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Showing drug card for Clofibrate (DB00636)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:08:08
Primary Accession Number DB00636
Secondary Accession Number
  • APRD00879
Name Clofibrate
Drug Type
  • Approved
  • Small Molecule
Description A fibric acid derivative used in the treatment of hyperlipoproteinemia type III and severe hypertriglyceridemia. (From Martindale, The Extra Pharmacopoeia, 30th ed, p986)
Synonyms
  1. CPIB
  2. Chlorfenisate
  3. Chlorphenisate
  4. Clofibate
  5. Clofibrato
  6. Clofibratum
  7. EPIB
  8. Ethyl chlorophenoxyisobutyrate
  9. Ethyl clofibrate
  10. Ethyl p-chlorophenoxyisobutyrate
  11. Ethyl para-chlorophenoxyisobutyrate
Brand Names
  1. Amotril
  2. Amotril S
  3. Angiokapsul
  4. Anparton
  5. Antilipid
  6. Antilipide
  7. Apolan
  8. Arterioflexin
  9. Arterosol
  10. Artes
  11. Artevil
  12. Ateculon
  13. Ateriosan
  14. Athebrate
  15. Atheromide
  16. Atheropront
  17. Athranid-Wirkstoff
  18. Atrolen
  19. Atromid
  20. Atromid S
  21. Atromid-S
  22. Atromida
  23. Atromidin
  24. Atrovis
  25. Azionyl
  26. Bioscleran
  27. Bresit
  28. Cartagyl
  29. Citiflus
  30. Claripex
  31. Claripex CPIB
  32. Cloberat
  33. Clobrat
  34. Clobren-5F
  35. Clobren-SF
  36. Clofar
  37. Clofibram
  38. Clofibrat
  39. Clofinit
  40. Clofipront
  41. Delipid
  42. Deliva
  43. Dura clofibrat
  44. ELPI
  45. Fibralem
  46. Gerastop
  47. Hyclorate
  48. Klofibrat
  49. Klofiran
  50. Levatrom
  51. Lipamid
  52. Lipavil
  53. Lipavlon
  54. Lipide 500
  55. Lipidsenker
  56. Lipofacton
  57. Lipomid
  58. Liponorm
  59. Liporeduct
  60. Liporil
  61. Liposid
  62. Liprin
  63. Liprinal
  64. Lobetrin
  65. Miscleron
  66. Negalip
  67. Neo-Atromid
  68. Normalip
  69. Normat
  70. Normolipol
  71. Novofibrate
  72. Oxan 600
  73. Persantinat
  74. Regardin
  75. Regelan
  76. Regelan N
  77. Robigram
  78. Scrobin
  79. Serofinex
  80. Serotinex
  81. Skerolip
  82. Sklerepmexe
  83. Sklero
  84. Sklero-Tablinen
  85. Sklero-tablinene
  86. Sklero-tabuls
  87. Sklerolip
  88. Skleromex
  89. Skleromexe
  90. Tetrasipton
  91. Thillate
  92. Thiosan
  93. Ticlobran
  94. Vincamin compositum
  95. Xyduril
  96. Yoclo
  97. neo-Atomid
Brand Mixtures Not Available
Chemical IUPAC Name ethyl 2-(4-chlorophenoxy)-2-methylpropanoate
Chemical Formula C12H15ClO3
Chemical Structure Structure
CAS Registry Number 637-07-0
InChI Identifier InChI=1/C12H15ClO3/c1-4-15-11(14)12(2,3)16-10-7-5-9(13)6-8-10/h5-8H,4H2,1-3H3
InChI Key KNHUKKLJHYUCFP-UHFFFAOYAE
KEGG Drug D00279 Link Image
KEGG Compound C06916 Link Image
PubChem Compound 2796 Link Image
PubChem Substance 9133 Link Image
ChEBI ID 3750 Link Image
PharmGKB ID PA449045 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 00002038 Link Image
RxList Link http://www.rxlist.com/cgi/generic2/clofibrate.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Clofibrate Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 242.6990
Monoisotopic Molecular Weight 242.0710
State Liquid
Melting Point < 25 oC (boiling point 148-150°C at 25 mm Hg)
Experimental Water Solubility Insoluble Source: PhysProp
Predicted Water Solubility 2.90e-02 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 3.3 Source: PhysProp
Predicted LogP 3.99 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -3.92 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point Not Available
Mass Spectrum Not Available
MOL File Show Link Image | Download Link Image
SDF File Show Link Image | Download Link Image
PDB File Show Link Image | Download Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Isomeric SMILES CCOC(=O)C(C)(C)OC1=CC=C(Cl)C=C1
Canonical SMILES CCOC(=O)C(C)(C)OC1=CC=C(Cl)C=C1
Drug Category
  • Anticholesteremic Agents
  • Antilipemic Agents
ATC Codes
AHFS Codes Not Available
Indication For Primary Dysbetalipoproteinemia (Type III hyperlipidemia) that does not respond adequately to diet.
