LIPL_HUMAN
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 03-AUG-2022, entry version 249.
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;
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;
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;
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;
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;
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;
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;
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 FCHL3 ASN-36 AND SER-318.
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 FCHL3 ASN-36, CHARACTERIZATION OF VARIANT
RP HLPP1 HIS-289, AND CHARACTERIZATION OF VARIANT FCHL3 ASN-36.
RX PubMed=8728326;
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 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 [65]
RP VARIANTS.
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 [66]
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 [67]
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 [68]
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 [69]
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 [70]
RP VARIANT HLPP1 THR-288, AND VARIANTS FCHL3 ASN-36 AND SER-318.
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 [71]
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 [72]
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 [73]
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 [74]
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 [75]
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 [76]
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 [77]
RP VARIANT HLPP1 ASP-210, AND CHARACTERIZATION OF VARIANT HLPP1 ASP-210.
RX PubMed=10787434;
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 [78]
RP VARIANT HLPP1 VAL-181, AND CHARACTERIZATION OF VARIANT HLPP1 VAL-181.
RX PubMed=11441134;
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 [79]
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 [80]
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;
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 [81]
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 [82]
RP VARIANTS FCHL3 ASN-36 AND SER-318.
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 [83]
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 [84]
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 [85]
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 [86]
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 [87]
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:8675619, PubMed:11342582, PubMed:27578112). 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:7592706, PubMed:12032167). 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 = (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: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)-octadecenoate + (9Z-octadecenoyl)-sn-glycero-3-phosphocholine +
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 = 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: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 = H(+) +
CC hexadecanoate + hexadecanoyl-sn-glycero-3-phosphocholine;
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 (PubMed:16179346, PubMed:26725083, PubMed:11893776)
CC (Probable). Interacts with GPIHBP1 with 1:1 stoichiometry
CC (PubMed:17997385, PubMed:27929370, PubMed:26725083, PubMed:27811232,
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; Q8TAB7: CCDC26; NbExp=3; IntAct=EBI-715909, EBI-10271580;
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:27578112,
CC ECO:0000269|PubMed:30559189}. Secreted, extracellular space,
CC extracellular matrix {ECO:0000269|PubMed:27811232}. Note=Newly
CC synthesized LPL binds to cell surface heparan proteoglycans and is then
CC released by heparanase. Subsequently, it becomes attached to heparan
CC proteoglycan on endothelial cells (PubMed:27811232). Locates to the
CC plasma membrane of microvilli of hepatocytes with triglyceride-rich
CC lipoproteins (TRL). Some of the bound LPL is then internalized and
CC located inside non-coated endocytic vesicles (By similarity).
CC {ECO:0000250|UniProtKB:P11151, ECO:0000269|PubMed:27811232}.
CC -!- TISSUE SPECIFICITY: Detected in blood plasma (PubMed:2340307,
CC PubMed:11893776, PubMed:12641539). 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:26725083,
CC ECO:0000269|PubMed:27578112, ECO:0000269|PubMed:30559189,
CC ECO:0000269|PubMed:7806969, ECO:0000269|PubMed:7906986,
CC ECO:0000269|PubMed:7912254, ECO:0000269|PubMed:7999071,
CC ECO:0000269|PubMed:8077845, ECO:0000269|PubMed:8096693,
CC ECO:0000269|PubMed:8135797, ECO:0000269|PubMed:8288243,
CC ECO:0000269|PubMed:8301230, ECO:0000269|PubMed:8325986,
CC ECO:0000269|PubMed:8486765, ECO:0000269|PubMed:8728326,
CC ECO:0000269|PubMed:8778602, ECO:0000269|PubMed:8858123,
CC ECO:0000269|PubMed:8956048, ECO:0000269|PubMed:8956052,
CC ECO:0000269|PubMed:9279761, ECO:0000269|PubMed:9298816,
CC ECO:0000269|PubMed:9498099, ECO:0000269|PubMed:9714430,
CC ECO:0000269|PubMed:9719626}. Note=The disease is caused by variants
CC affecting the gene represented in this 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";
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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_000237.2.
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 PDBsum; 6E7K; -.
DR PDBsum; 6OAU; -.
DR PDBsum; 6OAZ; -.
DR PDBsum; 6OB0; -.
DR PDBsum; 6WN4; -.
DR AlphaFoldDB; P06858; -.
DR SASBDB; P06858; -.
DR SMR; P06858; -.
DR BioGRID; 110205; 48.
