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Lipoprotein lipase (LPL) (EC 3.1.1.34)

 LIPL_HUMAN              Reviewed;         475 AA.
P06858; B2R5T9; Q16282; Q16283; Q96FC4;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
25-APR-2018, entry version 219.
RecName: Full=Lipoprotein lipase;
Short=LPL;
EC=3.1.1.34 {ECO:0000269|PubMed:11342582, ECO:0000269|PubMed:27578112};
Flags: Precursor;
Name=LPL; Synonyms=LIPD;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3823907; DOI=10.1126/science.3823907;
Wion K.L., Kirchgessner T.G., Lusis A.J., Schotz M.C., Lawn R.M.;
"Human lipoprotein lipase complementary DNA sequence.";
Science 235:1638-1641(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=2701938; DOI=10.1093/nar/17.6.2351;
Gotoda T., Senda M., Gamou T., Furuichi Y., Oka K.;
"Nucleotide sequence of human cDNA coding for a lipoprotein lipase
(LPL) cloned from placental cDNA library.";
Nucleic Acids Res. 17:2351-2352(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2243796; DOI=10.1093/nar/18.21.6436;
Takagi A., Ikeda Y., Yamamoto A.;
"DNA sequence of lipoprotein lipase cDNA cloned from human monocytic
leukemia THP-1 cells.";
Nucleic Acids Res. 18:6436-6436(1990).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1537564; DOI=10.1016/0378-1119(92)90658-C;
Chuat J.-C., Raisonnier A., Etienne J., Galibert F.;
"The lipoprotein lipase-encoding human gene: sequence from intron-6 to
intron-9 and presence in intron-7 of a 40-million-year-old Alu
sequence.";
Gene 110:257-261(1992).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-318.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-318.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
PubMed=1406652; DOI=10.1128/MCB.12.10.4622;
Enerbaeck S., Ohlsson B.G., Samuelsson L., Bjursell G.;
"Characterization of the human lipoprotein lipase (LPL) promoter:
evidence of two cis-regulatory regions, LP-alpha and LP-beta, of
importance for the differentiation-linked induction of the LPL gene
during adipogenesis.";
Mol. Cell. Biol. 12:4622-4633(1992).
[10]
PROTEIN SEQUENCE OF 28-44, AND SUBCELLULAR LOCATION.
TISSUE=Milk;
PubMed=2340307; DOI=10.1016/0005-2760(90)90213-H;
Zechner R.;
"Rapid and simple isolation procedure for lipoprotein lipase from
human milk.";
Biochim. Biophys. Acta 1044:20-25(1990).
[11]
HEPARIN-BINDING, CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=11342582; DOI=10.1172/JCI11774;
Lutz E.P., Merkel M., Kako Y., Melford K., Radner H., Breslow J.L.,
Bensadoun A., Goldberg I.J.;
"Heparin-binding defective lipoprotein lipase is unstable and causes
abnormalities in lipid delivery to tissues.";
J. Clin. Invest. 107:1183-1192(2001).
[12]
INTERACTION WITH GPIHBP1.
PubMed=17997385; DOI=10.1016/j.bbalip.2007.10.005;
Gin P., Beigneux A.P., Davies B., Young M.F., Ryan R.O., Bensadoun A.,
Fong L.G., Young S.G.;
"Normal binding of lipoprotein lipase, chylomicrons, and apo-AV to
GPIHBP1 containing a G56R amino acid substitution.";
Biochim. Biophys. Acta 1771:1464-1468(2007).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70.
TISSUE=Milk;
PubMed=18780401; DOI=10.1002/pmic.200701057;
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
"Identification of N-linked glycoproteins in human milk by hydrophilic
interaction liquid chromatography and mass spectrometry.";
Proteomics 8:3833-3847(2008).
[14]
3D-STRUCTURE MODELING.
PubMed=8308035;
van Tilbeurgh H., Roussel A., Lalouel J.-M., Cambillau C.;
"Lipoprotein lipase. Molecular model based on the pancreatic lipase X-
ray structure: consequences for heparin binding and catalysis.";
J. Biol. Chem. 269:4626-4633(1994).
[15]
INTERACTION WITH SEL1L AND LMF1.
PubMed=25066055; DOI=10.1016/j.cmet.2014.06.015;
Sha H., Sun S., Francisco A.B., Ehrhardt N., Xue Z., Liu L.,
Lawrence P., Mattijssen F., Guber R.D., Panhwar M.S., Brenna J.T.,
Shi H., Xue B., Kersten S., Bensadoun A., Peterfy M., Long Q., Qi L.;
"The ER-associated degradation adaptor protein Sel1L regulates LPL
secretion and lipid metabolism.";
Cell Metab. 20:458-470(2014).
[16]
REVIEW ON VARIANTS.
Hayden M.R., Ma Y., Brunzell J., Henderson H.E.;
"Genetic variants affecting human lipoprotein and hepatic lipases.";
Curr. Opin. Lipidol. 2:104-109(1991).
[17]
VARIANT LPL DEFICIENCY THR-271, AND INVOLVEMENT IN LPL.
PubMed=2121025;
Hata A., Emi M., Luc G., Basdevant A., Gambert P., Iverius P.-H.,
Lalouel J.-M.;
"Compound heterozygote for lipoprotein lipase deficiency: Ser-->Thr244
and transition in 3' splice site of intron 2 (AG-->AA) in the
lipoprotein lipase gene.";
Am. J. Hum. Genet. 47:721-726(1990).
[18]
VARIANT LPL DEFICIENCY GLU-215.
PubMed=1969408;
Emi M., Wilson D.E., Iverius P.H., Wiu L., Hata A., Hegele R.,
Williams R.R., Lalouel J.-M.;
"Missense mutation (Gly-->Glu188) of human lipoprotein lipase
imparting functional deficiency.";
J. Biol. Chem. 265:5910-5916(1990).
[19]
VARIANT LPL DEFICIENCY GLU-215.
PubMed=1975597; DOI=10.1172/JCI114769;
Monsalve M.V., Henderson H., Roederer G., Julien P., Deeb S.,
Kastelein J.J.P., Peritz L., Devlin R., Bruin T., Murthy M.R.V.,
Gagne C., Davignon J., Lupien P.J., Brunzell J.D., Hayden M.R.;
"A missense mutation at codon 188 of the human lipoprotein lipase gene
is a frequent cause of lipoprotein lipase deficiency in persons of
different ancestries.";
J. Clin. Invest. 86:728-734(1990).
[20]
VARIANT LPL DEFICIENCY THR-203.
PubMed=2110364; DOI=10.1073/pnas.87.9.3474;
Beg O.U., Meng M.S., Skarlatos S.I., Previato L., Brunzell J.D.,
Brewer H.B. Jr., Fojo S.S.;
"Lipoprotein lipase Bethesda: a single amino acid substitution (Ala-
176-->Thr) leads to abnormal heparin binding and loss of enzymic
activity.";
Proc. Natl. Acad. Sci. U.S.A. 87:3474-3478(1990).
[21]
VARIANTS LPL DEFICIENCY THR-221 AND HIS-270.
PubMed=1702428;
Dichek H.L., Fojo S.S., Beg O.U., Skarlatos S.I., Brunzell J.D.,
Cutler G.B. Jr., Brewer H.B. Jr.;
"Identification of two separate allelic mutations in the lipoprotein
lipase gene of a patient with the familial hyperchylomicronemia
syndrome.";
J. Biol. Chem. 266:473-477(1991).
[22]
VARIANT LPL DEFICIENCY GLY-183.
PubMed=1907278;
Faustinella F., Chang A., van Biervliet J.P., Rosseneu M.,
Vinaimont N., Smith L.C., Chen S.-H., Chan L.;
"Catalytic triad residue mutation (Asp156-->Gly) causing familial
lipoprotein lipase deficiency. Co-inheritance with a nonsense mutation
(Ser447-->Ter) in a Turkish family.";
J. Biol. Chem. 266:14418-14424(1991).
[23]
VARIANT LPL DEFICIENCY GLU-169.
