LIPP_HUMAN
ID LIPP_HUMAN Reviewed; 465 AA.
AC P16233; Q5VSQ2;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 211.
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|HGNC:HGNC:9155};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2479644; DOI=10.1016/s0021-9258(19)47215-3;
RA Lowe M.E., Rosenblum J.L., Strauss A.W.;
RT "Cloning and characterization of human pancreatic lipase cDNA.";
RL J. Biol. Chem. 264:20042-20048(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas;
RX PubMed=1379598; DOI=10.1016/s0021-9258(18)42032-7;
RA Giller T., Buchwald P., Blum-Kaelin D., Hunziker W.;
RT "Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2.
RT Differences in colipase dependence and in lipase activity.";
RL J. Biol. Chem. 267:16509-16516(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8406023; DOI=10.1016/0378-1119(93)90307-o;
RA Sims H.F., Jennens M.L., Lowe M.E.;
RT "The human pancreatic lipase-encoding gene: structure and conservation of
RT an Alu sequence in the lipase gene family.";
RL Gene 131:281-285(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [8]
RP CATALYTIC ACTIVITY, 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 [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17401110; DOI=10.1194/jlr.m600486-jlr200;
RA Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R.,
RA Carriere F., De Caro A.;
RT "Further biochemical characterization of human pancreatic lipase-related
RT protein 2 expressed in yeast cells.";
RL J. Lipid Res. 48:1539-1549(2007).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND REGION.
RX PubMed=26494624; DOI=10.1074/jbc.m115.683375;
RA Xiao X., Lowe M.E.;
RT "The beta5-Loop and Lid Domain Contribute to the Substrate Specificity of
RT Pancreatic Lipase-related Protein 2 (PNLIPRP2).";
RL J. Biol. Chem. 290:28847-28856(2015).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=2106079; DOI=10.1038/343771a0;
RA Winkler F.K., D'Arcy A., Hunziker W.;
RT "Structure of human pancreatic lipase.";
RL Nature 343:771-774(1990).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH CLPS.
RX PubMed=1522902; DOI=10.1038/359159a0;
RA van Tilbeurgh H., Sarda L., Verger R., Cambillau C.;
RT "Structure of the pancreatic lipase-procolipase complex.";
RL Nature 359:159-162(1992).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH CLPS, AND INTERACTION
RP WITH CLPS.
RX PubMed=8479519; DOI=10.1038/362814a0;
RA van Tilbeurgh H., Egloff M.-P., Martinez C., Rugani N., Verger R.,
RA Cambillau C.;
RT "Interfacial activation of the lipase-procolipase complex by mixed micelles
RT revealed by X-ray crystallography.";
RL Nature 362:814-820(1993).
RN [14]
RP STRUCTURE BY NMR OF 354-465.
RX PubMed=8029213; DOI=10.1093/protein/7.4.563;
RA Carriere F., Thirstrup K., Boel E., Verger R., Thim L.;
RT "Structure-function relationships in naturally occurring mutants of
RT pancreatic lipase.";
RL Protein Eng. 7:563-569(1994).
RN [15]
RP INVOLVEMENT IN PNLIPD, AND VARIANT PNLIPD MET-221.
RX PubMed=24262094; DOI=10.1194/jlr.p041103;
RA Behar D.M., Basel-Vanagaite L., Glaser F., Kaplan M., Tzur S., Magal N.,
RA Eidlitz-Markus T., Haimi-Cohen Y., Sarig G., Bormans C., Shohat M.,
RA Zeharia A.;
RT "Identification of a novel mutation in the PNLIP gene in two brothers with
RT congenital pancreatic lipase deficiency.";
RL J. Lipid Res. 55:307-312(2014).
RN [16]
RP CHARACTERIZATION OF VARIANT PNLIPD MET-221, SUBCELLULAR LOCATION, FUNCTION,
RP AND CATALYTIC ACTIVITY.
