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Pancreatic triacylglycerol lipase (PL) (PTL) (Pancreatic lipase) (EC 3.1.1.3)

 LIPP_MOUSE              Reviewed;         465 AA.
Q6P8U6;
30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
25-OCT-2017, entry version 107.
RecName: Full=Pancreatic triacylglycerol lipase;
Short=PL;
Short=PTL;
Short=Pancreatic lipase;
EC=3.1.1.3;
Flags: Precursor;
Name=Pnlip;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=ICR;
PubMed=15117679; DOI=10.1152/ajpgi.00505.2003;
Sans M.D., Lee S.H., D'Alecy L.G., Williams J.A.;
"Feeding activates protein synthesis in mouse pancreas at the
translational level without increase in mRNA.";
Am. J. Physiol. 287:G667-G675(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
PubMed=10769148; DOI=10.1021/bi9927235;
van Bennekum A.M., Fisher E.A., Blaner W.S., Harrison E.H.;
"Hydrolysis of retinyl esters by pancreatic triglyceride lipase.";
Biochemistry 39:4900-4906(2000).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver, Lung, Pancreas, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Plays an important role in fat metabolism. It
preferentially splits the esters of long-chain fatty acids at
positions 1 and 3, producing mainly 2-monoacylglycerol and free
fatty acids, and shows considerably higher activity against
insoluble emulsified substrates than against soluble ones (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Triacylglycerol + H(2)O = diacylglycerol + a
carboxylate. {ECO:0000269|PubMed:10769148}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- TISSUE SPECIFICITY: Pancreas. {ECO:0000269|PubMed:10769148}.
-!- INDUCTION: By colipase/CLPS in the presence of bile salts.
-!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY387690; AAQ90020.1; -; mRNA.
EMBL; CH466585; EDL01803.1; -; Genomic_DNA.
EMBL; BC061061; AAH61061.1; -; mRNA.
CCDS; CCDS29930.1; -.
RefSeq; NP_081201.2; NM_026925.3.
UniGene; Mm.20407; -.
ProteinModelPortal; Q6P8U6; -.
SMR; Q6P8U6; -.
STRING; 10090.ENSMUSP00000056377; -.
ESTHER; mouse-1plip; Pancreatic_lipase.
iPTMnet; Q6P8U6; -.
PhosphoSitePlus; Q6P8U6; -.
MaxQB; Q6P8U6; -.
PaxDb; Q6P8U6; -.
PRIDE; Q6P8U6; -.
Ensembl; ENSMUST00000057270; ENSMUSP00000056377; ENSMUSG00000046008.
GeneID; 69060; -.
KEGG; mmu:69060; -.
UCSC; uc008iaq.1; mouse.
CTD; 5406; -.
MGI; MGI:97722; Pnlip.
eggNOG; ENOG410IHRX; Eukaryota.
eggNOG; ENOG410Y92X; LUCA.
GeneTree; ENSGT00760000119069; -.
HOGENOM; HOG000038552; -.
HOVERGEN; HBG003243; -.
InParanoid; Q6P8U6; -.
KO; K14073; -.
OMA; AGKEVCF; -.
OrthoDB; EOG091G0DJ5; -.
PhylomeDB; Q6P8U6; -.
TreeFam; TF324997; -.
Reactome; R-MMU-192456; Digestion of dietary lipid.
Reactome; R-MMU-975634; Retinoid metabolism and transport.
ChiTaRS; Pnlip; mouse.
PRO; PR:Q6P8U6; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000046008; -.
Genevisible; Q6P8U6; MM.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0016298; F:lipase activity; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB.
GO; GO:0030299; P:intestinal cholesterol absorption; IMP:MGI.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0006629; P:lipid metabolic process; ISO:MGI.
GO; GO:0061365; P:positive regulation of triglyceride lipase activity; ISO:MGI.
CDD; cd00707; Pancreat_lipase_like; 1.
Gene3D; 2.60.60.20; -; 1.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR013818; Lipase/vitellogenin.
InterPro; IPR016272; Lipase_LIPH.
InterPro; IPR033906; Lipase_N.
InterPro; IPR002331; Lipase_panc.
InterPro; IPR001024; PLAT/LH2_dom.
InterPro; IPR036392; PLAT/LH2_dom_sf.
InterPro; IPR000734; TAG_lipase.
PANTHER; PTHR11610; PTHR11610; 1.
Pfam; PF00151; Lipase; 1.
Pfam; PF01477; PLAT; 1.
PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
PRINTS; PR00823; PANCLIPASE.
PRINTS; PR00821; TAGLIPASE.
SMART; SM00308; LH2; 1.
SUPFAM; SSF49723; SSF49723; 1.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS00120; LIPASE_SER; 1.
PROSITE; PS50095; PLAT; 1.
1: Evidence at protein level;
Calcium; Complete proteome; Disulfide bond; Hydrolase;
Lipid degradation; Lipid metabolism; Metal-binding;
Reference proteome; Secreted; Signal.
SIGNAL 1 16 {ECO:0000255}.
CHAIN 17 465 Pancreatic triacylglycerol lipase.
/FTId=PRO_0000401139.
DOMAIN 355 465 PLAT. {ECO:0000255|PROSITE-
ProRule:PRU00152}.
ACT_SITE 169 169 Nucleophile. {ECO:0000250}.
ACT_SITE 193 193 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10037}.
ACT_SITE 280 280 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10037}.
METAL 204 204 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 207 207 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 209 209 Calcium. {ECO:0000250}.
METAL 212 212 Calcium. {ECO:0000250}.
DISULFID 20 26 {ECO:0000255|PROSITE-ProRule:PRU00152}.
DISULFID 107 118 {ECO:0000255|PROSITE-ProRule:PRU00152}.
DISULFID 254 278 {ECO:0000255|PROSITE-ProRule:PRU00152}.
DISULFID 302 313 {ECO:0000255|PROSITE-ProRule:PRU00152}.
DISULFID 316 321 {ECO:0000255|PROSITE-ProRule:PRU00152}.
DISULFID 449 465 {ECO:0000255|PROSITE-ProRule:PRU00152}.
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


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