PubMed=2010533; DOI=10.1172/JCI115114;
Ameis D., Kobayashi J., Davis R.C., Ben-Zeev O., Malloy M.J.,
Kane J.P., Lee G., Wong H., Havel R.J., Schotz M.C.;
"Familial chylomicronemia (type I hyperlipoproteinemia) due to a
single missense mutation in the lipoprotein lipase gene.";
J. Clin. Invest. 87:1165-1170(1991).
[24]
VARIANT LPL DEFICIENCY THR-221.
PubMed=1674945; DOI=10.1172/JCI115229;
Henderson H.E., Ma Y., Hassan F., Monsalve M.V., Marais A.D.,
Winkler F., Gubernator K., Peterson J., Brunzell J.D., Hayden M.R.;
"Amino acid substitution (Ile194-->Thr) in exon 5 of the lipoprotein
lipase gene causes lipoprotein lipase deficiency in three unrelated
probands. Support for a multicentric origin.";
J. Clin. Invest. 87:2005-2011(1991).
[25]
VARIANTS LPL DEFICIENCY GLU-231 AND HIS-270, AND CHARACTERIZATION OF
VARIANTS LPL DEFICIENCY GLU-231 AND HIS-270.
PubMed=1752947; DOI=10.1172/JCI115507;
Gotoda T., Yamada N., Kawamura M., Kozaki K., Mori N., Ishibashi S.,
Shimano H., Takaku F., Yazaki Y., Furuichi Y., Murase T.;
"Heterogeneous mutations in the human lipoprotein lipase gene in
patients with familial lipoprotein lipase deficiency.";
J. Clin. Invest. 88:1856-1864(1991).
[26]
VARIANT LPL DEFICIENCY LEU-234.
PubMed=2038366; DOI=10.1056/NEJM199106203242502;
Ma Y., Henderson H.E., Ven Murthy M.R., Roederer G., Monsalve M.V.,
Clarke L.A., Normand T., Julien P., Gagne C., Lambert M., Davignon J.,
Lupien P.J., Brunzell J., Hayden M.R.;
"A mutation in the human lipoprotein lipase gene as the most common
cause of familial chylomicronemia in French Canadians.";
N. Engl. J. Med. 324:1761-1766(1991).
[27]
VARIANT LPL DEFICIENCY ARG-113.
PubMed=1598907;
Ishimura-Oka K., Faustinella F., Kihara S., Smith L.C., Oka K.,
Chan L.;
"A missense mutation (Trp86-->Arg) in exon 3 of the lipoprotein lipase
gene: a cause of familial chylomicronemia.";
Am. J. Hum. Genet. 50:1275-1280(1992).
[28]
VARIANT LPL DEFICIENCY ARG-184.
PubMed=1521525; DOI=10.1111/j.1432-1033.1992.tb17182.x;
Bruin T., Kastelein J.J., van Diermen D.E., Ma Y., Henderson H.E.,
Stuyt P.M., Stalenhoef A.F.H., Sturk A., Brunzell J.D., Hayden M.R.;
"A missense mutation Pro157Arg in lipoprotein lipase (LPLNijmegen)
resulting in loss of catalytic activity.";
Eur. J. Biochem. 208:267-272(1992).
[29]
VARIANT LPL DEFICIENCY ASN-277.
PubMed=1639392; DOI=10.1016/0888-7543(92)90136-G;
Ma Y., Wilson B.I., Bijvoet S., Henderson H.E., Cramb E., Roederer G.,
Ven Murthy M.R., Julien P., Bakker H.D., Kastelein J.J.,
Brunzell J.D., Hayden M.R.;
"A missense mutation (Asp250-->Asn) in exon 6 of the human lipoprotein
lipase gene causes chylomicronemia in patients of different
ancestries.";
Genomics 13:649-653(1992).
[30]
VARIANTS LPL DEFICIENCY ASN-183; GLY-183 AND SER-243.
PubMed=1730727;
Ma Y.H., Bruin T., Tuzgol S., Wilson B.I., Roederer G., Liu M.S.,
Davignon J., Kastelein J.J., Brunzell J.D., Hayden M.R.;
"Two naturally occurring mutations at the first and second bases of
codon aspartic acid 156 in the proposed catalytic triad of human
lipoprotein lipase. In vivo evidence that aspartic acid 156 is
essential for catalysis.";
J. Biol. Chem. 267:1918-1923(1992).
[31]
CHARACTERIZATION OF VARIANTS LPL DEFICIENCY ASN-183 AND GLY-183, AND
MUTAGENESIS OF SER-159 AND HIS-268.
PubMed=1371284;
Emmerich J., Beg O.U., Peterson J., Previato L., Brunzell J.D.,
Brewer H.B. Jr., Santamarina-Fojo S.;
"Human lipoprotein lipase. Analysis of the catalytic triad by site-
directed mutagenesis of Ser-132, Asp-156, and His-241.";
J. Biol. Chem. 267:4161-4165(1992).
[32]
VARIANT LPL DEFICIENCY GLU-222.
PubMed=1400331;
Hata A., Ridinger D.N., Sutherland S.D., Emi M., Kwong L.K.,
Shuhua J., Lubbers A., Guy-Grand B., Basdevant A., Iverius P.H.,
Wilson D.E., Lalouel J.-M.;
"Missense mutations in exon 5 of the human lipoprotein lipase gene.
Inactivation correlates with loss of dimerization.";
J. Biol. Chem. 267:20132-20139(1992).
[33]
VARIANTS LPL DEFICIENCY GLU-215; HIS-270 AND ASN-277.
PubMed=1619366;
Ishimura-Oka K., Semenkovich C.F., Faustinella F., Goldberg I.J.,
Shachter N., Smith L.C., Coleman T., Hide W.A., Brown W.V., Oka K.;
"A missense (Asp250-->Asn) mutation in the lipoprotein lipase gene in
two unrelated families with familial lipoprotein lipase deficiency.";
J. Lipid Res. 33:745-754(1992).
[34]
VARIANTS LPL DEFICIENCY ARG-113; ARG-163; GLU-215; THR-221 AND
SER-232.
PubMed=1479292;
Reina M., Brunzell J.D., Deeb S.S.;
"Molecular basis of familial chylomicronemia: mutations in the
lipoprotein lipase and apolipoprotein C-II genes.";
J. Lipid Res. 33:1823-1832(1992).
[35]
VARIANT LPL DEFICIENCY THR-361.
PubMed=8096693; DOI=10.1006/bbrc.1993.1323;
Kobayashi J., Sasaki N., Tashiro J., Inadera H., Saito Y., Yoshida S.;
"A missense mutation (Ala334-->Thr) in exon 7 of the lipoprotein
lipase gene in a case with type I hyperlipidemia.";
Biochem. Biophys. Res. Commun. 191:1046-1054(1993).
[36]
VARIANT LPL DEFICIENCY GLU-207.
PubMed=8288243; DOI=10.1006/geno.1993.1481;
Haubenwallner S., Horl G., Shachter N.S., Presta E., Fried S.K.,
Hofler G., Kostner G.M., Breslow J.L., Zechner R.;
"A novel missense mutation in the gene for lipoprotein lipase
resulting in a highly conservative amino acid substitution
(Asp180-->Glu) causes familial chylomicronemia (type I
hyperlipoproteinemia).";
Genomics 18:392-396(1993).
[37]
VARIANT LPL DEFICIENCY CYS-199.
PubMed=8486765; DOI=10.1172/JCI116414;
Ma Y., Liu M.-S., Ginzinger D., Frohlich J., Brunzell J.D.,
Hayden M.R.;
"Gene-environment interaction in the conversion of a mild-to-severe
phenotype in a patient homozygous for a Ser172-->Cys mutation in the
lipoprotein lipase gene.";
J. Clin. Invest. 91:1953-1958(1993).
[38]
VARIANT LPL DEFICIENCY SER-102.
PubMed=8325986; DOI=10.1172/JCI116551;
Wilson D.E., Hata A., Kwong L.K., Lingam A., Shuhua J., Ridinger D.N.,
Yeager C., Kaltenborn K.C., Iverius P.-H., Lalouel J.-M.;
"Mutations in exon 3 of the lipoprotein lipase gene segregating in a
family with hypertriglyceridemia, pancreatitis, and non-insulin-
dependent diabetes.";
J. Clin. Invest. 92:203-211(1993).
[39]
VARIANT LPL DEFICIENCY SER-181.
