PLPL8_HUMAN
ID PLPL8_HUMAN Reviewed; 782 AA.
AC Q9NP80; A4D0S1; C9JZI4; O95035; Q8N3I3; Q9H7T5; Q9NR17; Q9NUN2; Q9NZ79;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Calcium-independent phospholipase A2-gamma {ECO:0000305|PubMed:15695510, ECO:0000305|PubMed:15908428};
DE EC=3.1.1.- {ECO:0000269|PubMed:10744668, ECO:0000269|PubMed:10833412, ECO:0000269|PubMed:15695510, ECO:0000269|PubMed:15908428, ECO:0000269|PubMed:17213206, ECO:0000269|PubMed:18171998};
DE EC=3.1.1.5 {ECO:0000269|PubMed:15908428};
DE AltName: Full=Intracellular membrane-associated calcium-independent phospholipase A2 gamma {ECO:0000303|PubMed:15695510};
DE Short=iPLA2-gamma {ECO:0000303|PubMed:15695510};
DE AltName: Full=PNPLA-gamma;
DE AltName: Full=Patatin-like phospholipase domain-containing protein 8 {ECO:0000312|HGNC:HGNC:28900};
DE AltName: Full=iPLA2-2;
GN Name=PNPLA8 {ECO:0000312|HGNC:HGNC:28900}; Synonyms=IPLA22, IPLA2G;
GN ORFNames=BM-043;
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 [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, TOPOLOGY, AND TISSUE SPECIFICITY.
RX PubMed=10833412; DOI=10.1006/bbrc.2000.2776;
RA Tanaka H., Takeya R., Sumimoto H.;
RT "A novel intracellular membrane-bound calcium-independent phospholipase
RT A(2).";
RL Biochem. Biophys. Res. Commun. 272:320-326(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, TOPOLOGY, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=10744668; DOI=10.1074/jbc.275.14.9937;
RA Mancuso D.J., Jenkins C.M., Gross R.W.;
RT "The genomic organization, complete mRNA sequence, cloning, and expression
RT of a novel human intracellular membrane-associated calcium-independent
RT phospholipase A(2).";
RL J. Biol. Chem. 275:9937-9945(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Adipocyte, and Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-739 (ISOFORM 1).
RC TISSUE=Placenta;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 570-782 (ISOFORM 1).
RC TISSUE=Bone marrow;
RA Zhao M., Gu J., Li N., Peng Y., Han Z., Chen Z.;
RT "A novel gene expressed in human bone marrow.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=15629460; DOI=10.1016/j.bbrc.2004.12.016;
RA Kinsey G.R., Cummings B.S., Beckett C.S., Saavedra G., Zhang W.,
RA McHowat J., Schnellmann R.G.;
RT "Identification and distribution of endoplasmic reticulum iPLA2.";
RL Biochem. Biophys. Res. Commun. 327:287-293(2005).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15695510; DOI=10.1074/jbc.m413766200;
RA Murakami M., Masuda S., Ueda-Semmyo K., Yoda E., Kuwata H., Takanezawa Y.,
RA Aoki J., Arai H., Sumimoto H., Ishikawa Y., Ishii T., Nakatani Y., Kudo I.;
RT "Group VIB Ca2+-independent phospholipase A2gamma promotes cellular
RT membrane hydrolysis and prostaglandin production in a manner distinct from
RT other intracellular phospholipases A2.";
RL J. Biol. Chem. 280:14028-14041(2005).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY, AND TISSUE
RP SPECIFICITY.
RX PubMed=15908428; DOI=10.1074/jbc.m502358200;
RA Yan W., Jenkins C.M., Han X., Mancuso D.J., Sims H.F., Yang K., Gross R.W.;
RT "The highly selective production of 2-arachidonoyl lysophosphatidylcholine
RT catalyzed by purified calcium-independent phospholipase A2gamma:
RT identification of a novel enzymatic mediator for the generation of a key
RT branch point intermediate in eicosanoid signaling.";
RL J. Biol. Chem. 280:26669-26679(2005).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=17213206; DOI=10.1074/jbc.m607307200;
RA Mancuso D.J., Han X., Jenkins C.M., Lehman J.J., Sambandam N., Sims H.F.,
RA Yang J., Yan W., Yang K., Green K., Abendschein D.R., Saffitz J.E.,
RA Gross R.W.;
RT "Dramatic accumulation of triglycerides and precipitation of cardiac
RT hemodynamic dysfunction during brief caloric restriction in transgenic
RT myocardium expressing human calcium-independent phospholipase A2gamma.";
RL J. Biol. Chem. 282:9216-9227(2007).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=18171998; DOI=10.1152/ajprenal.00372.2007;
RA Cohen D., Papillon J., Aoudjit L., Li H., Cybulsky A.V., Takano T.;
RT "Role of calcium-independent phospholipase A2 in complement-mediated
RT glomerular epithelial cell injury.";
RL Am. J. Physiol. 294:F469-F479(2008).
