ID   LIPP_MOUSE              Reviewed;         465 AA.
AC   Q6P8U6;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 137.
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:0000269|PubMed:10769148};
DE   Flags: Precursor;
GN   Name=Pnlip {ECO:0000312|MGI:MGI:97722};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR;
RX   PubMed=15117679; DOI=10.1152/ajpgi.00505.2003;
RA   Sans M.D., Lee S.H., D'Alecy L.G., Williams J.A.;
RT   "Feeding activates protein synthesis in mouse pancreas at the translational
RT   level without increase in mRNA.";
RL   Am. J. Physiol. 287:G667-G675(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   CATALYTIC ACTIVITY, TISSUE SPECIFICITY, FUNCTION, AND ACTIVITY REGULATION.
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).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver, Lung, Pancreas, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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   -!- 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 = (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:0000269|PubMed:10769148};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC         Evidence={ECO:0000305|PubMed:10769148};
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=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:0000269|PubMed:10769148}.
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   -!- TISSUE SPECIFICITY: Pancreas. {ECO:0000269|PubMed:10769148}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; AY387690; AAQ90020.1; -; mRNA.
DR   EMBL; CH466585; EDL01803.1; -; Genomic_DNA.
DR   EMBL; BC061061; AAH61061.1; -; mRNA.
DR   CCDS; CCDS29930.1; -.
DR   RefSeq; NP_081201.2; NM_026925.3.
DR   AlphaFoldDB; Q6P8U6; -.
DR   SMR; Q6P8U6; -.
DR   STRING; 10090.ENSMUSP00000056377; -.
DR   ESTHER; mouse-1plip; Pancreatic_lipase.
DR   iPTMnet; Q6P8U6; -.
DR   PhosphoSitePlus; Q6P8U6; -.
DR   MaxQB; Q6P8U6; -.
DR   PaxDb; 10090-ENSMUSP00000056377; -.
DR   ProteomicsDB; 292261; -.
DR   Antibodypedia; 18720; 578 antibodies from 35 providers.
DR   DNASU; 69060; -.
DR   Ensembl; ENSMUST00000057270.9; ENSMUSP00000056377.8; ENSMUSG00000046008.9.
DR   GeneID; 69060; -.
DR   KEGG; mmu:69060; -.
DR   UCSC; uc008iaq.1; mouse.
DR   AGR; MGI:97722; -.
DR   CTD; 5406; -.
DR   MGI; MGI:97722; Pnlip.
DR   VEuPathDB; HostDB:ENSMUSG00000046008; -.
DR   eggNOG; ENOG502QUK7; Eukaryota.
DR   GeneTree; ENSGT00940000160632; -.
DR   HOGENOM; CLU_027171_0_2_1; -.
DR   InParanoid; Q6P8U6; -.
DR   OMA; RNIDLTP; -.
DR   OrthoDB; 3428256at2759; -.
DR   PhylomeDB; Q6P8U6; -.
DR   TreeFam; TF324997; -.
DR   Reactome; R-MMU-192456; Digestion of dietary lipid.
DR   Reactome; R-MMU-975634; Retinoid metabolism and transport.
DR   BioGRID-ORCS; 69060; 5 hits in 80 CRISPR screens.
DR   ChiTaRS; Pnlip; mouse.
DR   PRO; PR:Q6P8U6; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; Q6P8U6; Protein.
DR   Bgee; ENSMUSG00000046008; Expressed in pyloric antrum and 50 other cell types or tissues.
DR   ExpressionAtlas; Q6P8U6; baseline and differential.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0047376; F:all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity; IEA:RHEA.
DR   GO; GO:0016298; F:lipase activity; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB.
DR   GO; GO:0030299; P:intestinal cholesterol absorption; IMP:MGI.
DR   GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
DR   GO; GO:0006629; P:lipid metabolic process; ISO:MGI.
DR   GO; GO:0009791; P:post-embryonic development; ISO:MGI.
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.
DR   Genevisible; Q6P8U6; MM.
PE   1: Evidence at protein level;
KW   Calcium; Disulfide bond; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Metal-binding; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..465
FT                   /note="Pancreatic triacylglycerol lipase"
FT                   /id="PRO_0000401139"
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"
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"
FT   BINDING         207
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         209
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         212
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        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;  51428 MW;  5CD39E8ABDF43A64 CRC64;
     MLMLWTFAVL LGAVAGREVC FDKLGCFSDD APWSGTLDRP LKALPWSPAQ INTRFLLYTN
     ENPDNYQLIT SDASNIRNSN FRTNRKTRII IHGFIDKGEE NWLSDMCKNM FRVESVNCIC
     VDWKGGSRTT YTQATQNVRV VGAEVALLVN VLQSDLGYSL NNVHLIGHSL GSHIAGEAGK
     RTFGAIGRIT GLDPAEPYFQ GTPEEVRLDP TDAQFVDAIH TDAGPIIPNL GFGMSQTVGH
     LDFFPNGGIE MPGCQKNILS QIVDIDGIWE GTRNFAACNH LRSYKFYTDS IVNPTGFAGF
     SCSSYSLFTA NKCFPCGSGG CPQMGHYADR YPGKTSRLYQ TFYLNTGDKS NFARWRYQVT
     VTLSGQKVTG HILVSLFGNG GNSKQYEVFK GSLQPGTSHV NEFDSDVDVG DLQKVKFIWY
     NNVINPTLPK VGASRITVER NDGRVFNFCS QETVREDVLL TLSPC
//