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 27-MAR-2024, entry version 220. 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 10. 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; DB09093; Chlortetracycline. 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 GlyCosmos; P16233; 1 site, No reported glycans. DR GlyGen; P16233; 1 site. DR iPTMnet; P16233; -. DR PhosphoSitePlus; P16233; -. DR BioMuta; PNLIP; -. DR DMDM; 126318; -. DR MassIVE; P16233; -. DR PaxDb; 9606-ENSP00000358223; -. DR PeptideAtlas; P16233; -. DR ProteomicsDB; 53327; -. DR Antibodypedia; 18720; 578 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 AGR; HGNC:9155; -. 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; RNIDLTP; -. DR OrthoDB; 3428256at2759; -. DR PhylomeDB; P16233; -. DR TreeFam; TF324997; -. DR BioCyc; MetaCyc:HS10947-MONOMER; -. 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; 8 hits in 1149 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 89 other cell types or tissues. 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 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; P16233; HS. 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 //