PLPL8_RABIT
ID PLPL8_RABIT Reviewed; 786 AA.
AC Q5XTS1;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Calcium-independent phospholipase A2-gamma {ECO:0000305};
DE EC=3.1.1.- {ECO:0000250|UniProtKB:Q9NP80};
DE EC=3.1.1.5 {ECO:0000250|UniProtKB:Q9NP80};
DE AltName: Full=Group VIB calcium-independent phospholipase A2 {ECO:0000303|PubMed:15629460};
DE AltName: Full=Intracellular membrane-associated calcium-independent phospholipase A2 gamma {ECO:0000303|PubMed:15629460};
DE Short=iPLA2-gamma {ECO:0000303|PubMed:15629460};
DE AltName: Full=Patatin-like phospholipase domain-containing protein 8;
GN Name=PNPLA8 {ECO:0000250|UniProtKB:Q9NP80};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TOPOLOGY, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Heart;
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).
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. Hydrolyzes
CC phosphatidylethanolamine, phosphatidylcholine and probably
CC phosphatidylinositol with a possible preference for the former. Has
CC also a broad substrate specificity in terms of fatty acid moieties,
CC hydrolyzing saturated and mono-unsaturated fatty acids at nearly equal
CC rates from either the sn-1 or sn-2 position in diacyl
CC phosphatidylcholine. However, has a weak activity toward
CC polyunsaturated fatty acids at the sn-2 position, and thereby favors
CC the production of 2-arachidonoyl lysophosphatidylcholine, a key branch
CC point metabolite in eicosanoid signaling. On the other hand, can
CC produce arachidonic acid from the sn-1 position of diacyl phospholipid
CC and from the sn-2 position of arachidonate-containing plasmalogen
CC substrates. Therefore, plays an important role in the mobilization of
CC arachidonic acid in response to cellular stimuli and the generation of
CC lipid second messengers. Can also hydrolyze lysophosphatidylcholine. In
CC the mitochondrial compartment, catalyzes the hydrolysis and release of
CC oxidized aliphatic chains from cardiolipin and integrates mitochondrial
CC bioenergetics and signaling. It is essential for maintaining efficient
CC bioenergetic mitochondrial function through tailoring mitochondrial
CC membrane lipid metabolism and composition.
CC {ECO:0000250|UniProtKB:Q8K1N1, ECO:0000250|UniProtKB:Q9NP80}.
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:0000250|UniProtKB:Q9NP80};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000250|UniProtKB:Q9NP80};
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:0000250|UniProtKB:Q9NP80};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690;
CC Evidence={ECO:0000250|UniProtKB:Q9NP80};
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:0000250|UniProtKB:Q9NP80};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44605;
CC Evidence={ECO:0000250|UniProtKB:Q9NP80};
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:0000250|UniProtKB:Q9NP80};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44069;
CC Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC Evidence={ECO:0000250|UniProtKB:Q9NP80};
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:0000250|UniProtKB:Q9NP80};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40644;
CC Evidence={ECO:0000250|UniProtKB:Q9NP80};
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:0000250|UniProtKB:Q9NP80};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40652;
CC Evidence={ECO:0000250|UniProtKB:Q9NP80};
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:0000250|UniProtKB:Q9NP80};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000250|UniProtKB:Q9NP80};
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:0000250|UniProtKB:Q9NP80};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40820;
CC Evidence={ECO:0000250|UniProtKB:Q9NP80};
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:0000250|UniProtKB:Q9NP80};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000250|UniProtKB:Q9NP80};
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:0000250|UniProtKB:Q9NP80};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC Evidence={ECO:0000250|UniProtKB:Q9NP80};
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:0000250|UniProtKB:Q9NP80};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40640;
CC Evidence={ECO:0000250|UniProtKB:Q9NP80};
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:0000250|UniProtKB:Q9NP80};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40648;
CC Evidence={ECO:0000250|UniProtKB:Q9NP80};
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:0000250|UniProtKB:Q9NP80};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC Evidence={ECO:0000250|UniProtKB:Q9NP80};
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:0000250|UniProtKB:Q9NP80};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40572;
CC Evidence={ECO:0000250|UniProtKB:Q9NP80};
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:0000250|UniProtKB:Q9NP80};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40824;
CC Evidence={ECO:0000250|UniProtKB:Q9NP80};
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:0000250|UniProtKB:Q9NP80};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41064;
CC Evidence={ECO:0000250|UniProtKB:Q9NP80};
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:0000250|UniProtKB:Q9NP80};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40580;
CC Evidence={ECO:0000250|UniProtKB:Q9NP80};
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:0000250|UniProtKB:Q9NP80};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67157;
CC Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:72998;
CC Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000250|UniProtKB:Q9NP80};
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:0000250|UniProtKB:Q9NP80};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52813;
CC Evidence={ECO:0000250|UniProtKB:Q9NP80};
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:0000250|UniProtKB:Q9NP80};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67273;
CC Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC -!- ACTIVITY REGULATION: Calcium-independent phospholipase.
