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Showing drug card for Aminophylline (DB01223)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-02-19 16:04:19
Primary Accession Number DB01223
Secondary Accession Number
  • APRD00329
Name Aminophylline
Drug Type
  • Approved
  • Small Molecule
Description Aminophylline is a drug combination that contains theophylline and ethylenediamine in 2:1 ratio. [Wikipedia]
Synonyms
  1. Aminophyllin
  2. Aminophylline Anhydrous
  3. Aminophylline Dihydrate
  4. Aminophylline Dye Free
Brand Names
  1. Aminocardol
  2. Aminodur
  3. Ammophyllin
  4. Cardiofilina
  5. Cardiomin
  6. Cardophylin
  7. Cardophyllin
  8. Carena
  9. Cariomin
  10. Diaphylline
  11. Diophllin
  12. Diuxanthine
  13. Dobo
  14. Dura-Tab S.M. Aminophylline
  15. Ethophylline
  16. Etilen-Xantisan Tabl.
  17. Eurphyllin
  18. Euufillin
  19. Genophyllin
  20. Grifomin
  21. Inophylline
  22. Lasodex
  23. Linampheta
  24. Lixaminol
  25. Metaphyllin
  26. Metaphylline
  27. Methophylline
  28. Minaphil
  29. Miofilin
  30. Neophyiline
  31. Norofilina
  32. Peterphyllin
  33. Phylcardin
  34. Phyllindon
  35. Phyllocontin
  36. Phyllocontin-350
  37. Rectalad Aminophylline
  38. Rectalad-Aminophylline
  39. Somophyllin
  40. Somophyllin O
  41. Somophyllin-O
  42. Stenovasan
  43. Syntophyllin
  44. Theodrox
  45. Theolamine
  46. Theolone
  47. Theophyldine
  48. Theophyline Ethylenediamine
  49. Theophyllamine
  50. Theophyllaminum
  51. Theophyllin Aethylendiamin
  52. Theophyllin Ethylenediamine
  53. Theophylline Ethylenediamine
  54. Thephyldine
  55. Truphylline
  56. Variaphylline
  57. Vasofilina
Brand Mixtures
  1. Ami-Nesine Liq (Aminophylline + Guaifenesin)
  2. Quiex - Forte Syr (Aminophylline + Guaifenesin)
  3. Quiex Liq (Aminophylline + Guaifenesin)
  4. Quiex-K1 Syr (Aminophylline + Guaifenesin + Potassium Iodide)
  5. Quiex-Pred Sus (Aminophylline + Guaifenesin + Prednisolone)
Chemical IUPAC Name 1,3-dimethyl-7H-purine-2,6-dione; 1,3-dimethyl-7H-purine-2,6-dione; ethane-1,2-diamine
Chemical Formula C16H24N10O4
Chemical Structure Structure
CAS Registry Number 317-34-0
InChI Identifier InChI=1/2C7H8N4O2.C2H8N2/c2*1-10-5-4(8-3-9-5)6(12)11(2)7(10)13;3-1-2-4/h2*3H,1-2H3,(H,8,9);1-4H2/f/h2*8H;
InChI Key FQPFAHBPWDRTLU-MPRSSJFPCI
KEGG Drug D00227 Link Image
KEGG Compound Not Available
PubChem Compound 9433 Link Image
PubChem Substance 152642 Link Image
ChEBI ID Not Available
PharmGKB ID PA448378 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 00582662 Link Image
RxList Link Not Available
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Aminophylline Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 420.4264
Monoisotopic Molecular Weight 420.1982
State Solid
Melting Point Not Available
Experimental Water Solubility 2E+005 mg/L Source: PhysProp
Predicted Water Solubility Not Available Calculated using ALOGPS
Experimental LogP/Hydrophobicity -3.03 Source: PhysProp
Predicted LogP Not Available Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS Not Available 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 NCCN.CN1C(=O)N(C)C2=C(NC=N2)C1=O.CN1C(=O)N(C)C2=C(NC=N2)C1=O
Canonical SMILES NCCN.CN1C(=O)N(C)C2=C(NC=N2)C1=O.CN1C(=O)N(C)C2=C(NC=N2)C1=O
Drug Category
  • Bronchodilator Agents
  • Cardiotonic Agents
  • Phosphodiesterase Inhibitors
  • Respiratory Smooth Muscle Relaxants
ATC Codes
AHFS Codes
  • 86:16.00
Indication For the treatment of bronchospasm due to asthma, emphysema and chronic bronchitis.
