Adenylate cyclase type 2

Details

Name
Adenylate cyclase type 2
Synonyms
  • 4.6.1.1
  • Adenylate cyclase type II
  • Adenylyl cyclase 2
  • ATP pyrophosphate-lyase 2
  • KIAA1060
Gene Name
ADCY2
Organism
Humans
Amino acid sequence
>lcl|BSEQ0007169|Adenylate cyclase type 2
MWQEAMRRRRYLRDRSEEAAGGGDGLPRSRDWLYESYYCMSQQHPLIVFLLLIVMGSCLA
LLAVFFALGLEVEDHVAFLITVPTALAIFFAIFILVCIESVFKKLLRLFSLVIWICLVAM
GYLFMCFGGTVSPWDQVSFFLFIIFVVYTMLPFNMRDAIIASVLTSSSHTIVLSVCLSAT
PGGKEHLVWQILANVIIFICGNLAGAYHKHLMELALQQTYQDTCNCIKSRIKLEFEKRQQ
ERLLLSLLPAHIAMEMKAEIIQRLQGPKAGQMENTNNFHNLYVKRHTNVSILYADIVGFT
RLASDCSPGELVHMLNELFGKFDQIAKENECMRIKILGDCYYCVSGLPISLPNHAKNCVK
MGLDMCEAIKKVRDATGVDINMRVGVHSGNVLCGVIGLQKWQYDVWSHDVTLANHMEAGG
VPGRVHISSVTLEHLNGAYKVEEGDGDIRDPYLKQHLVKTYFVINPKGERRSPQHLFRPR
HTLDGAKMRASVRMTRYLESWGAAKPFAHLHHRDSMTTENGKISTTDVPMGQHNFQNRTL
RTKSQKKRFEEELNERMIQAIDGINAQKQWLKSEDIQRISLLFYNKVLEKEYRATALPAF
KYYVTCACLIFFCIFIVQILVLPKTSVLGISFGAAFLLLAFILFVCFAGQLLQCSKKASP
LLMWLLKSSGIIANRPWPRISLTIITTAIILMMAVFNMFFLSDSEETIPPTANTTNTSFS
ASNNQVAILRAQNLFFLPYFIYSCILGLISCSVFLRVNYELKMLIMMVALVGYNTILLHT
HAHVLGDYSQVLFERPGIWKDLKTMGSVSLSIFFITLLVLGRQNEYYCRLDFLWKNKFKK
EREEIETMENLNRVLLENVLPAHVAEHFLARSLKNEELYHQSYDCVCVMFASIPDFKEFY
TESDVNKEGLECLRLLNEIIADFDDLLSKPKFSGVEKIKTIGSTYMAATGLSAVPSQEHS
QEPERQYMHIGTMVEFAFALVGKLDAINKHSFNDFKLRVGINHGPVIAGVIGAQKPQYDI
WGNTVNVASRMDSTGVLDKIQVTEETSLVLQTLGYTCTCRGIINVKGKGDLKTYFVNTEM
SRSLSQSNVAS
Number of residues
1091
Molecular Weight
123602.25
Theoretical pI
8.15
GO Classification
Functions
adenylate cyclase activity / adenylate cyclase binding / ATP binding / magnesium ion binding / manganese ion binding / protein heterodimerization activity
Processes
activation of phospholipase C activity / activation of protein kinase A activity / adenylate cyclase-activating G-protein coupled receptor signaling pathway / adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway / adenylate cyclase-modulating G-protein coupled receptor signaling pathway / cAMP biosynthetic process / cAMP-mediated signaling / cellular response to forskolin / cellular response to glucagon stimulus / energy reserve metabolic process / epidermal growth factor receptor signaling pathway / fibroblast growth factor receptor signaling pathway / innate immune response / neurotrophin TRK receptor signaling pathway / renal water homeostasis / signal transduction / small molecule metabolic process / synaptic transmission / transmembrane transport / water transport
Components
cytoplasm / dendrite / integral component of plasma membrane / intracellular / membrane / membrane raft / plasma membrane
General Function
Protein heterodimerization activity
Specific Function
Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling (PubMed:15385642). Down-stream signaling cascades mediate changes in gene expression patterns and lead to increased IL6 production. Functions in signaling cascades downstream of the muscarinic acetylcholine receptors (By similarity).
