ID A0A3P8SZL5_AMPPE Unreviewed; 496 AA. AC A0A3P8SZL5; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 27-NOV-2024, entry version 26. DE RecName: Full=Hepatic triacylglycerol lipase {ECO:0000256|ARBA:ARBA00019624}; DE EC=3.1.1.3 {ECO:0000256|ARBA:ARBA00013279}; DE EC=3.1.1.32 {ECO:0000256|ARBA:ARBA00013179}; DE EC=3.1.1.5 {ECO:0000256|ARBA:ARBA00013274}; DE AltName: Full=Lipase member C {ECO:0000256|ARBA:ARBA00030539}; DE AltName: Full=Lysophospholipase {ECO:0000256|ARBA:ARBA00029723}; DE AltName: Full=Phospholipase A1 {ECO:0000256|ARBA:ARBA00031180}; OS Amphiprion percula (Orange clownfish) (Lutjanus percula). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Pomacentridae; Amphiprion. OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000017497.1, ECO:0000313|Proteomes:UP000265080}; RN [1] {ECO:0000313|Ensembl:ENSAPEP00000017497.1, ECO:0000313|Proteomes:UP000265080} RP NUCLEOTIDE SEQUENCE. RA Lehmann R.; RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome RT of the orange clownfish Amphiprion percula."; RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSAPEP00000017497.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2023) to UniProtKB. CC -!- FUNCTION: Catalyzes the hydrolysis of triglycerides and phospholipids CC present in circulating plasma lipoproteins, including chylomicrons, CC intermediate density lipoproteins (IDL), low density lipoproteins (LDL) CC of large size and high density lipoproteins (HDL), releasing free fatty CC acids (FFA) and smaller lipoprotein particles. Also exhibits CC lysophospholipase activity. Can hydrolyze both neutral lipid and CC phospholipid substrates but shows a greater binding affinity for CC neutral lipid substrates than phospholipid substrates. In native LDL, CC preferentially hydrolyzes the phosphatidylcholine species containing CC polyunsaturated fatty acids at sn-2 position. CC {ECO:0000256|ARBA:ARBA00045615}. CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = 2,3-di-(9Z)- CC octadecenoyl-sn-glycerol + (9Z)-octadecenoate + H(+); CC Xref=Rhea:RHEA:38391, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75824; CC Evidence={ECO:0000256|ARBA:ARBA00001610}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38392; CC Evidence={ECO:0000256|ARBA:ARBA00001610}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = di-(9Z)- CC octadecenoylglycerol + (9Z)-octadecenoate + H(+); CC Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945; CC Evidence={ECO:0000256|ARBA:ARBA00000652}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; CC Evidence={ECO:0000256|ARBA:ARBA00000652}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2,3-tributanoylglycerol + H2O = dibutanoylglycerol + CC butanoate + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020, CC ChEBI:CHEBI:76478; Evidence={ECO:0000256|ARBA:ARBA00001601}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476; CC Evidence={ECO:0000256|ARBA:ARBA00001601}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = CC (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + (9Z)-octadecenoate + CC H(+); Xref=Rhea:RHEA:38699, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30823, ChEBI:CHEBI:74669, ChEBI:CHEBI:76083; CC Evidence={ECO:0000256|ARBA:ARBA00001885}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38700; CC Evidence={ECO:0000256|ARBA:ARBA00001885}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = 2-(9Z- CC octadecenoyl)-glycerol + (9Z)-octadecenoate + H(+); CC Xref=Rhea:RHEA:38511, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:73990; CC Evidence={ECO:0000256|ARBA:ARBA00001101}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38512; CC Evidence={ECO:0000256|ARBA:ARBA00001101}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = CC hexadecanoyl-sn-glycero-3-phosphocholine + hexadecanoate + H(+); CC Xref=Rhea:RHEA:41384, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64563, ChEBI:CHEBI:72999; CC Evidence={ECO:0000256|ARBA:ARBA00000879}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41385; CC Evidence={ECO:0000256|ARBA:ARBA00000879}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,3-di-(9Z-octadecenoyl)-glycerol + H2O = 3-(9Z-octadecenoyl)- CC sn-glycerol + (9Z)-octadecenoate + H(+); Xref=Rhea:RHEA:38651, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, CC ChEBI:CHEBI:75735, ChEBI:CHEBI:75938; CC Evidence={ECO:0000256|ARBA:ARBA00000265}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38652; CC Evidence={ECO:0000256|ARBA:ARBA00000265}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = sn- CC