PubMed=8301230;
Bruin T., Tuzgol S., van Diermen D.E., Hoogerbrugge-Van der Linden N.,
Brunzell J.D., Hayden M.R., Kastelein J.J.;
"Recurrent pancreatitis and chylomicronemia in an extended Dutch
kindred is caused by a Gly154-->Ser substitution in lipoprotein
lipase.";
J. Lipid Res. 34:2109-2119(1993).
[40]
VARIANT LPL DEFICIENCY VAL-392.
PubMed=8135797; DOI=10.1006/bbrc.1994.1266;
Chimienti G.P.G., Resta F., di Perma V., Tarricone C., Lovecchio M.,
Collacicco A.M., Capurso A.;
"A new Italian case of lipoprotein lipase deficiency: a Leu365-> Val
change resulting in loss of enzyme activity.";
Biochem. Biophys. Res. Commun. 199:570-576(1994).
[41]
VARIANT LPL DEFICIENCY SER-70, AND CHARACTERIZATION OF VARIANT LPL
DEFICIENCY SER-70.
PubMed=7999071; DOI=10.1006/bbrc.1994.2694;
Kobayashi J., Inadera H., Fujita Y., Talley G., Morisaki N.,
Yoshida S., Saito Y., Fojo S.S., Brewer H.B. Jr.;
"A naturally occurring mutation at the second base of codon asparagine
43 in the proposed N-linked glycosylation site of human lipoprotein
lipase: in vivo evidence that asparagine 43 is essential for catalysis
and secretion.";
Biochem. Biophys. Res. Commun. 205:506-515(1994).
[42]
VARIANTS LPL DEFICIENCY HIS-270 AND CYS-270.
PubMed=7906986; DOI=10.1002/humu.1380030109;
Ma Y., Liu M.-S., Chitayat D., Bruin T., Beisiegel U., Benlian P.,
Foubert L., De Gennes J.L., Funke H., Forsythe I., Blaichman S.,
Papanikolaou M., Erkelens D.W., Kastelein J., Brunzell J.D.,
Hayden M.R.;
"Recurrent missense mutations at the first and second base of codon
Arg243 in human lipoprotein lipase in patients of different
ancestries.";
Hum. Mutat. 3:52-58(1994).
[43]
VARIANTS LPL DEFICIENCY LEU-96 AND GLU-215, AND CHARACTERIZATION OF
VARIANT LPL DEFICIENCY LEU-96.
PubMed=7912254;
Bruin T., Tuzgoel S., Mulder W.J., van den Ende A.E., Jansen H.,
Hayden M.R., Kastelein J.J.P.;
"A compound heterozygote for lipoprotein lipase deficiency,
Val69-->Leu and Gly188-->Glu: correlation between in vitro LPL
activity and clinical expression.";
J. Lipid Res. 35:438-445(1994).
[44]
VARIANTS LPL DEFICIENCY CYS-199; ARG-279; THR-288 AND SER-318, AND
CHARACTERIZATION OF VARIANTS LPL DEFICIENCY ARG-279 AND THR-288.
PubMed=8077845;
Ma Y., Ooi T.C., Liu M.-S., Zhang H., McPherson R., Edwards A.L.,
Forsythe I.J., Frohlich J., Brunzell J.D., Hayden M.R.;
"High frequency of mutations in the human lipoprotein lipase gene in
pregnancy-induced chylomicronemia: possible association with
apolipoprotein E2 isoform.";
J. Lipid Res. 35:1066-1075(1994).
[45]
VARIANT LPL DEFICIENCY VAL-437.
PubMed=7806969;
Previato L., Guardamagna O., Dugi K.A., Ronan R., Talley G.D.,
Santamarina-Fojo S., Brewer H.B. Jr.;
"A novel missense mutation in the C-terminal domain of lipoprotein
lipase (Glu410-->Val) leads to enzyme inactivation and familial
chylomicronemia.";
J. Lipid Res. 35:1552-1560(1994).
[46]
VARIANT LPL DEFICIENCY SER-318.
PubMed=7647785; DOI=10.1038/ng0595-28;
Reymer P.W.A., Gagne E., Groenemeyer B.E., Zhang H., Forsyth I.,
Jansen H., Seidell J.C., Kromhout D., Lie K.E., Kastelein J.J.,
Hayden M.R.;
"A lipoprotein lipase mutation (Asn291Ser) is associated with reduced
HDL cholesterol levels in premature atherosclerosis.";
Nat. Genet. 10:28-34(1995).
[47]
VARIANT LPL DEFICIENCY TYR-445, AND CHARACTERIZATION OF VARIANT LPL
DEFICIENCY TYR-445.
PubMed=8858123; DOI=10.1006/bbrc.1996.1487;
Henderson H.E., Hassan F., Marais D., Hayden M.R.;
"A new mutation destroying disulphide bridging in the C-terminal
domain of lipoprotein lipase.";
Biochem. Biophys. Res. Commun. 227:189-194(1996).
[48]
VARIANT LPL DEFICIENCY SER-318, AND VARIANT ASN-36.
PubMed=8872057; DOI=10.1111/j.1365-2362.1996.tb02146.x;
de Bruin T.W.A., Mailly F., van Barlingen H.H.J.J., Fisher R.,
Castro Cabezas M., Talmud P., Dallinga-Thie G.M., Humphries S.E.;
"Lipoprotein lipase gene mutations D9N and N291S in four pedigrees
with familial combined hyperlipidaemia.";
Eur. J. Clin. Invest. 26:631-639(1996).
[49]
VARIANTS LPL DEFICIENCY ASN-277 AND LYS-437.
PubMed=8956048;
DOI=10.1002/(SICI)1098-1004(1996)8:4<381::AID-HUMU16>3.0.CO;2-Z;
Wiebusch H., Funke H., Bruin T., Bucher H., von Eckardstein A.,
Kastelein J.J.P., Assmann G.;
"Compound heterozygosity for a known (D250N) and a novel (E410K)
missense mutation in the C-terminal domain of lipoprotein lipase
causes familial chylomicronemia.";
Hum. Mutat. 8:381-383(1996).
[50]
VARIANTS LPL DEFICIENCY GLY-190 AND GLU-215.
PubMed=8956052;
DOI=10.1002/(SICI)1098-1004(1996)8:4<392::AID-HUMU20>3.0.CO;2-X;
Wiebusch H., Funke H., Santer R., Richter W., Assmann G.;
"A novel missense (E163G) mutation in the catalytic subunit of
lipoprotein lipase causes familial chylomicronemia.";
Hum. Mutat. 8:392-392(1996).
[51]
VARIANT LPL DEFICIENCY HIS-289, VARIANT ASN-36, CHARACTERIZATION OF
VARIANT LPL DEFICIENCY HIS-289, AND CHARACTERIZATION OF VARIANT
ASN-36.
PubMed=8728326;
Rouis M., Lohse P., Dugi K.A., Lohse P., Beg O.U., Ronan R.,
Talley G.D., Brunzell J.D., Santamarina-Fojo S.;
"Homozygosity for two point mutations in the lipoprotein lipase (LPL)
gene in a patient with familial LPL deficiency: LPL(Asp9-->Asn,
Tyr262-->His).";
J. Lipid Res. 37:651-661(1996).
[52]
VARIANTS LPL DEFICIENCY ALA-128; GLU-215; ARG-215; CYS-270; ASN-277
AND PRO-313.
PubMed=8778602; DOI=10.1056/NEJM199609193351203;
Benlian P., De Gennes J.L., Foubert L., Zhang H., Gagne S.E.,
Hayden M.;
"Premature atherosclerosis in patients with familial chylomicronemia
caused by mutations in the lipoprotein lipase gene.";
N. Engl. J. Med. 335:848-854(1996).
[53]
VARIANT LPL DEFICIENCY ARG-286.
PubMed=9298816;
DOI=10.1002/(SICI)1098-1004(1997)10:3<179::AID-HUMU1>3.3.CO;2-N;
Foubert L., Bruin T., de Gennes J.-L., Ehrenborg E., Furioli J.,
Kastelein J.J., Benlian P., Hayden M.R.;
"A single Ser259Arg mutation in the gene for lipoprotein lipase causes
chylomicronemia in Moroccans of Berber ancestry.";
Hum. Mutat. 10:179-185(1997).
[54]
VARIANTS.