RX PubMed=25862608; DOI=10.1016/j.bbadis.2015.04.002;
RA Szabo A., Xiao X., Haughney M., Spector A., Sahin-Toth M., Lowe M.E.;
RT "A novel mutation in PNLIP causes pancreatic triglyceride lipase deficiency
RT through protein misfolding.";
RL Biochim. Biophys. Acta 1852:1372-1379(2015).
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:17401110}.
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-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:0000269|PubMed:25862608};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476;
CC Evidence={ECO:0000269|PubMed:25862608};
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, ECO:0000269|PubMed:17401110};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC Evidence={ECO:0000305|PubMed:10769148, ECO:0000305|PubMed:17401110};
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:0000269|PubMed:10769148};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934;
CC Evidence={ECO:0000305|PubMed:10769148};
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:0000269|PubMed:17401110};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38456;
CC Evidence={ECO:0000305|PubMed:17401110};
CC -!- ACTIVITY REGULATION: Inhibited by bile salts, is reactivated by
CC (pro)colipase/CLPS. {ECO:0000269|PubMed:10769148}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:17401110};
CC -!- SUBUNIT: Forms a 1:1 stoichiometric complex with (pro)colipase/CLPS.
CC {ECO:0000269|PubMed:8479519}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25862608}.
CC -!- DISEASE: Pancreatic lipase deficiency (PNLIPD) [MIM:614338]: An
CC autosomal recessive disorder characterized by exocrine pancreatic
CC failure. Clinical findings include oily/greasy stools from infancy or
CC early childhood, absence of discernible pancreatic disease, and
CC significantly decreased pancreatic lipolytic activity.
CC {ECO:0000269|PubMed:24262094, ECO:0000269|PubMed:25862608}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Pancreatic lipase entry;
CC URL="https://en.wikipedia.org/wiki/Pancreatic_lipase";
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DR EMBL; J05125; AAA36740.1; -; mRNA.
DR EMBL; M93285; AAA60129.1; -; mRNA.
DR EMBL; L24529; AAA99053.1; -; Genomic_DNA.
DR EMBL; L11242; AAA99053.1; JOINED; Genomic_DNA.
DR EMBL; L24502; AAA99053.1; JOINED; Genomic_DNA.
DR EMBL; L24522; AAA99053.1; JOINED; Genomic_DNA.
DR EMBL; L24523; AAA99053.1; JOINED; Genomic_DNA.
DR EMBL; L24525; AAA99053.1; JOINED; Genomic_DNA.
DR EMBL; L24526; AAA99053.1; JOINED; Genomic_DNA.
DR EMBL; L24527; AAA99053.1; JOINED; Genomic_DNA.
DR EMBL; L24528; AAA99053.1; JOINED; Genomic_DNA.
DR EMBL; AK313941; BAG36659.1; -; mRNA.
DR EMBL; AL731653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49451.1; -; Genomic_DNA.
DR EMBL; BC014309; AAH14309.1; -; mRNA.
DR CCDS; CCDS7594.1; -.
DR PIR; C43357; C43357.
DR RefSeq; NP_000927.1; NM_000936.3.
DR PDB; 1GPL; X-ray; 2.01 A; A=360-465.
DR PDB; 1LPA; X-ray; 3.04 A; B=17-465.
DR PDB; 1LPB; X-ray; 2.46 A; B=17-465.
DR PDB; 1N8S; X-ray; 3.04 A; A=17-465.
DR PDBsum; 1GPL; -.
DR PDBsum; 1LPA; -.
DR PDBsum; 1LPB; -.
DR PDBsum; 1N8S; -.
DR AlphaFoldDB; P16233; -.
DR SMR; P16233; -.
DR BioGRID; 111407; 10.
DR CORUM; P16233; -.
DR IntAct; P16233; 9.
DR MINT; P16233; -.
DR STRING; 9606.ENSP00000358223; -.
DR BindingDB; P16233; -.
DR ChEMBL; CHEMBL1812; -.
DR DrugBank; DB04233; (Hydroxyethyloxy)Tri(Ethyloxy)Octane.
DR DrugBank; DB02451; B-nonylglucoside.
