ID Q4SIE5_TETNG Unreviewed; 483 AA. AC Q4SIE5; DT 19-JUL-2005, integrated into UniProtKB/TrEMBL. DT 19-JUL-2005, sequence version 1. DT 27-NOV-2024, entry version 105. 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}; DE Flags: Fragment; GN ORFNames=GSTENG00017720001 {ECO:0000313|EMBL:CAF99587.1}; OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon OS nigroviridis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon. OX NCBI_TaxID=99883 {ECO:0000313|EMBL:CAF99587.1}; RN [1] {ECO:0000313|EMBL:CAF99587.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15496914; DOI=10.1038/nature03025; RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N., RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S., RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C., RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C., RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L., RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P., RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C., RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R., RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D., RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W., RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.; RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the RT early vertebrate proto-karyotype."; RL Nature 431:946-957(2004). RN [2] {ECO:0000313|EMBL:CAF99587.1} RP NUCLEOTIDE SEQUENCE. RG Genoscope; RG Whitehead Institute Centre for Genome Research; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:CAF99587.1}. 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 EMBL; CAAE01014581; CAF99587.1; -; Genomic_DNA. DR AlphaFoldDB; Q4SIE5; -. DR ESTHER; tetng-q4sie5; Hepatic_Lipase. DR KEGG; tng:GSTEN00017720G001; -. DR HOGENOM; CLU_027171_1_1_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:000441; Lipoprotein 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 Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..19 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 20..483 FT /note="Hepatic triacylglycerol lipase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004244004" FT DOMAIN 347..480 FT /note="PLAT" FT /evidence="ECO:0000259|PROSITE:PS50095" FT ACT_SITE 163 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1" FT ACT_SITE 189 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1" FT ACT_SITE 274 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1" FT BINDING 203 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2" FT BINDING 208 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2" FT NON_TER 483 FT /evidence="ECO:0000313|EMBL:CAF99587.1" SQ SEQUENCE 483 AA; 54273 MW; 200B7919EA599538 CRC64; MSVVKVLCCL LAIYQLNEAK KIRGNRADVM AAEPNGVLKE PHVSLSTFRL FAEGEDNCTV DPLQLHTLTS CGFNSSNPLI IITHGWSVDG MLESWVLKLA TALKSNLIDV NVVITDWLSL AQTHYPTAAK STRSVGKDIA HLLQALQARY QYPLRKVHLI GYSLGAHISG FAGSYLEGPE KIGRITGLDP AGPLFEGMSP SDRLSPDDAD FVDAIHTFTQ ERMGLSVGIK QAVGHYDFYP NGGDFQPGCD LRNIYEHISQ YGLLGFEQTV KCAHERSVHL FIDSLLNKDK QSRAYRCRDE RSFDRGVCLD CRKHRCNTLG YNINQVRTGT SKRLYLKTRS QMPYKLHHYQ FRVQFVNQME RIQPSLTISL TGTKEESGDI PITVTEPISG NTSLTFLITL DKDLGDLMFL KLRWDGAALW KNVWKRVQTM IPWGGAERQA QLTVGKISIK AGETQERTTF CAMVHDEQQV EISQDKVFVR CKE //