PubMed=9401010;
DOI=10.1002/(SICI)1098-1004(1997)10:6<465::AID-HUMU8>3.3.CO;2-3;
Mailly F., Palmen J., Muller D.P.R., Gibbs T., Lloyd J., Brunzell J.,
Durrington P., Mitropoulos K., Betteridge J., Watts G., Lithell H.,
Angelico F., Humphries S.E., Talmud P.J.;
"Familial lipoprotein lipase (LPL) deficiency: a catalogue of LPL gene
mutations identified in 20 patients from the UK, Sweden, and Italy.";
Hum. Mutat. 10:465-473(1997).
[55]
VARIANTS LPL DEFICIENCY ALA-128; HIS-183; GLU-215; ARG-215; LEU-234;
CYS-270 AND ASN-277.
PubMed=9279761; DOI=10.1136/jmg.34.8.672;
Foubert L., De Gennes J.L., Lagarde J.P., Ehrenborg E., Raisonnier A.,
Girardet J.P., Hayden M.R., Benlian P.;
"Assessment of French patients with LPL deficiency for French Canadian
mutations.";
J. Med. Genet. 34:672-675(1997).
[56]
VARIANTS LPL DEFICIENCY THR-252 AND HIS-270.
PubMed=9714430;
DOI=10.1002/(SICI)1096-8628(19980724)78:4<313::AID-AJMG1>3.0.CO;2-M;
Henderson H.E., Bijvoet S.M., Mannens M.A.M.M., Bruin T.,
Erkelens D.W., Hayden M.R., Kastelein J.J.P.;
"Ile225Thr loop mutation in the lipoprotein lipase (LPL) gene is a de
novo event.";
Am. J. Med. Genet. 78:313-316(1998).
[57]
VARIANT LPL DEFICIENCY LYS-448, AND CHARACTERIZATION OF VARIANT LPL
DEFICIENCY LYS-448.
PubMed=9498099; DOI=10.1016/S0009-8981(97)00144-7;
Henderson H., Leisegang F., Hassan F., Hayden M., Marais D.;
"A novel Glu421Lys substitution in the lipoprotein lipase gene in
pregnancy-induced hypertriglyceridemic pancreatitis.";
Clin. Chim. Acta 269:1-12(1998).
[58]
VARIANTS LPL DEFICIENCY GLU-215 AND GLY-286.
PubMed=10660334;
Evans D., Wendt D., Ahle S., Guerra A., Beisiegel U.;
"Compound heterozygosity for a new (S259G) and a previously described
(G188E) mutation in lipoprotein lipase (LPL) as a cause of
chylomicronemia.";
Hum. Mutat. 12:217-217(1998).
[59]
VARIANTS LPL DEFICIENCY THR-288 AND SER-318, AND VARIANT ASN-36.
PubMed=9719626; DOI=10.1006/mgme.1998.2712;
Zhang Q., Liu Y., Liu B.W., Fan P., Cavanna J., Galton D.J.;
"Common genetic variants of lipoprotein lipase and apolipoproteins AI-
CIII that relate to coronary artery disease: a study in Chinese and
European subjects.";
Mol. Genet. Metab. 64:177-183(1998).
[60]
VARIANT LPL DEFICIENCY SER-318, AND VARIANTS MET-370 AND ALA-379.
PubMed=9662394; DOI=10.1038/907;
Nickerson D.A., Taylor S.L., Weiss K.M., Clark A.G., Hutchinson R.G.,
Stengaerd J., Salomaa V., Vartiainen E., Boerwinkle E., Sing C.F.;
"DNA sequence diversity in a 9.7-kb region of the human lipoprotein
lipase gene.";
Nat. Genet. 19:233-240(1998).
[61]
VARIANT THR-427.
PubMed=10391209; DOI=10.1038/10290;
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[62]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
Nat. Genet. 23:373-373(1999).
[63]
VARIANT LPL DEFICIENCY LEU-297, AND CHARACTERIZATION OF VARIANT LPL
DEFICIENCY LEU-297.
PubMed=11068186; DOI=10.1016/S0925-4439(00)00067-3;
Takagi A., Ikeda Y., Takeda E., Yamamoto A.;
"A newly identified lipoprotein lipase (LPL) gene mutation (F270L) in
a Japanese patient with familial LPL deficiency.";
Biochim. Biophys. Acta 1502:433-446(2000).
[64]
VARIANTS LPL DEFICIENCY ARG-132 AND GLU-231, AND CHARACTERIZATION OF
VARIANTS LPL DEFICIENCY ARG-132 AND GLU-231.
PubMed=11099402; DOI=10.1042/cs0990569;
Ikeda Y., Goji K., Takagi A.;
"A compound heterozygote for a novel missense mutation (G105R) in exon
3 and a missense mutation (D204E) in exon 5 of the lipoprotein lipase
gene in a Japanese infant with hyperchylomicronaemia.";
Clin. Sci. 99:569-578(2000).
[65]
VARIANT LPL DEFICIENCY TRP-266.
PubMed=11134145; DOI=10.1210/jcem.85.12.7069;
Hoffmann M.M., Jacob S., Luft D., Schmuelling R.-M., Rett K.,
Maerz W., Haering H.-U., Matthaei S.;
"Type I hyperlipoproteinemia due to a novel loss of function mutation
of lipoprotein lipase, Cys(239)-->Trp, associated with recurrent
severe pancreatitis.";
J. Clin. Endocrinol. Metab. 85:4795-4798(2000).
[66]
VARIANT LPL DEFICIENCY ASP-210, AND CHARACTERIZATION OF VARIANT LPL
DEFICIENCY ASP-210.
PubMed=10787434;
Hoelzl B., Kraft H.G., Wiebusch H., Sandhofer A., Patsch J.,
Sandhofer F., Paulweber B.;
"Two novel mutations in the lipoprotein lipase gene in a family with
marked hypertriglyceridemia in heterozygous carriers. Potential
interaction with the polymorphic marker D1S104 on chromosome 1q21-
q23.";
J. Lipid Res. 41:734-741(2000).
[67]
VARIANT LPL DEFICIENCY VAL-181, AND CHARACTERIZATION OF VARIANT LPL
DEFICIENCY VAL-181.
PubMed=11441134;
Ikeda Y., Takagi A., Nakata Y., Sera Y., Hyoudou S., Hamamoto K.,
Nishi Y., Yamamoto A.;
"Novel compound heterozygous mutations for lipoprotein lipase
deficiency. A G-to-T transversion at the first position of exon 5
causing G154V missense mutation and a 5' splice site mutation of
intron 8.";
J. Lipid Res. 42:1072-1081(2001).
[68]
VARIANTS LPL DEFICIENCY THR-98; ILE-208; VAL-279; ARG-279; TYR-310;
ARG-325 AND PHE-365, AND CHARACTERIZATION OF VARIANTS LPL DEFICIENCY
THR-98; ILE-208; VAL-279; ARG-279; TYR-310; ARG-325 AND PHE-365.
PubMed=12204001; DOI=10.1002/humu.9054;
Chan L.Y.S., Lam C.-W., Mak Y.-T., Tomlinson B., Tsang M.-W., Baum L.,
Masarei J.R.L., Pang C.-P.;
"Genotype-phenotype studies of six novel LPL mutations in Chinese
patients with hypertriglyceridemia.";
Hum. Mutat. 20:232-233(2002).
[69]
VARIANT LPL DEFICIENCY PHE-303, AND CHARACTERIZATION OF VARIANT LPL
DEFICIENCY PHE-303.
PubMed=12641539; DOI=10.1046/j.1365-2362.2003.01129.x;
Saika Y., Sakai N., Takahashi M., Maruyama T., Kihara S., Ouchi N.,
Ishigami M., Hiraoka H., Nakamura T., Yamashita S., Matsuzawa Y.;
"Novel LPL mutation (L303F) found in a patient associated with
coronary artery disease and severe systemic atherosclerosis.";
Eur. J. Clin. Invest. 33:216-222(2003).
[70]
VARIANT LPL DEFICIENCY SER-318, AND VARIANT ASN-36.
PubMed=12966036; DOI=10.1093/hmg/ddg314;
Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S.,
Alvin G.B., Das K., Gilliam T.C.;
"Association of extreme blood lipid profile phenotypic variation with
11 reverse cholesterol transport genes and 10 non-genetic
cardiovascular disease risk factors.";
Hum. Mol. Genet. 12:2733-2743(2003).