Pharmacology Aminophylline is the ethylenediamine salt of theophylline. Theophylline stimulates the CNS, skeletal muscles, and cardiac muscle. It relaxes certain smooth muscles in the bronchi, produces diuresis, and causes an increase in gastric secretion.
Mechanism of Action Theophylline is structurally related to theobromine and caffeine. The precise mechanism of action of theophylline is not known.
Absorption Not Available
Toxicity Not Available
Protein Binding 60%
Biotransformation Not Available
Half Life 7-9 hours
Dosage Forms
Form Route
Solution Intravenous
Tablet Oral
Tablet, extended release Oral
Patient Information Not Available
Contraindications Not Available
Interactions Not Available
Drug Interactions
Drug Interaction
Aciclovir Acyclovir increases the effect and toxicity of theophylline
Adenosine This xanthine decreases the effect of adenosine
Amobarbital The barbiturate decreases the effect of theophylline
Aprobarbital The barbiturate decreases the effect of theophylline
Atracurium Theophylline decreases the effect of muscle relaxant
Butabarbital The barbiturate decreases the effect of theophylline
Butalbital The barbiturate decreases the effect of theophylline
Butethal The barbiturate decreases the effect of theophylline
Carbamazepine Carbamazepine increases or decreases the effect of theophylline
Carteolol Antagonism of action and increased effect of theophylline
Cimetidine Cimetidine increases the effect of theophylline
Ciprofloxacin The quinolone increases the effect of theophylline
Clarithromycin Clarithromycin increases the effect amd toxicity of theophylline
Dihydroquinidine barbiturate The barbiturate decreases the effect of theophylline
Disulfiram Disulfiram increases the effect and toxicity of theophylline
Doxacurium Theophylline decreases the effect of muscle relaxant
Enoxacin The quinolone increases the effect of theophylline
Erythromycin The macrolide increases the effect and toxicity of theophylline
Ethinyl Estradiol The contraceptive increases the effect and toxicity of theophylline
Ethotoin Decreased effect of both products
Fluvoxamine Fluvoxamine increases the effect and toxicity of theophylline
Fosphenytoin Decreased effect of both products
Gallamine Triethiodide Theophylline decreases the effect of muscle relaxant
Grepafloxacin The quinolone increases the effect of theophylline
Halothane Increased risk of cardiac arrhythmia
Heptabarbital The barbiturate decreases the effect of theophylline
Hexobarbital The barbiturate decreases the effect of theophylline
Interferon Alfa-2a, Recombinant Interferon increases the effect and toxicity of theophylline
Interferon Alfa-2b, Recombinant Interferon increases the effect and toxicity of theophylline
Interferon alfa-n1 Interferon increases the effect and toxicity of theophylline
Isoniazid Isoniazid increases the effect and toxicity of theophhylline
Josamycin The macrolide increases the effect and toxicity of theophylline
Lithium Theophylline decreases serum levels of lithium
Mephenytoin Decreased effect of both products
Mestranol The contraceptive increases the effect and toxicity of theophylline
Methohexital The barbiturate decreases the effect of theophylline
Methylphenobarbital The barbiturate decreases the effect of theophylline
Metocurine Theophylline decreases the effect of muscle relaxant
Mexiletine Mexiletine increases the effect and toxicity of theophylline
Mivacurium Theophylline decreases the effect of muscle relaxant
Nadolol Antagonism of action and increased effect of theophylline
Norfloxacin The quinolone increases the effect of theophylline
Pancuronium Theophylline decreases the effect of muscle relaxant
Pefloxacin The quinolone increases the effect of theophylline
Peginterferon alfa-2a Interferon increases the effect and toxicity of theophylline
Peginterferon alfa-2b Interferon increases the effect and toxicity of theophylline
Penbutolol Antagonism of action and increased effect of theophylline
Pentobarbital The barbiturate decreases the effect of theophylline
Pentoxifylline Pentoxyfylline increases the effect and toxicity of theophylline
Phenobarbital The barbiturate decreases the effect of theophylline
Phenytoin Decreased effect of both products
Pindolol Antagonism of action and increased effect of theophylline
Primidone The barbiturate decreases the effect of theophylline
Propafenone Propafenone increases the effect of theophylline
Propranolol Antagonism of action and increased effect of theophylline
Quinidine barbiturate The barbiturate decreases the effect of theophylline
Rifampin Rifampin decreases the effect of theophylline
Ritonavir Ritonavir decreases the effect of theophylline
Rofecoxib Rofecoxib increases the effect and toxicity of theophylline
Secobarbital The barbiturate decreases the effect of theophylline
Sotalol Antagonism of action and increased effect of theophylline
St. John's Wort St. John's Wort decreases the effect of theophylline
Tacrine Tacrine increases the effect and toxicity of theophylline
Talbutal The barbiturate decreases the effect of theophylline
Terbinafine Terbinafine increases the effect and toxicity of theophylline
Thiabendazole Thiabendazole increases the effect and toxicity of theophylline
Ticlopidine Ticlopidine increases the effect and toxicity of theophylline
Timolol Antagonism of action and increased effect of theophylline
Troleandomycin The macrolide increases the effect and toxicity of theophylline
Tubocurarine Theophylline decreases the effect of muscle relaxant
Vecuronium Theophylline decreases the effect of muscle relaxant
Verapamil Verapamil increases the effect of theophylline
Zileuton Zileuton increases the effect and toxicity of theophylline
Food Interactions
  • Limit caffeine intake.
