ID LIPL_HUMAN Reviewed; 475 AA. AC P06858; B2R5T9; Q16282; Q16283; Q96FC4; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 02-SEP-2026, entry version 268. DE RecName: Full=Lipoprotein lipase; DE Short=LPL; DE EC=3.1.1.34 {ECO:0000269|PubMed:11342582, ECO:0000269|PubMed:12032167, ECO:0000269|PubMed:1371284, ECO:0000269|PubMed:2340307, ECO:0000269|PubMed:27578112, ECO:0000269|PubMed:30559189, ECO:0000269|PubMed:7592706}; DE AltName: Full=Phospholipase A1; DE EC=3.1.1.32 {ECO:0000269|PubMed:12032167, ECO:0000269|PubMed:7592706}; DE Flags: Precursor; GN Name=LPL; Synonyms=LIPD; 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=3823907; DOI=10.1126/science.3823907; RA Wion K.L., Kirchgessner T.G., Lusis A.J., Schotz M.C., Lawn R.M.; RT "Human lipoprotein lipase complementary DNA sequence."; RL Science 235:1638-1641(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Placenta; RX PubMed=2701938; DOI=10.1093/nar/17.6.2351; RA Gotoda T., Senda M., Gamou T., Furuichi Y., Oka K.; RT "Nucleotide sequence of human cDNA coding for a lipoprotein lipase (LPL) RT cloned from placental cDNA library."; RL Nucleic Acids Res. 17:2351-2352(1989). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2243796; DOI=10.1093/nar/18.21.6436; RA Takagi A., Ikeda Y., Yamamoto A.; RT "DNA sequence of lipoprotein lipase cDNA cloned from human monocytic RT leukemia THP-1 cells."; RL Nucleic Acids Res. 18:6436-6436(1990). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1537564; DOI=10.1016/0378-1119(92)90658-c; RA Chuat J.-C., Raisonnier A., Etienne J., Galibert F.; RT "The lipoprotein lipase-encoding human gene: sequence from intron-6 to RT intron-9 and presence in intron-7 of a 40-million-year-old Alu sequence."; RL Gene 110:257-261(1992). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-318. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cerebellum; 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 [7] 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-318. RC TISSUE=Brain; 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 [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5. RX PubMed=1406652; DOI=10.1128/mcb.12.10.4622-4633.1992; RA Enerbaeck S., Ohlsson B.G., Samuelsson L., Bjursell G.; RT "Characterization of the human lipoprotein lipase (LPL) promoter: evidence RT of two cis-regulatory regions, LP-alpha and LP-beta, of importance for the RT differentiation-linked induction of the LPL gene during adipogenesis."; RL Mol. Cell. Biol. 12:4622-4633(1992). RN [10] RP PROTEIN SEQUENCE OF 28-44, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AND RP TISSUE SPECIFICITY. RC TISSUE=Milk; RX PubMed=2340307; DOI=10.1016/0005-2760(90)90213-h; RA Zechner R.; RT "Rapid and simple isolation procedure for lipoprotein lipase from human RT milk."; RL Biochim. Biophys. Acta 1044:20-25(1990). RN [11] RP FUNCTION, CATALYTIC ACTIVITY, REGION, AND MUTAGENESIS OF 244-ASN--VAL-264; RP 245-ILE--LEU-263; 245-ILE--ALA-248 AND 262-GLN--LEU-263. RX PubMed=7592706; DOI=10.1074/jbc.270.43.25396; RA Dugi K.A., Dichek H.L., Santamarina-Fojo S.; RT "Human hepatic and lipoprotein lipase: the loop covering the catalytic site RT mediates lipase substrate specificity."; RL J. Biol. Chem. 270:25396-25401(1995). RN [12] RP FUNCTION. RX PubMed=8675619; DOI=10.1172/jci118319; RA Weinstock P.H., Bisgaier C.L., Aalto-Setaelae K., Radner H., RA Ramakrishnan R., Levak-Frank S., Essenburg A.D., Zechner R., Breslow J.L.; RT "Severe hypertriglyceridemia, reduced high density lipoprotein, and RT neonatal death in lipoprotein lipase knockout mice. Mild RT hypertriglyceridemia with impaired very low density lipoprotein clearance RT in heterozygotes."; RL J. Clin. Invest. 96:2555-2568(1995). RN [13] RP HEPARIN-BINDING, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF LYS-430; ARG-432 AND LYS-434. RX PubMed=11342582; DOI=10.1172/jci11774; RA Lutz E.P., Merkel M., Kako Y., Melford K., Radner H., Breslow J.L., RA Bensadoun A., Goldberg I.J.; RT "Heparin-binding defective lipoprotein lipase is unstable and causes RT abnormalities in lipid delivery to tissues."; RL J. Clin. Invest. 107:1183-1192(2001). RN [14] RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION. RX PubMed=12032167; DOI=10.1016/s0022-2275(20)30466-1; RA McCoy M.G., Sun G.-S., Marchadier D., Maugeais C., Glick J.M., Rader D.J.; RT "Characterization of the lipolytic activity of endothelial lipase."; RL J. Lipid Res. 43:921-929(2002). RN [15] RP CATALYTIC ACTIVITY, SUBUNIT, AND CALCIUM BINDING. RX PubMed=16179346; DOI=10.1074/jbc.m507252200; RA Zhang L., Lookene A., Wu G., Olivecrona G.; RT "Calcium triggers folding of lipoprotein lipase into active dimers."; RL J. Biol. Chem. 280:42580-42591(2005). RN [16] RP INTERACTION WITH GPIHBP1. RX PubMed=17997385; DOI=10.1016/j.bbalip.2007.10.005; RA Gin P., Beigneux A.P., Davies B., Young M.F., Ryan R.O., Bensadoun A., RA Fong L.G., Young S.G.; RT "Normal binding of lipoprotein lipase, chylomicrons, and apo-AV to GPIHBP1 RT containing a G56R amino acid substitution."; RL Biochim. Biophys. Acta 1771:1464-1468(2007). RN [17] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70. RC TISSUE=Milk; RX PubMed=18780401; DOI=10.1002/pmic.200701057; RA Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.; RT "Identification of N-linked glycoproteins in human milk by hydrophilic RT interaction liquid chromatography and mass spectrometry."; RL Proteomics 8:3833-3847(2008). RN [18] RP INTERACTION WITH SORL1. RX PubMed=21385844; DOI=10.1242/jcs.072538; RA Klinger S.C., Glerup S., Raarup M.K., Mari M.C., Nyegaard M., Koster G., RA Prabakaran T., Nilsson S.K., Kjaergaard M.M., Bakke O., Nykjaer A., RA Olivecrona G., Petersen C.M., Nielsen M.S.; RT "SorLA regulates the activity of lipoprotein lipase by intracellular RT trafficking."; RL J. Cell Sci. 124:1095-1105(2011). RN [19] RP INTERACTION WITH SEL1L AND LMF1. RX PubMed=25066055; DOI=10.1016/j.cmet.2014.06.015; RA Sha H., Sun S., Francisco A.B., Ehrhardt N., Xue Z., Liu L., Lawrence P., RA Mattijssen F., Guber R.D., Panhwar M.S., Brenna J.T., Shi H., Xue B., RA Kersten S., Bensadoun A., Peterfy M., Long Q., Qi L.; RT "The ER-associated degradation adaptor protein Sel1L regulates LPL RT secretion and lipid metabolism."; RL Cell Metab. 20:458-470(2014). RN [20] RP FUNCTION, AND MUTAGENESIS OF TRP-417 AND 420-TRP-TRP-421. RX PubMed=24726386; DOI=10.1016/j.cmet.2014.01.017; RA Goulbourne C.N., Gin P., Tatar A., Nobumori C., Hoenger A., Jiang H., RA Grovenor C.R., Adeyo O., Esko J.D., Goldberg I.J., Reue K., Tontonoz P., RA Bensadoun A., Beigneux A.P., Young S.G., Fong L.G.; RT "The GPIHBP1-LPL complex is responsible for the margination of RT triglyceride-rich lipoproteins in capillaries."; RL Cell Metab. 19:849-860(2014). RN [21] RP ACTIVITY REGULATION, AND INTERACTION WITH GPIHBP1. RX PubMed=27929370; DOI=10.7554/elife.20958; RA Mysling S., Kristensen K.K., Larsson M., Kovrov O., Bensadouen A., RA Joergensen T.J., Olivecrona G., Young S.G., Ploug M.; RT "The angiopoietin-like protein ANGPTL4 catalyzes unfolding of the hydrolase RT domain in lipoprotein lipase and the endothelial membrane protein GPIHBP1 RT counteracts this unfolding."; RL Elife 5:0-0(2016). RN [22] RP CATALYTIC ACTIVITY, INTERACTION WITH GPIHBP1, SUBUNIT, AND CHARACTERIZATION RP OF VARIANT HLPP1 TYR-445. RX PubMed=26725083; DOI=10.7554/elife.12095; RA Mysling S., Kristensen K.K., Larsson M., Beigneux A.P., Gaardsvoll H., RA Fong L.G., Bensadouen A., Joergensen T.J., Young S.G., Ploug M.; RT "The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes RT lipoprotein lipase activity by preventing unfolding of its catalytic RT domain."; RL Elife 5:E12095-E12095(2016). RN [23] RP FUNCTION, INTERACTION WITH GPIHBP1, AND SUBCELLULAR LOCATION. RX PubMed=27811232; DOI=10.1194/jlr.m072520; RA Allan C.M., Larsson M., Jung R.S., Ploug M., Bensadoun A., Beigneux A.P., RA Fong L.G., Young S.G.; RT "Mobility of 'HSPG-bound' LPL explains how LPL is able to reach GPIHBP1 on RT capillaries."; RL J. Lipid Res. 58:216-225(2017). RN [24] RP INTERACTION WITH GPIHBP1, ACTIVITY REGULATION, AND CATALYTIC ACTIVITY. RX PubMed=29899144; DOI=10.1073/pnas.1806774115; RA Kristensen K.K., Midtgaard S.R., Mysling S., Kovrov O., Hansen L.B., RA Skar-Gislinge N., Beigneux A.P., Kragelund B.B., Olivecrona G., Young S.G., RA Joergensen T.J.D., Fong L.G., Ploug M.; RT "A disordered acidic domain in GPIHBP1 harboring a sulfated tyrosine RT regulates lipoprotein lipase."; RL Proc. Natl. Acad. Sci. U.S.A. 115:E6020-E6029(2018). RN [25] RP 3D-STRUCTURE MODELING. RX PubMed=8308035; DOI=10.1016/s0021-9258(17)41822-9; RA van Tilbeurgh H., Roussel A., Lalouel J.-M., Cambillau C.; RT "Lipoprotein lipase. Molecular model based on the pancreatic lipase X-ray RT structure: consequences for heparin binding and catalysis."; RL J. Biol. Chem. 269:4626-4633(1994). RN [26] RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 28-475 IN COMPLEX WITH GPIHBP1 RP AND CALCIUM ION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBCELLULAR LOCATION, RP SUBUNIT, DISULFIDE BOND, GLYCOSYLATION AT ASN-70 AND ASN-386, MUTAGENESIS RP OF SER-159 AND ASP-202, AND CHARACTERIZATION OF VARIANTS HLPP1 VAL-201; RP ARG-404 AND TYR-445. RX PubMed=30559189; DOI=10.1073/pnas.1817984116; RA Birrane G., Beigneux A.P., Dwyer B., Strack-Logue B., Kristensen K.K., RA Francone O.L., Fong L.G., Mertens H.D.T., Pan C.Q., Ploug M., Young S.G., RA Meiyappan M.; RT "Structure of the lipoprotein lipase-GPIHBP1 complex that mediates plasma RT triglyceride hydrolysis."; RL Proc. Natl. Acad. Sci. U.S.A. 116:1723-1732(2019). RN [27] RP REVIEW ON VARIANTS. RA Hayden M.R., Ma Y., Brunzell J., Henderson H.E.; RT "Genetic variants affecting human lipoprotein and hepatic lipases."; RL Curr. Opin. Lipidol. 