[71]
VARIANT LPL DEFICIENCY VAL-201.
PubMed=14984478; DOI=10.1111/j.0009-9163.2004.00205.x;
Abifadel M., Jambart S., Allard D., Rabes J.-P., Varret M., Derre A.,
Chouery E., Salem N., Junien C., Aydenian H., Boileau C.;
"Identification of the first Lebanese mutation in the LPL gene and
description of a rapid detection method.";
Clin. Genet. 65:158-161(2004).
[72]
VARIANTS LPL DEFICIENCY GLU-215 AND ARG-328.
PubMed=15185149; DOI=10.1007/s00431-004-1474-1;
Kavazarakis E., Stabouli S., Gourgiotis D., Roumeliotou K.,
Traeger-Synodinos J., Bossios A., Fretzayas A., Kanavakis E.;
"Severe hypertriglyceridaemia in a Greek infant: a clinical,
biochemical and genetic study.";
Eur. J. Pediatr. 163:462-466(2004).
[73]
VARIANTS LPL DEFICIENCY SER-70; ARG-132; VAL-181; GLU-215; THR-221;
ARG-225; ALA-227; GLU-231; CYS-270; HIS-270; THR-288; LEU-297;
ARG-305; PHE-330 AND THR-361.
PubMed=15256764; DOI=10.5551/jat.11.131;
The research committee on primary hyperlipidemia of the ministry of health and welfare of Japan;
Maruyama T., Yamashita S., Matsuzawa Y., Bujo H., Takahashi K.,
Saito Y., Ishibashi S., Ohashi K., Shionoiri F., Gotoda T., Yamada N.,
Kita T.;
"Mutations in Japanese subjects with primary hyperlipidemia -- results
from the Research Committee of the Ministry of Health and Welfare of
Japan since 1996.";
J. Atheroscler. Thromb. 11:131-145(2004).
[74]
VARIANTS LPL DEFICIENCY GLU-186; GLU-215 AND THR-221.
PubMed=15877202; DOI=10.1007/s10545-005-7060-5;
Santer R., Gokcay G., Demirkol M., Gal A., Lukacs Z.;
"Hyperchylomicronaemia due to lipoprotein lipase deficiency as a cause
of false-positive newborn screening for biotinidase deficiency.";
J. Inherit. Metab. Dis. 28:137-140(2005).
[75]
VARIANT LPL DEFICIENCY ARG-404, CHARACTERIZATION OF VARIANT LPL
DEFICIENCY ARG-404, FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR
LOCATION.
PubMed=27578112; DOI=10.1016/j.jacl.2016.02.015;
Pingitore P., Lepore S.M., Pirazzi C., Mancina R.M., Motta B.M.,
Valenti L., Berge K.E., Retterstoel K., Leren T.P., Wiklund O.,
Romeo S.;
"Identification and characterization of two novel mutations in the LPL
gene causing type I hyperlipoproteinemia.";
J. Clin. Lipidol. 10:816-823(2016).
-!- FUNCTION: The primary function of this lipase is the hydrolysis of
triglycerides of circulating chylomicrons and very low density
lipoproteins (VLDL) (PubMed:27578112). Binding to heparin sulfate
proteogylcans at the cell surface is vital to the function. The
apolipoprotein, APOC2, acts as a coactivator of LPL activity in
the presence of lipids on the luminal surface of vascular
endothelium (By similarity). {ECO:0000250,
ECO:0000269|PubMed:11342582, ECO:0000269|PubMed:27578112}.
-!- CATALYTIC ACTIVITY: Triacylglycerol + H(2)O = diacylglycerol + a
carboxylate. {ECO:0000269|PubMed:11342582,
ECO:0000269|PubMed:27578112}.
-!- SUBUNIT: Homodimer (By similarity). Interacts with APOC2; the
interaction activates LPL activity in the presence of lipids (By
similarity). Interacts with GPIHBP1 (PubMed:17997385). Interacts
with SEL1L and LMF1 (PubMed:25066055).
{ECO:0000250|UniProtKB:P11151, ECO:0000250|UniProtKB:P11152,
ECO:0000269|PubMed:17997385, ECO:0000269|PubMed:25066055}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor,
GPI-anchor {ECO:0000250}. Secreted {ECO:0000269|PubMed:2340307,
ECO:0000269|PubMed:27578112}. Note=Locates to the plasma membrane
of microvilli of hepatocytes with triacyl-glycerol-rich
lipoproteins (TRL). Some of the bound LPL is then internalized and
located inside non-coated endocytic vesicles (By similarity).
{ECO:0000250}.
-!- PTM: Tyrosine nitration after lipopolysaccharide (LPS) challenge
down-regulates the lipase activity.
{ECO:0000250|UniProtKB:Q06000}.
-!- DISEASE: Lipoprotein lipase deficiency (LPL deficiency)
[MIM:238600]: Recessive disorder usually manifesting in childhood.
On a normal diet, patients often present with abdominal pain,
hepatosplenomegaly, lipemia retinalis, eruptive xanthomata, and
massive hypertriglyceridemia, sometimes complicated with acute
pancreatitis. {ECO:0000269|PubMed:10660334,
ECO:0000269|PubMed:10787434, ECO:0000269|PubMed:11068186,
ECO:0000269|PubMed:11099402, ECO:0000269|PubMed:11134145,
ECO:0000269|PubMed:11441134, ECO:0000269|PubMed:12204001,
ECO:0000269|PubMed:12641539, ECO:0000269|PubMed:12966036,
ECO:0000269|PubMed:1400331, ECO:0000269|PubMed:1479292,
ECO:0000269|PubMed:14984478, ECO:0000269|PubMed:15185149,
ECO:0000269|PubMed:1521525, ECO:0000269|PubMed:15256764,
ECO:0000269|PubMed:15877202, ECO:0000269|PubMed:1598907,
ECO:0000269|PubMed:1619366, ECO:0000269|PubMed:1639392,
ECO:0000269|PubMed:1674945, ECO:0000269|PubMed:1702428,
ECO:0000269|PubMed:1730727, ECO:0000269|PubMed:1752947,
ECO:0000269|PubMed:1907278, ECO:0000269|PubMed:1969408,
ECO:0000269|PubMed:1975597, ECO:0000269|PubMed:2010533,
ECO:0000269|PubMed:2038366, ECO:0000269|PubMed:2110364,
ECO:0000269|PubMed:2121025, ECO:0000269|PubMed:27578112,
ECO:0000269|PubMed:7647785, ECO:0000269|PubMed:7806969,
ECO:0000269|PubMed:7906986, ECO:0000269|PubMed:7912254,
ECO:0000269|PubMed:7999071, ECO:0000269|PubMed:8077845,
ECO:0000269|PubMed:8096693, ECO:0000269|PubMed:8135797,
ECO:0000269|PubMed:8288243, ECO:0000269|PubMed:8301230,
ECO:0000269|PubMed:8325986, ECO:0000269|PubMed:8486765,
ECO:0000269|PubMed:8728326, ECO:0000269|PubMed:8778602,
ECO:0000269|PubMed:8858123, ECO:0000269|PubMed:8872057,
ECO:0000269|PubMed:8956048, ECO:0000269|PubMed:8956052,
ECO:0000269|PubMed:9279761, ECO:0000269|PubMed:9298816,
ECO:0000269|PubMed:9498099, ECO:0000269|PubMed:9662394,
ECO:0000269|PubMed:9714430, ECO:0000269|PubMed:9719626}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=LPL";
-!- WEB RESOURCE: Name=Wikipedia; Note=Lipoprotein lipase entry;
URL="https://en.wikipedia.org/wiki/Lipoprotein_lipase";
-----------------------------------------------------------------------
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EMBL; M15856; AAB59536.1; -; mRNA.
EMBL; X14390; CAA32564.1; -; mRNA.
EMBL; X54516; CAA38372.1; -; mRNA.
EMBL; M76722; AAA59528.1; -; Genomic_DNA.
EMBL; S76076; AAB21000.1; -; Genomic_DNA.
EMBL; S76077; AAB20999.1; -; Genomic_DNA.
EMBL; BT006726; AAP35372.1; -; mRNA.