  • Take with food.
  • Vitamin B6 needs increased, supplement recommended.
Pathways Not Available
General References
  1. Drugs.com Link Image
  2. Wikipedia Link Image
Organisms Affected
  • Humans and other mammals
Targets
  1. Adenosine A1 receptor
  2. Adenosine A3 receptor
  3. cGMP-inhibited 3',5'-cyclic phosphodiesterase A
Drug Target 1 [top]
Target 1 ID 16
Target 1 Name Adenosine A1 receptor
Target 1 Synonyms Not Available
Target 1 Gene Name ADORA1
Target 1 Protein Sequence >Adenosine A1 receptor 
MPPSISAFQAAYIGIEVLIALVSVPGNVLVIWAVKVNQALRDATFCFIVSLAVADVAVGA
LVIPLAILINIGPQTYFHTCLMVACPVLILTQSSILALLAIAVDRYLRVKIPLRYKMVVT
PRRAAVAIAGCWILSFVVGLTPMFGWNNLSAVERAWAANGSMGEPVIKCEFEKVISMEYM
VYFNFFVWVLPPLLLMVLIYLEVFYLIRKQLNKKVSASSGDPQKYYGKELKIAKSLALIL
FLFALSWLPLHILNCITLFCPSCHKPSILTYIAIFLTHGNSAMNPIVYAFRIQKFRVTFL
KIWNDHFRCQPAPPIDEDLPEERPDD
Target 1 Number of Residues 331
Target 1 Molecular Weight 36512
Target 1 Theoretical pI 8.75
Target 1 GO Classification
Function
signal transducer activity
receptor activity
transmembrane receptor activity
G-protein coupled receptor activity
rhodopsin-like receptor activity
nucleotide receptor activity, G-protein coupled
purinergic nucleotide receptor activity, G-protein coupled
adenosine receptor activity, G-protein coupled
A1 adenosine receptor activity, G-protein coupled
Process
cellular process
cell communication
signal transduction
cell surface receptor linked signal transduction
G-protein coupled receptor protein signaling pathway
Component
cell
membrane
intrinsic to membrane
integral to membrane
Target 1 General Function Involved in A1 adenosine receptor activity, G-protein coupled
Target 1 Specific Function Receptor for adenosine. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • 11-33
  • 47-69
  • 81-102
  • 124-146
  • 177-201
  • 236-259
  • 268-292
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 256155 Link Image
Target 1 UniProtKB/Swiss-Prot ID P30542 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name AA1R_HUMAN Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 1 Gene Sequence >981 bp 
ATGCCGCCCTCCATCTCAGCTTTCCAGGCCGCCTACATCGGCATCGAGGTGCTCATCGCC
CTGGTCTCTGTGCCCGGGAACGTGCTGGTGATCTGGGCGGTGAAGGTGAACCAGGCGCTG
CGGGATGCCACCTTCTGCTTCATCGTGTCGCTGGCGGTGGCTGATGTGGCCGTGGGTGCC
CTGGTCATCCCCCTCGCCATCCTCATCAACATTGGGCCACAGACCTACTTCCACACCTGC
CTCATGGTTGCCTGTCCGGTCCTCATCCTCACCCAGAGCTCCATCCTGGCCCTGCTGGCA
ATTGCGGTGGACCGCTACCTCCGGGTCAAGATCCCTCTCCGGTACAAGATGGTGGTGACC
CCCCGGAGGGCGGCGGTGGCCATAGCCGGCTGCTGGATCCTCTCCTTCGTGGTGGGACTG
ACCCCTATGTTTGGCTGGAACAATCTGAGTGCGGTGGAGCGGGCCTGGGCAGCCAACGGC
AGCATGGGGGAGCCCGTGATCAAGTGCGAGTTCGAGAAGGTCATCAGCATGGAGTACATG
