PLPL4_HUMAN
ID PLPL4_HUMAN Reviewed; 253 AA.
AC P41247; A8K1H3; B4E362; Q8WW83;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Patatin-like phospholipase domain-containing protein 4;
DE EC=3.1.1.3 {ECO:0000269|PubMed:15364929, ECO:0000269|PubMed:16150821, ECO:0000269|PubMed:17603008};
DE AltName: Full=Calcium-independent phospholipase A2-eta {ECO:0000303|PubMed:15364929};
DE Short=iPLA2-eta {ECO:0000303|PubMed:15364929};
DE EC=3.1.1.4 {ECO:0000269|PubMed:15364929};
DE AltName: Full=Protein GS2 {ECO:0000303|PubMed:17603008};
GN Name=PNPLA4 {ECO:0000312|HGNC:HGNC:24887};
GN Synonyms=DXS1283E, GS2 {ECO:0000303|PubMed:17603008};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=7806223; DOI=10.1006/geno.1994.1397;
RA Lee W.-C., Salido E., Yen P.H.;
RT "Isolation of a new gene GS2 (DXS1283E) from a CpG island between STS and
RT KAL1 on Xp22.3.";
RL Genomics 22:372-376(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Corpus callosum, and Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLY-48 AND
RP GLY-134.
RC TISSUE=Lung;
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=15364929; DOI=10.1074/jbc.m407841200;
RA Jenkins C.M., Mancuso D.J., Yan W., Sims H.F., Gibson B., Gross R.W.;
RT "Identification, cloning, expression, and purification of three novel human
RT calcium-independent phospholipase A2 family members possessing
RT triacylglycerol lipase and acylglycerol transacylase activities.";
RL J. Biol. Chem. 279:48968-48975(2004).
RN [7]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=16150821; DOI=10.1194/jlr.m500290-jlr200;
RA Lake A.C., Sun Y., Li J.-L., Kim J.E., Johnson J.W., Li D., Revett T.,
RA Shih H.H., Liu W., Paulsen J.E., Gimeno R.E.;
RT "Expression, regulation, and triglyceride hydrolase activity of Adiponutrin
RT family members.";
RL J. Lipid Res. 46:2477-2487(2005).
RN [8]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=17603008; DOI=10.1016/j.bbrc.2007.06.089;
RA Gao J.G., Simon M.;
RT "A comparative study of human GS2, its paralogues, and its rat
RT orthologue.";
RL Biochem. Biophys. Res. Commun. 360:501-506(2007).
RN [9]
RP SUBCELLULAR LOCATION, AND POSSIBLE INVOLVEMENT IN MITOCHONDRIAL DISORDERS.
RX PubMed=26741492; DOI=10.1371/journal.pgen.1005679;
RA Kohda M., Tokuzawa Y., Kishita Y., Nyuzuki H., Moriyama Y., Mizuno Y.,
RA Hirata T., Yatsuka Y., Yamashita-Sugahara Y., Nakachi Y., Kato H.,
RA Okuda A., Tamaru S., Borna N.N., Banshoya K., Aigaki T., Sato-Miyata Y.,
RA Ohnuma K., Suzuki T., Nagao A., Maehata H., Matsuda F., Higasa K.,
RA Nagasaki M., Yasuda J., Yamamoto M., Fushimi T., Shimura M.,
RA Kaiho-Ichimoto K., Harashima H., Yamazaki T., Mori M., Murayama K.,
RA Ohtake A., Okazaki Y.;
RT "A comprehensive genomic analysis reveals the genetic landscape of
RT mitochondrial respiratory chain complex deficiencies.";
RL PLoS Genet. 12:E1005679-E1005679(2016).
CC -!- FUNCTION: Has abundant triacylglycerol lipase activity
CC (PubMed:15364929, PubMed:16150821, PubMed:17603008). Transfers fatty
CC acid from triglyceride to retinol, hydrolyzes retinylesters, and
CC generates 1,3-diacylglycerol from triglycerides (PubMed:17603008).
CC Additionally possesses acylglycerol transacylase and phospholipase A2
CC activities (PubMed:15364929, PubMed:17603008).
