ID   LIPP_RAT                Reviewed;         465 AA.
AC   P27657;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   04-NOV-2026, entry version 153.
DE   RecName: Full=Pancreatic triacylglycerol lipase {ECO:0000305};
DE            Short=PL;
DE            Short=Pancreatic lipase;
DE            EC=3.1.1.3 {ECO:0000269|PubMed:10769148};
DE   Flags: Precursor;
GN   Name=Pnlip {ECO:0000312|RGD:3360};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=8203536; DOI=10.1152/ajpgi.1994.266.5.g914;
RA   Payne R.M., Sims H.F., Jennens M.L., Lowe M.E.;
RT   "Rat pancreatic lipase and two related proteins: enzymatic properties and
RT   mRNA expression during development.";
RL   Am. J. Physiol. 266:G914-G921(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 17-37.
RC   STRAIN=Sprague-Dawley; TISSUE=Pancreas;
RX   PubMed=8486693; DOI=10.1016/s0021-9258(18)82203-7;
RA   Wishart M.J., Andrews P.C., Nichols R., Blevins G.T. Jr., Logsdon C.D.,
RA   Williams J.A.;
RT   "Identification and cloning of GP-3 from rat pancreatic acinar zymogen
RT   granules as a glycosylated membrane-associated lipase.";
RL   J. Biol. Chem. 268:10303-10311(1993).
RN   [3]
RP   CATALYTIC ACTIVITY, AND FUNCTION.
RX   PubMed=10769148; DOI=10.1021/bi9927235;
RA   van Bennekum A.M., Fisher E.A., Blaner W.S., Harrison E.H.;
RT   "Hydrolysis of retinyl esters by pancreatic triglyceride lipase.";
RL   Biochemistry 39:4900-4906(2000).
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:10769148,
CC       ECO:0000269|PubMed:8203536}.
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:0000269|PubMed:10769148};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC         Evidence={ECO:0000305|PubMed:10769148};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = di-(9Z)-
CC         octadecenoylglycerol + (9Z)-octadecenoate + 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:0000269|PubMed:10769148, ECO:0000269|PubMed:8203536};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC         Evidence={ECO:0000305|PubMed:10769148, ECO:0000305|PubMed:8203536};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2,3-tributanoylglycerol + H2O = dibutanoylglycerol +
CC         butanoate + 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=all-trans-retinyl hexadecanoate + H2O = all-trans-retinol +
CC         hexadecanoate + H(+); 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-octadecenoyl)-
CC         glycerol + (9Z)-octadecenoate + 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:0000269|PubMed:8203536}.
CC   -!- SUBUNIT: Forms a 1:1 stoichiometric complex with (pro)colipase/CLPS.
CC       {ECO:0000250|UniProtKB:P16233}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:8203536}.
CC   -!- TISSUE SPECIFICITY: Expressed by the pancreas (PubMed:8203536).
CC       Pancreatic secretory (zymogen) granule. {ECO:0000269|PubMed:8203536}.
CC   -!- DEVELOPMENTAL STAGE: Expressed a low levels in pancreas at birth,
CC       expression increases through the suckling-weanling period to reach
CC       adult levels by the time of weaning. {ECO:0000269|PubMed:8203536}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; M58369; AAA79888.1; -; mRNA.
DR   RefSeq; NP_037293.2; NM_013161.3.
DR   AlphaFoldDB; P27657; -.
DR   SMR; P27657; -.
DR   FunCoup; P27657; 69.
DR   STRING; 10116.ENSRNOP00000024065; -.
DR   DrugCentral; P27657; -.
DR   GuidetoPHARMACOLOGY; 2590; -.
DR   ESTHER; ratno-1plip; Pancreatic_lipase.
DR   PhosphoSitePlus; P27657; -.
DR   PaxDb; 10116-ENSRNOP00000024065; -.
DR   GeneID; 25702; -.
DR   KEGG; rno:25702; -.
DR   AGR; RGD:3360; -.
DR   CTD; 5406; -.
DR   RGD; 3360; Pnlip.
DR   eggNOG; ENOG502QUK7; Eukaryota.
DR   InParanoid; P27657; -.