RN [15]
RP INVOLVEMENT IN MMLA.
RX PubMed=25512002; DOI=10.1002/humu.22743;
RA Saunders C.J., Moon S.H., Liu X., Thiffault I., Coffman K., LePichon J.B.,
RA Taboada E., Smith L.D., Farrow E.G., Miller N., Gibson M., Patterson M.,
RA Kingsmore S.F., Gross R.W.;
RT "Loss of function variants in human PNPLA8 encoding calcium-independent
RT phospholipase A2 gamma recapitulate the mitochondriopathy of the homologous
RT null mouse.";
RL Hum. Mutat. 36:301-306(2015).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=28442572; DOI=10.1074/jbc.m117.783068;
RA Liu G.Y., Moon S.H., Jenkins C.M., Li M., Sims H.F., Guan S., Gross R.W.;
RT "The phospholipase iPLA2gamma is a major mediator releasing oxidized
RT aliphatic chains from cardiolipin, integrating mitochondrial bioenergetics
RT and signaling.";
RL J. Biol. Chem. 292:10672-10684(2017).
CC -!- FUNCTION: Calcium-independent and membrane-bound phospholipase, that
CC catalyzes the esterolytic cleavage of fatty acids from
CC glycerophospholipids to yield free fatty acids and lysophospholipids,
CC hence regulating membrane physical properties and the release of lipid
CC second messengers and growth factors (PubMed:10833412, PubMed:10744668,
CC PubMed:15695510, PubMed:15908428, PubMed:17213206, PubMed:18171998,
CC PubMed:28442572). Hydrolyzes phosphatidylethanolamine,
CC phosphatidylcholine and probably phosphatidylinositol with a possible
CC preference for the former (PubMed:15695510). Has also a broad substrate
CC specificity in terms of fatty acid moieties, hydrolyzing saturated and
CC mono-unsaturated fatty acids at nearly equal rates from either the sn-1
CC or sn-2 position in diacyl phosphatidylcholine (PubMed:10833412,
CC PubMed:10744668, PubMed:15695510, PubMed:15908428). However, has a weak
CC activity toward polyunsaturated fatty acids at the sn-2 position, and
CC thereby favors the production of 2-arachidonoyl
CC lysophosphatidylcholine, a key branch point metabolite in eicosanoid
CC signaling (PubMed:15908428). On the other hand, can produce arachidonic
CC acid from the sn-1 position of diacyl phospholipid and from the sn-2
CC position of arachidonate-containing plasmalogen substrates
CC (PubMed:15908428). Therefore, plays an important role in the
CC mobilization of arachidonic acid in response to cellular stimuli and
CC the generation of lipid second messengers (PubMed:15695510,
CC PubMed:15908428). Can also hydrolyze lysophosphatidylcholine
CC (PubMed:15695510). In the mitochondrial compartment, catalyzes the
CC hydrolysis and release of oxidized aliphatic chains from cardiolipin
CC and integrates mitochondrial bioenergetics and signaling. It is
CC essential for maintaining efficient bioenergetic mitochondrial function
CC through tailoring mitochondrial membrane lipid metabolism and
CC composition (PubMed:28442572). {ECO:0000250|UniProtKB:Q8K1N1,
CC ECO:0000269|PubMed:10744668, ECO:0000269|PubMed:10833412,
CC ECO:0000269|PubMed:15695510, ECO:0000269|PubMed:15908428,
CC ECO:0000269|PubMed:17213206, ECO:0000269|PubMed:18171998,
CC ECO:0000269|PubMed:28442572}.