DR ComplexPortal; CPX-6091; LPL-GPIHBP1 triglyceride-rich lipoprotein processing complex.
DR IntAct; P06858; 30.
DR MINT; P06858; -.
DR STRING; 9606.ENSP00000309757; -.
DR BindingDB; P06858; -.
DR ChEMBL; CHEMBL2060; -.
DR DrugBank; DB13751; Glycyrrhizic acid.
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; 2940; 18 N-Linked glycans (1 site).
DR GlyGen; P06858; 2 sites, 21 N-linked glycans (1 site).
DR iPTMnet; P06858; -.
DR PhosphoSitePlus; P06858; -.
DR BioMuta; LPL; -.
DR DMDM; 126314; -.
DR EPD; P06858; -.
DR jPOST; P06858; -.
DR MassIVE; P06858; -.
DR MaxQB; P06858; -.
DR PaxDb; P06858; -.
DR PeptideAtlas; P06858; -.
DR PRIDE; P06858; -.
DR ProteomicsDB; 51936; -.
DR ABCD; P06858; 1 sequenced antibody.
DR Antibodypedia; 9132; 564 antibodies from 35 providers.
DR DNASU; 4023; -.
DR Ensembl; ENST00000650287.1; ENSP00000497642.1; ENSG00000175445.17.
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 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 neXtProt; NX_P06858; -.
DR OpenTargets; ENSG00000175445; -.
DR Orphanet; 309015; Familial lipoprotein lipase deficiency.
DR PharmGKB; PA232; -.
DR VEuPathDB; HostDB:ENSG00000175445; -.
DR eggNOG; ENOG502QQ7P; Eukaryota.
DR GeneTree; ENSGT00940000157178; -.
DR HOGENOM; CLU_027171_1_0_1; -.
DR InParanoid; P06858; -.
DR OMA; TIWITLG; -.
DR OrthoDB; 534956at2759; -.
DR PhylomeDB; P06858; -.
DR TreeFam; TF324997; -.
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 SignaLink; P06858; -.
DR SIGNOR; P06858; -.
DR BioGRID-ORCS; 4023; 8 hits in 1084 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 184 other tissues.
DR ExpressionAtlas; P06858; baseline and differential.
DR Genevisible; P06858; HS.
DR GO; GO:1902494; C:catalytic complex; IPI:ComplexPortal.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0034185; F:apolipoprotein binding; IPI:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; 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:0016298; F:lipase activity; IBA:GO_Central.
DR GO; GO:0004465; F:lipoprotein lipase activity; IDA:UniProtKB.
DR GO; GO:0071813; F:lipoprotein particle binding; IDA:UniProtKB.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; IDA:UniProtKB.
DR GO; GO:0004620; F:phospholipase activity; ISS:BHF-UCL.
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:0017129; F:triglyceride binding; IEA:Ensembl.
DR GO; GO:0004806; F:triglyceride 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:0016042; P:lipid catabolic process; IBA:GO_Central.
DR GO; GO:0055096; P:low-density lipoprotein particle mediated signaling; IMP:BHF-UCL.
DR GO; GO:1900077; P:negative regulation of cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0006644; P:phospholipid metabolic process; ISS: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; ISS:ARUK-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; IC:BHF-UCL.
DR GO; GO:0010890; P:positive regulation of sequestering of triglyceride; IMP:BHF-UCL.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:ARUK-UCL.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR GO; GO:0009409; P:response to cold; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; ISS:AgBase.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0019432; P:triglyceride biosynthetic 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; 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 Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013818; Lipase.
DR InterPro; IPR016272; Lipase_LIPH.
DR InterPro; IPR033906; Lipase_N.
DR InterPro; IPR002330; Lipo_Lipase.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610; PTHR11610; 1.
DR PANTHER; PTHR11610:SF3; PTHR11610:SF3; 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; SSF49723; SSF49723; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR03230; lipo_lipase; 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; Reference proteome; 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 (in FCHL3; associated with disease
FT susceptibility; has approximately 80% of the specific
FT activity of wild-type enzyme; 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)"
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 /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)"
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 /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)"
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; loss of activity)"
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 /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 /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 /id="VAR_004231"
FT VARIANT 243
FT /note="C -> S (in HLPP1; loss of activity)"
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 /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 FCHL3; associated with disease
FT susceptibility; loss of activity; frequent mutation;
FT 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:9662394,
FT ECO:0000269|PubMed:9719626, 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 /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 /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)"
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 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