CC {ECO:0000250|UniProtKB:Q9NP80}.
CC -!- PATHWAY: Phospholipid metabolism. {ECO:0000250|UniProtKB:Q9NP80}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15629460}; Single-pass membrane protein
CC {ECO:0000305|PubMed:15629460}. Mitochondrion membrane
CC {ECO:0000250|UniProtKB:Q9NP80}; Single-pass membrane protein
CC {ECO:0000305|PubMed:15629460}. Peroxisome membrane
CC {ECO:0000250|UniProtKB:Q9NP80}; Single-pass membrane protein
CC {ECO:0000305|PubMed:15629460}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney, heart and brain.
CC {ECO:0000269|PubMed:15629460}.
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DR EMBL; AY738591; AAU85256.1; -; mRNA.
DR RefSeq; NP_001164743.1; NM_001171272.1.
DR AlphaFoldDB; Q5XTS1; -.
DR SMR; Q5XTS1; -.
DR STRING; 9986.ENSOCUP00000019643; -.
DR GeneID; 100328577; -.
DR KEGG; ocu:100328577; -.
DR CTD; 50640; -.
DR eggNOG; KOG4231; Eukaryota.
DR InParanoid; Q5XTS1; -.
DR OrthoDB; 1209603at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISS: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; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0047499; F:calcium-independent phospholipase A2 activity; ISS: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:0019369; P:arachidonic acid metabolic process; ISS:UniProtKB.
DR GO; GO:0032048; P:cardiolipin metabolic process; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0055088; P:lipid homeostasis; ISS:UniProtKB.
DR GO; GO:0070328; P:triglyceride homeostasis; ISS: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 Endoplasmic reticulum; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Mitochondrion; Peroxisome; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..786
FT /note="Calcium-independent phospholipase A2-gamma"
FT /id="PRO_0000303216"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 449..644
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 158..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 453..458
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 485..489
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 631..633
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 225..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 487
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 631
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOD_RES 740
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8K1N1"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 786 AA; 88177 MW; AB130C143E718367 CRC64;
MSINLTIDIC IYLLSNARNL CGKHRSKQLH LVCSPNHCWK IRHVSLQRGL HPHKVRCKWT
KSETHSCSKH YYSPSNHGLH IGILKLSTSA PKGLTKVSIR MSRIKSTLNS VSKAVFGSQN
EMISRLAQFK PSSRILRKVS DSGWLKQESI KQAIRSLKKY SDKSTEKSPV PEGRNHIIDK
EDDIGKQSLF HYTGNITTKF GESFYFLSNH INSYFKRAEK MSQDKENSHF QEKSELEGKK
VEEGKSSSLD PGILTSQADK PDPKSSAGTM DKATSPSGTP ESLPISTKQS IANFLSRPTE
GVQALVGGYI GGLVPKLKYD SKSQAEEQEE PAKSEPAGSK DKTVEEKKHL SLQREKIIAR
VSIDNRTRAL VQALRRTADP KLCITRVEEL TFHLLEFPEG KGVAVKERLI PCLLRLRQMK
DETLQAAVRE ILALIGYVDP VKGRGIRILT IDGGGTRGVV ALQTLRKLVE LTQKPVHQLF
DYICGVSTGA ILAFMLGLFH LPLDECEELY RKLGSDIFSQ NVIVGTVKMS WSHAFYDSQT
WEKILKERMG SALMIETARN PMCPKVAAVS TIVNRGSTPK AFVFRNYGHF PGSQSHYLGG
CQYKMWQAIR ASSAAPGYFA EYALGNDLHQ DGGLLLNNPS ALAMHECKCL WPDAPLECIV
SLGTGRYESD VRNNTTYTSL KTKLSNVINS ATDTEEVHIM LDGLLPPDTY FRFNPVMCEN
IPLDESRNEK LDQLQLEGSK YIERNEHKMK KVAKILSQEK TTLQKINDWI KLKTDMYEGL
PFFSKL