Pharmacology Clofibrate is an antilipidemic agent similar to gemfibrozil. It acts to lower elevated serum lipids by reducing the very low-density lipoprotein fraction (Sf 20-400) rich in triglycerides. Serum cholesterol may be decreased, particularly in those patients whose cholesterol elevation is due to the presence of IDL as a result of Type III hyperlipoproteinemia. Several investigators have observed in their studies that clofibrate may produce a decrease in cholesterol linoleate but an increase in palmitoleate and oleate, the latter being considered atherogenic in experimental animals. The significance of this finding is unknown at this time. Reduction of triglycerides in some patients treated with clofibrate or certain of its chemically and clinically similar analogs may be associated with an increase in LDL cholesterol. Increase in LDL cholesterol has been observed in patients whose cholesterol is initially normal. Animal studies suggest that clofibrate interrupts cholesterol biosynthesis prior to mevalonate formation.
Mechanism of Action Clofibrate increases the activity of extrahepatic lipoprotein lipase (LL), thereby increasing lipoprotein triglyceride lipolysis. Chylomicrons are degraded, VLDLs are converted to LDLs, and LDLs are converted to HDL. This is accompanied by a slight increase in secretion of lipids into the bile and ultimately the intestine. Clofibrate also inhibits the synthesis and increases the clearance of apolipoprotein B, a carrier molecule for VLDL.
Absorption Completely but slowly absorbed from the intestine. Between 95% and 99% of an oral dose of clofibrate is excreted in the urine as free and conjugated clofibric acid; thus, the absorption of clofibrate is virtually complete.
Toxicity Oral, mouse: LD50 = 1220 mg/kg; Oral, rabbit: LD50 = 1370 mg/kg; Oral, rat: LD50 = 940 mg/kg. No reported case of overdosage in humans.
Protein Binding Highly protein-bound (95% to 97%).
Biotransformation Hepatic and gastrointestinal: rapid de-esterification occurs in the gastrointestinal tract and/or on first-pass metabolism to produce the active form, clofibric acid (chlorophenoxy isobutyric acid [CPIB]).
Half Life Half-life in normal volunteers averages 18 to 22 hours (range 14 to 35 hours) but can vary by up to 7 hours in the same subject at different times.
Dosage Forms
Form Route
Capsule Oral
Patient Information Not Available
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Acenocoumarol The fibrate increases the anticoagulant effect
Acetohexamide The agent increases the effect of sulfonylurea
Anisindione The fibrate increases the anticoagulant effect
Chlorpropamide The agent increases the effect of sulfonylurea
Dicumarol The fibrate increases the anticoagulant effect
Glibenclamide The agent increases the effect of sulfonylurea
Gliclazide The agent increases the effect of sulfonylurea
Glipizide The agent increases the effect of sulfonylurea
Glisoxepide The agent increases the effect of sulfonylurea
Glycodiazine The agent increases the effect of sulfonylurea
Insulin Increases the effect of insulin
Insulin-aspart Increases the effect of insulin
Insulin-detemir Increases the effect of insulin
Insulin-glargine Increases the effect of insulin
Insulin-glulisine Increases the effect of insulin
Insulin-lispro Increases the effect of insulin
Tolazamide The agent increases the effect of sulfonylurea
Tolbutamide The agent increases the effect of sulfonylurea
Ursodeoxycholic acid The fibric acid derivative decreases the effect of ursodiol
Warfarin The fibrate increases the anticoagulant effect
Food Interactions
  • Take with food, since it may reduce gastric irritation.