glycero-3-phospho-L-serine + (9Z)-octadecenoate + H(+); CC Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617; CC Evidence={ECO:0000256|ARBA:ARBA00000834}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500; CC Evidence={ECO:0000256|ARBA:ARBA00000834}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = sn-glycerol CC 3-phosphocholine + hexadecanoate + H(+); Xref=Rhea:RHEA:40435, CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; CC Evidence={ECO:0000256|ARBA:ARBA00000597}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; CC Evidence={ECO:0000256|ARBA:ARBA00000597}; 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; EC=3.1.1.32; CC Evidence={ECO:0000256|ARBA:ARBA00000111}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = sn-glycerol 3- CC phosphocholine + a fatty acid + H(+); 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:0000256|ARBA:ARBA00000960}; 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:0000256|ARBA:ARBA00001024}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}. CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family. CC {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|RuleBase:RU004262}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; A0A3P8SZL5; -. DR STRING; 161767.ENSAPEP00000017497; -. DR Ensembl; ENSAPET00000017993.1; ENSAPEP00000017497.1; ENSAPEG00000012523.1. DR GeneTree; ENSGT00940000157602; -. DR OMA; FVRCKED; -. DR Proteomes; UP000265080; Chromosome 1. DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW. DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC. DR GO; GO:0034185; F:apolipoprotein binding; IEA:TreeGrafter. DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW. DR GO; GO:0004465; F:lipoprotein lipase activity; IEA:TreeGrafter. DR GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC. DR GO; GO:0008970; F:phospholipase A1 activity; IEA:UniProtKB-EC. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:TreeGrafter. DR GO; GO:0019433; P:triglyceride catabolic process; IEA:TreeGrafter. DR CDD; cd00707; Pancreat_lipase_like; 1. DR CDD; cd01758; PLAT_LPL; 1. DR FunFam; 2.60.60.20:FF:000010; hepatic triacylglycerol lipase; 1. DR FunFam; 3.40.50.1820:FF:000101; Hepatic triacylglycerol lipase; 1. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 1. DR InterPro; IPR029058; AB_hydrolase_fold. DR InterPro; IPR013818; Lipase. DR InterPro; IPR002333; Lipase_hep. DR InterPro; IPR016272; Lipase_LIPH. DR InterPro; IPR033906; Lipase_N. DR InterPro; IPR001024; PLAT/LH2_dom. DR InterPro; IPR036392; PLAT/LH2_dom_sf. DR InterPro; IPR000734; TAG_lipase. DR PANTHER; PTHR11610:SF2; HEPATIC TRIACYLGLYCEROL LIPASE; 1. DR PANTHER; PTHR11610; LIPASE; 1. DR Pfam; PF00151; Lipase; 1. DR Pfam; PF01477; PLAT; 1. DR PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1. DR PRINTS; PR00824; HEPLIPASE. DR PRINTS; PR00821; TAGLIPASE. DR SMART; SM00308; LH2; 1. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1. DR PROSITE; PS50095; PLAT; 1. PE 3: Inferred from homology; KW Calcium {ECO:0000256|PIRSR:PIRSR000865-2}; KW HDL {ECO:0000256|ARBA:ARBA00022850}; KW Heparin-binding {ECO:0000256|ARBA:ARBA00022674}; KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000865-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000265080}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..19 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 20..496 FT /note="Hepatic triacylglycerol lipase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5018269106" FT DOMAIN 349..482 FT /note="PLAT" FT /evidence="ECO:0000259|PROSITE:PS50095" FT ACT_SITE 165 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1" FT ACT_SITE 191 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1" FT ACT_SITE 276 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1" FT BINDING 205 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2" FT BINDING 210 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2" SQ SEQUENCE 496 AA; 55770 MW; 76781F646027793C CRC64; MLGVKILCCL LLTCHLSGGK KIKGERASVA DIEQRIVLRV KEPYVSSSAF SLFLGGEDTC TLDPLQLHTL TSCGFNSSNP LIIITHGWSV DGMMESWVLR LASALKTNLV SVNVVLTDWL SLAHQHYPMA VQSTRTVGKD ISHLLQTLQE QYQYPVKKVH LIGYSLGAHI SGFAGSYLEG SEKIGRITGL DPAGPLFEGM SPTDRLSPDD AEFVDAIHTF THERMGLSVG IKQAVAHFDF YPNGGDFQPG CDLQNIYEHI TEYGLLGFEQ TVKCAHERSV HLFIDSLLNK DKQSMAYRCS DNNAFVKGVC LDCRKNRCNT LGYDIKKVRT VTSKRLYLKT RSRMPYKLYH YQFRIQFINQ VENIDPTLTV ALTGTKEESG DVVITFNEKI SGNTTFPFLI TLDKDLGDLM LVKLHWEGLA LWKNVWNRVQ TIIPWGGKET KPLLTVGRIS VKAGETQERT SFCAMTDDGQ QIEVSQDKVF VRCKEDIPKQ RRRKHN //