ID LIPP_HORSE Reviewed; 461 AA. AC P29183; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 2. DT 08-NOV-2023, entry version 146. DE RecName: Full=Pancreatic triacylglycerol lipase {ECO:0000305}; DE Short=PL; DE Short=PTL; DE Short=Pancreatic lipase; DE EC=3.1.1.3 {ECO:0000250|UniProtKB:P16233}; DE Flags: Precursor; Fragment; GN Name=PNLIP; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, MUTAGENESIS OF RP SER-165, AND FUNCTION. RX PubMed=1587279; DOI=10.1111/j.1432-1033.1992.tb16926.x; RA Kerfelec B., Foglizzo E., Bonicel J., Bougis P.E., Chapus C.; RT "Sequence of horse pancreatic lipase as determined by protein and cDNA RT sequencing. Implications for p-nitrophenyl acetate hydrolysis by pancreatic RT lipases."; RL Eur. J. Biochem. 206:279-287(1992). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX PubMed=8182745; DOI=10.1006/jmbi.1994.1331; RA Bourne Y., Martinez C., Kerfelec B., Lombardo D., Chapus C., Cambillau C.; RT "Horse pancreatic lipase. The crystal structure refined at 2.3-A RT resolution."; RL J. Mol. Biol. 238:709-732(1994). CC -!- FUNCTION: Plays an important role in fat metabolism. It preferentially CC splits the esters of long-chain fatty acids at positions 1 and 3, CC producing mainly 2-monoacylglycerol and free fatty acids, and shows CC considerably higher activity against insoluble emulsified substrates CC than against soluble ones. {ECO:0000269|PubMed:1587279}. 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:0000250|UniProtKB:P16233}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; CC Evidence={ECO:0000250|UniProtKB:P16233}; 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:0000250|UniProtKB:P16233}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476; CC Evidence={ECO:0000250|UniProtKB:P16233}; 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:0000250|UniProtKB:P16233}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; CC Evidence={ECO:0000250|UniProtKB:P16233}; CC -!- CATALYTIC ACTIVITY: CC Reaction=all-trans-retinyl hexadecanoate + H2O = all-trans-retinol + CC H(+) + hexadecanoate; Xref=Rhea:RHEA:13933, ChEBI:CHEBI:7896, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, CC ChEBI:CHEBI:17616; Evidence={ECO:0000250|UniProtKB:P16233}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934; CC Evidence={ECO:0000250|UniProtKB:P16233}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + CC (9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:38455, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, CC ChEBI:CHEBI:52323, ChEBI:CHEBI:75937; CC Evidence={ECO:0000250|UniProtKB:P16233}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38456; CC Evidence={ECO:0000250|UniProtKB:P16233}; CC -!- ACTIVITY REGULATION: Inhibited by bile salts, is reactivated by CC (pro)colipase/CLPS. {ECO:0000250|UniProtKB:P16233}. CC -!- SUBUNIT: Forms a 1:1 stoichiometric complex with (pro)colipase/CLPS. CC {ECO:0000250|UniProtKB:P16233}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P16233}. CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family. CC {ECO:0000305}. 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; X66218; CAA46961.1; -; mRNA. DR PIR; S21223; S21223. DR RefSeq; NP_001157421.1; NM_001163949.1. DR PDB; 1HPL; X-ray; 2.30 A; A/B=13-461. DR PDBsum; 1HPL; -. DR AlphaFoldDB; P29183; -. DR SMR; P29183; -. DR STRING; 9796.ENSECAP00000007877; -. DR ESTHER; horse-1plip; Pancreatic_lipase. DR PaxDb; 9796-ENSECAP00000007877; -. DR GeneID; 100034202; -. DR KEGG; ecb:100034202; -. DR CTD; 5406; -. DR HOGENOM; CLU_027171_0_2_1; -. DR InParanoid; P29183; -. DR OrthoDB; 3428256at2759; -. DR EvolutionaryTrace; P29183; -. DR Proteomes; UP000002281; Unplaced. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0047376; F:all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity; IEA:RHEA. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004806; F:triglyceride lipase activity; ISS:UniProtKB. DR GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central. DR CDD; cd00707; Pancreat_lipase_like; 1. DR CDD; cd01759; PLAT_PL; 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. DR InterPro; IPR013818; Lipase. DR InterPro; IPR016272; Lipase_LIPH. DR InterPro; IPR033906; Lipase_N. DR InterPro; IPR002331; Lipase_panc. DR InterPro; IPR001024; PLAT/LH2_dom. DR InterPro; IPR036392; PLAT/LH2_dom_sf. DR InterPro; IPR000734; TAG_lipase. DR PANTHER; PTHR11610; LIPASE; 1. DR PANTHER; PTHR11610:SF147; PANCREATIC TRIACYLGLYCEROL LIPASE; 1. DR Pfam; PF00151; Lipase; 1. DR Pfam; PF01477; PLAT; 1. DR PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1. DR PRINTS; PR00823; PANCLIPASE. 