GTCTACTTCAACTTCTTTGTGTGGGTGCTCCCCCCGCTTCTCCTCATGGTCCTCATCTAC
CTGGAGGTCTTCTACCTAATCCGCAAGCAGCTCAACAAGAAGGTGTCGGCCTCCTCCGGC
GACCCGCAGAAGTACTATGGGAAGGAGCTGAAGATCGCCAAGTCGCTGGCCCTCATCCTC
TTCCTCTTTGCCCTCAGCTGGCTGCCTTTGCACATCCTCAACTGCATCACCCTCTTCTGC
CCGTCCTGCCACAAGCCCAGCATCCTTACCTACATTGCCATCTTCCTCACGCACGGCAAC
TCGGCCATGAACCCCATTGTCTATGCCTTCCGCATCCAGAAGTTCCGCGTCACCTTCCTT
AAGATTTGGAATGACCATTTCCGCTGCCAGCCTGCACCTCCCATTGACGAGGATCTCCCA
GAAGAGAGGCCTGATGACTAG
Target 1 GenBank Gene ID
Target 1 GeneCard ID ADORA1 Link Image
Target 1 GenAtlas ID ADORA1 Link Image
Target 1 HGNC ID HGNC:262 Link Image
Target 1 Chromosome Location 1
Target 1 Locus 1q32.1
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Townsend-Nicholson A, Shine J: Molecular cloning and characterisation of a human brain A1 adenosine receptor cDNA. Brain Res Mol Brain Res. 1992 Dec;16(3-4):365-70. [PubMed Link Image]
  2. Libert F, Van Sande J, Lefort A, Czernilofsky A, Dumont JE, Vassart G, Ensinger HA, Mendla KD: Cloning and functional characterization of a human A1 adenosine receptor. Biochem Biophys Res Commun. 1992 Sep 16;187(2):919-26. [PubMed Link Image]
  3. Ren H, Stiles GL: Characterization of the human A1 adenosine receptor gene. Evidence for alternative splicing. J Biol Chem. 1994 Jan 28;269(4):3104-10. [PubMed Link Image]
Target 1 Drug References
  1. Yamamoto S, Nakanishi O, Matsui T, Shinohara N, Kinoshita H, Lambert C, Ishikawa T: Intrathecal adenosine A1 receptor agonist attenuates hyperalgesia without inhibiting spinal glutamate release in the rat. Cell Mol Neurobiol. 2003 Apr;23(2):175-85. [PubMed Link Image]
  2. Lerman BB: Response of nonreentrant catecholamine-mediated ventricular tachycardia to endogenous adenosine and acetylcholine. Evidence for myocardial receptor-mediated effects. Circulation. 1993 Feb;87(2):382-90. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 390
Target 2 Name Adenosine A3 receptor
Target 2 Synonyms Not Available
Target 2 Gene Name ADORA3
Target 2 Protein Sequence >Adenosine A3 receptor 
MPNNSTALSLANVTYITMEIFIGLCAIVGNVLVICVVKLNPSLQTTTFYFIVSLALADIA
VGVLVMPLAIVVSLGITIHFYSCLFMTCLLLIFTHASIMSLLAIAVDRYLRVKLTVRYKR
VTTHRRIWLALGLCWLVSFLVGLTPMFGWNMKLTSEYHRNVTFLSCQFVSVMRMDYMVYF
SFLTWIFIPLVVMCAIYLDIFYIIRNKLSLNLSNSKETGAFYGREFKTAKSLFLVLFLFA
LSWLPLSIINCIIYFNGEVPQLVLYMGILLSHANSMMNPIVYAYKIKKFKETYLLILKAC
VVCHPSDSLDTSIEKNSE
Target 2 Number of Residues 323
Target 2 Molecular Weight 36185
Target 2 Theoretical pI 9.04
Target 2 GO Classification
Function
signal transducer activity
receptor activity
transmembrane receptor activity
G-protein coupled receptor activity
rhodopsin-like receptor activity