DR DrugBank; DB06586; Cetilistat.
DR DrugBank; DB08909; Glycerol phenylbutyrate.
DR DrugBank; DB08222; METHOXYUNDECYLPHOSPHINIC ACID.
DR DrugBank; DB01083; Orlistat.
DR DrugCentral; P16233; -.
DR GuidetoPHARMACOLOGY; 2590; -.
DR SwissLipids; SLP:000000529; -.
DR ESTHER; human-PNLIP; Pancreatic_lipase.
DR GlyGen; P16233; 1 site.
DR iPTMnet; P16233; -.
DR PhosphoSitePlus; P16233; -.
DR BioMuta; PNLIP; -.
DR DMDM; 126318; -.
DR MassIVE; P16233; -.
DR PaxDb; P16233; -.
DR PeptideAtlas; P16233; -.
DR PRIDE; P16233; -.
DR ProteomicsDB; 53327; -.
DR Antibodypedia; 18720; 514 antibodies from 35 providers.
DR DNASU; 5406; -.
DR Ensembl; ENST00000369221.2; ENSP00000358223.2; ENSG00000175535.6.
DR GeneID; 5406; -.
DR KEGG; hsa:5406; -.
DR MANE-Select; ENST00000369221.2; ENSP00000358223.2; NM_000936.4; NP_000927.1.
DR UCSC; uc001lcm.4; human.
DR CTD; 5406; -.
DR DisGeNET; 5406; -.
DR GeneCards; PNLIP; -.
DR HGNC; HGNC:9155; PNLIP.
DR HPA; ENSG00000175535; Tissue enriched (pancreas).
DR MalaCards; PNLIP; -.
DR MIM; 246600; gene.
DR MIM; 614338; phenotype.
DR neXtProt; NX_P16233; -.
DR OpenTargets; ENSG00000175535; -.
DR PharmGKB; PA33478; -.
DR VEuPathDB; HostDB:ENSG00000175535; -.
DR eggNOG; ENOG502QUK7; Eukaryota.
DR GeneTree; ENSGT00940000160632; -.
DR HOGENOM; CLU_027171_0_2_1; -.
DR InParanoid; P16233; -.
DR OMA; SPWAGIV; -.
DR OrthoDB; 534956at2759; -.
DR PhylomeDB; P16233; -.
DR TreeFam; TF324997; -.
DR BioCyc; MetaCyc:HS10947-MON; -.
DR BRENDA; 3.1.1.3; 2681.
DR PathwayCommons; P16233; -.
DR Reactome; R-HSA-192456; Digestion of dietary lipid.
DR Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR SABIO-RK; P16233; -.
DR SignaLink; P16233; -.
DR BioGRID-ORCS; 5406; 7 hits in 1065 CRISPR screens.
DR ChiTaRS; PNLIP; human.
DR EvolutionaryTrace; P16233; -.
DR GeneWiki; Pancreatic_lipase; -.
DR GenomeRNAi; 5406; -.
DR Pharos; P16233; Tclin.
DR PRO; PR:P16233; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P16233; protein.
DR Bgee; ENSG00000175535; Expressed in body of pancreas and 88 other tissues.
DR Genevisible; P16233; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0047376; F:all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity; IEA:RHEA.
DR GO; GO:0016298; F:lipase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004806; F:triglyceride lipase activity; ISS:UniProtKB.
DR GO; GO:0030299; P:intestinal cholesterol absorption; IEA:Ensembl.
DR GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IMP:UniProtKB.
DR GO; GO:0061365; P:positive regulation of triglyceride lipase activity; IDA:CACAO.