EMBL; AK312311; BAG35236.1; -; mRNA.
EMBL; CH471080; EAW63764.1; -; Genomic_DNA.
EMBL; BC011353; AAH11353.1; -; mRNA.
EMBL; X68111; CAA48230.1; -; Genomic_DNA.
CCDS; CCDS6012.1; -.
PIR; A26082; LIHUL.
RefSeq; NP_000228.1; NM_000237.2.
UniGene; Hs.180878; -.
ProteinModelPortal; P06858; -.
BioGrid; 110205; 19.
IntAct; P06858; 15.
MINT; P06858; -.
STRING; 9606.ENSP00000309757; -.
BindingDB; P06858; -.
ChEMBL; CHEMBL2060; -.
DrugBank; DB09278; Activated charcoal.
DrugBank; DB06439; Tyloxapol.
SwissLipids; SLP:000000568; -.
ESTHER; human-LPL; Lipoprotein_Lipase.
iPTMnet; P06858; -.
PhosphoSitePlus; P06858; -.
BioMuta; LPL; -.
DMDM; 126314; -.
EPD; P06858; -.
MaxQB; P06858; -.
PaxDb; P06858; -.
PeptideAtlas; P06858; -.
PRIDE; P06858; -.
DNASU; 4023; -.
Ensembl; ENST00000311322; ENSP00000309757; ENSG00000175445.
GeneID; 4023; -.
KEGG; hsa:4023; -.
UCSC; uc003wzk.5; human.
CTD; 4023; -.
DisGeNET; 4023; -.
EuPathDB; HostDB:ENSG00000175445.14; -.
GeneCards; LPL; -.
GeneReviews; LPL; -.
HGNC; HGNC:6677; LPL.
HPA; HPA048749; -.
MalaCards; LPL; -.
MIM; 238600; phenotype.
MIM; 609708; gene.
neXtProt; NX_P06858; -.
OpenTargets; ENSG00000175445; -.
Orphanet; 309015; Familial lipoprotein lipase deficiency.
Orphanet; 70470; Hyperlipoproteinemia type 5.
PharmGKB; PA232; -.
eggNOG; ENOG410IJUA; Eukaryota.
eggNOG; ENOG4111GMM; LUCA.
GeneTree; ENSGT00760000119069; -.
HOGENOM; HOG000038553; -.
HOVERGEN; HBG002259; -.
InParanoid; P06858; -.
KO; K01059; -.
OMA; HYQVKIH; -.
OrthoDB; EOG091G052B; -.
PhylomeDB; P06858; -.
TreeFam; TF324997; -.
BRENDA; 3.1.1.34; 2681.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-HSA-8963889; Assembly of active LPL and LIPC lipase complexes.
Reactome; R-HSA-8963901; Chylomicron remodeling.
Reactome; R-HSA-975634; Retinoid metabolism and transport.
SIGNOR; P06858; -.
GeneWiki; Lipoprotein_lipase; -.
GenomeRNAi; 4023; -.
PRO; PR:P06858; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000175445; -.
CleanEx; HS_LPL; -.
ExpressionAtlas; P06858; baseline and differential.
Genevisible; P06858; HS.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
GO; GO:0034185; F:apolipoprotein binding; IPI:BHF-UCL.
GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
GO; GO:0004465; F:lipoprotein lipase activity; IDA:UniProtKB.
GO; GO:0004620; F:phospholipase activity; ISS:BHF-UCL.
GO; GO:0005102; F:receptor binding; IPI:BHF-UCL.
GO; GO:0017129; F:triglyceride binding; IEA:Ensembl.
GO; GO:0004806; F:triglyceride lipase activity; IDA:BHF-UCL.
GO; GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL.
GO; GO:0034371; P:chylomicron remodeling; TAS:Reactome.
GO; GO:0006633; P:fatty acid biosynthetic process; IDA:BHF-UCL.
GO; GO:0055096; P:low-density lipoprotein particle mediated signaling; IMP:BHF-UCL.
GO; GO:0006644; P:phospholipid metabolic process; ISS:BHF-UCL.
GO; GO:0090197; P:positive regulation of chemokine secretion; IMP:BHF-UCL.
GO; GO:0010886; P:positive regulation of cholesterol storage; IMP:BHF-UCL.
GO; GO:0050729; P:positive regulation of inflammatory response; IC:BHF-UCL.
GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IC:BHF-UCL.
GO; GO:0010890; P:positive regulation of sequestering of triglyceride; IMP:BHF-UCL.
GO; GO:0051004; P:regulation of lipoprotein lipase activity; TAS:Reactome.
GO; GO:0009409; P:response to cold; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0009749; P:response to glucose; ISS:AgBase.
GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
GO; GO:0019432; P:triglyceride biosynthetic process; IDA:UniProtKB.
GO; GO:0019433; P:triglyceride catabolic process; IDA:UniProtKB.
GO; GO:0070328; P:triglyceride homeostasis; IGI:BHF-UCL.
GO; GO:0006641; P:triglyceride metabolic process; ISS:BHF-UCL.
GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IDA:BHF-UCL.
CDD; cd00707; Pancreat_lipase_like; 1.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR013818; Lipase/vitellogenin.
InterPro; IPR016272; Lipase_LIPH.
InterPro; IPR033906; Lipase_N.
InterPro; IPR002330; Lipo_Lipase.
InterPro; IPR001024; PLAT/LH2_dom.
InterPro; IPR036392; PLAT/LH2_dom_sf.
InterPro; IPR000734; TAG_lipase.
PANTHER; PTHR11610; PTHR11610; 1.
PANTHER; PTHR11610:SF3; PTHR11610:SF3; 1.
Pfam; PF00151; Lipase; 1.
Pfam; PF01477; PLAT; 1.
PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
PRINTS; PR00822; LIPOLIPASE.
PRINTS; PR00821; TAGLIPASE.
SMART; SM00308; LH2; 1.
SUPFAM; SSF49723; SSF49723; 1.
SUPFAM; SSF53474; SSF53474; 1.
TIGRFAMs; TIGR03230; lipo_lipase; 1.
PROSITE; PS00120; LIPASE_SER; 1.
PROSITE; PS50095; PLAT; 1.
1: Evidence at protein level;
Cell membrane; Chylomicron; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; GPI-anchor; Heparin-binding; Hydrolase; Hyperlipidemia;
Lipid degradation; Lipid metabolism; Lipoprotein; Membrane; Nitration;
Polymorphism; Reference proteome; Secreted; Signal; VLDL.
SIGNAL 1 27 {ECO:0000269|PubMed:2340307}.
CHAIN 28 475 Lipoprotein lipase.
/FTId=PRO_0000017775.
DOMAIN 341 464 PLAT. {ECO:0000255|PROSITE-
ProRule:PRU00152}.
REGION 346 441 Heparin-binding. {ECO:0000250}.
ACT_SITE 159 159 Nucleophile.
ACT_SITE 183 183 Charge relay system.
ACT_SITE 268 268 Charge relay system.
MOD_RES 121 121 Nitrated tyrosine.
{ECO:0000250|UniProtKB:Q06000}.
MOD_RES 191 191 Nitrated tyrosine.
{ECO:0000250|UniProtKB:Q06000}.
MOD_RES 343 343 Nitrated tyrosine.
{ECO:0000250|UniProtKB:Q06000}.
CARBOHYD 70 70 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18780401}.
CARBOHYD 386 386 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 54 67 {ECO:0000255|PROSITE-ProRule:PRU00152}.
DISULFID 243 266 {ECO:0000255|PROSITE-ProRule:PRU00152}.
DISULFID 291 310 {ECO:0000255|PROSITE-ProRule:PRU00152}.
DISULFID 302 305 {ECO:0000255|PROSITE-ProRule:PRU00152}.
DISULFID 445 465 {ECO:0000255|PROSITE-ProRule:PRU00152}.
VARIANT 36 36 D -> N (in LPL deficiency; has
approximately 80% of the specific
activity of wild-type enzyme;
dbSNP:rs1801177).
{ECO:0000269|PubMed:12966036,
ECO:0000269|PubMed:8728326,
ECO:0000269|PubMed:8872057,
ECO:0000269|PubMed:9719626}.
/FTId=VAR_011948.
VARIANT 70 70 N -> S (in LPL deficiency; produces an
inactive protein which is not secreted
into the media).