nucleotide receptor activity, G-protein coupled
purinergic nucleotide receptor activity, G-protein coupled
adenosine receptor activity, G-protein coupled
A3 adenosine receptor activity, G-protein coupled
Process
cellular process
cell communication
signal transduction
cell surface receptor linked signal transduction
G-protein coupled receptor protein signaling pathway
Component
cell
membrane
intrinsic to membrane
integral to membrane
Target 2 General Function Involved in A3 adenosine receptor activity, G-protein coupled
Target 2 Specific Function Receptor for adenosine. The activity of this receptor is mediated by G proteins which inhibits adenylyl cyclase. Possible role in reproduction
Target 2 Pathways Not Available
Target 2 Reactions Not Available
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • 15-37
  • 49-72
  • 85-106
  • 127-148
  • 178-198
  • 232-255
  • 262-284
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 349449 Link Image
Target 2 UniProtKB/Swiss-Prot ID P33765 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name AA3R_HUMAN Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 2 Gene Sequence >957 bp 
ATGCCCAACAACAGCACTACTCTGTCATTGGCCAATGTTACCTACATCACCATGGAAATT
TTCATTGGACTCTGCGCCATAGTGGGCAACGTGCTGGTCATCTGCGTGGTCAAGCTGAAC
CCCAGCCTGCAGACCACCACCTTCTATTTCATTGTCTCTCTAGCCCTGGCTGACATTGCT
GTTGGGGTGCTGGTCATGCCTTTGGCCATTGTTGTCAGCCTGGGCATCACAATCCACTTC
TACAGCTGCCTTTTTATGACTTGCCTACTGCTTATCTTTACCCACGCCTCCATCATGTCC
TTGCTGGCCATCGCTGTGGACCGATACTTGCGGGTCAAGCTTACCGTCAGATACAAGAGG
GTCACCACTCACAGAAGAATATGGCTGGCCCTGGGCCTTTGCTGGCTGGTGTCATTCCTG
GTGGGATTGACCCCCATGTTTGGCTGGAACATGAAACTGACCTCAGAGTACCACAGAAAT
GTCACCTTCCTTTCATGCCAATTTGTTTCCGTCATGAGAATGGACTACATGGTATACTTC
AGCTTCCTCACCTGGATTTTCATCCCCCTGGTTGTCATGTGCGCCATCTATCTTGACATC
TTTTACATCATTCGGAACAAACTCAGTCTGAACTTATCTAACTCCAAAGAGACAGGTGCA
TTTTATGGACGGGAGTTCAAGACGGCTAAGTCCTTGTTTCTGGTTCTTTTCTTGTTTGCT
CTGTCATGGCTGCCTTTATCTATCATCAACTGCATCATCTACTTTAATGGTGAGGTACCA
CAGCTTGTGCTGTACATGGGCATCCTGCTGTCCCATGCCAACTCCATGATGAACCCTATC
GTCTATGCCTATAAAATAAAGAAGTTCAAGGAAACCTACCTTTTGATCCTCAAAGCCTGT
GTGGTCTGCCATCCCTCTGATTCTTTGGACACAAGCATTGAGAAGAATTCTGAGTAG
Target 2 GenBank Gene ID
Target 2 GeneCard ID ADORA3 Link Image
Target 2 GenAtlas ID ADORA3 Link Image
Target 2 HGNC ID HGNC:268 Link Image
Target 2 Chromosome Location 1
Target 2 Locus 1p13.2
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Murphy WJ, Eizirik E, Johnson WE, Zhang YP, Ryder OA, O'Brien SJ: Molecular phylogenetics and the origins of placental mammals. Nature. 2001 Feb 1;409(6820):614-8. [PubMed Link Image]