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;
CC Evidence={ECO:0000269|PubMed:10744668, ECO:0000269|PubMed:10833412,
CC ECO:0000269|PubMed:15695510, ECO:0000269|PubMed:15908428,
CC ECO:0000269|PubMed:17213206, ECO:0000269|PubMed:28442572};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000305|PubMed:15908428};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875;
CC Evidence={ECO:0000269|PubMed:15908428};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690;
CC Evidence={ECO:0000305|PubMed:15908428};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + H2O = a 1-
CC acyl-sn-glycero-3-phosphoethanolamine + a fatty acid + H(+);
CC Xref=Rhea:RHEA:44604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:64381, ChEBI:CHEBI:64612;
CC Evidence={ECO:0000269|PubMed:15695510, ECO:0000269|PubMed:18171998};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44605;
CC Evidence={ECO:0000305|PubMed:15695510};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-alkenyl)-2-acyl-sn-glycero-3-phosphocholine + H2O = 1-
CC O-(1Z-alkenyl)-sn-glycero-3-phosphocholine + a fatty acid + H(+);
CC Xref=Rhea:RHEA:44068, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:77286, ChEBI:CHEBI:77287;
CC Evidence={ECO:0000269|PubMed:28442572};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44069;
CC Evidence={ECO:0000305|PubMed:28442572};
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:15908428};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC Evidence={ECO:0000305|PubMed:15908428};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-acyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphocholine
CC + H2O = (9Z,12Z)-octadecadienoate + a 1-acyl-sn-glycero-3-
CC phosphocholine + H(+); Xref=Rhea:RHEA:40643, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:60000; Evidence={ECO:0000269|PubMed:15695510};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40644;
CC Evidence={ECO:0000305|PubMed:15695510};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-acyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-
CC phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + a 1-acyl-
CC sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40651,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395,
CC ChEBI:CHEBI:58168, ChEBI:CHEBI:75063;
CC Evidence={ECO:0000269|PubMed:15695510};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40652;
CC Evidence={ECO:0000305|PubMed:15695510};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003;
CC Evidence={ECO:0000269|PubMed:10744668, ECO:0000269|PubMed:28442572};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000305|PubMed:28442572};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H2O = (9Z)-octadecenoate + 1-octadecanoyl-sn-glycero-3-
CC phosphocholine + H(+); Xref=Rhea:RHEA:40819, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:73858,
CC ChEBI:CHEBI:75034; Evidence={ECO:0000269|PubMed:15908428};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40820;
CC Evidence={ECO:0000305|PubMed:15908428};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73001; Evidence={ECO:0000269|PubMed:10744668,
CC ECO:0000269|PubMed:15908428, ECO:0000269|PubMed:17213206};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000305|PubMed:17213206};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-
CC glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73002;
CC Evidence={ECO:0000269|PubMed:10744668};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC Evidence={ECO:0000305|PubMed:10744668};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-acyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-
CC phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + a 1-acyl-sn-
CC glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40639,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245,
CC ChEBI:CHEBI:64381, ChEBI:CHEBI:75069;
CC Evidence={ECO:0000269|PubMed:15695510};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40640;
CC Evidence={ECO:0000305|PubMed:15695510};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-acyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-
CC phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + a 1-
CC acyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40647,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395,
CC ChEBI:CHEBI:64381, ChEBI:CHEBI:75067;
CC Evidence={ECO:0000269|PubMed:15695510, ECO:0000269|PubMed:18171998};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40648;
CC Evidence={ECO:0000305|PubMed:15695510};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009;
CC Evidence={ECO:0000269|PubMed:18171998};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC Evidence={ECO:0000305|PubMed:18171998};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:40571, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:73003, ChEBI:CHEBI:76079;
CC Evidence={ECO:0000269|PubMed:15908428, ECO:0000269|PubMed:28442572};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40572;
CC Evidence={ECO:0000305|PubMed:15908428};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+) +
CC octadecanoate; Xref=Rhea:RHEA:40823, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:75034,
CC ChEBI:CHEBI:76071; Evidence={ECO:0000269|PubMed:15908428};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40824;
CC Evidence={ECO:0000305|PubMed:15908428};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phosphocholine + H2O = 2-(4Z,7Z,10Z,13Z,16Z,19Z-