2:104-109(1991). RN [28] RP VARIANT HLPP1 THR-271, AND INVOLVEMENT IN HLPP1. RX PubMed=2121025; RA Hata A., Emi M., Luc G., Basdevant A., Gambert P., Iverius P.-H., RA Lalouel J.-M.; RT "Compound heterozygote for lipoprotein lipase deficiency: Ser-->Thr244 and RT transition in 3' splice site of intron 2 (AG-->AA) in the lipoprotein RT lipase gene."; RL Am. J. Hum. Genet. 47:721-726(1990). RN [29] RP VARIANT HLPP1 GLU-215. RX PubMed=1969408; DOI=10.1016/s0021-9258(19)39449-9; RA Emi M., Wilson D.E., Iverius P.H., Wiu L., Hata A., Hegele R., RA Williams R.R., Lalouel J.-M.; RT "Missense mutation (Gly-->Glu188) of human lipoprotein lipase imparting RT functional deficiency."; RL J. Biol. Chem. 265:5910-5916(1990). RN [30] RP VARIANT HLPP1 GLU-215. RX PubMed=1975597; DOI=10.1172/jci114769; RA Monsalve M.V., Henderson H., Roederer G., Julien P., Deeb S., RA Kastelein J.J.P., Peritz L., Devlin R., Bruin T., Murthy M.R.V., Gagne C., RA Davignon J., Lupien P.J., Brunzell J.D., Hayden M.R.; RT "A missense mutation at codon 188 of the human lipoprotein lipase gene is a RT frequent cause of lipoprotein lipase deficiency in persons of different RT ancestries."; RL J. Clin. Invest. 86:728-734(1990). RN [31] RP VARIANT HLPP1 THR-203. RX PubMed=2110364; DOI=10.1073/pnas.87.9.3474; RA Beg O.U., Meng M.S., Skarlatos S.I., Previato L., Brunzell J.D., RA Brewer H.B. Jr., Fojo S.S.; RT "Lipoprotein lipase Bethesda: a single amino acid substitution (Ala- RT 176-->Thr) leads to abnormal heparin binding and loss of enzymic RT activity."; RL Proc. Natl. Acad. Sci. U.S.A. 87:3474-3478(1990). RN [32] RP VARIANTS HLPP1 THR-221 AND HIS-270. RX PubMed=1702428; DOI=10.1016/s0021-9258(18)52459-5; RA Dichek H.L., Fojo S.S., Beg O.U., Skarlatos S.I., Brunzell J.D., RA Cutler G.B. Jr., Brewer H.B. Jr.; RT "Identification of two separate allelic mutations in the lipoprotein lipase RT gene of a patient with the familial hyperchylomicronemia syndrome."; RL J. Biol. Chem. 266:473-477(1991). RN [33] RP VARIANT HLPP1 GLY-183. RX PubMed=1907278; DOI=10.1016/s0021-9258(18)98701-6; RA Faustinella F., Chang A., van Biervliet J.P., Rosseneu M., Vinaimont N., RA Smith L.C., Chen S.-H., Chan L.; RT "Catalytic triad residue mutation (Asp156-->Gly) causing familial RT lipoprotein lipase deficiency. Co-inheritance with a nonsense mutation RT (Ser447-->Ter) in a Turkish family."; RL J. Biol. Chem. 266:14418-14424(1991). RN [34] RP VARIANT HLPP1 GLU-169. RX PubMed=2010533; DOI=10.1172/jci115114; RA Ameis D., Kobayashi J., Davis R.C., Ben-Zeev O., Malloy M.J., Kane J.P., RA Lee G., Wong H., Havel R.J., Schotz M.C.; RT "Familial chylomicronemia (type I hyperlipoproteinemia) due to a single RT missense mutation in the lipoprotein lipase gene."; RL J. Clin. Invest. 87:1165-1170(1991). RN [35] RP VARIANT HLPP1 THR-221. RX PubMed=1674945; DOI=10.1172/jci115229; RA Henderson H.E., Ma Y., Hassan F., Monsalve M.V., Marais A.D., Winkler F., RA Gubernator K., Peterson J., Brunzell J.D., Hayden M.R.; RT "Amino acid substitution (Ile194-->Thr) in exon 5 of the lipoprotein lipase RT gene causes lipoprotein lipase deficiency in three unrelated probands. RT Support for a multicentric origin."; RL J. Clin. Invest. 87:2005-2011(1991). RN [36] RP VARIANTS HLPP1 GLU-231 AND HIS-270, AND CHARACTERIZATION OF VARIANTS HLPP1 RP GLU-231 AND HIS-270. RX PubMed=1752947; DOI=10.1172/jci115507; RA Gotoda T., Yamada N., Kawamura M., Kozaki K., Mori N., Ishibashi S., RA Shimano H., Takaku F., Yazaki Y., Furuichi Y., Murase T.; RT "Heterogeneous mutations in the human lipoprotein lipase gene in patients RT with familial lipoprotein lipase deficiency."; RL J. Clin. Invest. 88:1856-1864(1991). RN [37] RP VARIANT HLPP1 LEU-234. RX PubMed=2038366; DOI=10.1056/nejm199106203242502; RA Ma Y., Henderson H.E., Ven Murthy M.R., Roederer G., Monsalve M.V., RA Clarke L.A., Normand T., Julien P., Gagne C., Lambert M., Davignon J., RA Lupien P.J., Brunzell J., Hayden M.R.; RT "A mutation in the human lipoprotein lipase gene as the most common cause RT of familial chylomicronemia in French Canadians."; RL N. Engl. J. Med. 324:1761-1766(1991). RN [38] RP VARIANT HLPP1 ARG-113. RX PubMed=1598907; RA Ishimura-Oka K., Faustinella F., Kihara S., Smith L.C., Oka K., Chan L.; RT "A missense mutation (Trp86-->Arg) in exon 3 of the lipoprotein lipase RT gene: a cause of familial chylomicronemia."; RL Am. J. Hum. Genet. 50:1275-1280(1992). RN [39] RP VARIANT HLPP1 ARG-184. RX PubMed=1521525; DOI=10.1111/j.1432-1033.1992.tb17182.x; RA Bruin T., Kastelein J.J., van Diermen D.E., Ma Y., Henderson H.E., RA Stuyt P.M., Stalenhoef A.F.H., Sturk A., Brunzell J.D., Hayden M.R.; RT "A missense mutation Pro157Arg in lipoprotein lipase (LPLNijmegen) RT resulting in loss of catalytic activity."; RL Eur. J. Biochem. 208:267-272(1992). RN [40] RP VARIANT HLPP1 ASN-277. RX PubMed=1639392; DOI=10.1016/0888-7543(92)90136-g; RA Ma Y., Wilson B.I., Bijvoet S., Henderson H.E., Cramb E., Roederer G., RA Ven Murthy M.R., Julien P., Bakker H.D., Kastelein J.J., Brunzell J.D., RA Hayden M.R.; RT "A missense mutation (Asp250-->Asn) in exon 6 of the human lipoprotein RT lipase gene causes chylomicronemia in patients of different ancestries."; RL Genomics 13:649-653(1992). RN [41] RP VARIANTS HLPP1 ASN-183; GLY-183 AND SER-243. RX PubMed=1730727; DOI=10.1016/s0021-9258(18)46034-6; RA Ma Y.H., Bruin T., Tuzgol S., Wilson B.I., Roederer G., Liu M.S., RA Davignon J., Kastelein J.J., Brunzell J.D., Hayden M.R.; RT "Two naturally occurring mutations at the first and second bases of codon RT aspartic acid 156 in the proposed catalytic triad of human lipoprotein RT lipase. In vivo evidence that aspartic acid 156 is essential for RT catalysis."; RL J. Biol. Chem. 267:1918-1923(1992). RN [42] RP CHARACTERIZATION OF VARIANTS HLPP1 ASN-183 AND GLY-183, MUTAGENESIS OF RP SER-159 AND HIS-268, CATALYTIC ACTIVITY, ACTIVE SITE, SUBCELLULAR LOCATION, RP AND HEPARIN-BINDING. RX PubMed=1371284; DOI=10.1016/s0021-9258(19)50642-1; RA Emmerich J., Beg O.U., Peterson J., Previato L., Brunzell J.D., RA Brewer H.B. Jr., Santamarina-Fojo S.; RT "Human lipoprotein lipase. Analysis of the catalytic triad by site-directed RT mutagenesis of Ser-132, Asp-156, and His-241."; RL J. Biol. Chem. 267:4161-4165(1992). RN [43] RP VARIANT HLPP1 GLU-222. RX PubMed=1400331; DOI=10.1016/s0021-9258(19)88676-3; RA Hata A., Ridinger D.N., Sutherland S.D., Emi M., Kwong L.K., Shuhua J., RA Lubbers A., Guy-Grand B., Basdevant A., Iverius P.H., Wilson D.E., RA Lalouel J.-M.; RT "Missense mutations in exon 5 of the human lipoprotein lipase gene. RT Inactivation correlates with loss of dimerization."; RL J. Biol. Chem. 267:20132-20139(1992). RN [44] RP VARIANTS HLPP1 GLU-215; HIS-270 AND ASN-277. RX PubMed=1619366; DOI=10.1016/s0022-2275(20)41438-5; RA Ishimura-Oka K., Semenkovich C.F., Faustinella F., Goldberg I.J., RA Shachter N., Smith L.C., Coleman T., Hide W.A., Brown W.V., Oka K.; RT "A missense (Asp250-->Asn) mutation in the lipoprotein lipase gene in two RT unrelated families with familial lipoprotein lipase deficiency."; RL J. Lipid Res. 33:745-754(1992). RN [45] RP VARIANTS HLPP1 ARG-113; ARG-163; GLU-215; THR-221 AND SER-232. RX PubMed=1479292; DOI=10.1016/s0022-2275(20)41340-9; RA Reina M., Brunzell J.D., Deeb S.S.; RT "Molecular basis of familial chylomicronemia: mutations in the lipoprotein RT lipase and apolipoprotein C-II genes."; RL J. Lipid Res. 33:1823-1832(1992). RN [46] RP VARIANT HLPP1 THR-361. RX PubMed=8096693; DOI=10.1006/bbrc.1993.1323; RA Kobayashi J., Sasaki N., Tashiro J., Inadera H., Saito Y., Yoshida S.; RT "A missense mutation (Ala334-->Thr) in exon 7 of the lipoprotein lipase RT gene in a case with type I hyperlipidemia."; RL Biochem. Biophys. Res. Commun. 191:1046-1054(1993). RN [47] RP VARIANT HLPP1 GLU-207. RX PubMed=8288243; DOI=10.1006/geno.1993.1481; RA Haubenwallner S., Horl G., Shachter N.S., Presta E., Fried S.K., Hofler G., RA Kostner G.M., Breslow J.L., Zechner R.; RT "A novel missense mutation in the gene for lipoprotein lipase resulting in RT a highly conservative amino acid substitution (Asp180-->Glu) causes RT familial chylomicronemia (type I hyperlipoproteinemia)."; RL Genomics 18:392-396(1993). RN [48] RP VARIANT HLPP1 CYS-199. RX PubMed=8486765; DOI=10.1172/jci116414; RA Ma Y., Liu M.-S., Ginzinger D., Frohlich J., Brunzell J.D., Hayden M.R.; RT "Gene-environment interaction in the conversion of a mild-to-severe RT phenotype in a patient homozygous for a Ser172-->Cys mutation in the RT lipoprotein lipase gene."; RL J. Clin. Invest. 91:1953-1958(1993). RN [49] RP VARIANT HLPP1 SER-102. RX PubMed=8325986; DOI=10.1172/jci116551; RA Wilson D.E., Hata A., Kwong L.K., Lingam A., Shuhua J., Ridinger D.N., RA Yeager C., Kaltenborn K.C., Iverius P.-H., Lalouel J.-M.; RT "Mutations in exon 3 of the lipoprotein lipase gene segregating in a family RT with hypertriglyceridemia, pancreatitis, and non-insulin-dependent RT diabetes."; RL J. Clin. Invest. 