ADCY5

Adenylate cyclase 5

PDB rendering based on 1azs.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1azs, 1cjk, 1cjt, 1cju, 1cjv, 1cs4, 1cul, 1tl7, 1u0h, 2gvd, 2gvz

Identifiers

Symbols

ADCY5 ; AC5; FDFM

External IDs

OMIM: 600293 MGI: 99673 HomoloGene: 11213 IUPHAR: 1282 ChEMBL: 3189 GeneCards: ADCY5 Gene

EC number

4.6.1.1

Gene ontology
Molecular function	• adenylate cyclase activity • ATP binding • adenylate cyclase binding • metal ion binding • protein heterodimerization activity
Cellular component	• intracellular • plasma membrane • integral component of membrane • primary cilium
Biological process	• adenosine receptor signaling pathway • renal water homeostasis • energy reserve metabolic process • cAMP biosynthetic process • water transport • signal transduction • epidermal growth factor receptor signaling pathway • adenylate cyclase-activating G-protein coupled receptor signaling pathway • adenylate cyclase-activating dopamine receptor signaling pathway • adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway • adenylate cyclase-inhibiting dopamine receptor signaling pathway • activation of phospholipase C activity • synaptic transmission • locomotory behavior • fibroblast growth factor receptor signaling pathway • activation of protein kinase A activity • intracellular signal transduction • small molecule metabolic process • innate immune response • neurotrophin TRK receptor signaling pathway • neuromuscular process controlling balance • transmembrane transport • cellular response to glucagon stimulus
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

111

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 3:
123.28 – 123.45 Mb

Chr 16:
35.15 – 35.31 Mb

PubMed search

Adenylyl cyclase type 5 is an enzyme that in humans is encoded by the ADCY5 gene.^[1]^[2]

Interactions

ADCY5 has been shown to interact with RGS2.^[3]

References

↑ Raimundo S, Giray J, Volff JN, Schwab M, Altenbuchner J, Ratge D, Wisser H (October 1999). "Cloning and sequence of partial cDNAs encoding the human type V and VI adenylyl cyclases and subsequent RNA-quantification in various tissues". Clin Chim Acta 285 (1–2): 155–61. doi:10.1016/S0009-8981(99)00067-4. PMID 10481931.
↑ "Entrez Gene: ADCY5 adenylate cyclase 5".
↑ Salim S, Sinnarajah S, Kehrl JH, Dessauer CW (May 2003). "Identification of RGS2 and type V adenylyl cyclase interaction sites". J. Biol. Chem. 278 (18): 15842–9. doi:10.1074/jbc.M210663200. PMID 12604604.