  2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  3. Salvatore CA, Jacobson MA, Taylor HE, Linden J, Johnson RG: Molecular cloning and characterization of the human A3 adenosine receptor. Proc Natl Acad Sci U S A. 1993 Nov 1;90(21):10365-9. [PubMed Link Image]
  4. Sajjadi FG, Firestein GS: cDNA cloning and sequence analysis of the human A3 adenosine receptor. Biochim Biophys Acta. 1993 Oct 7;1179(1):105-7. [PubMed Link Image]
Target 2 Drug References
  1. Stella L, de Novellis V, Marabese I, Berrino L, Maione S, Filippelli A, Rossi F: The role of A3 adenosine receptors in central regulation of arterial blood pressure. Br J Pharmacol. 1998 Oct;125(3):437-40. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 485
Target 3 Name cGMP-inhibited 3',5'-cyclic phosphodiesterase A
Target 3 Synonyms
  1. CGI-PDE A
  2. Cyclic GMP-inhibited phosphodiesterase A
  3. EC 3.1.4.17
Target 3 Gene Name PDE3A
Target 3 Protein Sequence >cGMP-inhibited 3',5'-cyclic phosphodiesterase A 
MAVPGDAARVRDKPVHSGVSQAPTAGRDCHHRADPASPRDSGCRGCWGDLVLQPLRSSRK
LSSALCAGSLSFLLALLVRLVRGEVGCDLEQCKEAAAAEEEEAAPGAEGGVFPGPRGGAP
GGGARLSPWLQPSALLFSLLCAFFWMGLYLLRAGVRLPLAVALLAACCGGEALVQIGLGV
GEDHLLSLPAAGVVLSCLAAATWLVLRLRLGVLMIALTSAVRTVSLISLERFKVAWRPYL
AYLAGVLGILLARYVEQILPQSAEAAPREHLGSQLIAGTKEDIPVFKRRRRSSSVVSAEM
SGCSSKSHRRTSLPCIPREQLMGHSEWDHKRGPRGSQSSGTSITVDIAVMGEAHGLITDL
LADPSLPPNVCTSLRAVSNLLSTQLTFQAIHKPRVNPVTSLSENYTCSDSEESSEKDKLA
IPKRLRRSLPPGLLRRVSSTWTTTTSATGLPTLEPAPVRRDRSTSIKLQEAPSSSPDSWN
NPVMMTLTKSRSFTSSYAISAANHVKAKKQSRPGALAKISPLSSPCSSPLQGTPASSLVS
KISAVQFPESADTTAKQSLGSHRALTYTQSAPDLSPQILTPPVICSSCGRPYSQGNPADE
PLERSGVATRTPSRTDDTAQVTSDYETNNNSDSSDIVQNEDETECLREPLRKASACSTYA
PETMMFLDKPILAPEPLVMDNLDSIMEQLNTWNFPIFDLVENIGRKCGRILSQVSYRLFE
DMGLFEAFKIPIREFMNYFHALEIGYRDIPYHNRIHATDVLHAVWYLTTQPIPGLSTVIN
DHGSTSDSDSDSGFTHGHMGYVFSKTYNVTDDKYGCLSGNIPALELMALYVAAAMHDYDH
PGRTNAFLVATSAPQAVLYNDRSVLENHHAAAAWNLFMSRPEYNFLINLDHVEFKHFRFL
VIEAILATDLKKHFDFVAKFNGKVNDDVGIDWTNENDRLLVCQMCIKLADINGPAKCKEL
HLQWTDGIVNEFYEQGDEEASLGLPISPFMDRSAPQLANLQESFISHIVGPLCNSYDSAG
LMPGKWVEDSDESGDTDDPEEEEEEAPAPNEEETCENNESPKKKTFKRRKIYCQITQHLL
QNHKMWKKVIEEEQRLAGIENQSLDQTPQSHSSEQIQAIKEEEEEKGKPRGEEIPTQKPD
Q
Target 3 Number of Residues 1160
Target 3 Molecular Weight 124980
Target 3 Theoretical pI 5.87
Target 3 GO Classification
Function
hydrolase activity
hydrolase activity, acting on ester bonds
phosphoric ester hydrolase activity
phosphoric diester hydrolase activity
cyclic-nucleotide phosphodiesterase activity
3',5'-cyclic-nucleotide phosphodiesterase activity
catalytic activity
Process
cellular process
cell communication
signal transduction
Component
Not Available
Target 3 General Function Involved in cyclic nucleotide phosphodiesterase activity
