LIPP_HORSE
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 03-AUG-2022, entry version 142.
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}.
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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; P29183; -.
DR GeneID; 100034202; -.
DR KEGG; ecb:100034202; -.
DR CTD; 5406; -.
DR HOGENOM; CLU_027171_0_2_1; -.
DR InParanoid; P29183; -.
DR OrthoDB; 534956at2759; -.
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:0016298; F:lipase activity; IBA:GO_Central.
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 Gene3D; 3.40.50.1820; -; 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; PTHR11610; 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; SSF49723; SSF49723; 1.
DR SUPFAM; SSF53474; SSF53474; 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
