ID A0A1D8I1N4_SOUCH Unreviewed; 500 AA. AC A0A1D8I1N4; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 14-DEC-2022, entry version 16. 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 Name=LIPC {ECO:0000313|EMBL:AOT98812.1}; OS Sousa chinensis (Indo-pacific humpbacked dolphin) (Steno chinensis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti; OC Delphinidae; Sousa. OX NCBI_TaxID=103600 {ECO:0000313|EMBL:AOT98812.1}; RN [1] {ECO:0000313|EMBL:AOT98812.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=27651393; RA Wang Z., Xu S., Du K., Huang F., Chen Z., Zhou K., Ren W., Yang G.; RT "Evolution of Digestive Enzymes and RNASE1 Provides Insights into Dietary RT Switch of Cetaceans."; RL Mol. Biol. Evol. 0:0-0(2016). 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; KX057402; AOT98812.1; -; mRNA. DR AlphaFoldDB; A0A1D8I1N4; -. DR ESTHER; souch-a0a1d8i1n4; 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:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. 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: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 2: Evidence at transcript level; KW Calcium {ECO:0000256|PIRSR:PIRSR000865-2}; KW HDL {ECO:0000256|ARBA:ARBA00022850}; 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..21 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 22..500 FT /note="Hepatic triacylglycerol lipase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5009107646" FT DOMAIN 353..487 FT /note="PLAT" FT /evidence="ECO:0000259|PROSITE:PS50095" FT ACT_SITE 168 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1" FT ACT_SITE 194 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1" FT ACT_SITE 279 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1" FT BINDING 208 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2" FT BINDING 213 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2" FT NON_TER 500 FT /evidence="ECO:0000313|EMBL:AOT98812.1" SQ SEQUENCE 500 AA; 56548 MW; 1E9226054C1F5AF7 CRC64; MENSLCVSIF LVLCIFIQSS AHGQSLGLES FGRRSRAAET KETLQETRTR FLLFKEETNK GCQIRLNHSD TLQQCGFNSS LPLVMIVHGW LMEASLENWI WQMVAALKSQ VARPVNVGLA EWVTLAHTHY SIAVRNTRLV GQEIAALLQW LEESVHFSPS NVHLIGYSLG AHVSGFAGSY MSRKHKVGRI TGLDAAGLLF KRASPSDRLS PDDANFVDAI HTFTQEHMGL SVGIKQPIAH YDFYPNGGSY QPGCHFLELY KHIAKHGLNA ITQAIKCAHE RSVHLFIDSL LHADMQSTAY PCRDMDSFSQ GLCLSCKKGR CNTLGYYARQ EPQSKKSKSL FLVTRAQSPF KVYHYQLKIQ FSNEIEKPAE PTFAMSLLGT KEEMQKIPIT LNKGITSNKT YSFLITLDLD IGELIMTKFK WENSLVWSNV WNTVQTIIPW GRESLHSGLV LKSIRVKAGE TQQRMTFCSE NMNDLQLHPT QEKTFVRCES NSKKLKRKIR //