Target 3 Specific Function Hydrolyzes both cyclic AMP (cAMP) and cyclic GMP (cGMP)
Target 3 Pathways
Name SMPDB Link KEGG Link
Purine metabolism SMP00050 Link Image map00230 Link Image
Target 3 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
Target 3 Pfam Domain Function
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • 61-83; 129-151; 158-180; 184-206; 238-255
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 38201493 Link Image
Target 3 UniProtKB/Swiss-Prot ID Q14432 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name PDE3A_HUMAN Link Image
Target 3 PDB ID Not Available
Target 3 Cellular Location
  • Membrane
  • peripheral membrane protein (Potential)
Target 3 Gene Sequence >3426 bp 
ATGGCAGTGCCCGGCGACGCTGCACGAGTCAGGGACAAGCCCGTCCACAGTGGGGTGAGT
CAAGCCCCCACGGCGGGCCGGGACTGCCACCATCGTGCGGACCCCGCATCGCCGCGGGAC
TCGGGCTGCCGTGGCTGCTGGGGAGACCTGGTGCTGCAGCCGCTCCGGAGCTCTCGGAAA
CTTTCCTCCGCGCTGTGCGCGGGCTCCCTATCCTTTCTGCTGGCGCTGCTGGTGAGGCTG
GTCCGCGGGGAGGTCGGCTGTGACCTGGAGCAGTGTAAGGAGGCGGCGGCGGCGGAGGAG
GAGGAAGCAGCCCCGGGAGCAGAAGGGGGCGTCTTCCCGGGGCCTCGGGGAGGTGCTCCC
GGGGGCGGTGCGCGGCTCAGCCCCTGGCTGCAGCCCTCGGCGCTGCTCTTCAGTCTCCTG
TGTGCCTTCTTCTGGATGGGCTTGTACCTCCTGCGCGCCGGGGTGCGCCTGCCTCTGGCT
GTCGCGCTGCTGGCCGCCTGCTGCGGGGGGGAAGCGCTCGTCCAGATTGGGCTGGGCGTC
GGGGAGGATCACTTACTCTCACTCCCCGCTGCGGGGGTGGTGCTCAGCTGCTTGGCCGCC
GCGACATGGCTGGTGCTGAGGCTGAGGCTGGGCGTCCTCATGATCGCCTTGACTAGCGCG
GTCAGGACCGTGTCCCTCATTTCCTTAGAGAGGTTCAAGGTCGCCTGGAGACCTTACCTG
GCGTACCTGGCCGGCGTGCTGGGGATCCTCTTGGCCAGGTACGTGGAACAAATCTTGCCG
CAGTCCGCGGAGGCGGCTCCAAGGGAGCATTTGGGGTCCCAGCTGATTGCTGGGACCAAG
GAAGATATCCCGGTGTTTAAGAGGAGGAGGCGGTCCAGCTCCGTCGTGTCCGCCGAGATG
TCCGGCTGCAGCAGCAAGTCCCATCGGAGGACCTCCCTGCCCTGTATACCGAGGGAACAG
CTCATGGGGCATTCAGAATGGGACCACAAACGAGGGCCAAGAGGATCACAGTCTTCAGGA
ACCAGTATTACTGTGGACATCGCCGTCATGGGCGAAGCCCACGGCCTCATTACCGACCTC
CTGGCAGACCCTTCTCTTCCACCAAACGTGTGCACATCCTTGAGAGCCGTGAGCAACTTG
CTCAGCACACAGCTCACCTTCCAGGCCATTCACAAGCCCAGAGTGAATCCCGTTACTTCG
CTCAGTGAAAACTATACCTGTTCTGACTCTGAAGAGAGCTCTGAAAAAGACAAGCTTGCT
ATTCCAAAGCGCCTGAGAAGGAGTTTGCCTCCTGGCTTGTTGAGACGAGTTTCTTCCACT
TGGACCACCACCACCTCGGCCACAGGTCTACCCACCTTGGAGCCTGCACCAGTACGGAGA
GACCGCAGCACCAGCATCAAACTGCAGGAAGCACCTTCATCCAGTCCTGATTCTTGGAAT
AATCCAGTGATGATGACCCTCACCAAAAGCAGATCCTTTACTTCATCCTATGCTATTTCT
GCAGCTAACCATGTAAAGGCTAAAAAGCAAAGTCGACCAGGTGCCCTCGCTAAAATTTCA
CCTCTTTCATCGCCCTGCTCCTCACCTCTCCAAGGGACTCCTGCCAGCAGCCTGGTCAGC
AAAATTTCTGCAGTGCAGTTTCCAGAATCTGCTGACACAACTGCCAAACAAAGCCTAGGT
TCTCACAGGGCCTTAACTTACACTCAGAGTGCCCCAGACCTATCCCCTCAAATCCTGACT
CCACCTGTTATATGTAGCAGCTGTGGCAGACCATATTCCCAAGGGAATCCTGCTGATGAG
CCCCTGGAGAGAAGTGGGGTAGCCACTCGGACACCAAGTCGAACAGATGACACTGCTCAA
GTTACCTCTGATTATGAAACCAATAACAACAGTGACAGCAGTGACATTGTACAGAATGAA