{ECO:0000269|PubMed:15256764,
ECO:0000269|PubMed:7999071}.
/FTId=VAR_057914.
VARIANT 71 71 H -> Q (in dbSNP:rs11542065).
/FTId=VAR_049819.
VARIANT 96 96 V -> L (in LPL deficiency; gives rise to
a 80% decrease in specific catalytic
activity; dbSNP:rs373088068).
{ECO:0000269|PubMed:7912254}.
/FTId=VAR_057915.
VARIANT 98 98 A -> T (in LPL deficiency; decreases the
specific activity of the enzyme; reduces
the secretion of the mutant protein
significantly; the total LPL mass is
reduced compared to that of the wild-type
construct; dbSNP:rs145657341).
{ECO:0000269|PubMed:12204001}.
/FTId=VAR_057916.
VARIANT 102 102 R -> S (in LPL deficiency;
dbSNP:rs118204073).
{ECO:0000269|PubMed:8325986}.
/FTId=VAR_004211.
VARIANT 113 113 W -> G (in LPL deficiency).
/FTId=VAR_004212.
VARIANT 113 113 W -> R (in LPL deficiency;
dbSNP:rs118204069).
{ECO:0000269|PubMed:1479292,
ECO:0000269|PubMed:1598907}.
/FTId=VAR_004213.
VARIANT 128 128 T -> A (in LPL deficiency).
{ECO:0000269|PubMed:8778602,
ECO:0000269|PubMed:9279761}.
/FTId=VAR_057917.
VARIANT 132 132 G -> R (in LPL deficiency; synthesized as
a catalytically inactive form).
{ECO:0000269|PubMed:11099402,
ECO:0000269|PubMed:15256764}.
/FTId=VAR_057918.
VARIANT 163 163 H -> R (in LPL deficiency).
{ECO:0000269|PubMed:1479292}.
/FTId=VAR_004214.
VARIANT 169 169 G -> E (in LPL deficiency; loss of
activity; dbSNP:rs118204063).
{ECO:0000269|PubMed:2010533}.
/FTId=VAR_004215.
VARIANT 181 181 G -> S (in LPL deficiency).
{ECO:0000269|PubMed:8301230}.
/FTId=VAR_004216.
VARIANT 181 181 G -> V (in LPL deficiency; synthesized as
a catalytically inactive form).
{ECO:0000269|PubMed:11441134,
ECO:0000269|PubMed:15256764}.
/FTId=VAR_057919.
VARIANT 183 183 D -> G (in LPL deficiency; lacks both
triolein and tributyrin esterase
activities; dbSNP:rs118204064).
{ECO:0000269|PubMed:1371284,
ECO:0000269|PubMed:1730727,
ECO:0000269|PubMed:1907278}.
/FTId=VAR_004217.
VARIANT 183 183 D -> H (in LPL deficiency;
dbSNP:rs781614031).
{ECO:0000269|PubMed:9279761}.
/FTId=VAR_057920.
VARIANT 183 183 D -> N (in LPL deficiency; lacks both
triolein and tributyrin esterase
activities). {ECO:0000269|PubMed:1371284,
ECO:0000269|PubMed:1730727}.
/FTId=VAR_004218.
VARIANT 184 184 P -> R (in LPL deficiency; Nijmegen; loss
of activity).
{ECO:0000269|PubMed:1521525}.
/FTId=VAR_004219.
VARIANT 185 185 A -> T (in LPL deficiency; 3.2% of
activity; dbSNP:rs748349562).
/FTId=VAR_004220.
VARIANT 186 186 G -> E (in LPL deficiency).
{ECO:0000269|PubMed:15877202}.
/FTId=VAR_057921.
VARIANT 190 190 E -> G (in LPL deficiency).
{ECO:0000269|PubMed:8956052}.
/FTId=VAR_057922.
VARIANT 199 199 S -> C (in LPL deficiency; mild
hypertriglyceridemia; partial activity;
dbSNP:rs118204072).
{ECO:0000269|PubMed:8077845,
ECO:0000269|PubMed:8486765}.
/FTId=VAR_004221.
VARIANT 201 201 D -> V (in LPL deficiency).
{ECO:0000269|PubMed:14984478}.
/FTId=VAR_057923.
VARIANT 203 203 A -> T (in LPL deficiency; Bethesda; loss
of activity and abnormal heparin binding;
dbSNP:rs118204056).
{ECO:0000269|PubMed:2110364}.
/FTId=VAR_004222.
VARIANT 207 207 D -> E (in LPL deficiency;
dbSNP:rs118204076).
{ECO:0000269|PubMed:8288243}.
/FTId=VAR_004223.
VARIANT 208 208 V -> I (in LPL deficiency; decreases the
specific activity of the enzyme; has a
mild effect on the secretion of the
mutant enzyme; the total LPL mass is
reduced compared to that of the wild-type
construct; dbSNP:rs568397156).
{ECO:0000269|PubMed:12204001}.
/FTId=VAR_057924.
VARIANT 210 210 H -> D (in LPL deficiency; complete loss
of enzyme activity).
{ECO:0000269|PubMed:10787434}.
/FTId=VAR_057925.
VARIANT 210 210 H -> Q (in LPL deficiency; loss of
activity).
/FTId=VAR_004224.
VARIANT 215 215 G -> E (in LPL deficiency; loss of
activity; dbSNP:rs118204057).
{ECO:0000269|PubMed:10660334,
ECO:0000269|PubMed:1479292,
ECO:0000269|PubMed:15185149,
ECO:0000269|PubMed:15256764,
ECO:0000269|PubMed:15877202,
ECO:0000269|PubMed:1619366,
ECO:0000269|PubMed:1969408,
ECO:0000269|PubMed:1975597,
ECO:0000269|PubMed:7912254,
ECO:0000269|PubMed:8778602,
ECO:0000269|PubMed:8956052,
ECO:0000269|PubMed:9279761}.
/FTId=VAR_004225.
VARIANT 215 215 G -> R (in LPL deficiency).
{ECO:0000269|PubMed:8778602,
ECO:0000269|PubMed:9279761}.
/FTId=VAR_057926.
VARIANT 220 220 S -> R (in LPL deficiency; 2.0% of
activity; dbSNP:rs757546424).
/FTId=VAR_004226.
VARIANT 221 221 I -> T (in LPL deficiency; loss of
activity; dbSNP:rs118204061).
{ECO:0000269|PubMed:1479292,
ECO:0000269|PubMed:15256764,
ECO:0000269|PubMed:15877202,
ECO:0000269|PubMed:1674945,
ECO:0000269|PubMed:1702428}.
/FTId=VAR_004227.
VARIANT 222 222 G -> E (in LPL deficiency;
dbSNP:rs118204075).
{ECO:0000269|PubMed:1400331}.
/FTId=VAR_004228.
VARIANT 225 225 K -> R (in LPL deficiency).
{ECO:0000269|PubMed:15256764}.
/FTId=VAR_057927.
VARIANT 227 227 V -> A (in LPL deficiency;
dbSNP:rs528243561).
{ECO:0000269|PubMed:15256764}.
/FTId=VAR_057928.
VARIANT 231 231 D -> E (in LPL deficiency; loss of
activity; dbSNP:rs118204067).
{ECO:0000269|PubMed:11099402,
ECO:0000269|PubMed:15256764,
ECO:0000269|PubMed:1752947}.
/FTId=VAR_004229.
VARIANT 232 232 I -> S (in LPL deficiency;
dbSNP:rs770601263).
{ECO:0000269|PubMed:1479292}.
/FTId=VAR_004230.
VARIANT 234 234 P -> L (in LPL deficiency; loss of
activity; dbSNP:rs118204060).
{ECO:0000269|PubMed:2038366,
ECO:0000269|PubMed:9279761}.
/FTId=VAR_004231.
VARIANT 243 243 C -> S (in LPL deficiency; loss of
activity). {ECO:0000269|PubMed:1730727}.
/FTId=VAR_004232.
VARIANT 252 252 I -> T (in LPL deficiency;
dbSNP:rs118204080).
{ECO:0000269|PubMed:9714430}.
/FTId=VAR_057929.
VARIANT 266 266 C -> W (in LPL deficiency;
dbSNP:rs118204082).