Pfam Domain Function
Transmembrane Regions
46-66 76-96 108-128 133-153 159-179 187-207 602-622 628-652 680-701 734-755 763-780 801-821
Cellular Location
Membrane
Gene sequence
>lcl|BSEQ0012604|Adenylate cyclase type 2 (ADCY2)
ATGTGGCAGGAGGCGATGCGGCGCCGCCGCTACCTGCGGGACCGCTCCGAGGAGGCGGCG
GGCGGCGGAGACGGGCTGCCGCGGTCCCGGGACTGGCTCTACGAGTCCTACTACTGCATG
AGCCAGCAGCACCCGCTCATCGTCTTCCTGCTGCTCATCGTCATGGGCTCCTGCCTCGCC
CTGCTCGCCGTCTTCTTCGCGCTCGGGCTGGAAGTTGAAGACCATGTGGCGTTTCTAATA
ACAGTTCCAACTGCCCTGGCGATTTTCTTTGCGATATTTATCCTGGTCTGCATCGAGTCT
GTGTTTAAGAAGCTGCTGCGCCTCTTCTCGTTGGTGATATGGATATGCCTTGTTGCCATG
GGATACCTGTTCATGTGTTTTGGAGGCACCGTCTCTCCCTGGGACCAGGTATCGTTCTTC
CTCTTCATCATCTTCGTGGTGTACACCATGCTGCCCTTCAACATGCGAGACGCCATCATT
GCCAGCGTCCTCACCTCCTCCTCCCACACCATCGTGCTTAGCGTCTGCCTGTCTGCAACA
CCGGGAGGCAAGGAGCACCTGGTCTGGCAGATCCTGGCCAATGTGATCATTTTCATCTGT
GGGAACCTGGCGGGAGCCTACCATAAGCACCTCATGGAACTCGCTCTTCAGCAAACATAT
CAGGACACCTGTAATTGCATCAAGTCGCGGATCAAGTTGGAATTTGAAAAACGTCAACAG
GAGCGGCTTCTGCTCTCCCTGCTGCCGGCCCACATCGCCATGGAGATGAAAGCGGAGATC
ATCCAGAGGCTGCAGGGCCCCAAGGCGGGCCAGATGGAGAACACAAATAACTTCCACAAC
CTGTATGTGAAGCGGCATACAAACGTGAGCATCTTATACGCTGACATCGTTGGCTTTACC
CGGCTGGCAAGTGACTGCTCCCCGGGAGAACTAGTCCACATGCTGAATGAGCTCTTTGGA
AAGTTTGATCAAATTGCAAAGGAGAATGAATGCATGAGAATTAAAATTTTAGGAGACTGC
TACTACTGTGTATCTGGACTCCCTATATCTCTCCCTAACCATGCCAAGAACTGTGTGAAA
ATGGGGCTGGACATGTGTGAAGCCATAAAGAAAGTGAGGGATGCTACTGGAGTTGATATC
AACATGCGCGTGGGCGTGCATTCTGGGAATGTCCTGTGTGGCGTGATTGGTCTGCAGAAG
TGGCAATATGATGTGTGGTCACATGATGTGACCTTGGCCAACCACATGGAAGCTGGAGGG
GTCCCTGGACGTGTTCACATTTCTTCTGTCACCCTGGAGCACTTGAATGGCGCTTATAAA
GTGGAGGAGGGAGATGGTGACATTAGGGACCCATATTTAAAACAGCACCTGGTGAAAACC
TACTTTGTGATCAACCCCAAGGGAGAACGACGGAGCCCCCAGCATCTCTTCAGACCTCGC
CACACCCTTGATGGAGCCAAAATGAGGGCCTCGGTCCGCATGACCCGGTACTTGGAGTCC
TGGGGGGCAGCCAAGCCCTTTGCACACCTACATCACAGGGACAGCATGACCACAGAGAAC
GGCAAGATCAGCACCACGGATGTACCCATGGGTCAGCATAATTTTCAAAATCGCACCTTA
AGAACCAAGTCACAAAAGAAGAGATTTGAAGAAGAATTGAATGAAAGGATGATTCAAGCA
ATTGATGGGATTAATGCACAGAAGCAATGGCTCAAGTCTGAAGACATTCAGAGAATCTCA
CTGCTTTTCTATAACAAAGTACTAGAAAAAGAGTACCGGGCCACGGCACTGCCAGCGTTC
AAGTATTATGTGACTTGTGCCTGTCTCATATTCTTCTGCATCTTCATTGTGCAGATTCTC
GTGCTGCCAAAAACGTCCGTCCTGGGCATCTCCTTTGGGGCTGCGTTTCTCTTGCTGGCC
TTCATCCTCTTCGTCTGCTTTGCTGGACAGCTTCTGCAATGCAGCAAAAAAGCCTCTCCC
CTGCTCATGTGGCTTTTGAAGTCCTCGGGCATCATTGCCAACCGCCCCTGGCCACGGATC
TCTCTCACGATCATCACCACAGCCATCATATTAATGATGGCCGTGTTCAACATGTTTTTC
CTGAGTGACTCAGAGGAAACAATCCCTCCAACTGCCAACACAACAAACACAAGCTTTTCA
GCCTCAAATAATCAGGTGGCGATTCTGCGTGCGCAGAATTTATTTTTCCTCCCGTACTTT
ATCTACAGCTGCATTCTGGGACTGATATCCTGTTCCGTGTTCCTGCGGGTAAACTATGAG
CTGAAGATGTTGATCATGATGGTGGCCTTGGTGGGCTACAACACCATCCTACTCCACACC
CACGCCCACGTCCTGGGCGACTACAGCCAGGTCTTATTTGAGAGACCAGGCATTTGGAAA
GACCTGAAGACCATGGGCTCTGTGTCTCTCTCTATATTCTTCATCACACTGCTTGTTCTG