DR   OrthoDB; 6422033at2759; -.
DR   PhylomeDB; P27657; -.
DR   Reactome; R-RNO-192456; Digestion of dietary lipid.
DR   Reactome; R-RNO-975634; Retinoid metabolism and transport.
DR   PRO; PR:P27657; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IDA:RGD.
DR   GO; GO:0047376; F:all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity; ISS:UniProtKB.
DR   GO; GO:0120516; F:diacylglycerol lipase activity; IEA:RHEA.
DR   GO; GO:0008970; F:glycerophospholipid phospholipase A1 activity; IBA:GO_Central.
DR   GO; GO:0016298; F:lipase activity; IDA:RGD.
DR   GO; GO:0004465; F:lipoprotein lipase activity; IBA:GO_Central.
DR   GO; GO:0050253; F:retinyl-palmitate esterase activity; ISO:RGD.
DR   GO; GO:0004806; F:triacylglycerol lipase activity; IDA:RGD.
DR   GO; GO:0042632; P:cholesterol homeostasis; IBA:GO_Central.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0034375; P:high-density lipoprotein particle remodeling; IBA:GO_Central.
DR   GO; GO:0030299; P:intestinal cholesterol absorption; ISO:RGD.
DR   GO; GO:0006629; P:lipid metabolic process; ISO:RGD.
DR   GO; GO:0061365; P:positive regulation of triglyceride lipase activity; ISO:RGD.
DR   GO; GO:0009791; P:post-embryonic development; IDA:RGD.
DR   GO; GO:0033993; P:response to lipid; IEP:RGD.
DR   GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR   GO; GO:0001523; P:retinoid metabolic process; ISO:RGD.
DR   GO; GO:0019433; P:triglyceride catabolic process; IBA:GO_Central.
DR   CDD; cd00707; Pancreat_lipase_like; 1.
DR   CDD; cd01759; PLAT_PL; 1.
DR   FunFam; 3.40.50.1820:FF:000033; Pancreatic triacylglycerol lipase; 1.
DR   FunFam; 2.60.60.20:FF:000003; Triacylglycerol lipase; 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_fold.
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   Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Metal-binding; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000269|PubMed:8486693"
FT   CHAIN           17..465
FT                   /note="Pancreatic triacylglycerol lipase"
FT                   /id="PRO_0000017788"
FT   DOMAIN          355..465
FT                   /note="PLAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT   ACT_SITE        169
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P54317"
FT   ACT_SITE        193
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        280
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   BINDING         204
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P16233"
FT   BINDING         207
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P16233"
FT   BINDING         209
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P16233"
FT   BINDING         212
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P16233"
FT   DISULFID        20..26
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT   DISULFID        107..118
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT   DISULFID        254..278
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT   DISULFID        302..313
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT   DISULFID        316..321
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT   DISULFID        449..465
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
SQ   SEQUENCE   465 AA;  51440 MW;  CF014D58AA09A6A2 CRC64;
     MLMLWTFAVL LGAVAGKEVC FDKLGCFSDD APWSGTIDRP LKALPWSPAQ INTRFLLYTN
     ENQDNYQKIT SDASSIRNSN FKTNRKTRII IHGFIDKGEE NWLSDMCKNM FKVESVNCIC
     VDWKGGSRAT YTQATQNVRV VGAEVALLVN VLKSDLGHPP DNVHLIGHSL GSHVAGEAGK
     RTFGAIGRIT GLDAAEPYFQ GTPEEVRLDP TDAQFVDAIH TDAAPIIPNL GFGMSQTVGH
     LDFFPNGGME MPGCQKNILS QIVDIDGIWE GTRDFAACNH LRSYKYYTDS IVNPTGFSGF
     SCSSYNVFSA NKCFPCGSEG CPQMGHYADK YPGKTKELYQ KFYLNTGDKS NFARWRYQVT
     VTLSGQKVTG HILVSLFGNG GNSKQYEVFK GSLHPGDTHV KEFDSDMDVG DLQKVKFIWY
     NNVINPTLPK VGASRISVER NDGRVFNFCS QDTVREDVLL TLSAC
//