92:203-211(1993). RN [50] RP VARIANT HLPP1 SER-181. RX PubMed=8301230; DOI=10.1016/s0022-2275(20)35352-9; RA Bruin T., Tuzgol S., van Diermen D.E., Hoogerbrugge-Van der Linden N., RA Brunzell J.D., Hayden M.R., Kastelein J.J.; RT "Recurrent pancreatitis and chylomicronemia in an extended Dutch kindred is RT caused by a Gly154-->Ser substitution in lipoprotein lipase."; RL J. Lipid Res. 34:2109-2119(1993). RN [51] RP VARIANT HLPP1 VAL-392. RX PubMed=8135797; DOI=10.1006/bbrc.1994.1266; RA Chimienti G.P.G., Resta F., di Perma V., Tarricone C., Lovecchio M., RA Collacicco A.M., Capurso A.; RT "A new Italian case of lipoprotein lipase deficiency: a Leu365-> Val change RT resulting in loss of enzyme activity."; RL Biochem. Biophys. Res. Commun. 199:570-576(1994). RN [52] RP VARIANT HLPP1 SER-70, AND CHARACTERIZATION OF VARIANT HLPP1 SER-70. RX PubMed=7999071; DOI=10.1006/bbrc.1994.2694; RA Kobayashi J., Inadera H., Fujita Y., Talley G., Morisaki N., Yoshida S., RA Saito Y., Fojo S.S., Brewer H.B. Jr.; RT "A naturally occurring mutation at the second base of codon asparagine 43 RT in the proposed N-linked glycosylation site of human lipoprotein lipase: in RT vivo evidence that asparagine 43 is essential for catalysis and RT secretion."; RL Biochem. Biophys. Res. Commun. 205:506-515(1994). RN [53] RP VARIANTS HLPP1 HIS-270 AND CYS-270. RX PubMed=7906986; DOI=10.1002/humu.1380030109; RA Ma Y., Liu M.-S., Chitayat D., Bruin T., Beisiegel U., Benlian P., RA Foubert L., De Gennes J.L., Funke H., Forsythe I., Blaichman S., RA Papanikolaou M., Erkelens D.W., Kastelein J., Brunzell J.D., Hayden M.R.; RT "Recurrent missense mutations at the first and second base of codon Arg243 RT in human lipoprotein lipase in patients of different ancestries."; RL Hum. Mutat. 3:52-58(1994). RN [54] RP VARIANTS HLPP1 LEU-96 AND GLU-215, AND CHARACTERIZATION OF VARIANT HLPP1 RP LEU-96. RX PubMed=7912254; DOI=10.1016/s0022-2275(20)41188-5; RA Bruin T., Tuzgoel S., Mulder W.J., van den Ende A.E., Jansen H., RA Hayden M.R., Kastelein J.J.P.; RT "A compound heterozygote for lipoprotein lipase deficiency, Val69-->Leu and RT Gly188-->Glu: correlation between in vitro LPL activity and clinical RT expression."; RL J. Lipid Res. 35:438-445(1994). RN [55] RP VARIANTS HLPP1 CYS-199; ARG-279 AND THR-288, AND CHARACTERIZATION OF RP VARIANTS HLPP1 ARG-279 AND THR-288. RX PubMed=8077845; DOI=10.1016/s0022-2275(20)40102-6; RA Ma Y., Ooi T.C., Liu M.-S., Zhang H., McPherson R., Edwards A.L., RA Forsythe I.J., Frohlich J., Brunzell J.D., Hayden M.R.; RT "High frequency of mutations in the human lipoprotein lipase gene in RT pregnancy-induced chylomicronemia: possible association with apolipoprotein RT E2 isoform."; RL J. Lipid Res. 35:1066-1075(1994). RN [56] RP VARIANT HLPP1 VAL-437. RX PubMed=7806969; DOI=10.1016/s0022-2275(20)41153-8; RA Previato L., Guardamagna O., Dugi K.A., Ronan R., Talley G.D., RA Santamarina-Fojo S., Brewer H.B. Jr.; RT "A novel missense mutation in the C-terminal domain of lipoprotein lipase RT (Glu410-->Val) leads to enzyme inactivation and familial chylomicronemia."; RL J. Lipid Res. 35:1552-1560(1994). RN [57] RP VARIANT FCHL3 SER-318. RX PubMed=7647785; DOI=10.1038/ng0595-28; RA Reymer P.W.A., Gagne E., Groenemeyer B.E., Zhang H., Forsyth I., Jansen H., RA Seidell J.C., Kromhout D., Lie K.E., Kastelein J.J., Hayden M.R.; RT "A lipoprotein lipase mutation (Asn291Ser) is associated with reduced HDL RT cholesterol levels in premature atherosclerosis."; RL Nat. Genet. 10:28-34(1995). RN [58] RP VARIANT HLPP1 TYR-445, AND CHARACTERIZATION OF VARIANT HLPP1 TYR-445. RX PubMed=8858123; DOI=10.1006/bbrc.1996.1487; RA Henderson H.E., Hassan F., Marais D., Hayden M.R.; RT "A new mutation destroying disulphide bridging in the C-terminal domain of RT lipoprotein lipase."; RL Biochem. Biophys. Res. Commun. 227:189-194(1996). RN [59] RP VARIANTS ASN-36 AND SER-318, AND INVOLVEMENT IN FCHL3. RX PubMed=8872057; DOI=10.1111/j.1365-2362.1996.tb02146.x; RA de Bruin T.W.A., Mailly F., van Barlingen H.H.J.J., Fisher R., RA Castro Cabezas M., Talmud P., Dallinga-Thie G.M., Humphries S.E.; RT "Lipoprotein lipase gene mutations D9N and N291S in four pedigrees with RT familial combined hyperlipidaemia."; RL Eur. J. Clin. Invest. 26:631-639(1996). RN [60] RP VARIANTS HLPP1 ASN-277 AND LYS-437. RX PubMed=8956048; RX DOI=10.1002/(sici)1098-1004(1996)8:4<381::aid-humu16>3.0.co;2-z; RA Wiebusch H., Funke H., Bruin T., Bucher H., von Eckardstein A., RA Kastelein J.J.P., Assmann G.; RT "Compound heterozygosity for a known (D250N) and a novel (E410K) missense RT mutation in the C-terminal domain of lipoprotein lipase causes familial RT chylomicronemia."; RL Hum. Mutat. 8:381-383(1996). RN [61] RP VARIANTS HLPP1 GLY-190 AND GLU-215. RX PubMed=8956052; DOI=10.1002/humu.1380080402; RA Wiebusch H., Funke H., Santer R., Richter W., Assmann G.; RT "A novel missense (E163G) mutation in the catalytic subunit of lipoprotein RT lipase causes familial chylomicronemia."; RL Hum. Mutat. 8:392-392(1996). RN [62] RP VARIANT HLPP1 HIS-289, VARIANT ASN-36, CHARACTERIZATION OF VARIANT HLPP1 RP HIS-289, CHARACTERIZATION OF VARIANT ASN-36, AND INVOLVEMENT IN FCHL3. RX PubMed=8728326; DOI=10.1016/s0022-2275(20)37606-9; RA Rouis M., Lohse P., Dugi K.A., Lohse P., Beg O.U., Ronan R., Talley G.D., RA Brunzell J.D., Santamarina-Fojo S.; RT "Homozygosity for two point mutations in the lipoprotein lipase (LPL) gene RT in a patient with familial LPL deficiency: LPL(Asp9-->Asn, Tyr262-->His)."; RL J. Lipid Res. 37:651-661(1996). RN [63] RP VARIANTS HLPP1 ALA-128; GLU-215; ARG-215; CYS-270; ASN-277 AND PRO-313. RX PubMed=8778602; DOI=10.1056/nejm199609193351203; RA Benlian P., De Gennes J.L., Foubert L., Zhang H., Gagne S.E., Hayden M.; RT "Premature atherosclerosis in patients with familial chylomicronemia caused RT by mutations in the lipoprotein lipase gene."; RL N. Engl. J. Med. 335:848-854(1996). RN [64] RP VARIANT HLPP1 CYS-278. RX PubMed=8973094; DOI=10.1016/0300-2977(96)00043-5; RA Bijvoet S.M., Wiebusch H., Ma Y., Reymer P.W., Bruin T., Bakker H.D., RA Funke H., Assmann G., Hayden M.R., Kastelein J.J.; RT "Compound heterozygosity for a known and a novel defect in the lipoprotein RT lipase gene (Asp250-->Asn; Ser251-->Cys) resulting in lipoprotein lipase RT (LPL) deficiency."; RL Neth. J. Med. 49:189-195(1996). RN [65] RP VARIANT HLPP1 ARG-286. RX PubMed=9298816; RX DOI=10.1002/(sici)1098-1004(1997)10:3<179::aid-humu1>3.0.co;2-e; RA Foubert L., Bruin T., de Gennes J.-L., Ehrenborg E., Furioli J., RA Kastelein J.J., Benlian P., Hayden M.R.; RT "A single Ser259Arg mutation in the gene for lipoprotein lipase causes RT chylomicronemia in Moroccans of Berber ancestry."; RL Hum. Mutat. 10:179-185(1997). RN [66] RP VARIANTS HLPP1 GLY-113; THR-185; GLN-210; GLU-215; ARG-220; LEU-234; RP SER-318; THR-328 AND PRO-330. RX PubMed=9401010; RX DOI=10.1002/(sici)1098-1004(1997)10:6<465::aid-humu8>3.0.co;2-c; RA Mailly F., Palmen J., Muller D.P.R., Gibbs T., Lloyd J., Brunzell J., RA Durrington P., Mitropoulos K., Betteridge J., Watts G., Lithell H., RA Angelico F., Humphries S.E., Talmud P.J.; RT "Familial lipoprotein lipase (LPL) deficiency: a catalogue of LPL gene RT mutations identified in 20 patients from the UK, Sweden, and Italy."; RL Hum. Mutat. 10:465-473(1997). RN [67] RP VARIANTS HLPP1 ALA-128; HIS-183; GLU-215; ARG-215; LEU-234; CYS-270 AND RP ASN-277. RX PubMed=9279761; DOI=10.1136/jmg.34.8.672; RA Foubert L., De Gennes J.L., Lagarde J.P., Ehrenborg E., Raisonnier A., RA Girardet J.P., Hayden M.R., Benlian P.; RT "Assessment of French patients with LPL deficiency for French Canadian RT mutations."; RL J. Med. Genet. 34:672-675(1997). RN [68] RP VARIANTS HLPP1 THR-252 AND HIS-270. RX PubMed=9714430; RX DOI=10.1002/(sici)1096-8628(19980724)78:4<313::aid-ajmg1>3.0.co;2-m; RA Henderson H.E., Bijvoet S.M., Mannens M.A.M.M., Bruin T., Erkelens D.W., RA Hayden M.R., Kastelein J.J.P.; RT "Ile225Thr loop mutation in the lipoprotein lipase (LPL) gene is a de novo RT event."; RL Am. J. Med. Genet. 78:313-316(1998). RN [69] RP VARIANT HLPP1 LYS-448, AND CHARACTERIZATION OF VARIANT HLPP1 LYS-448. RX PubMed=9498099; DOI=10.1016/s0009-8981(97)00144-7; RA Henderson H., Leisegang F., Hassan F., Hayden M., Marais D.; RT "A novel Glu421Lys substitution in the lipoprotein lipase gene in RT pregnancy-induced hypertriglyceridemic pancreatitis."; RL Clin. Chim. Acta 269:1-12(1998). RN [70] RP VARIANTS HLPP1 GLU-215 AND GLY-286. RX PubMed=10660334; RA Evans D., Wendt D., Ahle S., Guerra A., Beisiegel U.; RT "Compound heterozygosity for a new (S259G) and a previously described RT (G188E) mutation in lipoprotein lipase (LPL) as a cause of RT chylomicronemia."; RL Hum. Mutat. 12:217-217(1998). RN [71] RP VARIANT HLPP1 THR-288, VARIANTS ASN-36 AND SER-318, AND INVOLVEMENT IN RP FCHL3. RX PubMed=9719626; DOI=10.1006/mgme.1998.2712; RA Zhang Q., Liu Y., Liu B.W., Fan P., Cavanna J., Galton D.J.; RT "Common genetic variants of lipoprotein lipase and apolipoproteins AI-CIII RT that relate to coronary artery disease: a study in Chinese and European RT subjects."; RL Mol. Genet. Metab. 64:177-183(1998). RN [72] RP VARIANT FCHL3 SER-318, AND VARIANTS MET-370 AND ALA-379. RX PubMed=9662394; DOI=10.1038/907; RA Nickerson D.A., Taylor S.L., Weiss K.M., Clark A.G., Hutchinson R.G., RA Stengaerd J., Salomaa V., Vartiainen E., Boerwinkle E., Sing C.F.; RT "DNA sequence diversity in a 9.7-kb region of the human lipoprotein lipase RT gene."; RL Nat. Genet. 19:233-240(1998). RN [73] RP VARIANT THR-427. RX PubMed=10391209; DOI=10.1038/10290; RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RT "Characterization of single-nucleotide polymorphisms in coding regions of RT human genes."; RL Nat. Genet. 