CC docosahexaenoyl)-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:41063, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:74963, ChEBI:CHEBI:76085;
CC Evidence={ECO:0000269|PubMed:15908428};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41064;
CC Evidence={ECO:0000305|PubMed:15908428};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z)-hexadecenyl-2 (5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate +
CC 1-(1Z-hexadecenyl)-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:40579, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:73850, ChEBI:CHEBI:77292;
CC Evidence={ECO:0000269|PubMed:15908428};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40580;
CC Evidence={ECO:0000305|PubMed:15908428};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-hexadecenyl)-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + H2O = (9Z)-octadecenoate + 1-(1Z-hexadecenyl)-sn-
CC glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:67156,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:73850, ChEBI:CHEBI:86232;
CC Evidence={ECO:0000269|PubMed:10744668};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67157;
CC Evidence={ECO:0000305|PubMed:10744668};
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:15908428};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000305|PubMed:15908428};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1',3'-bis-[1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phospho]-glycerol + H2O = (9Z,12Z)-octadecadienoate + 1'-[1,2-di-
CC (9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-3'-[1-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phospho]-glycerol + H(+);
CC Xref=Rhea:RHEA:52812, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:83580, ChEBI:CHEBI:83581;
CC Evidence={ECO:0000269|PubMed:28442572};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52813;
CC Evidence={ECO:0000305|PubMed:28442572};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1'-[1-acyl-2-(9-hydroxy-(10E,12Z)-octadecadienoyl)-sn-glycero-
CC 3-phospho]-3'-[1,2-diacyl-sn-glycero-3-phospho]-glycerol + H2O = 1'-
CC [1,2-diacyl-sn-glycero-3-phospho],3'-[1-acyl-sn-glycero-3-phospho]-
CC glycerol + 9-hydroxy-(10E,12Z)-octadecadienoate + H(+);
CC Xref=Rhea:RHEA:67272, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:64743, ChEBI:CHEBI:133820, ChEBI:CHEBI:167908;
CC Evidence={ECO:0000269|PubMed:28442572};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67273;
CC Evidence={ECO:0000305|PubMed:28442572};
CC -!- ACTIVITY REGULATION: Calcium-independent phospholipase
CC (PubMed:10833412, PubMed:10744668). Inhibited by (E)-6-bromomethylene-
CC 3-1-naphthalenyl-2H-tetrahydropyran-2-one (BEL) (PubMed:10744668,
CC PubMed:15908428, PubMed:18171998). The activity toward 1-hexadecanoyl-
CC 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine is
CC stimulated by cardiolipin (PubMed:28442572).
CC {ECO:0000269|PubMed:10744668, ECO:0000269|PubMed:10833412,
CC ECO:0000269|PubMed:15908428, ECO:0000269|PubMed:18171998,
CC ECO:0000269|PubMed:28442572}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000305|PubMed:10744668};
CC -!- PATHWAY: Phospholipid metabolism. {ECO:0000305|PubMed:15908428}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q5XTS1}; Single-pass membrane protein
CC {ECO:0000305|PubMed:10744668, ECO:0000305|PubMed:10833412}.
CC Mitochondrion membrane {ECO:0000305|PubMed:17213206}; Single-pass
CC membrane protein {ECO:0000305|PubMed:10744668,
CC ECO:0000305|PubMed:10833412}. Peroxisome membrane
CC {ECO:0000269|PubMed:15695510}; Single-pass membrane protein
CC {ECO:0000305|PubMed:10744668, ECO:0000305|PubMed:10833412}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NP80-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NP80-2; Sequence=VSP_028005;
CC Name=3;
CC IsoId=Q9NP80-3; Sequence=VSP_045594;
CC -!- TISSUE SPECIFICITY: Expressed in parenchymal tissues including heart,
CC skeletal muscle, placenta, brain, liver and pancreas. Also expressed in
CC bronchial epithelial cells and kidney. Highest expression is observed
CC in skeletal muscle and heart. {ECO:0000269|PubMed:10744668,
CC ECO:0000269|PubMed:10833412, ECO:0000269|PubMed:15629460,
CC ECO:0000269|PubMed:15695510, ECO:0000269|PubMed:15908428}.
CC -!- DISEASE: Mitochondrial myopathy with lactic acidosis (MMLA)
CC [MIM:251950]: An autosomal recessive disorder characterized by
CC progressive muscle weakness, hypotonia, seizures, poor weight gain,
CC lactic acidosis, and elevated serum pyruvate concentration. Some
CC patients manifest growth failure and moderate neural deafness.
CC {ECO:0000269|PubMed:25512002}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF67630.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA92090.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAL24384.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB041261; BAA94997.1; -; mRNA.
DR EMBL; AF263613; AAF75269.1; -; mRNA.
DR EMBL; AF263947; AAF81246.1; -; mRNA.
DR EMBL; AL834147; CAD38859.1; -; mRNA.
DR EMBL; BX647865; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC005058; AAD08847.1; -; Genomic_DNA.
DR EMBL; CH236947; EAL24384.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH236947; EAL24385.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83433.1; -; Genomic_DNA.
DR EMBL; BC032999; AAH32999.1; -; mRNA.
DR EMBL; AK002115; BAA92090.1; ALT_INIT; mRNA.