Pathways Not Available
General References
  1. Wikipedia Link Image
  2. RxList Link Image
Organisms Affected
  • Humans and other mammals
Phase 1 Metabolizing Enzymes
  1. Cytochrome P450 2E1 (CYP2E1)
  2. Cytochrome P450 3A4 (CYP3A4)
  3. Glutathione S-transferase A2
Targets
  1. Peroxisome proliferator-activated receptor alpha
  2. Lipoprotein lipase
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Cytochrome P450 2E1 (CYP2E1)
Enzyme 1 Gene Name CYP2E1
Enzyme 1 SwissProt ID P05181 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >sp|P05181|CP2E1_HUMAN Cytochrome P450 2E1 (EC 1.14.14.1)
MSALGVTVALLVWAAFLLLVSMWRQVHSSWNLPPGPFPLPIIGNLFQLELKNIPKSFTRL
AQRFGPVFTLYVGSQRMVVMHGYKAVKEALLDYKDEFSGRGDLPAFHAHRDRGIIFNNGP
TWKDIRRFSLTTLRNYGMGKQGNESRIQREAHFLLEALRKTQGQPFDPTFLIGCAPCNVI
ADILFRKHFDYNDEKFLRLMYLFNENFHLLSTPWLQLYNNFPSFLHYLPGSHRKVIKNVA
EVKEYVSERVKEHHQSLDPNCPRDLTDCLLVEMEKEKHSAERLYTMDGITVTVADLFFAG
TETTSTTLRYGLLILMKYPEIEEKLHEEIDRVIGPSRIPAIKDRQEMPYMDAVVHEIQRF
ITLVPSNLPHEATRDTIFRGYLIPKGTVVVPTLDSVLYDNQEFPDPEKFKPEHFLNENGK
FKYSDYFKPFSTGKRVCAGEGLARMELFLLLCAILQHFNLKPLVDPKDIDLSPIHIGFGC
IPPRYKLCVIPRS
Phase 1 Metabolizing Enzyme 2 [top]
Enzyme 2 Name Cytochrome P450 3A4 (CYP3A4)
Enzyme 2 Gene Name CYP3A4
Enzyme 2 SwissProt ID P08684 Link Image
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 Protein Sequence >sp|P08684|CP3A4_HUMAN Cytochrome P450 3A4 (EC 1.14.13.67)
ALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFD
MECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIA
EDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYSM
DVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVF
PREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSII
FIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMVVN
ETLRLFPIAMRLERVCKKDVEINGMFIPKGWVVMIPSYALHRDPKYWTEPEKFLPERFSK
KNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGG
LLQPEKPVVLKVESRDGTVSGA
Phase 1 Metabolizing Enzyme 3 [top]
Enzyme 3 Name Glutathione S-transferase A2
Enzyme 3 Gene Name GSTA2
Enzyme 3 SwissProt ID P09210 Link Image
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 Protein Sequence >sp|P09210|GSTA2_HUMAN Glutathione S-transferase A2
AEKPKLHYSNIRGRMESIRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQQVPMVEID
GMKLVQTRAILNYIASKYNLYGKDIKEKALIDMYIEGIADLGEMILLLPFTQPEEQDAKL
ALIQEKTKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLVELLYYVEELDSSLISSFPLL
KALKTRISNLPTVKKFLQPGSPRKPPMDEKSLEESRKIFRF
Drug Target 1 [top]
Target 1 ID 80
Target 1 Name Peroxisome proliferator-activated receptor alpha
Target 1 Synonyms
  1. PPAR-alpha
Target 1 Gene Name PPARA
Target 1 Protein Sequence >Peroxisome proliferator-activated receptor alpha
MVDTESPLCPLSPLEAGDLESPLSEEFLQEMGNIQEISQSIGEDSSGSFGFTEYQYLGSC
PGSDGSVITDTLSPASSPSSVTYPVVPGSVDESPSGALNIECRICGDKASGYHYGVHACE
GCKGFFRRTIRLKLVYDKCDRSCKIQKKNRNKCQYCRFHKCLSVGMSHNAIRFGRMPRSE
KAKLKAEILTCEHDIEDSETADLKSLAKRIYEAYLKNFNMNKVKARVILSGKASNNPPFV
IHDMETLCMAEKTLVAKLVANGIQNKEAEVRIFHCCQCTSVETVTELTEFAKAIPGFANL
DLNDQVTLLKYGVYEAIFAMLSSVMNKDGMLVAYGNGFITREFLKSLRKPFCDIMEPKFD
FAMKFNALELDDSDISLFVAAIICCGDRPGLLNVGHIEKMQEGIVHVLRLHLQSNHPDDI
FLFPKLLQKMADLRQLVTEHAQLVQIIKKTESDAALHPLLQEIYRDMY
Target 1 Number of Residues 475
Target 1 Molecular Weight 52226
Target 1 Theoretical pI 6.20