22:231-238(1999). RN [74] RP ERRATUM OF PUBMED:10391209. RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RL Nat. Genet. 23:373-373(1999). RN [75] RP VARIANT HLPP1 LEU-297, AND CHARACTERIZATION OF VARIANT HLPP1 LEU-297. RX PubMed=11068186; DOI=10.1016/s0925-4439(00)00067-3; RA Takagi A., Ikeda Y., Takeda E., Yamamoto A.; RT "A newly identified lipoprotein lipase (LPL) gene mutation (F270L) in a RT Japanese patient with familial LPL deficiency."; RL Biochim. Biophys. Acta 1502:433-446(2000). RN [76] RP VARIANTS HLPP1 ARG-132 AND GLU-231, AND CHARACTERIZATION OF VARIANTS HLPP1 RP ARG-132 AND GLU-231. RX PubMed=11099402; DOI=10.1042/cs0990569; RA Ikeda Y., Goji K., Takagi A.; RT "A compound heterozygote for a novel missense mutation (G105R) in exon 3 RT and a missense mutation (D204E) in exon 5 of the lipoprotein lipase gene in RT a Japanese infant with hyperchylomicronaemia."; RL Clin. Sci. 99:569-578(2000). RN [77] RP VARIANT HLPP1 TRP-266. RX PubMed=11134145; DOI=10.1210/jcem.85.12.7069; RA Hoffmann M.M., Jacob S., Luft D., Schmuelling R.-M., Rett K., Maerz W., RA Haering H.-U., Matthaei S.; RT "Type I hyperlipoproteinemia due to a novel loss of function mutation of RT lipoprotein lipase, Cys(239)-->Trp, associated with recurrent severe RT pancreatitis."; RL J. Clin. Endocrinol. Metab. 85:4795-4798(2000). RN [78] RP VARIANT HLPP1 ASP-210, AND CHARACTERIZATION OF VARIANT HLPP1 ASP-210. RX PubMed=10787434; DOI=10.1016/s0022-2275(20)32382-8; RA Hoelzl B., Kraft H.G., Wiebusch H., Sandhofer A., Patsch J., Sandhofer F., RA Paulweber B.; RT "Two novel mutations in the lipoprotein lipase gene in a family with marked RT hypertriglyceridemia in heterozygous carriers. Potential interaction with RT the polymorphic marker D1S104 on chromosome 1q21-q23."; RL J. Lipid Res. 41:734-741(2000). RN [79] RP VARIANT HLPP1 VAL-181, AND CHARACTERIZATION OF VARIANT HLPP1 VAL-181. RX PubMed=11441134; DOI=10.1016/s0022-2275(20)31596-0; RA Ikeda Y., Takagi A., Nakata Y., Sera Y., Hyoudou S., Hamamoto K., Nishi Y., RA Yamamoto A.; RT "Novel compound heterozygous mutations for lipoprotein lipase deficiency. A RT G-to-T transversion at the first position of exon 5 causing G154V missense RT mutation and a 5' splice site mutation of intron 8."; RL J. Lipid Res. 42:1072-1081(2001). RN [80] RP VARIANTS HLPP1 THR-98; ILE-208; VAL-279; ARG-279; TYR-310; ARG-325 AND RP PHE-365, AND CHARACTERIZATION OF VARIANTS HLPP1 THR-98; ILE-208; VAL-279; RP ARG-279; TYR-310; ARG-325 AND PHE-365. RX PubMed=12204001; DOI=10.1002/humu.9054; RA Chan L.Y.S., Lam C.-W., Mak Y.-T., Tomlinson B., Tsang M.-W., Baum L., RA Masarei J.R.L., Pang C.-P.; RT "Genotype-phenotype studies of six novel LPL mutations in Chinese patients RT with hypertriglyceridemia."; RL Hum. Mutat. 20:232-233(2002). RN [81] RP CHARACTERIZATION OF VARIANTS HLPP1 THR-203; GLU-215; THR-221; SER-232 AND RP LEU-234, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=11893776; DOI=10.1016/s0022-2275(20)30146-2; RA Peterson J., Ayyobi A.F., Ma Y., Henderson H., Reina M., Deeb S.S., RA Santamarina-Fojo S., Hayden M.R., Brunzell J.D.; RT "Structural and functional consequences of missense mutations in exon 5 of RT the lipoprotein lipase gene."; RL J. Lipid Res. 43:398-406(2002). RN [82] RP VARIANT HLPP1 PHE-303, CHARACTERIZATION OF VARIANT HLPP1 PHE-303, RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=12641539; DOI=10.1046/j.1365-2362.2003.01129.x; RA Saika Y., Sakai N., Takahashi M., Maruyama T., Kihara S., Ouchi N., RA Ishigami M., Hiraoka H., Nakamura T., Yamashita S., Matsuzawa Y.; RT "Novel LPL mutation (L303F) found in a patient associated with coronary RT artery disease and severe systemic atherosclerosis."; RL Eur. J. Clin. Invest. 33:216-222(2003). RN [83] RP VARIANTS ASN-36 AND SER-318, AND INVOLVEMENT IN FCHL3. RX PubMed=12966036; DOI=10.1093/hmg/ddg314; RA Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S., RA Alvin G.B., Das K., Gilliam T.C.; RT "Association of extreme blood lipid profile phenotypic variation with 11 RT reverse cholesterol transport genes and 10 non-genetic cardiovascular RT disease risk factors."; RL Hum. Mol. Genet. 12:2733-2743(2003). RN [84] RP VARIANT HLPP1 VAL-201. RX PubMed=14984478; DOI=10.1111/j.0009-9163.2004.00205.x; RA Abifadel M., Jambart S., Allard D., Rabes J.-P., Varret M., Derre A., RA Chouery E., Salem N., Junien C., Aydenian H., Boileau C.; RT "Identification of the first Lebanese mutation in the LPL gene and RT description of a rapid detection method."; RL Clin. Genet. 65:158-161(2004). RN [85] RP VARIANTS HLPP1 GLU-215 AND ARG-328. RX PubMed=15185149; DOI=10.1007/s00431-004-1474-1; RA Kavazarakis E., Stabouli S., Gourgiotis D., Roumeliotou K., RA Traeger-Synodinos J., Bossios A., Fretzayas A., Kanavakis E.; RT "Severe hypertriglyceridaemia in a Greek infant: a clinical, biochemical RT and genetic study."; RL Eur. J. Pediatr. 163:462-466(2004). RN [86] RP VARIANTS HLPP1 SER-70; ARG-132; VAL-181; GLU-215; THR-221; ARG-225; RP ALA-227; GLU-231; CYS-270; HIS-270; THR-288; LEU-297; ARG-305; PHE-330 AND RP THR-361. RX PubMed=15256764; DOI=10.5551/jat.11.131; RG The research committee on primary hyperlipidemia of the ministry of health and welfare of Japan; RA Maruyama T., Yamashita S., Matsuzawa Y., Bujo H., Takahashi K., Saito Y., RA Ishibashi S., Ohashi K., Shionoiri F., Gotoda T., Yamada N., Kita T.; RT "Mutations in Japanese subjects with primary hyperlipidemia -- results from RT the Research Committee of the Ministry of Health and Welfare of Japan since RT 1996."; RL J. Atheroscler. Thromb. 11:131-145(2004). RN [87] RP VARIANTS HLPP1 GLU-186; GLU-215 AND THR-221. RX PubMed=15877202; DOI=10.1007/s10545-005-7060-5; RA Santer R., Gokcay G., Demirkol M., Gal A., Lukacs Z.; RT "Hyperchylomicronaemia due to lipoprotein lipase deficiency as a cause of RT false-positive newborn screening for biotinidase deficiency."; RL J. Inherit. Metab. Dis. 28:137-140(2005). RN [88] RP VARIANT HLPP1 GLN-210, CHARACTERIZATION OF VARIANT HLPP1 GLN-210, AND RP SUBCELLULAR LOCATION. RX PubMed=24291057; DOI=10.1016/j.cca.2013.11.025; RA Martin-Campos J.M., Julve J., Roig R., Martinez S., Errico T.L., RA Martinez-Couselo S., Escola-Gil J.C., Mendez-Gonzalez J., Blanco-Vaca F.; RT "Molecular analysis of chylomicronemia in a clinical laboratory setting: RT diagnosis of 13 cases of lipoprotein lipase deficiency."; RL Clin. Chim. Acta 429:61-68(2014). RN [89] RP VARIANT HLPP1 ARG-404, CHARACTERIZATION OF VARIANT HLPP1 ARG-404, FUNCTION, RP CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=27578112; DOI=10.1016/j.jacl.2016.02.015; RA Pingitore P., Lepore S.M., Pirazzi C., Mancina R.M., Motta B.M., RA Valenti L., Berge K.E., Retterstoel K., Leren T.P., Wiklund O., Romeo S.; RT "Identification and characterization of two novel mutations in the LPL gene RT causing type I hyperlipoproteinemia."; RL J. Clin. Lipidol. 10:816-823(2016). CC -!- FUNCTION: Key enzyme in triglyceride metabolism. Catalyzes the CC hydrolysis of triglycerides from circulating chylomicrons and very low CC density lipoproteins (VLDL), and thereby plays an important role in CC lipid clearance from the blood stream, lipid utilization and storage CC (PubMed:11342582, PubMed:27578112, PubMed:8675619). Although it has CC both phospholipase and triglyceride lipase activities it is primarily a CC triglyceride lipase with low but detectable phospholipase activity CC (PubMed:12032167, PubMed:7592706). Mediates margination of CC triglyceride-rich lipoprotein particles in capillaries CC (PubMed:24726386). Recruited to its site of action on the luminal CC surface of vascular endothelium by binding to GPIHBP1 and cell surface CC heparan sulfate proteoglycans (PubMed:11342582, PubMed:27811232). CC {ECO:0000269|PubMed:11342582, ECO:0000269|PubMed:12032167, CC ECO:0000269|PubMed:24726386, ECO:0000269|PubMed:27578112, CC ECO:0000269|PubMed:27811232, ECO:0000269|PubMed:7592706, CC ECO:0000269|PubMed:8675619}. 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=3.1.1.34; CC Evidence={ECO:0000269|PubMed:11342582, ECO:0000269|PubMed:11893776, CC ECO:0000269|PubMed:12032167, ECO:0000269|PubMed:1371284, CC ECO:0000269|PubMed:16179346, ECO:0000269|PubMed:2340307, CC ECO:0000269|PubMed:26725083, ECO:0000269|PubMed:27578112, CC ECO:0000269|PubMed:29899144, ECO:0000269|PubMed:30559189, CC ECO:0000269|PubMed:7592706}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn- CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; CC Evidence={ECO:0000269|PubMed:12032167, ECO:0000269|PubMed:7592706}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = di-(9Z)- CC octadecenoylglycerol + (9Z)-octadecenoate + 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:12032167}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; CC Evidence={ECO:0000305|PubMed:12032167}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = CC (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + (9Z)-octadecenoate + CC H(+); Xref=Rhea:RHEA:38699, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30823, ChEBI:CHEBI:74669, ChEBI:CHEBI:76083; CC Evidence={ECO:0000269|PubMed:7592706}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38700; CC Evidence={ECO:0000305|PubMed:7592706}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2,3-tributanoylglycerol + H2O = dibutanoylglycerol + CC butanoate + 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:7592706}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476; CC Evidence={ECO:0000305|PubMed:7592706}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = CC hexadecanoyl-sn-glycero-3-phosphocholine + hexadecanoate + H(+); CC Xref=Rhea:RHEA:41384, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64563, ChEBI:CHEBI:72999; CC Evidence={ECO:0000269|PubMed:12032167}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41385; CC Evidence={ECO:0000305|PubMed:12032167}; CC -!