LIPP_FELCA
ID LIPP_FELCA Reviewed; 25 AA.
AC P83629;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 25-MAY-2022, entry version 73.
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: Fragment;
GN Name=PNLIP;
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE.
RC TISSUE=Pancreas {ECO:0000269|PubMed:12524043};
RX PubMed=12524043; DOI=10.1016/s1096-4959(02)00222-1;
RA Steiner J.M., Wilson B.G., Williams D.A.;
RT "Purification and partial characterization of feline classical pancreatic
RT lipase.";
RL Comp. Biochem. Physiol. 134B:151-159(2003).
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:0000250|UniProtKB:P16233}.
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:0000255}.
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DR AlphaFoldDB; P83629; -.
DR SMR; P83629; -.
DR STRING; 9685.ENSFCAP00000001406; -.
DR ESTHER; felca-lipp; Pancreatic_lipase.
DR eggNOG; ENOG502QUK7; Eukaryota.
DR HOGENOM; CLU_027171_0_2_1; -.
DR TreeFam; TF324997; -.
DR Proteomes; UP000011712; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0047376; F:all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity; IEA:RHEA.
DR GO; GO:0004806; F:triglyceride lipase activity; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR002331; Lipase_panc.
DR PRINTS; PR00823; PANCLIPASE.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Hydrolase; Lipid degradation;
KW Lipid metabolism; Reference proteome; Secreted.
FT CHAIN 1..>25
FT /note="Pancreatic triacylglycerol lipase"
FT /id="PRO_0000090355"
FT DISULFID 4..10
FT /evidence="ECO:0000250"
FT UNSURE 4
FT UNSURE 10
FT NON_TER 25
FT /evidence="ECO:0000303|PubMed:12524043"
SQ SEQUENCE 25 AA; 2791 MW; F12B9DB124B139CD CRC64;
KEICFPRLGC FSDDAPWAGI AQRPL
