; 10090.ENSMUSP00000044078; -.
DR ChEMBL; CHEMBL3259499; -.
DR SwissLipids; SLP:000001853; -.
DR iPTMnet; A2AJ88; -.
DR PhosphoSitePlus; A2AJ88; -.
DR EPD; A2AJ88; -.
DR jPOST; A2AJ88; -.
DR MaxQB; A2AJ88; -.
DR PaxDb; A2AJ88; -.
DR PeptideAtlas; A2AJ88; -.
DR PRIDE; A2AJ88; -.
DR ProteomicsDB; 289767; -. [A2AJ88-1]
DR ProteomicsDB; 289768; -. [A2AJ88-2]
DR ProteomicsDB; 289769; -. [A2AJ88-3]
DR Antibodypedia; 2428; 10 antibodies from 8 providers.
DR DNASU; 241274; -.
DR Ensembl; ENSMUST00000045295; ENSMUSP00000044078; ENSMUSG00000036833. [A2AJ88-1]
DR GeneID; 241274; -.
DR KEGG; mmu:241274; -.
DR UCSC; uc008ipv.2; mouse. [A2AJ88-1]
DR UCSC; uc012brs.1; mouse. [A2AJ88-2]
DR CTD; 375775; -.
DR MGI; MGI:2385325; Pnpla7.
DR VEuPathDB; HostDB:ENSMUSG00000036833; -.
DR eggNOG; KOG2968; Eukaryota.
DR GeneTree; ENSGT00940000156763; -.
DR HOGENOM; CLU_000960_1_0_1; -.
DR InParanoid; A2AJ88; -.
DR OMA; FTMNFTT; -.
DR OrthoDB; 253518at2759; -.
DR PhylomeDB; A2AJ88; -.
DR TreeFam; TF300519; -.
DR BioGRID-ORCS; 241274; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Pnpla7; mouse.
DR PRO; PR:A2AJ88; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2AJ88; protein.
DR Bgee; ENSMUSG00000036833; Expressed in left lobe of liver and 219 other tissues.
DR ExpressionAtlas; A2AJ88; baseline and differential.
DR Genevisible; A2AJ88; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; ISO: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:0034638; P:phosphatidylcholine catabolic process; IDA:UniProtKB.
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; 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.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Hydrolase; Lipid degradation;
KW Lipid droplet; Lipid metabolism; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..1352
FT /note="Patatin-like phospholipase domain-containing protein
FT 7"
FT /id="PRO_0000293490"
FT TOPO_DOM 1..36
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:28887301"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..1352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28887301"
FT DOMAIN 950..1116
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 340..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..967
FT /note="Involved in the binding to lipid droplets"
FT /evidence="ECO:0000269|PubMed:28887301"
FT REGION 1295..1352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 954..959
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 981..985
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1103..1105
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 389..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1317..1339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 983
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1103
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT BINDING 170..297
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
FT BINDING 499..585
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
FT BINDING 613..718
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZV29"
FT MOD_RES 1280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1284
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5BK26"
FT VAR_SEQ 780..833
FT /note="GPVLLLTSDNIKQRLGSAALDSIHEYRLSSWLGQQEDIHRIVLYQADGTLTP
FT WT -> ASMSTGSPVGWASRRTSNGLCCIRQTAHSHRGPSAASGRLTASSSWAWVSKSQ
FT Q (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:22326266"
FT /id="VSP_053967"
FT VAR_SEQ 834..1352
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:22326266"
FT /id="VSP_053968"
FT VAR_SEQ 1313..1326
FT /note="EYEPSMLQGPPSLT -> VRNMSLRCCKDPPA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:22326266"
FT /id="VSP_026506"
FT VAR_SEQ 1327..1352
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:22326266"
FT /id="VSP_026507"
FT CONFLICT 113..116
FT /note="RTKV -> PRVR (in Ref. 3; AAH25621)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="S -> R (in Ref. 1; BAE41783)"
FT /evidence="ECO:0000305"
FT CONFLICT 604
FT /note="S -> P (in Ref. 4; ABX89593/ABY82074/ABY89725)"
FT /evidence="ECO:0000305"
FT CONFLICT 1343
FT /note="D -> N (in Ref. 1; BAE28519)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1352 AA; 150494 MW; ADF5362282EA1607 CRC64;
MQNEEDACLE AGYCLGTTLS SWRLHFMEEQ SQSTMLMGIG IGALLTLAFV GITFFFVYRR
VRRLRRAEPT PQYRFRKRDK VMFYGRKIMR KVTTLPHTLV GNTSAPRQRV RKRTKVLSLA
KRILRFKKEY PTLQPKEPPP SLLEADLTEF DVKNSHLPSE VLYMLKNVRV LGHFEKPLFL
ELCKHMVFVQ LQEGEHVFQP GEPDISIYVV QDGRLEVCIQ DADGTEVVVK EVLPGDSVHS
LLSILDVITG HTAPYKTVSA RAAVSSTVLW LPAAAFQGVF EKYPETLVRV VQIIMVRLQR
VTFLALHNYL GLTTELFNPE SQAIPLLSVA SVAGRAKRQM SYGPEEQLER SLRPSEFSSS
DHGSSCVTVS GPLLKRSCSV PLPSNHGEVD ELRQSQGSGS NTSAFQESHE GATSDLGMAY
NRARILPHSD EQLGNSLASK SKKSVVAETP SAIFHYSENF RDETGACGKT DAIFRAATKD
LLTLMKLDDP SLLDGRVAFL HVPAGTLVSK QGDQDVNILF VVSGMLHVYQ QKIDSLEDTC
LFLTHPGEMV GQLAVLTGEP LMFTIRANRD CSFLSISKAH FYEIMRKRPD VVLGVAHTVV
KRMSSFVRQI DFALDWMEVE AGRAIYRQGD KSDCTYIVLS GRLRSVIRKD DGKKRLAGEY
GRGDLVGVVE TLTHQARATT VHAVRDSELA KLPAGALTSI KRRYPQVVTR LIHLLGEKIL
GSLQQGSATG HQLGFNTASS KWDLGNPPGN LSTVAALPAS EDVPLTAFAL ELQHALSAIG
PVLLLTSDNI KQRLGSAALD SIHEYRLSSW LGQQEDIHRI VLYQADGTLT PWTQRCIRQA
DCILIVGLGE QEPAVGELEQ MLESTAVRAQ KQLILLHKED GPVPSRTVEW LNMRSWCSGH
LHLCCPRRVF SKRSLPKLVE MYTRVFQRPP DRHSDFSRLA RMLTGNAIAL VLGGGGARGC
AQVGILRALA ECGVPVDIIG GTSIGAFMGA LFAEERSYSQ TRIRAKQWAE GMTSMMKTIL
DLTYPITSMF SGTGFNSSIS NIFKDRQIED LWLPYFAITT DITASAMRVH TDGSLWRYVR
ASMSLSGYMP PLCDPKDGHL LMDGGYINNL PADVARSMGA KVVIAIDVGS RDETDLTNYG
DALSGWWLLW KRWNPLATKV KVLNMAEIQT RLAYVCCVRQ LEMVKNSDYC EYLRPPIDSY
RTLDFGKFDE ICEVGYQHGR TVFDIWVRSG VLEKMLQDQQ GTSKRKDCGV FTCPNSSFTD
LAEIVSRIEP AKVAAVDDES DYQTEYEEEL PAIPKETYAD FQSTGIELDS DSEYEPSMLQ
GPPSLTSPEQ SQDSFPWLPN QDDQGPRLEH PS