- ACTIVITY REGULATION: The apolipoprotein APOC2 acts as a coactivator of CC LPL activity (PubMed:12032167). Ca(2+) binding promotes protein CC stability and formation of the active homodimer (PubMed:16179346). CC Interaction with GPIHBP1 protects LPL against inactivation by ANGPTL4 CC (PubMed:27929370, PubMed:29899144). Inhibited by NaCl CC (PubMed:12032167). {ECO:0000269|PubMed:12032167, CC ECO:0000269|PubMed:16179346, ECO:0000269|PubMed:27929370, CC ECO:0000269|PubMed:29899144}. CC -!- SUBUNIT: Homodimer (Probable) (PubMed:11893776, PubMed:16179346, CC PubMed:26725083). Interacts with GPIHBP1 with 1:1 stoichiometry CC (PubMed:17997385, PubMed:26725083, PubMed:27811232, PubMed:27929370, CC PubMed:29899144, PubMed:30559189). Interacts with APOC2; the CC interaction activates LPL activity in the presence of lipids (By CC similarity). Interaction with heparan sulfate proteoglycans is required CC to protect LPL against loss of activity (PubMed:11342582). Associates CC with lipoprotein particles in blood plasma (PubMed:11342582, CC PubMed:11893776). Interacts with LMF1 and SEL1L; interaction with SEL1L CC is required to prevent aggregation of newly synthesized LPL in the CC endoplasmic reticulum (ER), and for normal export of LPL from the ER to CC the extracellular space (PubMed:25066055). Interacts with SORL1; SORL1 CC acts as a sorting receptor, promoting LPL localization to endosomes and CC later to lysosomes, leading to degradation of newly synthesized LPL CC (PubMed:21385844). {ECO:0000250|UniProtKB:P11151, CC ECO:0000269|PubMed:11342582, ECO:0000269|PubMed:11893776, CC ECO:0000269|PubMed:16179346, ECO:0000269|PubMed:17997385, CC ECO:0000269|PubMed:21385844, ECO:0000269|PubMed:25066055, CC ECO:0000269|PubMed:26725083, ECO:0000269|PubMed:27811232, CC ECO:0000269|PubMed:27929370, ECO:0000269|PubMed:29899144, CC ECO:0000269|PubMed:30559189, ECO:0000305|PubMed:30559189}. CC -!- INTERACTION: CC P06858; Q9UI10: EIF2B4; NbExp=3; IntAct=EBI-715909, EBI-2340132; CC P06858; Q8IV16: GPIHBP1; NbExp=7; IntAct=EBI-715909, EBI-9080234; CC P06858; O00746: NME4; NbExp=3; IntAct=EBI-715909, EBI-744871; CC P06858; C9J082: NPHP1; NbExp=3; IntAct=EBI-715909, EBI-25830675; CC P06858; O14744: PRMT5; NbExp=3; IntAct=EBI-715909, EBI-351098; CC P06858; Q8TAS3: PRRG2; NbExp=3; IntAct=EBI-715909, EBI-10272071; CC P06858; O00233: PSMD9; NbExp=3; IntAct=EBI-715909, EBI-750973; CC P06858; Q8IYM2: SLFN12; NbExp=3; IntAct=EBI-715909, EBI-2822550; CC P06858; Q9UMY4: SNX12; NbExp=3; IntAct=EBI-715909, EBI-1752602; CC P06858; O43493-5: TGOLN2; NbExp=3; IntAct=EBI-715909, EBI-25830716; CC P06858; Q8NFB2: TMEM185A; NbExp=3; IntAct=EBI-715909, EBI-21757569; CC P06858; Q8N0U8: VKORC1L1; NbExp=3; IntAct=EBI-715909, EBI-11337915; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P11151}; CC Peripheral membrane protein {ECO:0000250|UniProtKB:P11151}; CC Extracellular side {ECO:0000250|UniProtKB:P11151}. Secreted CC {ECO:0000269|PubMed:11342582, ECO:0000269|PubMed:11893776, CC ECO:0000269|PubMed:12641539, ECO:0000269|PubMed:1371284, CC ECO:0000269|PubMed:2340307, ECO:0000269|PubMed:24291057, CC ECO:0000269|PubMed:27578112, ECO:0000269|PubMed:30559189}. Secreted, CC extracellular space, extracellular matrix CC {ECO:0000269|PubMed:27811232}. Note=Newly synthesized LPL binds to cell CC surface heparan proteoglycans and is then released by heparanase. CC Subsequently, it becomes attached to heparan proteoglycan on CC endothelial cells (PubMed:27811232). Locates to the plasma membrane of CC microvilli of hepatocytes with triglyceride-rich lipoproteins (TRL). CC Some of the bound LPL is then internalized and located inside non- CC coated endocytic vesicles (By similarity). CC {ECO:0000250|UniProtKB:P11151, ECO:0000269|PubMed:27811232}. CC -!- TISSUE SPECIFICITY: Detected in blood plasma (PubMed:11893776, CC PubMed:12641539, PubMed:2340307). Detected in milk (at protein level) CC (PubMed:2340307). {ECO:0000269|PubMed:11893776, CC ECO:0000269|PubMed:12641539, ECO:0000269|PubMed:2340307}. CC -!- PTM: Tyrosine nitration after lipopolysaccharide (LPS) challenge down- CC regulates the lipase activity. {ECO:0000250|UniProtKB:Q06000}. CC -!- DISEASE: Hyperlipoproteinemia 1 (HLPP1) [MIM:238600]: An autosomal CC recessive metabolic disorder characterized by defective breakdown of CC dietary fats, impaired clearance of chylomicrons from plasma causing CC the plasma to have a milky appearance, and severe hypertriglyceridemia. CC On a normal diet, patients often present with abdominal pain, CC hepatosplenomegaly, lipemia retinalis, eruptive xanthomata, and massive CC hypertriglyceridemia, sometimes complicated with acute pancreatitis. CC {ECO:0000269|PubMed:10660334, ECO:0000269|PubMed:10787434, CC ECO:0000269|PubMed:11068186, ECO:0000269|PubMed:11099402, CC ECO:0000269|PubMed:11134145, ECO:0000269|PubMed:11441134, CC ECO:0000269|PubMed:11893776, ECO:0000269|PubMed:12204001, CC ECO:0000269|PubMed:12641539, ECO:0000269|PubMed:1371284, CC ECO:0000269|PubMed:1400331, ECO:0000269|PubMed:1479292, CC ECO:0000269|PubMed:14984478, ECO:0000269|PubMed:15185149, CC ECO:0000269|PubMed:1521525, ECO:0000269|PubMed:15256764, CC ECO:0000269|PubMed:15877202, ECO:0000269|PubMed:1598907, CC ECO:0000269|PubMed:1619366, ECO:0000269|PubMed:1639392, CC ECO:0000269|PubMed:1674945, ECO:0000269|PubMed:1702428, CC ECO:0000269|PubMed:1730727, ECO:0000269|PubMed:1752947, CC ECO:0000269|PubMed:1907278, ECO:0000269|PubMed:1969408, CC ECO:0000269|PubMed:1975597, ECO:0000269|PubMed:2010533, CC ECO:0000269|PubMed:2038366, ECO:0000269|PubMed:2110364, CC ECO:0000269|PubMed:2121025, ECO:0000269|PubMed:24291057, CC ECO:0000269|PubMed:26725083, ECO:0000269|PubMed:27578112, CC ECO:0000269|PubMed:30559189, ECO:0000269|PubMed:7806969, CC ECO:0000269|PubMed:7906986, ECO:0000269|PubMed:7912254, CC ECO:0000269|PubMed:7999071, ECO:0000269|PubMed:8077845, CC ECO:0000269|PubMed:8096693, ECO:0000269|PubMed:8135797, CC ECO:0000269|PubMed:8288243, ECO:0000269|PubMed:8301230, CC ECO:0000269|PubMed:8325986, ECO:0000269|PubMed:8486765, CC ECO:0000269|PubMed:8728326, ECO:0000269|PubMed:8778602, CC ECO:0000269|PubMed:8858123, ECO:0000269|PubMed:8956048, CC ECO:0000269|PubMed:8956052, ECO:0000269|PubMed:8973094, CC ECO:0000269|PubMed:9279761, ECO:0000269|PubMed:9298816, CC ECO:0000269|PubMed:9401010, ECO:0000269|PubMed:9498099, CC ECO:0000269|PubMed:9714430, ECO:0000269|PubMed:9719626}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Hyperlipidemia, familial combined, 3 (FCHL3) [MIM:144250]: A CC disorder characterized by a variable pattern of elevated levels of CC serum total cholesterol, triglycerides or both. It is observed in a CC percentage of individuals with premature coronary heart disease. FCHL3 CC inheritance is autosomal dominant. {ECO:0000269|PubMed:12966036, CC ECO:0000269|PubMed:7647785, ECO:0000269|PubMed:8728326, CC ECO:0000269|PubMed:8872057, ECO:0000269|PubMed:9662394, CC ECO:0000269|PubMed:9719626}. Note=Disease susceptibility is associated CC with variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Lipoprotein lipase entry; CC URL="https://en.wikipedia.org/wiki/Lipoprotein_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; M15856; AAB59536.1; -; mRNA. DR EMBL; X14390; CAA32564.1; -; mRNA. DR EMBL; X54516; CAA38372.1; -; mRNA. DR EMBL; M76722; AAA59528.1; -; Genomic_DNA. DR EMBL; S76076; AAB21000.1; -; Genomic_DNA. DR EMBL; S76077; AAB20999.1; -; Genomic_DNA. DR EMBL; BT006726; AAP35372.1; -; mRNA. DR EMBL; AK312311; BAG35236.1; -; mRNA. DR EMBL; CH471080; EAW63764.1; -; Genomic_DNA. DR EMBL; BC011353; AAH11353.1; -; mRNA. DR EMBL; X68111; CAA48230.1; -; Genomic_DNA. DR CCDS; CCDS6012.1; -. DR PIR; A26082; LIHUL. DR RefSeq; NP_000228.1; NM_000237.3. DR PDB; 6E7K; X-ray; 2.80 A; A/B=28-475. DR PDB; 6OAU; X-ray; 2.48 A; A/B=28-475. DR PDB; 6OAZ; X-ray; 3.04 A; A/B/C/D=28-475. DR PDB; 6OB0; X-ray; 2.81 A; A/B/C/D=28-475. DR PDB; 6WN4; X-ray; 2.80 A; C/D=410-423. DR AlphaFoldDB; P06858; -. DR MDRepo; P06858; -. DR SASBDB; P06858; -. DR SMR; P06858; -. DR BioGRID; 110205; 55. DR ComplexPortal; CPX-6091; LPL-GPIHBP1 triglyceride-rich lipoprotein processing complex. DR FunCoup; P06858; 160. DR IntAct; P06858; 39. DR MINT; P06858; -. DR NDEx; IQUERY-CP-LPL; 27 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000497642; -. DR BindingDB; P06858; -. DR ChEMBL; CHEMBL2060; -. DR DrugBank; DB13521; Alipogene tiparvovec. DR DrugBank; DB00636; Clofibrate. DR DrugBank; DB01241; Gemfibrozil. DR DrugBank; DB13751; Glycyrrhizic acid. DR DrugBank; DB19502; Ibrolipim. DR DrugBank; DB09568; Omega-3-carboxylic acids. DR DrugBank; DB13928; Semaglutide. DR DrugBank; DB06439; Tyloxapol. DR DrugCentral; P06858; -. DR SwissLipids; SLP:000000568; -. DR ESTHER; human-LPL; Lipoprotein_Lipase. DR GlyConnect; P06858; 18 N-Linked glycans (1 site). DR GlyCosmos; P06858; 2 sites, 24 glycans. DR GlyGen; P06858; 4 sites, 25 N-linked glycans (1 site), 1 O-linked glycan (1 site). DR iPTMnet; P06858; -. DR PhosphoSitePlus; P06858; -. DR SwissPalm; P06858; -. DR BioMuta; LPL; -. DR DMDM; 126314; -. DR jPOST; P06858; -. DR MassIVE; P06858; -. DR PaxDb; 