DR EMBL; AK024335; BAB14890.1; -; mRNA.
DR EMBL; AF217519; AAF67630.1; ALT_INIT; mRNA.
DR CCDS; CCDS34733.1; -. [Q9NP80-1]
DR CCDS; CCDS59075.1; -. [Q9NP80-3]
DR CCDS; CCDS59508.1; -. [Q9NP80-2]
DR PIR; JC7284; JC7284.
DR RefSeq; NP_001242936.1; NM_001256007.2. [Q9NP80-1]
DR RefSeq; NP_001242937.1; NM_001256008.2. [Q9NP80-1]
DR RefSeq; NP_001242938.1; NM_001256009.2. [Q9NP80-2]
DR RefSeq; NP_001242939.1; NM_001256010.2. [Q9NP80-3]
DR RefSeq; NP_001242940.1; NM_001256011.2. [Q9NP80-3]
DR RefSeq; NP_056538.1; NM_015723.4. [Q9NP80-1]
DR RefSeq; XP_005250453.1; XM_005250396.4. [Q9NP80-2]
DR RefSeq; XP_011514576.1; XM_011516274.2.
DR AlphaFoldDB; Q9NP80; -.
DR SMR; Q9NP80; -.
DR BioGRID; 119111; 52.
DR IntAct; Q9NP80; 11.
DR STRING; 9606.ENSP00000410804; -.
DR ChEMBL; CHEMBL2189126; -.
DR SwissLipids; SLP:000000564; -.
DR GlyGen; Q9NP80; 2 sites.
DR iPTMnet; Q9NP80; -.
DR PhosphoSitePlus; Q9NP80; -.
DR BioMuta; PNPLA8; -.
DR DMDM; 74734299; -.
DR EPD; Q9NP80; -.
DR jPOST; Q9NP80; -.
DR MassIVE; Q9NP80; -.
DR MaxQB; Q9NP80; -.
DR PaxDb; Q9NP80; -.
DR PeptideAtlas; Q9NP80; -.
DR PRIDE; Q9NP80; -.
DR ProteomicsDB; 12404; -.
DR ProteomicsDB; 81923; -. [Q9NP80-1]
DR ProteomicsDB; 81924; -. [Q9NP80-2]
DR Antibodypedia; 17333; 177 antibodies from 23 providers.
DR DNASU; 50640; -.
DR Ensembl; ENST00000257694.13; ENSP00000257694.8; ENSG00000135241.17. [Q9NP80-1]
DR Ensembl; ENST00000422087.5; ENSP00000410804.1; ENSG00000135241.17. [Q9NP80-1]
DR Ensembl; ENST00000426128.6; ENSP00000394988.2; ENSG00000135241.17. [Q9NP80-2]
DR Ensembl; ENST00000436062.5; ENSP00000406779.1; ENSG00000135241.17. [Q9NP80-1]
DR Ensembl; ENST00000453144.5; ENSP00000387789.1; ENSG00000135241.17. [Q9NP80-3]
DR GeneID; 50640; -.
DR KEGG; hsa:50640; -.
DR MANE-Select; ENST00000257694.13; ENSP00000257694.8; NM_001256007.3; NP_001242936.1.
DR UCSC; uc003vff.3; human. [Q9NP80-1]
DR CTD; 50640; -.
DR DisGeNET; 50640; -.
DR GeneCards; PNPLA8; -.
DR HGNC; HGNC:28900; PNPLA8.
DR HPA; ENSG00000135241; Low tissue specificity.
DR MalaCards; PNPLA8; -.
DR MIM; 251950; phenotype.
DR MIM; 612123; gene.
DR neXtProt; NX_Q9NP80; -.
DR OpenTargets; ENSG00000135241; -.
DR PharmGKB; PA145148236; -.
DR VEuPathDB; HostDB:ENSG00000135241; -.
DR eggNOG; KOG4231; Eukaryota.
DR GeneTree; ENSGT00940000154738; -.
DR InParanoid; Q9NP80; -.
DR OMA; YKLWQAI; -.
DR OrthoDB; 1209603at2759; -.
DR PhylomeDB; Q9NP80; -.
DR TreeFam; TF319230; -.
DR PathwayCommons; Q9NP80; -.
DR Reactome; R-HSA-1482788; Acyl chain remodelling of PC.
DR Reactome; R-HSA-1482839; Acyl chain remodelling of PE.
DR SignaLink; Q9NP80; -.
DR BioGRID-ORCS; 50640; 31 hits in 1076 CRISPR screens.