GATGAAACAGAGTGCCTGAGAGAGCCTCTGAGGAAAGCATCGGCTTGCAGCACCTATGCT
CCTGAGACCATGATGTTTCTGGACAAACCAATTCTTGCTCCCGAACCTCTTGTCATGGAT
AACCTGGACTCAATTATGGAGCAGCTAAATACTTGGAATTTTCCAATTTTTGATTTAGTG
GAAAATATAGGAAGAAAATGTGGCCGTATTCTTAGTCAGGTATCTTACAGACTTTTTGAA
GACATGGGCCTCTTTGAAGCTTTTAAAATTCCAATTAGGGAATTTATGAATTATTTTCAT
GCTTTGGAGATTGGATATAGGGATATTCCTTATCATAACAGAATCCATGCCACTGATGTT
TTACATGCTGTTTGGTATCTTACTACACAGCCTATTCCAGGCCTCTCAACTGTGATTAAT
GATCATGGTTCAACCAGTGATTCAGATTCTGACAGTGGATTTACACATGGACATATGGGA
TATGTATTCTCAAAAACGTATAATGTGACAGATGATAAATACGGATGTCTGTCTGGGAAT
ATCCCTGCCTTGGAGTTGATGGCGCTGTATGTGGCTGCAGCCATGCACGATTATGATCAT
CCAGGAAGGACTAATGCTTTCCTGGTTGCAACTAGTGCTCCTCAGGCGGTGCTATATAAC
GATCGTTCAGTTTTGGAGAATCATCACGCAGCTGCTGCATGGAATCTTTTCATGTCCCGG
CCAGAGTATAACTTCTTAATTAACCTTGACCATGTGGAATTTAAGCATTTCCGTTTCCTT
GTCATTGAAGCAATTTTGGCCACTGACCTGAAGAAACACTTTGACTTCGTAGCCAAATTT
AATGGCAAGGTAAATGATGATGTTGGAATAGATTGGACCAATGAAAATGATCGTCTACTG
GTTTGTCAAATGTGTATAAAGTTGGCTGATATCAATGGTCCAGCTAAATGTAAAGAACTC
CATCTTCAGTGGACAGATGGTATTGTCAATGAATTTTATGAACAGGGTGATGAAGAGGCC
AGCCTTGGATTACCCATAAGCCCCTTCATGGATCGTTCTGCTCCTCAGCTGGCCAACCTT
CAGGAATCCTTCATCTCTCACATTGTGGGGCCTCTGTGCAACTCCTATGATTCAGCAGGA
CTAATGCCTGGAAAATGGGTGGAAGACAGCGATGAGTCAGGAGATACTGATGACCCAGAA
GAAGAGGAGGAAGAAGCACCAGCACCAAATGAAGAGGAAACCTGTGAAAATAATGAATCT
CCAAAAAAGAAGACTTTCAAAAGGAGAAAAATCTACTGCCAAATAACTCAGCACCTCTTA
CAGAACCACAAGATGTGGAAGAAAGTCATTGAAGAGGAGCAACGGTTGGCAGGCATAGAA
AATCAATCCCTGGACCAGACCCCTCAGTCGCACTCTTCAGAACAGATCCAGGCTATCAAG
GAAGAAGAAGAAGAGAAAGGGAAACCAAGAGGCGAGGAGATACCAACCCAAAAGCCAGAC
CAGTGA
Target 3 GenBank Gene ID
Target 3 GeneCard ID PDE3A Link Image
Target 3 GenAtlas ID PDE3A Link Image
Target 3 HGNC ID HGNC:8778 Link Image
Target 3 Chromosome Location 12
Target 3 Locus 12p12
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Meacci E, Taira M, Moos M Jr, Smith CJ, Movsesian MA, Degerman E, Belfrage P, Manganiello V: Molecular cloning and expression of human myocardial cGMP-inhibited cAMP phosphodiesterase. Proc Natl Acad Sci U S A. 1992 May 1;89(9):3721-5. [PubMed Link Image]
  2. Cheung PP, Xu H, McLaughlin MM, Ghazaleh FA, Livi GP, Colman RW: Human platelet cGI-PDE: expression in yeast and localization of the catalytic domain by deletion mutagenesis. Blood. 1996 Aug 15;88(4):1321-9. [PubMed Link Image]
Target 3 Drug References
  1. Hirota K, Yoshioka H, Kabara S, Koizumi Y, Abe H, Sato T, Matsuki A: Spasmolytic effects of colforsin daropate on serotonin-induced pulmonary hypertension and bronchoconstriction in dogs. Acta Anaesthesiol Scand. 2002 Mar;46(3):297-302. [PubMed Link Image]

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.