CC {ECO:0000269|PubMed:15364929, ECO:0000269|PubMed:16150821,
CC ECO:0000269|PubMed:17603008}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC Evidence={ECO:0000269|PubMed:15364929, ECO:0000269|PubMed:16150821,
CC ECO:0000269|PubMed:17603008};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000269|PubMed:16150821, ECO:0000305|PubMed:15364929};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 1-(9Z-octadecenoyl)-glycerol = 1,2-di-(9Z-octadecenoyl)-
CC glycerol + glycerol; Xref=Rhea:RHEA:38323, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:52323, ChEBI:CHEBI:75342;
CC Evidence={ECO:0000269|PubMed:15364929};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38324;
CC Evidence={ECO:0000305|PubMed:15364929};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-glycerol + 1-(9Z-octadecenoyl)-
CC glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + glycerol;
CC Xref=Rhea:RHEA:38327, ChEBI:CHEBI:17754, ChEBI:CHEBI:52323,
CC ChEBI:CHEBI:53753, ChEBI:CHEBI:75342;
CC Evidence={ECO:0000269|PubMed:15364929};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38328;
CC Evidence={ECO:0000305|PubMed:15364929};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,3-di-(9Z-octadecenoyl)-glycerol + 1-(9Z-octadecenoyl)-
CC glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + glycerol;
CC Xref=Rhea:RHEA:38331, ChEBI:CHEBI:17754, ChEBI:CHEBI:53753,
CC ChEBI:CHEBI:75342, ChEBI:CHEBI:75735;
CC Evidence={ECO:0000269|PubMed:15364929};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38332;
CC Evidence={ECO:0000305|PubMed:15364929};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + 1,2-di-(9Z-octadecenoyl)-glycerol + H(+)
CC = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O; Xref=Rhea:RHEA:38379,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:52323, ChEBI:CHEBI:53753;
CC Evidence={ECO:0000269|PubMed:17603008};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38381;
CC Evidence={ECO:0000305|PubMed:17603008};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-
CC octadecenoate + 1,3-di-(9Z-octadecenoyl)-glycerol + H(+);
CC Xref=Rhea:RHEA:38387, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75735;
CC Evidence={ECO:0000269|PubMed:17603008};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38388;
CC Evidence={ECO:0000305|PubMed:17603008};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinyl hexadecanoate + H2O = all-trans-retinol +
CC H(+) + hexadecanoate; Xref=Rhea:RHEA:13933, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336,
CC ChEBI:CHEBI:17616; Evidence={ECO:0000269|PubMed:17603008};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934;
CC Evidence={ECO:0000305|PubMed:17603008};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + all-trans-retinol =
CC all-trans-retinyl 9Z-octadecenoate + di-(9Z)-octadecenoylglycerol;
CC Xref=Rhea:RHEA:39987, ChEBI:CHEBI:17336, ChEBI:CHEBI:53753,
CC ChEBI:CHEBI:70760, ChEBI:CHEBI:75945;
CC Evidence={ECO:0000269|PubMed:17603008};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39988;
CC Evidence={ECO:0000305|PubMed:17603008};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000269|PubMed:15364929};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000305|PubMed:15364929};
CC -!- ACTIVITY REGULATION: The triglyceride lipase activity is inhibited by
CC BEL ((E)-6-(bromomethylene)-3-(1-naphthalenyl)-2H-tetrahydropyran-2-
CC one), a suicide substrate inhibitor. {ECO:0000269|PubMed:15364929}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:26741492}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P41247-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P41247-2; Sequence=VSP_043089;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined, including heart,
CC brain, placenta, lung, liver, muscle, kidney, pancreas and spleen.
CC {ECO:0000269|PubMed:7806223}.
CC -!- DISEASE: Note=Defects in PNPLA4 may play a role in mitochondrial
CC disorders characterized by complex IV deficiency.
CC {ECO:0000269|PubMed:26741492}.
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DR EMBL; U03886; AAA16491.1; -; mRNA.
DR EMBL; U08893; AAA17838.1; -; Genomic_DNA.
DR EMBL; U08888; AAA17838.1; JOINED; Genomic_DNA.
DR EMBL; U08889; AAA17838.1; JOINED; Genomic_DNA.
DR EMBL; U08890; AAA17838.1; JOINED; Genomic_DNA.
DR EMBL; U08891; AAA17838.1; JOINED; Genomic_DNA.
DR EMBL; U08892; AAA17838.1; JOINED; Genomic_DNA.
DR EMBL; AK289888; BAF82577.1; -; mRNA.
DR EMBL; AK304586; BAG65374.1; -; mRNA.
DR EMBL; AC005296; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471074; EAW98752.1; -; Genomic_DNA.
DR EMBL; BC020746; AAH20746.1; -; mRNA.
DR CCDS; CCDS14129.1; -. [P41247-1]
DR CCDS; CCDS55368.1; -. [P41247-2]
DR PIR; A55183; A55183.
DR RefSeq; NP_001135861.1; NM_001142389.1. [P41247-1]
DR RefSeq; NP_001166143.1; NM_001172672.1. [P41247-2]
DR RefSeq; NP_004641.1; NM_004650.2. [P41247-1]
DR RefSeq; XP_011543890.1; XM_011545588.1. [P41247-1]
DR AlphaFoldDB; P41247; -.
DR SMR; P41247; -.
DR BioGRID; 113861; 14.
DR IntAct; P41247; 3.
DR STRING; 9606.ENSP00000370430; -.
DR SwissLipids; SLP:000000312; -.
DR iPTMnet; P41247; -.
DR PhosphoSitePlus; P41247; -.
