ID G7Z069_ACISI Unreviewed; 499 AA. AC G7Z069; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 25-MAY-2022, entry version 37. 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}; GN Name=HL {ECO:0000313|EMBL:ACT22637.1}; OS Acipenser sinensis (Chinese sturgeon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Chondrostei; Acipenseriformes; Acipenseridae; Acipenser. OX NCBI_TaxID=61970 {ECO:0000313|EMBL:ACT22637.1}; RN [1] {ECO:0000313|EMBL:ACT22637.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=20672411; DOI=10.3724/SP.J.1141.2010.03239; RA Huang Y., Liang X.F., Wang L., Li G.Z., Liu X.X., Yao Y.; RT "Molecular characterization and evolutional analysis of liportein lipase RT and hepatic lipase gene in Chinese Sturgeon and other six freshwater RT fishes."; RL Dong Wu Xue Yan Jiu 31:239-249(2010). 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 --------------------------------------------------------------------------- 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; FJ436062; ACT22637.1; -; mRNA. DR ESTHER; acibe-a0a075ekg6; Hepatic_Lipase. 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 2: Evidence at transcript level; 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..499 FT /note="Hepatic triacylglycerol lipase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5003506593" FT DOMAIN 351..484 FT /note="PLAT" FT /evidence="ECO:0000259|PROSITE:PS50095" FT ACT_SITE 167 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1" FT ACT_SITE 193 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1" FT ACT_SITE 278 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1" FT METAL 207 FT /note="Calcium; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2" FT METAL 212 FT /note="Calcium" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2" SQ SEQUENCE 499 AA; 56318 MW; 6FE046C7CF76C8F1 CRC64; MGIVRGLVFI LFIYHISDAK RLLVNKTDTK DKSQPILKQK VHYVPKSNFR LYTSGDAMDD TCTILPFDSG TLDRCSFNST APLVIIVHGW SVDGMLESWV TKLAAALKSK LRYSNVVIAD WLSLAHQHYA IAVQNTRLVG QEIADLLEWL EESHQFSTEN VHLIGYSLGA HVSGFAGSYV SGSRNIGRIT GLDPAGPLFE GMSYTDRLSP DDANFVDAIH TFTQQHMGLS VGIKQPVAHY DFYPNGAPFQ PGCHIKNLYD HLSQYGLSGF QQNVKCAHER SVHLFIDSLL NDDKQSMAYW CNDNKSFDKG ICLDCRKNRC NTLGYNIKKV RTGTSKRLYL KTRSHMPYKV YHYQFKIQFI NQIAQLEPML TISLMGTKED VQNLPITLVE EITGNKTYTL LITLDTDIGD LMVLKFKWEG SAVWANIWNK VQTIMPWRKG GKGPELTVGR IRVKAGETQK KTSFCSQSDD STHILPAQEK TFVRCERNSN RGKKKTTLA //