Target 1 GO Classification
Function
steroid hormone receptor activity
transcription factor activity
signal transducer activity
receptor activity
ligand-dependent nuclear receptor activity
binding
nucleic acid binding
DNA binding
Process
regulation of biological process
regulation of physiological process
regulation of metabolism
regulation of cellular metabolism
regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
regulation of transcription
regulation of transcription, DNA-dependent
Component
organelle
membrane-bound organelle
intracellular membrane-bound organelle
nucleus
Target 1 General Function Involved in DNA binding
Target 1 Specific Function Receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the receptor binds to a promoter element in the gene for acyl-CoA oxidase and activates its transcription. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 307341 Link Image
Target 1 UniProtKB/Swiss-Prot ID Q07869 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name PPARA_HUMAN Link Image
Target 1 PDB ID 1K7L Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Nucleus
Target 1 Gene Sequence >1407 bp
ATGGTGGACACGGAAAGCCCACTCTGCCCCCTCTCCCCACTCGAGGCCGGCGATCTAGAG
AGCCCGTTATCTGAAGAGTTCCTGCAAGAAATGGGAAACATCCAAGAGATTTCGCAATCC
ATCGGCGAGGATAGTTCTGGAAGCTTTGGCTTTACGGAATACCAGTATTTAGGAAGCTGT
CCTGGCTCAGATGGCTCGGTCATCACGGACACGCTTTCACCAGCTTCGAGCCCCTCCTCG
GTGACTTATCCTGTGGTCCCCGGCAGCGTGGACGAGTCTCCCAGTGGAGCATTGAACATC
GAATGTAGAATCTGCGGGGACAAGGCCTCAGGCTATCATTACGGAGTCCACGCGTGTGAA
GGCTGCAAGGGCTTCTTTCGGCGAACGATTCGACTCAAGCTGGTGTATGACAAGTGCGAC
CGCAGCTGCAAGATCCAGAAAAAGAACAGAAACAAATGCCAGTATTGTCGATTTCACAAG
TGCCTTTCTGTCGGGATGTCACACAACGCGATTCGTTTTGGACGAATGCCAAGATCTGAG
AAAGCAAAACTGAAAGCAGAAATTCTTACCTGTGAACATGACATAGAAGATTCTGAAACT
GCAGATCTCAAATCTCTGGCCAAGAGAATCTACGAGGCCTACTTGAAGAACTTCAACATG
AACAAGGTCAAAGCCCGGGTCATCCTCTCAGGAAAGGCCAGTAACAATCCACCTTTTGTC
ATACATGATATGGAGACACTGTGTATGGCTGAGAAGACGCTGGTGGCCAAGCTGGTGGCC
AATGGCATCCAGAACAAGGAGGTGGAGGTCCGCATCTTTCACTGCTGCCAGTGCACGTCA
GTGGAGACCGTCACGGAGCTCACGGAATTCGCCAAGGCCATCCCAGCGTTCGCAAACTTG
GACCTGAACGATCAAGTGACATTGCTAAAATACGGAGTTTATGAGGCCATATTCGCCATG
CTGTCTTCTGTGATGAACAAAGACGGGATGCTGGTAGCGTATGGAAATGGGTTTATAACT
CGTGAATTCCTAAAAAGCCTAAGGAAACCGTTCTGTGATATCATGGAACCCAAGTTTGAT
TTTGCCATGAAGTTCAATGCACTGGAACTGGATGACAGTGATATCTCCCTTTTTGTGGCT
GCTATCATTTGCTGTGGAGATCGTCCTGGCCTTCTAAACGTAGGACACATTGAAAAAATG
CAGGAGGGTATTGTACATGTGCTCAGACTCCACCTGCAGAGCAACCACCCGGACGATATC
TTTCTCTTCCCAAAACTTCTTCAAAAAATGGCAGACCTCCGGCAGCTGGTGACGGAGCAT
GCGCAGCTGGTGCAGATCATCAAGAAGACGGAGTCGGATGCTGCGCTGCACCCGCTACTG
CAGGAGATCTACAGGGACATGTACTGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID PPARA Link Image
Target 1 GenAtlas ID PPARA Link Image
Target 1 HGNC ID HGNC:9232 Link Image
Target 1 Chromosome Location 22
Target 1 Locus 22q12-q13.1|22q13.31
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  2. Caira F, Antonson P, Pelto-Huikko M, Treuter E, Gustafsson JA: Cloning and characterization of RAP250, a novel nuclear receptor coactivator. J Biol Chem. 2000 Feb 25;275(8):5308-17. [PubMed Link Image]
  3. Sher T, Yi HF, McBride OW, Gonzalez FJ: cDNA cloning, chromosomal mapping, and functional characterization of the human peroxisome proliferator activated receptor. Biochemistry. 1993 Jun 1;32(21):5598-604. [PubMed Link Image]