Yoshimura M, Cooper DM (1992). "Cloning and expression of a Ca(2+)-inhibitable adenylyl cyclase from NCB-20 cells". Proc. Natl. Acad. Sci. U.S.A. 89 (15): 6716–20. doi:10.1073/pnas.89.15.6716. PMC 49574. PMID 1379717.
Iwami G, Kawabe J, Ebina T, Cannon PJ, Homcy CJ, Ishikawa Y (1995). "Regulation of adenylyl cyclase by protein kinase A". J. Biol. Chem. 270 (21): 12481–4. doi:10.1074/jbc.270.21.12481. PMID 7759492.
Haber N, Stengel D, Defer N, Roeckel N, Mattei MG, Hanoune J (1994). "Chromosomal mapping of human adenylyl cyclase genes type III, type V and type VI". Hum. Genet. 94 (1): 69–73. doi:10.1007/BF02272844. PMID 8034296.
Kawabe J, Iwami G, Ebina T, Ohno S, Katada T, Ueda Y, Homcy CJ, Ishikawa Y (1994). "Differential activation of adenylyl cyclase by protein kinase C isoenzymes". J. Biol. Chem. 269 (24): 16554–8. PMID 8206971.
Scholich K, Barbier AJ, Mullenix JB, Patel TB (1997). "Characterization of soluble forms of nonchimeric type V adenylyl cyclases". Proc. Natl. Acad. Sci. U.S.A. 94 (7): 2915–20. doi:10.1073/pnas.94.7.2915. PMC 20297. PMID 9096321.
Sunahara RK, Dessauer CW, Whisnant RE, Kleuss C, Gilman AG (1997). "Interaction of Gsalpha with the cytosolic domains of mammalian adenylyl cyclase". J. Biol. Chem. 272 (35): 22265–71. doi:10.1074/jbc.272.35.22265. PMID 9268375.
Scholich K, Wittpoth C, Barbier AJ, Mullenix JB, Patel TB (1997). "Identification of an intramolecular interaction between small regions in type V adenylyl cyclase that influences stimulation of enzyme activity by Gsα". Proc. Natl. Acad. Sci. U.S.A. 94 (18): 9602–7. doi:10.1073/pnas.94.18.9602. PMC 23231. PMID 9275169.
Dessauer CW, Tesmer JJ, Sprang SR, Gilman AG (1998). "Identification of a Gialpha binding site on type V adenylyl cyclase". J. Biol. Chem. 273 (40): 25831–9. doi:10.1074/jbc.273.40.25831. PMID 9748257.
Barcova M, Speth C, Kacani L, Uberall F, Stoiber H, Dierich MP (1999). "Involvement of adenylate cyclase and p70(S6)-kinase activation in IL-10 up-regulation in human monocytes by gp41 envelope protein of human immunodeficiency virus type 1". Pflugers Arch. 437 (4): 538–46. doi:10.1007/s004240050815. PMID 10089566.
Speth C, Joebstl B, Barcova M, Dierich MP (2000). "HIV-1 envelope protein gp41 modulates expression of interleukin-10 and chemokine receptors on monocytes, astrocytes and neurones". AIDS 14 (6): 629–36. doi:10.1097/00002030-200004140-00001. PMID 10807185.
Patke CL, Shearer WT (2000). "gp120- and TNF-alpha-induced modulation of human B cell function: proliferation, cyclic AMP generation, Ig production, and B-cell receptor expression". J. Allergy Clin. Immunol. 105 (5): 975–82. doi:10.1067/mai.2000.105315. PMID 10808179.
Patrizio M, Colucci M, Levi G (2001). "Human immunodeficiency virus type 1 Tat protein decreases cyclic AMP synthesis in rat microglia cultures". J. Neurochem. 77 (2): 399–407. doi:10.1046/j.1471-4159.2001.00249.x. PMID 11299302.
Côté M, Guillon G, Payet MD, Gallo-Payet N (2001). "Expression and regulation of adenylyl cyclase isoforms in the human adrenal gland". J. Clin. Endocrinol. Metab. 86 (9): 4495–503. doi:10.1210/jc.86.9.4495. PMID 11549699.
Speth C, Schabetsberger T, Mohsenipour I, Stöckl G, Würzner R, Stoiber H, Lass-Flörl C, Dierich MP (2002). "Mechanism of Human Immunodeficiency Virus-Induced Complement Expression in Astrocytes and Neurons". J. Virol. 76 (7): 3179–88. doi:10.1128/JVI.76.7.3179-3188.2002. PMC 136041. PMID 11884542.
Ludwig MG, Seuwen K (2003). "Characterization of the human adenylyl cyclase gene family: cDNA, gene structure, and tissue distribution of the nine isoforms". J. Recept. Signal Transduct. Res. 22 (1–4): 79–110. doi:10.1081/RRS-120014589. PMID 12503609.
Salim S, Sinnarajah S, Kehrl JH, Dessauer CW (2003). "Identification of RGS2 and type V adenylyl cyclase interaction sites". J. Biol. Chem. 278 (18): 15842–9. doi:10.1074/jbc.M210663200. PMID 12604604.
Bauman AL, Soughayer J, Nguyen BT, Willoughby D, Carnegie GK, Wong W, Hoshi N, Langeberg LK, Cooper DM, Dessauer CW, Scott JD (2006). "Dynamic regulation of cAMP synthesis through anchored PKA-adenylyl cyclase V/VI complexes". Mol. Cell 23 (6): 925–31. doi:10.1016/j.molcel.2006.07.025. PMID 16973443.
Wang SC, Lai HL, Chiu YT, Ou R, Huang CL, Chern Y (2007). "Regulation of type V adenylate cyclase by Ric8a, a guanine nucleotide exchange factor". Biochem J 406 (3): 383–8. doi:10.1042/BJ20070512. PMC 2049038. PMID 17593019.

PDB gallery

1azs: COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE

1cjk: COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH ADENOSINE 5'-(ALPHA THIO)-TRIPHOSPHATE (RP), MG, AND MN

1cjt: COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH BETA-L-2',3'-DIDEOXYATP, MN, AND MG

1cju: COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH BETA-L-2',3'-DIDEOXYATP AND MG

1cjv: COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH BETA-L-2',3'-DIDEOXYATP, MG, AND ZN

1cs4: COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH 2'-DEOXY-ADENOSINE 3'-MONOPHOSPHATE, PYROPHOSPHATE AND MG

1cul: COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH 2',5'-DIDEOXY-ADENOSINE 3'-TRIPHOSPHATE AND MG

1tl7: Complex Of Gs- With The Catalytic Domains Of Mammalian Adenylyl Cyclase: Complex With 2'(3')-O-(N-methylanthraniloyl)-guanosine 5'-triphosphate and Mn

1u0h: STRUCTURAL BASIS FOR THE INHIBITION OF MAMMALIAN ADENYLYL CYCLASE BY MANT-GTP

2gvd: Complex Of Gs- With The Catalytic Domains Of Mammalian Adenylyl Cyclase: Complex With TNP-ATP and Mn

2gvz: Crystal Structure of Complex of Gs- with The Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with MANT-ATP and Mn

Phosphorus-oxygen lyases (EC 4.6)

4.6.1

Adenylate cyclase
(4.6.1.1)

intracellular	ADCY1 ADCY2 ADCY3 ADCY4 ADCY5 ADCY6 ADCY7 ADCY8 ADCY9 ADCY10

extracellular	Extracellular adenylate cyclase

Guanylate cyclase
(4.6.1.2)

soluble guanylyl cyclase	GUCY1A2 GUCY1A3 GUCY1B2 GUCY1B3

guanylate cyclase-coupled receptor	GUCY2C GUCY2D ANP (NPR1 NPR2)

Other

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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ADCY5

Interactions

References

Further reading