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; PS00120; LIPASE_SER; 1. DR PROSITE; PS50095; PLAT; 1. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Direct protein sequencing; Disulfide bond; KW Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding; KW Reference proteome; Secreted; Signal. FT SIGNAL <1..12 FT CHAIN 13..461 FT /note="Pancreatic triacylglycerol lipase" FT /id="PRO_0000017784" FT DOMAIN 351..461 FT /note="PLAT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152" FT ACT_SITE 165 FT /note="Nucleophile" FT ACT_SITE 189 FT /note="Charge relay system" FT ACT_SITE 276 FT /note="Charge relay system" FT BINDING 200 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 203 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 205 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 208 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT DISULFID 16..22 FT DISULFID 103..114 FT DISULFID 250..274 FT DISULFID 298..309 FT DISULFID 312..317 FT DISULFID 445..461 FT MUTAGEN 165 FT /note="S->X: 80% loss of P-nitrophenyl acetate hydrolysis FT activity." FT /evidence="ECO:0000269|PubMed:1587279" FT NON_TER 1 FT STRAND 14..17 FT /evidence="ECO:0007829|PDB:1HPL" FT TURN 18..20 FT /evidence="ECO:0007829|PDB:1HPL" FT STRAND 21..24 FT /evidence="ECO:0007829|PDB:1HPL" FT STRAND 29..32 FT /evidence="ECO:0007829|PDB:1HPL" FT HELIX 44..47 FT /evidence="ECO:0007829|PDB:1HPL" FT STRAND 50..55 FT /evidence="ECO:0007829|PDB:1HPL" FT STRAND 58..65 FT /evidence="ECO:0007829|PDB:1HPL" FT HELIX 69..74 FT /evidence="ECO:0007829|PDB:1HPL" FT STRAND 81..87 FT /evidence="ECO:0007829|PDB:1HPL" FT HELIX 98..109 FT /evidence="ECO:0007829|PDB:1HPL" FT STRAND 112..118 FT /evidence="ECO:0007829|PDB:1HPL" FT HELIX 120..123 FT /evidence="ECO:0007829|PDB:1HPL" FT HELIX 127..152 FT /evidence="ECO:0007829|PDB:1HPL" FT HELIX 156..158 FT /evidence="ECO:0007829|PDB:1HPL" FT STRAND 159..164 FT /evidence="ECO:0007829|PDB:1HPL" FT HELIX 167..177 FT /evidence="ECO:0007829|PDB:1HPL" FT TURN 178..180 FT /evidence="ECO:0007829|PDB:1HPL" FT STRAND 182..189 FT /evidence="ECO:0007829|PDB:1HPL" FT TURN 193..197 FT /evidence="ECO:0007829|PDB:1HPL" FT TURN 200..202 FT /evidence="ECO:0007829|PDB:1HPL" FT HELIX 206..208 FT /evidence="ECO:0007829|PDB:1HPL" FT STRAND 209..215 FT /evidence="ECO:0007829|PDB:1HPL" FT HELIX 222..225 FT /evidence="ECO:0007829|PDB:1HPL" FT STRAND 235..241 FT /evidence="ECO:0007829|PDB:1HPL" FT HELIX 261..265 FT /evidence="ECO:0007829|PDB:1HPL" FT HELIX 274..288 FT /evidence="ECO:0007829|PDB:1HPL" FT HELIX 301..305 FT /evidence="ECO:0007829|PDB:1HPL" FT STRAND 319..321 FT /evidence="ECO:0007829|PDB:1HPL" FT HELIX 324..326 FT /evidence="ECO:0007829|PDB:1HPL" FT TURN 328..331 FT /evidence="ECO:0007829|PDB:1HPL" FT STRAND 332..340 FT /evidence="ECO:0007829|PDB:1HPL" FT STRAND 344..347 FT /evidence="ECO:0007829|PDB:1HPL" FT STRAND 351..361 FT /evidence="ECO:0007829|PDB:1HPL" FT STRAND 364..374 FT /evidence="ECO:0007829|PDB:1HPL" FT STRAND 382..389 FT /evidence="ECO:0007829|PDB:1HPL" FT STRAND 394..403 FT /evidence="ECO:0007829|PDB:1HPL" FT STRAND 407..417 FT /evidence="ECO:0007829|PDB:1HPL" FT STRAND 427..435 FT /evidence="ECO:0007829|PDB:1HPL" FT STRAND 441..445 FT /evidence="ECO:0007829|PDB:1HPL" FT STRAND 456..461 FT /evidence="ECO:0007829|PDB:1HPL" SQ SEQUENCE 461 AA; 50921 MW; 382F33F3CE446738 CRC64; WTLSLLLGAV VGNEVCYERL GCFSDDSPWA GIVERPLKIL PWSPEKVNTR FLLYTNENPD NFQEIVADPS TIQSSNFNTG RKTRFIIHGF IDKGEESWLS TMCQNMFKVE SVNCICVDWK SGSRTAYSQA SQNVRIVGAE VAYLVGVLQS SFDYSPSNVH IIGHSLGSHA AGEAGRRTNG AVGRITGLDP AEPCFQGTPE LVRLDPSDAQ FVDVIHTDIA PFIPNLGFGM SQTAGHLDFF PNGGKEMPGC QKNVLSQIVD IDGIWQGTRD FAACNHLRSY KYYTDSILNP DGFAGFSCAS YSDFTANKCF PCSSEGCPQM GHYADRFPGR TKGVGQLFYL NTGDASNFAR WRYRVDVTLS GKKVTGHVLV SLFGNKGNSR QYEIFQGTLK PDNTYSNEFD SDVEVGDLEK VKFIWYNNVI NLTLPKVGAS KITVERNDGS VFNFCSEETV REDVLLTLTA C //