9606-ENSP00000497642; -. DR PeptideAtlas; P06858; -. DR ProteomicsDB; 51936; -. DR Pumba; P06858; -. DR ABCD; P06858; 1 sequenced antibody. DR Antibodypedia; 9132; 592 antibodies from 39 providers. DR DNASU; 4023; -. DR Ensembl; ENST00000650287.1; ENSP00000497642.1; ENSG00000175445.18. DR Ensembl; ENST00000965928.1; ENSP00000635987.1; ENSG00000175445.18. DR GeneID; 4023; -. DR KEGG; hsa:4023; -. DR MANE-Select; ENST00000650287.1; ENSP00000497642.1; NM_000237.3; NP_000228.1. DR UCSC; uc003wzk.5; human. DR AGR; HGNC:6677; -. DR ClinPGx; PA232; -. DR CTD; 4023; -. DR DisGeNET; 4023; -. DR GeneCards; LPL; -. DR GeneReviews; LPL; -. DR HGNC; HGNC:6677; LPL. DR HPA; ENSG00000175445; Tissue enhanced (adipose tissue, heart muscle). DR MalaCards; LPL; -. DR MIM; 144250; phenotype. DR MIM; 238600; phenotype. DR MIM; 609708; gene. DR OpenTargets; ENSG00000175445; -. DR Orphanet; 309015; Familial lipoprotein lipase deficiency. DR VEuPathDB; HostDB:ENSG00000175445; -. DR eggNOG; ENOG502QQ7P; Eukaryota. DR GeneTree; ENSGT00940000157178; -. DR HOGENOM; CLU_027171_1_0_1; -. DR InParanoid; P06858; -. DR OMA; AIFVKCS; -. DR OrthoDB; 199913at2759; -. DR PAN-GO; P06858; 9 GO annotations based on evolutionary models. DR PhylomeDB; P06858; -. DR BRENDA; 3.1.1.34; 2681. DR PathwayCommons; P06858; -. DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation. DR Reactome; R-HSA-8963889; Assembly of active LPL and LIPC lipase complexes. DR Reactome; R-HSA-8963901; Chylomicron remodeling. DR Reactome; R-HSA-975634; Retinoid metabolism and transport. DR Reactome; R-HSA-9841922; MLL4 and MLL3 complexes regulate expression of PPARG target genes in adipogenesis and hepatic steatosis. DR SignaLink; P06858; -. DR SIGNOR; P06858; -. DR Agora; ENSG00000175445; -. DR BioGRID-ORCS; 4023; 8 hits in 1170 CRISPR screens. DR ChiTaRS; LPL; human. DR GeneWiki; Lipoprotein_lipase; -. DR GenomeRNAi; 4023; -. DR Pharos; P06858; Tchem. DR PRO; PR:P06858; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; P06858; protein. DR Bgee; ENSG00000175445; Expressed in olfactory bulb and 186 other cell types or tissues. DR ExpressionAtlas; P06858; baseline and differential. DR GO; GO:1902494; C:catalytic complex; IPI:ComplexPortal. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0034185; F:apolipoprotein binding; IPI:BHF-UCL. DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB. DR GO; GO:0004620; F:glycerophospholipase activity; ISS:BHF-UCL. DR GO; GO:0008970; F:glycerophospholipid phospholipase A1 activity; IDA:UniProtKB. DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; IMP:UniProtKB. DR GO; GO:0008201; F:heparin binding; IDA:UniProtKB. DR GO; GO:0004465; F:lipoprotein lipase activity; IDA:UniProtKB. DR GO; GO:0071813; F:lipoprotein particle binding; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0043495; F:protein-membrane adaptor activity; TAS:ARUK-UCL. DR GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL. DR GO; GO:0004806; F:triacylglycerol lipase activity; IDA:UniProtKB. DR GO; GO:0071398; P:cellular response to fatty acid; ISS:ARUK-UCL. DR GO; GO:0031670; P:cellular response to nutrient; ISS:ARUK-UCL. DR GO; GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL. DR GO; GO:0034371; P:chylomicron remodeling; IMP:UniProtKB. DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:BHF-UCL. DR GO; GO:0006631; P:fatty acid metabolic process; IDA:UniProtKB. DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IBA:GO_Central. DR GO; GO:0055096; P:low-density lipoprotein particle mediated signaling; IMP:BHF-UCL. DR GO; GO:0006644; P:phospholipid metabolic process; ISS:BHF-UCL. DR GO; GO:1904179; P:positive regulation of adipose tissue development; IMP:BHF-UCL. DR GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; ISS:ARUK-UCL. DR GO; GO:0032722; P:positive regulation of chemokine production; IMP:BHF-UCL. DR GO; GO:0010886; P:positive regulation of cholesterol storage; IMP:BHF-UCL. DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IMP:ARUK-UCL. DR GO; GO:0050729; P:positive regulation of inflammatory response; IMP:BHF-UCL. DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISS:ARUK-UCL. DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISS:ARUK-UCL. DR GO; GO:0010884; P:positive regulation of lipid storage; TAS:ARUK-UCL. DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IMP:BHF-UCL. DR GO; GO:1905885; P:positive regulation of triglyceride transport; IMP:BHF-UCL. DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:ARUK-UCL. DR GO; GO:0009749; P:response to glucose; ISS:AgBase. DR GO; GO:0001523; P:retinoid metabolic process; IEA:Ensembl. DR GO; GO:0019433; P:triglyceride catabolic process; IDA:UniProtKB. DR GO; GO:0070328; P:triglyceride homeostasis; IGI:BHF-UCL. DR GO; GO:0006641; P:triglyceride metabolic process; IMP:BHF-UCL. DR GO; GO:0034447; P:very-low-density lipoprotein particle clearance; ISS:BHF-UCL. DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IDA:BHF-UCL. DR CDD; cd00707; Pancreat_lipase_like; 1. DR CDD; cd01758; PLAT_LPL; 1. DR FunFam; 2.60.60.20:FF:000006; Lipoprotein lipase; 1. DR FunFam; 3.40.50.1820:FF:000031; Lipoprotein lipase; 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_fold. DR InterPro; IPR013818; Lipase. DR InterPro; IPR016272; Lipase_LIPH. DR InterPro; IPR033906; Lipase_N. DR InterPro; IPR002330; Lipo_Lipase. DR InterPro; IPR001024; PLAT/LH2_dom. DR InterPro; IPR036392; PLAT/LH2_dom_sf. DR InterPro; IPR000734; TAG_lipase. DR NCBIfam; TIGR03230; lipo_lipase; 1. DR PANTHER; PTHR11610; LIPASE; 1. DR PANTHER; PTHR11610:SF3; LIPOPROTEIN LIPASE; 1. DR Pfam; PF00151; Lipase; 1. DR Pfam; PF01477; PLAT; 1. DR PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1. DR PRINTS; PR00822; LIPOLIPASE. 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. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Cell membrane; Chylomicron; KW Direct protein sequencing; Disease variant; Disulfide bond; KW Extracellular matrix; Glycoprotein; Heparin-binding; Hydrolase; KW Hyperlipidemia; Lipid degradation; Lipid metabolism; Membrane; KW Metal-binding; Nitration; Proteomics identification; Reference proteome; KW Secreted; Signal; VLDL. FT SIGNAL 1..27 FT /evidence="ECO:0000269|PubMed:2340307" FT CHAIN 28..475 FT /note="Lipoprotein lipase" FT /id="PRO_0000017775" FT DOMAIN 341..464 FT /note="PLAT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152" FT REGION 32..53 FT /note="Interaction with GPIHBP1" FT /evidence="ECO:0000269|PubMed:30559189" FT REGION 243..266 FT /note="Essential for determining substrate specificity" FT /evidence="ECO:0000269|PubMed:7592706" FT REGION 417..421 FT /note="Important for interaction with lipoprotein FT particles" FT /evidence="ECO:0000269|PubMed:27929370" FT REGION 430..434 FT /note="Important for heparin binding" FT /evidence="ECO:0000269|PubMed:11342582" FT REGION 443..467 FT /note="Interaction with GPIHBP1" FT /evidence="ECO:0000269|PubMed:26725083, FT ECO:0000269|PubMed:30559189" FT ACT_SITE 159 FT /note="Nucleophile" FT /evidence="ECO:0000269|PubMed:1371284, FT ECO:0000269|PubMed:30559189" FT ACT_SITE 183 FT /note="Charge relay system" FT /evidence="ECO:0000269|PubMed:1371284, FT ECO:0000305|PubMed:30559189" FT ACT_SITE 268 FT /note="Charge relay system" FT /evidence="ECO:0000269|PubMed:1371284, FT ECO:0000305|PubMed:30559189" FT BINDING 194 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000305|PubMed:30559189" FT BINDING 197 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000305|PubMed:30559189" FT BINDING 199 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000305|PubMed:30559189" FT BINDING 202 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000305|PubMed:30559189" FT MOD_RES 121 FT /note="3'-nitrotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q06000" FT MOD_RES 191 FT /note="3'-nitrotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q06000" FT MOD_RES 343 FT /note="3'-nitrotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q06000" FT CARBOHYD 70 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18780401, FT ECO:0000269|PubMed:30559189, ECO:0007744|PDB:6E7K" FT CARBOHYD 386 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:30559189, FT ECO:0007744|PDB:6E7K" FT DISULFID 54..67 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152, FT ECO:0000269|PubMed:30559189, ECO:0007744|PDB:6E7K" FT DISULFID 243..266 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152, FT ECO:0000269|PubMed:30559189, ECO:0007744|PDB:6E7K" FT DISULFID 291..310 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152, FT ECO:0000269|PubMed:30559189, ECO:0007744|PDB:6E7K" FT DISULFID 302..305 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152, FT ECO:0000269|PubMed:30559189, ECO:0007744|PDB:6E7K" FT DISULFID 445..465 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152, FT ECO:0000269|PubMed:30559189, ECO:0007744|PDB:6E7K" FT VARIANT 36 FT /note="D -> N (risk factor for FCHL3; has approximately 80% FT of the specific activity of wild-type enzyme; FT dbSNP:rs1801177)" FT /evidence="ECO:0000269|PubMed:12966036, FT ECO:0000269|PubMed:8728326, ECO:0000269|PubMed:8872057, FT ECO:0000269|PubMed:9719626" FT /id="VAR_011948" FT VARIANT 70 FT /note="N -> S (in HLPP1; produces an inactive protein which FT is not secreted into the media; dbSNP:rs2069901707)" FT /evidence="ECO:0000269|PubMed:15256764, FT ECO:0000269|PubMed:7999071" FT /id="VAR_057914" FT VARIANT 71 FT /note="H -> Q (in dbSNP:rs11542065)" FT /id="VAR_049819" FT VARIANT 96 FT /note="V -> L (in