DR ChiTaRS; PNPLA8; human.
DR GeneWiki; PNPLA8; -.
DR GenomeRNAi; 50640; -.
DR Pharos; Q9NP80; Tbio.
DR PRO; PR:Q9NP80; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9NP80; protein.
DR Bgee; ENSG00000135241; Expressed in endothelial cell and 191 other tissues.
DR ExpressionAtlas; Q9NP80; baseline and differential.
DR Genevisible; Q9NP80; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; NAS:UniProtKB.
DR GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IDA:UniProtKB.
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:0008970; F:phospholipase A1 activity; IEA:RHEA.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0019369; P:arachidonic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0050482; P:arachidonic acid secretion; IDA:UniProtKB.
DR GO; GO:0032048; P:cardiolipin metabolic process; IDA:UniProtKB.
DR GO; GO:0008219; P:cell death; IDA:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IDA:UniProtKB.
DR GO; GO:0043651; P:linoleic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0055088; P:lipid homeostasis; IMP:UniProtKB.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; IDA:UniProtKB.
DR GO; GO:0046338; P:phosphatidylethanolamine catabolic process; IDA:UniProtKB.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IDA:UniProtKB.
DR GO; GO:1900407; P:regulation of cellular response to oxidative stress; IEA:Ensembl.
DR GO; GO:0070328; P:triglyceride homeostasis; IMP:UniProtKB.
DR CDD; cd07211; Pat_PNPLA8; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR045217; PNPLA8-like.
DR InterPro; IPR002641; PNPLA_dom.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS51635; PNPLA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW Lipid degradation; Lipid metabolism; Membrane; Mitochondrion; Peroxisome;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..782
FT /note="Calcium-independent phospholipase A2-gamma"
FT /id="PRO_0000303214"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 445..640
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 219..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 449..454
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 481..485
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 627..629
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 219..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 483
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 627
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOD_RES 736
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8K1N1"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..100
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_045594"
FT VAR_SEQ 565..626
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_028005"
FT CONFLICT 570..575
FT /note="NRGITP -> IGGITH (in Ref. 9; AAF67630)"
FT /evidence="ECO:0000305"
FT CONFLICT 570..571
FT /note="NR -> GI (in Ref. 8; BAA92090)"
FT /evidence="ECO:0000305"
FT CONFLICT 622
FT /note="N -> S (in Ref. 8; BAA92090)"
FT /evidence="ECO:0000305"
FT CONFLICT 623
FT /note="D -> G (in Ref. 3; BX647865)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 782 AA; 88477 MW; C66AD18A53AF649A CRC64;
MSINLTVDIY IYLLSNARSV CGKQRSKQLY FLFSPKHYWR ISHISLQRGF HTNIIRCKWT
KSEAHSCSKH CYSPSNHGLH IGILKLSTSA PKGLTKVNIC MSRIKSTLNS VSKAVFGNQN
EMISRLAQFK PSSQILRKVS DSGWLKQKNI KQAIKSLKKY SDKSAEKSPF PEEKSHIIDK
EEDIGKRSLF HYTSSITTKF GDSFYFLSNH INSYFKRKEK MSQQKENEHF RDKSELEDKK
VEEGKLRSPD PGILAYKPGS ESVHTVDKPT SPSAIPDVLQ VSTKQSIANF LSRPTEGVQA
LVGGYIGGLV PKLKYDSKSQ SEEQEEPAKT DQAVSKDRNA EEKKRLSLQR EKIIARVSID
NRTRALVQAL RRTTDPKLCI TRVEELTFHL LEFPEGKGVA VKERIIPYLL RLRQIKDETL
QAAVREILAL IGYVDPVKGR GIRILSIDGG GTRGVVALQT LRKLVELTQK PVHQLFDYIC
GVSTGAILAF MLGLFHMPLD ECEELYRKLG SDVFSQNVIV GTVKMSWSHA FYDSQTWENI
LKDRMGSALM IETARNPTCP KVAAVSTIVN RGITPKAFVF RNYGHFPGIN SHYLGGCQYK
MWQAIRASSA APGYFAEYAL GNDLHQDGGL LLNNPSALAM HECKCLWPDV PLECIVSLGT
GRYESDVRNT VTYTSLKTKL SNVINSATDT EEVHIMLDGL LPPDTYFRFN PVMCENIPLD
ESRNEKLDQL QLEGLKYIER NEQKMKKVAK ILSQEKTTLQ KINDWIKLKT DMYEGLPFFS
KL
