ID Q4SIE5_TETNG Unreviewed; 483 AA. AC Q4SIE5; DT 19-JUL-2005, integrated into UniProtKB/TrEMBL. DT 19-JUL-2005, sequence version 1. DT 25-MAY-2022, entry version 97. 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 -!- CATALYTIC ACTIVITY: CC Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)- CC octadecenoate + 2,3-di-(9Z)-octadecenoyl-sn-glycerol + 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 = (9Z)- CC octadecenoate + di-(9Z)-octadecenoylglycerol + 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 = butanoate + CC dibutanoylglycerol + 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)-octadecenoate + (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 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 = (9Z)- CC octadecenoate + 2-(9Z-octadecenoyl)-glycerol + 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 = H(+) + CC hexadecanoate + hexadecanoyl-sn-glycero-3-phosphocholine; 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 = (9Z)-octadecenoate + CC 3-(9Z-octadecenoyl)-sn-glycerol + 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 = CC (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine; 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 = 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: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 = 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: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 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:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC. 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:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC. DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro. DR CDD; cd00707; Pancreat_lipase_like; 1. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. 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; PTHR11610; 1. DR PANTHER; PTHR11610:SF2; PTHR11610:SF2; 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; SSF49723; SSF49723; 1. DR SUPFAM; SSF53474; SSF53474; 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 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 METAL 203 FT /note="Calcium; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2" FT METAL 208 FT /note="Calcium" 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 //