LIPP_RABIT
ID LIPP_RABIT Reviewed; 465 AA.
AC Q02157;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 122.
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;
GN Name=PNLIP;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1445366; DOI=10.1016/0006-291x(92)91326-l;
RA Aleman-Gomez J.A., Colwell N.S., Sasser T., Kumar V.B.;
RT "Molecular cloning and characterization of rabbit pancreatic triglyceride
RT lipase.";
RL Biochem. Biophys. Res. Commun. 188:964-971(1992).
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:0000305}.
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DR EMBL; M99365; AAA31489.1; -; mRNA.
DR PIR; JC1318; JC1318.
DR RefSeq; NP_001075786.1; NM_001082317.1.
DR AlphaFoldDB; Q02157; -.
DR SMR; Q02157; -.
DR STRING; 9986.ENSOCUP00000012518; -.
DR ESTHER; rabit-1plip; Pancreatic_lipase.
DR GeneID; 100009157; -.
DR KEGG; ocu:100009157; -.
DR CTD; 5406; -.
DR eggNOG; ENOG502QUK7; Eukaryota.
DR InParanoid; Q02157; -.
DR OrthoDB; 534956at2759; -.
DR Proteomes; UP000001811; 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: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; 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; 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 2: Evidence at transcript level;
KW Calcium; Disulfide bond; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000250"
FT CHAIN 17..465
FT /note="Pancreatic triacylglycerol lipase"
FT /id="PRO_0000017787"
FT DOMAIN 355..465
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT ACT_SITE 170
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 194
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 281
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 20..26
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 108..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 255..279
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 303..314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 317..321
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 449..465
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
SQ SEQUENCE 465 AA; 51162 MW; 47F53275997BBA19 CRC64;
MLLLWALPLL LGAVAGLEVC YERLGCFGNR IPWSGGTLER PFSTLPSTPK IVNTRFLLYT
NENPNNFQEI SADASTIRGS NFRTDRKTRF IIHGFTDKGE ENWLSNLCEN LFQVETVNCI
CVDWKGGSRT TYPQATQNIR IVGAEVAYLV GTLQSSLGYS PSNIHVIGHS LGAHAAGEVG
RRTNGTIGRI TGLDPAEPYF QGTPEIVRLD PSDAQFVDVI HTDAAPMVPN LGFGMSQTVG
HLDFFPNGGK EMPGCQKNVL SQIVDINGVW EGTRDFVACN HLRSYKYYAD SIVNPNGFAG
FSCASYTAFS ANKCFPCSNG CPQMGHYADR FSRKTDGVGQ TFYLNTGDSS NFARWRYQVA
VTLSGRRVTG HVLVSLYGSK GNSKQYEIFT GLLKPGDTHL NEFDSDVDVG DVQKVKFVWY
NNVINPTLPK VGASQITVEQ NDGRVFKFCS TDTVREDILL TLTPC