DR BioMuta; PNPLA4; -.
DR DMDM; 116242718; -.
DR EPD; P41247; -.
DR jPOST; P41247; -.
DR MassIVE; P41247; -.
DR MaxQB; P41247; -.
DR PaxDb; P41247; -.
DR PeptideAtlas; P41247; -.
DR PRIDE; P41247; -.
DR ProteomicsDB; 55451; -. [P41247-1]
DR ProteomicsDB; 55452; -. [P41247-2]
DR Antibodypedia; 480; 92 antibodies from 20 providers.
DR DNASU; 8228; -.
DR Ensembl; ENST00000381042.9; ENSP00000370430.4; ENSG00000006757.12. [P41247-1]
DR Ensembl; ENST00000444736.5; ENSP00000415245.1; ENSG00000006757.12. [P41247-1]
DR Ensembl; ENST00000537427.5; ENSP00000443157.1; ENSG00000006757.12. [P41247-2]
DR GeneID; 8228; -.
DR KEGG; hsa:8228; -.
DR MANE-Select; ENST00000381042.9; ENSP00000370430.4; NM_004650.3; NP_004641.1.
DR UCSC; uc011mhq.2; human. [P41247-1]
DR CTD; 8228; -.
DR DisGeNET; 8228; -.
DR GeneCards; PNPLA4; -.
DR HGNC; HGNC:24887; PNPLA4.
DR HPA; ENSG00000006757; Low tissue specificity.
DR MIM; 300102; gene.
DR neXtProt; NX_P41247; -.
DR OpenTargets; ENSG00000006757; -.
DR PharmGKB; PA134910531; -.
DR VEuPathDB; HostDB:ENSG00000006757; -.
DR eggNOG; KOG3773; Eukaryota.
DR GeneTree; ENSGT00940000162022; -.
DR HOGENOM; CLU_018371_4_0_1; -.
DR InParanoid; P41247; -.
DR OMA; AMFPPNQ; -.
DR PhylomeDB; P41247; -.
DR TreeFam; TF314272; -.
DR PathwayCommons; P41247; -.
DR Reactome; R-HSA-163560; Triglyceride catabolism.
DR SignaLink; P41247; -.
DR BioGRID-ORCS; 8228; 8 hits in 705 CRISPR screens.
DR GenomeRNAi; 8228; -.
DR Pharos; P41247; Tbio.
DR PRO; PR:P41247; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P41247; protein.
DR Bgee; ENSG00000006757; Expressed in oocyte and 195 other tissues.
DR ExpressionAtlas; P41247; baseline and differential.
DR Genevisible; P41247; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0016411; F:acylglycerol O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047376; F:all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity; IEA:RHEA.
DR GO; GO:0051265; F:diolein transacylation activity; IDA:UniProtKB.
DR GO; GO:0051264; F:mono-olein transacylation activity; IDA:UniProtKB.
DR GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0050253; F:retinyl-palmitate esterase activity; EXP:Reactome.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0019433; P:triglyceride catabolic process; IBA:GO_Central.
DR CDD; cd07222; Pat_PNPLA4; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR033562; PLPL.
DR InterPro; IPR033902; PNPLA4.
DR InterPro; IPR002641; PNPLA_dom.
DR PANTHER; PTHR12406; PTHR12406; 1.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS51635; PNPLA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Lipid degradation; Lipid metabolism;
KW Mitochondrion; Primary mitochondrial disease; Reference proteome.
FT CHAIN 1..253
FT /note="Patatin-like phospholipase domain-containing protein
FT 4"
FT /id="PRO_0000058460"
FT DOMAIN 6..176
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 41..45
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 163..165
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 43
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 163
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT VAR_SEQ 1..87
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043089"
FT VARIANT 48
FT /note="V -> G (in dbSNP:rs17856615)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_028068"
FT VARIANT 113
FT /note="V -> I (in dbSNP:rs2231791)"
FT /id="VAR_053816"
FT VARIANT 134
FT /note="D -> G (in dbSNP:rs17851825)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_028069"
FT VARIANT 187
FT /note="R -> Q (in dbSNP:rs2231793)"
FT /id="VAR_028070"
SQ SEQUENCE 253 AA; 27980 MW; 6FFA94F460BA03AC CRC64;
MKHINLSFAA CGFLGIYHLG AASALCRHGK KLVKDVKAFA GASAGSLVAS VLLTAPEKIE
ECNQFTYKFA EEIRRQSFGA VTPGYDFMAR LRSGMESILP PSAHELAQNR LHVSITNAKT
RENHLVSTFS SREDLIKVLL ASSFVPIYAG LKLVEYKGQK WVDGGLTNAL PILPVGRTVT
ISPFSGRLDI SPQDKGQLDL YVNIAKQDIM LSLANLVRLN QALFPPSKRK MESLYQCGFD
DTVKFLLKEN WFE