  4. Mukherjee R, Jow L, Noonan D, McDonnell DP: Human and rat peroxisome proliferator activated receptors (PPARs) demonstrate similar tissue distribution but different responsiveness to PPAR activators. J Steroid Biochem Mol Biol. 1994 Nov;51(3-4):157-66. [PubMed Link Image]
  5. Tugwood JD, Aldridge TC, Lambe KG, Macdonald N, Woodyatt NJ: Peroxisome proliferator-activated receptors: structures and function. Ann N Y Acad Sci. 1996 Dec 27;804:252-65. [PubMed Link Image]
  6. Li H, Gomes PJ, Chen JD: RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2. Proc Natl Acad Sci U S A. 1997 Aug 5;94(16):8479-84. [PubMed Link Image]
Target 1 Drug References
  1. Barclay TB, Peters JM, Sewer MB, Ferrari L, Gonzalez FJ, Morgan ET: Modulation of cytochrome P-450 gene expression in endotoxemic mice is tissue specific and peroxisome proliferator-activated receptor-alpha dependent. J Pharmacol Exp Ther. 1999 Sep;290(3):1250-7. [PubMed Link Image]
  2. Murata M, Kaji H, Takahashi Y, Iida K, Mizuno I, Okimura Y, Abe H, Chihara K: Stimulation by eicosapentaenoic acids of leptin mRNA expression and its secretion in mouse 3T3-L1 adipocytes in vitro. Biochem Biophys Res Commun. 2000 Apr 13;270(2):343-8. [PubMed Link Image]
  3. Hunt MC, Lindquist PJ, Peters JM, Gonzalez FJ, Diczfalusy U, Alexson SE: Involvement of the peroxisome proliferator-activated receptor alpha in regulating long-chain acyl-CoA thioesterases. J Lipid Res. 2000 May;41(5):814-23. [PubMed Link Image]
  4. Casas F, Domenjoud L, Rochard P, Hatier R, Rodier A, Daury L, Bianchi A, Kremarik-Bouillaud P, Becuwe P, Keller J, Schohn H, Wrutniak-Cabello C, Cabello G, Dauca M: A 45 kDa protein related to PPARgamma2, induced by peroxisome proliferators, is located in the mitochondrial matrix. FEBS Lett. 2000 Jul 28;478(1-2):4-8. [PubMed Link Image]
  5. Komuves LG, Hanley K, Lefebvre AM, Man MQ, Ng DC, Bikle DD, Williams ML, Elias PM, Auwerx J, Feingold KR: Stimulation of PPARalpha promotes epidermal keratinocyte differentiation in vivo. J Invest Dermatol. 2000 Sep;115(3):353-60. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 266
Target 2 Name Lipoprotein lipase
Target 2 Synonyms
  1. EC 3.1.1.34
  2. LPL
  3. Lipoprotein lipase precursor
Target 2 Gene Name LPL
Target 2 Protein Sequence >Lipoprotein lipase precursor
MESKALLVLTLAVWLQSLTASRGGVAAADQRRDFIDIESKFALRTPEDTAEDTCHLIPGV
AESVATCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQEH
YPVSAGYTKLVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRIT
GLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQ
PGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCSSKEAFEKG
LCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESETHTNQ
AFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMLKLKWKSDSYFSWSDW
WSSPGFAIQKIRVKAGETQKKVIFCSREKVSHLQKGKAPAVFVKCHDKSLNKKSG
Target 2 Number of Residues 482
Target 2 Molecular Weight 53163
Target 2 Theoretical pI 8.26
Target 2 GO Classification
Function
hydrolase activity
hydrolase activity, acting on ester bonds
carboxylic ester hydrolase activity
lipase activity
lipoprotein lipase activity
catalytic activity
Process
physiological process
metabolism