HLPP1; gives rise to a 80% decrease in FT specific catalytic activity; dbSNP:rs373088068)" FT /evidence="ECO:0000269|PubMed:7912254" FT /id="VAR_057915" FT VARIANT 98 FT /note="A -> T (in HLPP1; decreases the specific activity of FT the enzyme; reduces the secretion of the mutant protein FT significantly; the total LPL mass is reduced compared to FT that of the wild-type construct; dbSNP:rs145657341)" FT /evidence="ECO:0000269|PubMed:12204001" FT /id="VAR_057916" FT VARIANT 102 FT /note="R -> S (in HLPP1; dbSNP:rs118204073)" FT /evidence="ECO:0000269|PubMed:8325986" FT /id="VAR_004211" FT VARIANT 113 FT /note="W -> G (in HLPP1)" FT /evidence="ECO:0000269|PubMed:9401010" FT /id="VAR_004212" FT VARIANT 113 FT /note="W -> R (in HLPP1; dbSNP:rs118204069)" FT /evidence="ECO:0000269|PubMed:1479292, FT ECO:0000269|PubMed:1598907" FT /id="VAR_004213" FT VARIANT 128 FT /note="T -> A (in HLPP1)" FT /evidence="ECO:0000269|PubMed:8778602, FT ECO:0000269|PubMed:9279761" FT /id="VAR_057917" FT VARIANT 132 FT /note="G -> R (in HLPP1; synthesized as a catalytically FT inactive form)" FT /evidence="ECO:0000269|PubMed:11099402, FT ECO:0000269|PubMed:15256764" FT /id="VAR_057918" FT VARIANT 163 FT /note="H -> R (in HLPP1)" FT /evidence="ECO:0000269|PubMed:1479292" FT /id="VAR_004214" FT VARIANT 169 FT /note="G -> E (in HLPP1; loss of activity; FT dbSNP:rs118204063)" FT /evidence="ECO:0000269|PubMed:2010533" FT /id="VAR_004215" FT VARIANT 181 FT /note="G -> S (in HLPP1; dbSNP:rs747009924)" FT /evidence="ECO:0000269|PubMed:8301230" FT /id="VAR_004216" FT VARIANT 181 FT /note="G -> V (in HLPP1; synthesized as a catalytically FT inactive form)" FT /evidence="ECO:0000269|PubMed:11441134, FT ECO:0000269|PubMed:15256764" FT /id="VAR_057919" FT VARIANT 183 FT /note="D -> G (in HLPP1; lacks both triolein and tributyrin FT esterase activities; dbSNP:rs118204064)" FT /evidence="ECO:0000269|PubMed:1371284, FT ECO:0000269|PubMed:1730727, ECO:0000269|PubMed:1907278" FT /id="VAR_004217" FT VARIANT 183 FT /note="D -> H (in HLPP1; dbSNP:rs781614031)" FT /evidence="ECO:0000269|PubMed:9279761" FT /id="VAR_057920" FT VARIANT 183 FT /note="D -> N (in HLPP1; lacks both triolein and tributyrin FT esterase activities; dbSNP:rs781614031)" FT /evidence="ECO:0000269|PubMed:1371284, FT ECO:0000269|PubMed:1730727" FT /id="VAR_004218" FT VARIANT 184 FT /note="P -> R (in HLPP1; Nijmegen; loss of activity)" FT /evidence="ECO:0000269|PubMed:1521525" FT /id="VAR_004219" FT VARIANT 185 FT /note="A -> T (in HLPP1; 3.2% of activity; FT dbSNP:rs748349562)" FT /evidence="ECO:0000269|PubMed:9401010" FT /id="VAR_004220" FT VARIANT 186 FT /note="G -> E (in HLPP1)" FT /evidence="ECO:0000269|PubMed:15877202" FT /id="VAR_057921" FT VARIANT 190 FT /note="E -> G (in HLPP1)" FT /evidence="ECO:0000269|PubMed:8956052" FT /id="VAR_057922" FT VARIANT 199 FT /note="S -> C (in HLPP1; mild hypertriglyceridemia; partial FT activity; dbSNP:rs118204072)" FT /evidence="ECO:0000269|PubMed:8077845, FT ECO:0000269|PubMed:8486765" FT /id="VAR_004221" FT VARIANT 201 FT /note="D -> V (in HLPP1; almost complete loss of enzyme FT activity; dbSNP:rs2069961955)" FT /evidence="ECO:0000269|PubMed:14984478, FT ECO:0000269|PubMed:30559189" FT /id="VAR_057923" FT VARIANT 203 FT /note="A -> T (in HLPP1; Bethesda; loss of activity and FT abnormal heparin binding; dbSNP:rs118204056)" FT /evidence="ECO:0000269|PubMed:11893776, FT ECO:0000269|PubMed:2110364" FT /id="VAR_004222" FT VARIANT 207 FT /note="D -> E (in HLPP1; dbSNP:rs118204076)" FT /evidence="ECO:0000269|PubMed:8288243" FT /id="VAR_004223" FT VARIANT 208 FT /note="V -> I (in HLPP1; decreases the specific activity of FT the enzyme; has a mild effect on the secretion of the FT mutant enzyme; the total LPL mass is reduced compared to FT that of the wild-type construct; dbSNP:rs568397156)" FT /evidence="ECO:0000269|PubMed:12204001" FT /id="VAR_057924" FT VARIANT 210 FT /note="H -> D (in HLPP1; complete loss of enzyme activity)" FT /evidence="ECO:0000269|PubMed:10787434" FT /id="VAR_057925" FT VARIANT 210 FT /note="H -> Q (in HLPP1; severely decreased lipoprotein FT lipase activity; decreased secretion)" FT /evidence="ECO:0000269|PubMed:24291057, FT ECO:0000269|PubMed:9401010" FT /id="VAR_004224" FT VARIANT 215 FT /note="G -> E (in HLPP1; loss of activity; FT dbSNP:rs118204057)" FT /evidence="ECO:0000269|PubMed:10660334, FT ECO:0000269|PubMed:11893776, ECO:0000269|PubMed:1479292, FT ECO:0000269|PubMed:15185149, ECO:0000269|PubMed:15256764, FT ECO:0000269|PubMed:15877202, ECO:0000269|PubMed:1619366, FT ECO:0000269|PubMed:1969408, ECO:0000269|PubMed:1975597, FT ECO:0000269|PubMed:7912254, ECO:0000269|PubMed:8778602, FT ECO:0000269|PubMed:8956052, ECO:0000269|PubMed:9279761, FT ECO:0000269|PubMed:9401010" FT /id="VAR_004225" FT VARIANT 215 FT /note="G -> R (in HLPP1)" FT /evidence="ECO:0000269|PubMed:8778602, FT ECO:0000269|PubMed:9279761" FT /id="VAR_057926" FT VARIANT 220 FT /note="S -> R (in HLPP1; 2.0% of activity; FT dbSNP:rs757546424)" FT /evidence="ECO:0000269|PubMed:9401010" FT /id="VAR_004226" FT VARIANT 221 FT /note="I -> T (in HLPP1; loss of activity; FT dbSNP:rs118204061)" FT /evidence="ECO:0000269|PubMed:11893776, FT ECO:0000269|PubMed:1479292, ECO:0000269|PubMed:15256764, FT ECO:0000269|PubMed:15877202, ECO:0000269|PubMed:1674945, FT ECO:0000269|PubMed:1702428" FT /id="VAR_004227" FT VARIANT 222 FT /note="G -> E (in HLPP1; dbSNP:rs118204075)" FT /evidence="ECO:0000269|PubMed:1400331" FT /id="VAR_004228" FT VARIANT 225 FT /note="K -> R (in HLPP1)" FT /evidence="ECO:0000269|PubMed:15256764" FT /id="VAR_057927" FT VARIANT 227 FT /note="V -> A (in HLPP1; dbSNP:rs528243561)" FT /evidence="ECO:0000269|PubMed:15256764" FT /id="VAR_057928" FT VARIANT 231 FT /note="D -> E (in HLPP1; loss of activity; FT dbSNP:rs118204067)" FT /evidence="ECO:0000269|PubMed:11099402, FT ECO:0000269|PubMed:15256764, ECO:0000269|PubMed:1752947" FT /id="VAR_004229" FT VARIANT 232 FT /note="I -> S (in HLPP1; loss of activity; FT dbSNP:rs770601263)" FT /evidence="ECO:0000269|PubMed:11893776, FT ECO:0000269|PubMed:1479292" FT /id="VAR_004230" FT VARIANT 234 FT /note="P -> L (in HLPP1; loss of activity; FT dbSNP:rs118204060)" FT /evidence="ECO:0000269|PubMed:11893776, FT ECO:0000269|PubMed:2038366, ECO:0000269|PubMed:9279761, FT ECO:0000269|PubMed:9401010" FT /id="VAR_004231" FT VARIANT 243 FT /note="C -> S (in HLPP1; loss of activity; FT dbSNP:rs2069963510)" FT /evidence="ECO:0000269|PubMed:1730727" FT /id="VAR_004232" FT VARIANT 252 FT /note="I -> T (in HLPP1; dbSNP:rs118204080)" FT /evidence="ECO:0000269|PubMed:9714430" FT /id="VAR_057929" FT VARIANT 266 FT /note="C -> W (in HLPP1; dbSNP:rs118204082)" FT /evidence="ECO:0000269|PubMed:11134145" FT /id="VAR_057930" FT VARIANT 270 FT /note="R -> C (in HLPP1; dbSNP:rs118204077)" FT /evidence="ECO:0000269|PubMed:15256764, FT ECO:0000269|PubMed:7906986, ECO:0000269|PubMed:8778602, FT ECO:0000269|PubMed:9279761" FT /id="VAR_057931" FT VARIANT 270 FT /note="R -> H (in HLPP1; loss of activity; FT dbSNP:rs118204062)" FT /evidence="ECO:0000269|PubMed:15256764, FT ECO:0000269|PubMed:1619366, ECO:0000269|PubMed:1702428, FT ECO:0000269|PubMed:1752947, ECO:0000269|PubMed:7906986, FT ECO:0000269|PubMed:9714430" FT /id="VAR_004233" FT VARIANT 271 FT /note="S -> T (in HLPP1; dbSNP:rs118204059)" FT /evidence="ECO:0000269|PubMed:2121025" FT /id="VAR_004234" FT VARIANT 277 FT /note="D -> N (in HLPP1; 5% of full activity; FT dbSNP:rs118204068)" FT /evidence="ECO:0000269|PubMed:1619366, FT ECO:0000269|PubMed:1639392, ECO:0000269|PubMed:8778602, FT ECO:0000269|PubMed:8956048, ECO:0000269|PubMed:9279761" FT /id="VAR_004235" FT VARIANT 278 FT /note="S -> C (in HLPP1)" FT /evidence="ECO:0000269|PubMed:8973094" FT /id="VAR_004236" FT VARIANT 279 FT /note="L -> R (in HLPP1; decreases the specific activity of FT the enzyme; the total LPL mass is reduced compared to that FT of the wild-type construct; dbSNP:rs35414700)" FT /evidence="ECO:0000269|PubMed:12204001, FT ECO:0000269|PubMed:8077845" FT /id="VAR_057932" FT VARIANT 279 FT /note="L -> V (in HLPP1; decreases the specific activity of FT the enzyme; the total LPL mass is reduced compared to that FT of the wild-type construct; dbSNP:rs371282890)" FT /evidence="ECO:0000269|PubMed:12204001" FT /id="VAR_057933" FT VARIANT 286 FT /note="S -> G (in HLPP1)" FT /evidence="ECO:0000269|PubMed:10660334" FT /id="VAR_004237" FT VARIANT 286 FT /note="S -> R (in HLPP1)" FT /evidence="ECO:0000269|PubMed:9298816" FT /id="VAR_004238" FT VARIANT 288 FT /note="A -> T (in HLPP1; the LPL mass level is FT approximately 67% of the normal; the activity is 32% of the FT nornal; dbSNP:rs1800011)" FT /evidence="ECO:0000269|PubMed:15256764, FT ECO:0000269|PubMed:8077845, ECO:0000269|PubMed:9719626" FT /id="VAR_011949" FT VARIANT 289 FT /note="Y -> H (in HLPP1; no enzyme activity; FT dbSNP:rs1161884343)" FT /evidence="ECO:0000269|PubMed:8728326" FT /id="VAR_057934" FT VARIANT 297 FT /note="F -> L (in HLPP1 and hyperlipidemia; synthesized as FT a catalytically inactive form; total amount is almost equal FT to that of the normal enzyme; non-releasable by heparin due FT to the abnormal structure of the mutant protein)" FT /evidence="ECO:0000269|PubMed:11068186, FT ECO:0000269|PubMed:15256764" FT /id="VAR_057935" FT VARIANT 303 FT /note="L -> F (in HLPP1; approximately 6% of normal LPL FT activity and 40% of LPL mass are detected in the patient's FT postheparin plasma; results in the production of a FT functionally inactive enzyme)" FT /evidence="ECO:0000269|PubMed:12641539" FT /id="VAR_057936" FT VARIANT 305 FT /note="C -> R (in HLPP1; dbSNP:rs773235712)" FT /evidence="ECO:0000269|PubMed:15256764" FT /id="VAR_057937" FT VARIANT 310 FT /note="C -> Y (in HLPP1; decreases the specific activity of FT the enzyme; reduces the secretion of the mutant protein FT significantly; the total LPL mass is reduced compared to FT that of the wild-type construct; dbSNP:rs1409123950)" FT /evidence="ECO:0000269|PubMed:12204001" FT /id="VAR_057938" FT VARIANT 313 FT /note="L -> P (in HLPP1)" FT /evidence="ECO:0000269|PubMed:8778602" FT /id="VAR_057939" FT VARIANT 318 FT /note="N -> S (in HLPP1; risk factor for FCHL3; loss of FT activity; dbSNP:rs268)" FT /evidence="ECO:0000269|PubMed:12966036, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7647785, FT ECO:0000269|PubMed:8872057, ECO:0000269|PubMed:9401010, FT ECO:0000269|PubMed:9662394, ECO:0000269|PubMed:9719626, FT ECO:0000269|Ref.5" FT /id="VAR_004239" FT VARIANT 325 FT /note="S -> R (in HLPP1; has no effect on the specific FT activity of the enzyme; has a mild effect on the secretion FT of the mutant enzyme; the total LPL mass is reduced FT compared to that of the wild-type construct; FT dbSNP:rs761265900)" FT /evidence="ECO:0000269|PubMed:12204001" FT /id="VAR_057940" FT VARIANT 328 FT /note="M -> R (in HLPP1)" FT /evidence="ECO:0000269|PubMed:15185149" FT /id="VAR_057941" FT VARIANT 328 FT /note="M -> T (in HLPP1; dbSNP:rs1181582051)" FT /evidence="ECO:0000269|PubMed:9401010" FT /id="VAR_004240" FT VARIANT 330 FT /note="L -> F (in HLPP1)" FT /evidence="ECO:0000269|PubMed:15256764" FT /id="VAR_057942" FT VARIANT 330 FT /note="L -> P (in HLPP1)" FT /evidence="ECO:0000269|PubMed:9401010" FT /id="VAR_004241" FT VARIANT 361 FT /note="A -> T (in HLPP1; dbSNP:rs118204071)" FT /evidence="ECO:0000269|PubMed:15256764, FT ECO:0000269|PubMed:8096693" FT /id="VAR_004242" FT VARIANT 365 FT /note="S -> F (in HLPP1; increases the specific activity of FT the enzyme; has a mild effect on the secretion of the FT mutant enzyme; the total LPL mass is reduced compared to FT that of the wild-type construct; dbSNP:rs546542623)" FT /evidence="ECO:0000269|PubMed:12204001" FT /id="VAR_057943" FT VARIANT 370 FT /note="V -> M (in dbSNP:rs298)" FT /evidence="ECO:0000269|PubMed:9662394" FT /id="VAR_011950" FT VARIANT 379 FT /note="T -> A (in dbSNP:rs300)" FT /evidence="ECO:0000269|PubMed:9662394" FT /id="VAR_011951" FT VARIANT 392 FT /note="L -> V (in HLPP1; loss of activity; FT dbSNP:rs118204078)" FT /evidence="ECO:0000269|PubMed:8135797" FT /id="VAR_004243" FT VARIANT 404 FT /note="M -> R (in HLPP1; decreased protein secretion; loss FT of interaction with GPIHBP1; decreased lipoprotein lipase FT activity)" FT /evidence="ECO:0000269|PubMed:27578112, FT ECO:0000269|PubMed:30559189" FT /id="VAR_077541" FT VARIANT 423..424 FT /note="Missing (in HLPP1; affects the protein folding)" FT /id="VAR_004244" FT VARIANT 427 FT /note="A -> T (in dbSNP:rs5934)" FT /evidence="ECO:0000269|PubMed:10391209" FT /id="VAR_011952" FT VARIANT 437 FT /note="E -> K (in HLPP1; dbSNP:rs2070034219)" FT /evidence="ECO:0000269|PubMed:8956048" FT /id="VAR_004245" FT VARIANT 437 FT /note="E -> V (in HLPP1)" FT /evidence="ECO:0000269|PubMed:7806969" FT /id="VAR_004246" FT VARIANT 445 FT /note="C -> Y (in HLPP1; has 48% of normal activity in FT vitro; decreased levels of activity account for by the FT lower protein mass levels of the mutants rather than by FT decreased enzymatic activities; loss of interaction with FT GPIHBP1; dbSNP:rs118204079)" FT /evidence="ECO:0000269|PubMed:26725083, FT ECO:0000269|PubMed:30559189, ECO:0000269|PubMed:8858123" FT /id="VAR_057944" FT VARIANT 448 FT /note="E -> K (in HLPP1; results in a moderate reduction in FT catalytic activity; dbSNP:rs149089920)" FT /evidence="ECO:0000269|PubMed:9498099" FT /id="VAR_057945" FT MUTAGEN 159 FT /note="S->G: Loss of enzyme activity with triolein and FT tributyrin." FT /evidence="ECO:0000269|PubMed:1371284, FT ECO:0000269|PubMed:30559189" FT MUTAGEN 159 FT /note="S->T: Loss of enzyme activity with triolein and FT tributyrin." FT /evidence="ECO:0000269|PubMed:1371284" FT MUTAGEN 183 FT /note="D->G,N: Loss of enzyme activity with triolein and FT tributyrin." FT /evidence="ECO:0000269|PubMed:1371284" FT MUTAGEN 199 FT /note="S->G: Loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:1371284" FT MUTAGEN 201 FT /note="D->E: No effect on enzyme activity." FT /evidence="ECO:0000269|PubMed:30559189" FT MUTAGEN 202 FT /note="D->E: Loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:30559189" FT MUTAGEN 244..264 FT /note="NIGEAIRVIAERGLGDVDQLV->HFLELYRHIAQHGFNAITQTI: FT Reduced triglyceride hydrolase activity and increased FT phospholipase activity." FT /evidence="ECO:0000269|PubMed:7592706" FT MUTAGEN 245..263 FT /note="IGEAIRVIAERGLGDVDQL->GIAEIRVIEARGGLDVDLQ: Loss of FT both triglyceride hydrolase and phospholipase activity." FT /evidence="ECO:0000269|PubMed:7592706" FT MUTAGEN 245..248 FT /note="IGEA->GIAE: Loss of triglyceride hydrolase activity FT while phospholipase activity remains intact." FT /evidence="ECO:0000269|PubMed:7592706" FT MUTAGEN 262..263 FT /note="QL->LQ: Loss of triglyceride hydrolase activity FT while phospholipase activity remains intact." FT /evidence="ECO:0000269|PubMed:7592706" FT MUTAGEN 268 FT /note="H->G: Loss of enzyme activity with triolein and FT tributyrin." FT /evidence="ECO:0000269|PubMed:1371284" FT MUTAGEN 268 FT /note="H->Q: Loss of enzyme activity with triolein and FT tributyrin." FT /evidence="ECO:0000269|PubMed:1371284" FT MUTAGEN 417 FT /note="W->A: Loss of interaction with lipoprotein FT particles, but no effect on interaction with GPIHBP1; when FT associated with 420-A-A-421." FT /evidence="ECO:0000269|PubMed:24726386" FT MUTAGEN 420..421 FT /note="WW->AA: Loss of interaction with lipoprotein FT particles, but no effect on interaction with GPIHBP1; when FT associated with A-417." FT /evidence="ECO:0000269|PubMed:24726386" FT MUTAGEN 430 FT /note="K->N: Impaired heparin-binding; when associated with FT N-432 and N-437." FT /evidence="ECO:0000269|PubMed:11342582" FT MUTAGEN 432 FT /note="R->N: Impaired heparin-binding; when associated with FT N-430 and N-437." FT /evidence="ECO:0000269|PubMed:11342582" FT MUTAGEN 434 FT /note="K->N: Impaired heparin-binding; when associated with FT N-430 and N-432." FT /evidence="ECO:0000269|PubMed:11342582" FT HELIX 31..34 FT /evidence="ECO:0007829|PDB:6OAU" FT STRAND 40..44 FT /evidence="ECO:0007829|PDB:6OAU" FT STRAND 54..56 FT /evidence="ECO:0007829|PDB:6OAU" FT HELIX 61..66 FT /evidence="ECO:0007829|PDB:6OAU" FT STRAND 71..73 FT /evidence="ECO:0007829|PDB:6OB0" FT STRAND 75..79 FT /evidence="ECO:0007829|PDB:6OAU" FT STRAND 84..87 FT /evidence="ECO:0007829|PDB:6E7K" FT HELIX 91..102 FT /evidence="ECO:0007829|PDB:6OAU" FT STRAND 106..112 FT /evidence="ECO:0007829|PDB:6OAU" FT HELIX 114..117 FT /evidence="ECO:0007829|PDB:6OAU" FT HELIX 121..124 FT /evidence="ECO:0007829|PDB:6OAU" FT TURN 125..127 FT /evidence="ECO:0007829|PDB:6OAU" FT HELIX 128..146 FT /evidence="ECO:0007829|PDB:6OAU" FT HELIX 150..152 FT /evidence="ECO:0007829|PDB:6OAU" FT STRAND 153..158 FT /evidence="ECO:0007829|PDB:6OAU" FT HELIX 160..169 FT /evidence="ECO:0007829|PDB:6OAU" FT STRAND 172..174 FT /evidence="ECO:0007829|PDB:6OAU" FT STRAND 176..183 FT /evidence="ECO:0007829|PDB:6OAU" FT TURN 187..189 FT /evidence="ECO:0007829|PDB:6OAU" FT HELIX 194..196 FT /evidence="ECO:0007829|PDB:6OAU" FT HELIX 200..202 FT /evidence="ECO:0007829|PDB:6OAU" FT STRAND 203..209 FT /evidence="ECO:0007829|PDB:6OAU" FT STRAND 219..222 FT /evidence="ECO:0007829|PDB:6OAU" FT STRAND 228..234 FT /evidence="ECO:0007829|PDB:6OAU" FT TURN 235..238 FT /evidence="ECO:0007829|PDB:6OAU" FT TURN 241..243 FT /evidence="ECO:0007829|PDB:6OB0" FT HELIX 247..253 FT /evidence="ECO:0007829|PDB:6OB0" FT HELIX 262..280 FT /evidence="ECO:0007829|PDB:6OAU" FT STRAND 282..284 FT /evidence="ECO:0007829|PDB:6OAU" FT STRAND 287..290 FT /evidence="ECO:0007829|PDB:6OAU" FT HELIX 294..298 FT /evidence="ECO:0007829|PDB:6OAU" FT STRAND 308..314 FT /evidence="ECO:0007829|PDB:6OAU" FT STRAND 326..330 FT /evidence="ECO:0007829|PDB:6OAU" FT STRAND 334..337 FT /evidence="ECO:0007829|PDB:6OAU" FT STRAND 341..350 FT /evidence="ECO:0007829|PDB:6OAU" FT STRAND 356..370 FT /evidence="ECO:0007829|PDB:6OAU" FT STRAND 372..384 FT /evidence="ECO:0007829|PDB:6OAU" FT STRAND 387..397 FT /evidence="ECO:0007829|PDB:6OAU" FT STRAND 401..409 FT /evidence="ECO:0007829|PDB:6OAU" FT HELIX 417..421 FT /evidence="ECO:0007829|PDB:6WN4" FT HELIX 422..424 FT /evidence="ECO:0007829|PDB:6OAU" FT STRAND 425..428 FT /evidence="ECO:0007829|PDB:6OAU" FT STRAND 430..435 FT /evidence="ECO:0007829|PDB:6OAU" FT TURN 436..439 FT /evidence="ECO:0007829|PDB:6OAU" FT STRAND 440..454 FT /evidence="ECO:0007829|PDB:6OAU" FT STRAND 460..469 FT /evidence="ECO:0007829|PDB:6OAU" SQ SEQUENCE 475 AA; 53162 MW; FBD00FCD334FB8AA CRC64; MESKALLVLT LAVWLQSLTA SRGGVAAADQ RRDFIDIESK FALRTPEDTA EDTCHLIPGV AESVATCHFN HSSKTFMVIH GWTVTGMYES WVPKLVAALY KREPDSNVIV VDWLSRAQEH YPVSAGYTKL VGQDVARFIN WMEEEFNYPL DNVHLLGYSL GAHAAGIAGS LTNKKVNRIT GLDPAGPNFE YAEAPSRLSP DDADFVDVLH TFTRGSPGRS IGIQKPVGHV DIYPNGGTFQ PGCNIGEAIR VIAERGLGDV DQLVKCSHER SIHLFIDSLL NEENPSKAYR CSSKEAFEKG LCLSCRKNRC NNLGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIHFS GTESETHTNQ AFEISLYGTV AESENIPFTL PEVSTNKTYS FLIYTEVDIG ELLMLKLKWK SDSYFSWSDW WSSPGFAIQK IRVKAGETQK KVIFCSREKV SHLQKGKAPA VFVKCHDKSL NKKSG //