{ECO:0000269|PubMed:11134145}.
/FTId=VAR_057930.
VARIANT 270 270 R -> C (in LPL deficiency;
dbSNP:rs118204077).
{ECO:0000269|PubMed:15256764,
ECO:0000269|PubMed:7906986,
ECO:0000269|PubMed:8778602,
ECO:0000269|PubMed:9279761}.
/FTId=VAR_057931.
VARIANT 270 270 R -> H (in LPL deficiency; loss of
activity; dbSNP:rs118204062).
{ECO:0000269|PubMed:15256764,
ECO:0000269|PubMed:1619366,
ECO:0000269|PubMed:1702428,
ECO:0000269|PubMed:1752947,
ECO:0000269|PubMed:7906986,
ECO:0000269|PubMed:9714430}.
/FTId=VAR_004233.
VARIANT 271 271 S -> T (in LPL deficiency;
dbSNP:rs118204059).
{ECO:0000269|PubMed:2121025}.
/FTId=VAR_004234.
VARIANT 277 277 D -> N (in LPL deficiency; 5% of full
activity; dbSNP:rs118204068).
{ECO:0000269|PubMed:1619366,
ECO:0000269|PubMed:1639392,
ECO:0000269|PubMed:8778602,
ECO:0000269|PubMed:8956048,
ECO:0000269|PubMed:9279761}.
/FTId=VAR_004235.
VARIANT 278 278 S -> C (in LPL deficiency).
/FTId=VAR_004236.
VARIANT 279 279 L -> R (in LPL deficiency; decreases the
specific activity of the enzyme; the
total LPL mass is reduced compared to
that of the wild-type construct;
dbSNP:rs35414700).
{ECO:0000269|PubMed:12204001,
ECO:0000269|PubMed:8077845}.
/FTId=VAR_057932.
VARIANT 279 279 L -> V (in LPL deficiency; decreases the
specific activity of the enzyme; the
total LPL mass is reduced compared to
that of the wild-type construct;
dbSNP:rs371282890).
{ECO:0000269|PubMed:12204001}.
/FTId=VAR_057933.
VARIANT 286 286 S -> G (in LPL deficiency).
{ECO:0000269|PubMed:10660334}.
/FTId=VAR_004237.
VARIANT 286 286 S -> R (in LPL deficiency).
{ECO:0000269|PubMed:9298816}.
/FTId=VAR_004238.
VARIANT 288 288 A -> T (in LPL deficiency; the LPL mass
level is approximately 67% of the normal;
the activity is 32% of the nornal;
dbSNP:rs1800011).
{ECO:0000269|PubMed:15256764,
ECO:0000269|PubMed:8077845,
ECO:0000269|PubMed:9719626}.
/FTId=VAR_011949.
VARIANT 289 289 Y -> H (in LPL deficiency; no enzyme
activity). {ECO:0000269|PubMed:8728326}.
/FTId=VAR_057934.
VARIANT 297 297 F -> L (in LPL deficiency and
hyperlipidemia; synthesized as a
catalytically inactive form; total amount
is almost equal to that of the normal
enzyme; non-releasable by heparin due to
the abnormal structure of the mutant
protein). {ECO:0000269|PubMed:11068186,
ECO:0000269|PubMed:15256764}.
/FTId=VAR_057935.
VARIANT 303 303 L -> F (in LPL deficiency; approximately
6% of normal LPL activity and 40% of LPL
mass are detected in the patient's
postheparin plasma; results in the
production of a functionally inactive
enzyme). {ECO:0000269|PubMed:12641539}.
/FTId=VAR_057936.
VARIANT 305 305 C -> R (in LPL deficiency;
dbSNP:rs773235712).
{ECO:0000269|PubMed:15256764}.
/FTId=VAR_057937.
VARIANT 310 310 C -> Y (in LPL deficiency; decreases the
specific activity of the enzyme; reduces
the secretion of the mutant protein
significantly; the total LPL mass is
reduced compared to that of the wild-type
construct).
{ECO:0000269|PubMed:12204001}.
/FTId=VAR_057938.
VARIANT 313 313 L -> P (in LPL deficiency).
{ECO:0000269|PubMed:8778602}.
/FTId=VAR_057939.
VARIANT 318 318 N -> S (in LPL deficiency; loss of
activity; frequent mutation;
dbSNP:rs268).
{ECO:0000269|PubMed:12966036,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7647785,
ECO:0000269|PubMed:8077845,
ECO:0000269|PubMed:8872057,
ECO:0000269|PubMed:9662394,
ECO:0000269|PubMed:9719626,
ECO:0000269|Ref.5}.
/FTId=VAR_004239.
VARIANT 325 325 S -> R (in LPL deficiency; has no effect
on the specific activity of the enzyme;
has a mild effect on the secretion of the
mutant enzyme; the total LPL mass is
reduced compared to that of the wild-type
construct; dbSNP:rs761265900).
{ECO:0000269|PubMed:12204001}.
/FTId=VAR_057940.
VARIANT 328 328 M -> R (in LPL deficiency).
{ECO:0000269|PubMed:15185149}.
/FTId=VAR_057941.
VARIANT 328 328 M -> T (in LPL deficiency).
/FTId=VAR_004240.
VARIANT 330 330 L -> F (in LPL deficiency).
{ECO:0000269|PubMed:15256764}.
/FTId=VAR_057942.
VARIANT 330 330 L -> P (in LPL deficiency).
/FTId=VAR_004241.
VARIANT 361 361 A -> T (in LPL deficiency;
dbSNP:rs118204071).
{ECO:0000269|PubMed:15256764,
ECO:0000269|PubMed:8096693}.
/FTId=VAR_004242.
VARIANT 365 365 S -> F (in LPL deficiency; increases the
specific activity of the enzyme; has a
mild effect on the secretion of the
mutant enzyme; the total LPL mass is
reduced compared to that of the wild-type
construct; dbSNP:rs546542623).
{ECO:0000269|PubMed:12204001}.
/FTId=VAR_057943.
VARIANT 370 370 V -> M (in dbSNP:rs298).
{ECO:0000269|PubMed:9662394}.
/FTId=VAR_011950.
VARIANT 379 379 T -> A (in dbSNP:rs300).
{ECO:0000269|PubMed:9662394}.
/FTId=VAR_011951.
VARIANT 392 392 L -> V (in LPL deficiency; loss of
activity; dbSNP:rs118204078).
{ECO:0000269|PubMed:8135797}.
/FTId=VAR_004243.
VARIANT 404 404 M -> R (in LPL deficiency; decreased
protein secretion; loss of lipoprotein
lipase activity).
{ECO:0000269|PubMed:27578112}.
/FTId=VAR_077541.
VARIANT 423 424 Missing (in LPL deficiency; affects the
protein folding).
/FTId=VAR_004244.
VARIANT 427 427 A -> T (in dbSNP:rs5934).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_011952.
VARIANT 437 437 E -> K (in LPL deficiency).
{ECO:0000269|PubMed:8956048}.
/FTId=VAR_004245.
VARIANT 437 437 E -> V (in LPL deficiency).
{ECO:0000269|PubMed:7806969}.
/FTId=VAR_004246.
VARIANT 445 445 C -> Y (in LPL deficiency; has 48% of
normal activity in vitro; decreased
levels of activity account for by the
lower protein mass levels of the mutants
rather than by decreased enzymatic
activities; dbSNP:rs118204079).
{ECO:0000269|PubMed:8858123}.
/FTId=VAR_057944.
VARIANT 448 448 E -> K (in LPL deficiency; results in a
moderate reduction in catalytic activity;
dbSNP:rs149089920).
{ECO:0000269|PubMed:9498099}.
/FTId=VAR_057945.
MUTAGEN 159 159 S->G: Lacks both triolein and tributyrin
esterase activities.
{ECO:0000269|PubMed:1371284}.
MUTAGEN 159 159 S->T: Lacks both triolein and tributyrin
esterase activities.
{ECO:0000269|PubMed:1371284}.
MUTAGEN 268 268 H->G: Lacks both triolein and tributyrin
esterase activities.
{ECO:0000269|PubMed:1371284}.
MUTAGEN 268 268 H->Q: Lacks both triolein and tributyrin
esterase activities.
{ECO:0000269|PubMed:1371284}.
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


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