primary metabolism
lipid metabolism
Component
Not Available
Target 2 General Function Involved in lipoprotein lipase activity
Target 2 Specific Function The primary function of this lipase is the hydrolysis of triglycerides of circulating chylomicrons and very low density lipoproteins (VLDL). The enzyme functions in the presence of apolipoprotein C-2 on the luminal surface of vascular endothelium
Target 2 Pathways
Name SMPDB Link KEGG Link
Glycerolipid metabolism SMP00039 Link Image map00561 Link Image
Target 2 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate
Target 2 Pfam Domain Function
Target 2 Signals
  • 1-27
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 307138 Link Image
Target 2 UniProtKB/Swiss-Prot ID P06858 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name LIPL_HUMAN Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location
  • Cell membrane
  • GPI-anchor
  • lipid-anchor
Target 2 Gene Sequence >1428 bp
ATGGAGAGCAAAGCCCTGCTCGTGCTGACTCTGGCCGTGTGGCTCCAGAGTCTGACCGCC
TCCCGCGGAGGGGTGGCCGCCGCCGACCAAAGAAGAGATTTTATCGACATCGAAAGTAAA
TTTGCCCTAAGGACCCCTGAAGACACAGCTGAGGACACTTGCCACCTCATTCCCGGAGTA
GCAGAGTCCGTGGCTACCTGTCATTTCAATCACAGCAGCAAAACCTTCATGGTGATCCAT
GGCTGGACGGTAACAGGAATGTATGAGAGTTGGGTGCCAAAACTTGTGGCCGCCCTGTAC
AAGAGAGAACCAGACTCCAATGTCATTGTGGTGGACTGGCTGTCACGGGCTCAGGAGCAT
TACCCAGTGTCCGCGGGCTACACCAAACTGGTGGGACAGGATGTGGCCCGGTTTATCAAC
TGGATGGAGGAGGAGTTTAACTACCCTCTGGACAATGTCCATCTCTTGGGATACAGCCTT
GGAGCCCATGCTGCTGGCATTGCAGGAAGTCTGACCAATAAGAAAGTCAACAGAATTACT
GGCCTCGATCCAGCTGGACCTAACTTTGAGTATGCAGAAGCCCCGAGTCGTCTTTCTCCT
GATGATGCAGATTTTGTAGACGTCTTACACACATTCACCAGAGGGTCCCCTGGTCGAAGC
ATTGGAATCCAGAAACCAGTTGGGCATGTTGACATTTACCCGAATGGAGGTACTTTTCAG
CCAGGATGTAACATTGGAGAAGCTATCCGCGTGATTGCAGAGAGAGGACTTGGAGATGTG
GACCAGCTAGTGAAGTGCTCCCACGAGCGCTCCATTCATCTCTTCATCGACTCTCTGTTG
AATGAAGAAAATCCAAGTAAGGCCTACAGGTGCAGTTCCAAGGAAGCCTTTGAGAAAGGG
CTCTGCTTGAGTTGTAGAAAGAACCGCTGCAACAATCTGGGCTATGAGATCAATAAAGTC
AGAGCCAAAAGAAGCAGCAAAATGTACCTGAAGACTCGTTCTCAGATGCCCTACAAAGTC
TTCCATTACCAAGTAAAGATTCATTTTTCTGGGACTGAGAGTGAAACCCATACCAATCAG
GCCTTTGAGATTTCTCTGTATGGCACCGTGGCCGAGAGTGAGAACATCCCATTCACTCTG
CCTGAAGTTTCCACAAATAAGACCTACTCCTTCCTAATTTACACAGAGGTAGATATTGGA
GAACTACTCATGTTGAAGCTCAAATGGAAGAGTGATTCATACTTTAGCTGGTCAGACTGG
TGGAGCAGTCCCGGCTTCGCCATTCAGAAGATCAGAGTAAAAGCAGGAGAGACTCAGAAA
AAGGTGATCTTCTGTTCTAGGGAGAAAGTGTCTCATTTGCAGAAAGGAAAGGCACCTGCG
GTATTTGTGAAATGCCATGACAAGTCTCTGAATAAGAAGTCAGGCTGA
Target 2 GenBank Gene ID
Target 2 GeneCard ID LPL Link Image
Target 2 GenAtlas ID LPL Link Image
Target 2 HGNC ID HGNC:6677 Link Image
Target 2 Chromosome Location 8
Target 2 Locus 8p22
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
  2. Morabia A, Cayanis E, Costanza MC, Ross BM, Flaherty MS, Alvin GB, Das K, Gilliam TC: 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. 2003 Nov 1;12(21):2733-43. Epub 2003 Sep 9. [PubMed Link Image]
  3. Emmerich J, Beg OU, Peterson J, Previato L, Brunzell JD, Brewer HB 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. 1992 Feb 25;267(6):4161-5. [PubMed Link Image]
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Target 2 Drug References
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This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.