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 3D-structure; Calcium; Disease variant; Disulfide bond; Glycoprotein;
KW Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..16
FT CHAIN 17..465
FT /note="Pancreatic triacylglycerol lipase"
FT /id="PRO_0000017785"
FT DOMAIN 355..465
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT ACT_SITE 169
FT /note="Nucleophile"
FT ACT_SITE 193
FT /note="Charge relay system"
FT ACT_SITE 280
FT /note="Charge relay system"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 20..26
FT DISULFID 107..118
FT DISULFID 254..278
FT DISULFID 302..313
FT DISULFID 316..321
FT DISULFID 449..465
FT VARIANT 221
FT /note="T -> M (in PNLIPD; loss of function in lipid
FT catabolic process; the mutant is not secreted;
FT dbSNP:rs746000327)"
FT /evidence="ECO:0000269|PubMed:24262094,
FT ECO:0000269|PubMed:25862608"
FT /id="VAR_078977"
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:1LPB"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:1LPB"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1LPB"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:1LPB"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:1LPB"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:1LPB"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:1LPB"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:1LPB"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1LPB"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:1LPB"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:1LPB"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:1LPB"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:1LPB"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:1LPB"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:1LPB"
FT HELIX 131..156
FT /evidence="ECO:0007829|PDB:1LPB"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:1LPB"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:1LPB"
FT HELIX 170..180
FT /evidence="ECO:0007829|PDB:1LPB"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:1LPB"
FT STRAND 186..193
FT /evidence="ECO:0007829|PDB:1LPB"
FT TURN 197..201
FT /evidence="ECO:0007829|PDB:1LPB"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:1LPB"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:1LPB"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:1LPB"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:1LPB"
FT STRAND 239..245
FT /evidence="ECO:0007829|PDB:1LPB"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:1LPB"
FT HELIX 258..262
FT /evidence="ECO:0007829|PDB:1LPB"
FT HELIX 268..291
FT /evidence="ECO:0007829|PDB:1LPB"
FT TURN 294..297
FT /evidence="ECO:0007829|PDB:1LPB"
FT HELIX 305..309
FT /evidence="ECO:0007829|PDB:1LPB"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:1LPB"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:1LPB"
FT TURN 332..335
FT /evidence="ECO:0007829|PDB:1LPB"
FT STRAND 336..344
FT /evidence="ECO:0007829|PDB:1LPB"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:1LPB"
FT STRAND 360..365
FT /evidence="ECO:0007829|PDB:1GPL"
FT STRAND 368..380
FT /evidence="ECO:0007829|PDB:1GPL"
FT STRAND 382..393
FT /evidence="ECO:0007829|PDB:1GPL"
FT STRAND 398..407
FT /evidence="ECO:0007829|PDB:1GPL"
FT STRAND 411..423
FT /evidence="ECO:0007829|PDB:1GPL"
FT STRAND 430..439
FT /evidence="ECO:0007829|PDB:1GPL"
FT STRAND 445..449
FT /evidence="ECO:0007829|PDB:1GPL"
FT STRAND 460..464
FT /evidence="ECO:0007829|PDB:1GPL"
SQ SEQUENCE 465 AA; 51157 MW; 2BC49CC7F0E2DF52 CRC64;
MLPLWTLSLL LGAVAGKEVC YERLGCFSDD SPWSGITERP LHILPWSPKD VNTRFLLYTN
ENPNNFQEVA ADSSSISGSN FKTNRKTRFI IHGFIDKGEE NWLANVCKNL FKVESVNCIC
VDWKGGSRTG YTQASQNIRI VGAEVAYFVE FLQSAFGYSP SNVHVIGHSL GAHAAGEAGR
RTNGTIGRIT GLDPAEPCFQ GTPELVRLDP SDAKFVDVIH TDGAPIVPNL GFGMSQVVGH
LDFFPNGGVE MPGCKKNILS QIVDIDGIWE GTRDFAACNH LRSYKYYTDS IVNPDGFAGF
PCASYNVFTA NKCFPCPSGG CPQMGHYADR YPGKTNDVGQ KFYLDTGDAS NFARWRYKVS
VTLSGKKVTG HILVSLFGNK GNSKQYEIFK GTLKPDSTHS NEFDSDVDVG DLQMVKFIWY
NNVINPTLPR VGASKIIVET NVGKQFNFCS PETVREEVLL TLTPC
