LIPP_MOUSE
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 03-AUG-2022, entry version 128.
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; Q6P8U6; -.
DR PRIDE; Q6P8U6; -.
DR ProteomicsDB; 292261; -.
DR Antibodypedia; 18720; 514 antibodies from 35 providers.
DR DNASU; 69060; -.
DR Ensembl; ENSMUST00000057270; ENSMUSP00000056377; ENSMUSG00000046008.
DR GeneID; 69060; -.
DR KEGG; mmu:69060; -.
DR UCSC; uc008iaq.1; mouse.
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; FQTENCF; -.
DR OrthoDB; 534956at2759; -.
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 75 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 tissues.
DR ExpressionAtlas; Q6P8U6; baseline and differential.
DR Genevisible; Q6P8U6; MM.
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:0061365; P:positive regulation of triglyceride lipase activity; ISO:MGI.
DR GO; GO:0009791; P:post-embryonic development; ISO:MGI.
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 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