GGTAGACAGAATGAATATTACTGTAGGTTAGACTTCTTATGGAAGAACAAATTCAAAAAA
GAGCGGGAGGAGATAGAGACCATGGAGAACCTGAACCGCGTGCTGCTGGAGAACGTGCTT
CCCGCGCACGTGGCTGAGCACTTCCTGGCCAGGAGCCTGAAGAATGAGGAGCTATACCAC
CAGTCCTATGACTGCGTCTGCGTCATGTTTGCCTCCATTCCGGATTTCAAAGAATTTTAT
ACAGAATCCGACGTGAACAAGGAGGGCTTGGAATGCCTTCGGCTCCTGAACGAGATCATC
GCTGACTTTGATGATCTTCTTTCCAAGCCAAAATTCAGTGGAGTTGAAAAGATTAAGACC
ATTGGCAGCACATACATGGCAGCAACAGGTCTGAGCGCTGTGCCCAGCCAGGAGCACTCC
CAGGAGCCCGAGCGGCAGTACATGCACATTGGCACCATGGTGGAGTTTGCTTTTGCCCTG
GTAGGGAAGCTGGATGCCATCAACAAGCACTCCTTCAACGACTTCAAATTGCGAGTGGGT
ATTAACCATGGACCTGTGATAGCTGGTGTGATTGGAGCTCAGAAGCCACAATATGATATC
TGGGGCAACACTGTCAATGTGGCCAGTAGGATGGACAGCACCGGAGTCCTGGACAAAATA
CAGGTTACCGAGGAGACGAGCCTCGTCCTGCAGACCCTCGGATACACGTGCACCTGTCGA
GGAATAATCAACGTGAAAGGAAAGGGGGACCTGAAGACGTACTTTGTAAACACAGAAATG
TCAAGGTCCCTTTCCCAGAGCAACGTGGCATCCTGA
Chromosome Location
5
Locus
5p15.3
External Identifiers
ResourceLink
UniProtKB IDQ08462
UniProtKB Entry NameADCY2_HUMAN
GenBank Protein ID33150814
GenBank Gene IDAF410885
HGNC IDHGNC:233
General References
  1. 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 TO, 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. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [Article]
  2. Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [Article]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  4. Kikuno R, Nagase T, Ishikawa K, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Jun 30;6(3):197-205. [Article]
  5. Stengel D, Parma J, Gannage MH, Roeckel N, Mattei MG, Barouki R, Hanoune J: Different chromosomal localization of two adenylyl cyclase genes expressed in human brain. Hum Genet. 1992 Sep-Oct;90(1-2):126-30. [Article]
  6. Hellevuo K, Yoshimura M, Kao M, Hoffman PL, Cooper DM, Tabakoff B: A novel adenylyl cyclase sequence cloned from the human erythroleukemia cell line. Biochem Biophys Res Commun. 1993 Apr 15;192(1):311-8. [Article]
  7. Cote M, Guillon G, Payet MD, Gallo-Payet N: Expression and regulation of adenylyl cyclase isoforms in the human adrenal gland. J Clin Endocrinol Metab. 2001 Sep;86(9):4495-503. [Article]
  8. Ding Q, Gros R, Gray ID, Taussig R, Ferguson SS, Feldman RD: Raf kinase activation of adenylyl cyclases: isoform-selective regulation. Mol Pharmacol. 2004 Oct;66(4):921-8. [Article]
  9. Bogard AS, Xu C, Ostrom RS: Human bronchial smooth muscle cells express adenylyl cyclase isoforms 2, 4, and 6 in distinct membrane microdomains. J Pharmacol Exp Ther. 2011 Apr;337(1):209-17. doi: 10.1124/jpet.110.177923. Epub 2011 Jan 12. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB068432',5'-DIDEOXY-ADENOSINE 3'-MONOPHOSPHATEexperimentalunknownDetails
DB02587Colforsinexperimental, investigationalunknownDetails
DB09121Aurothioglucoseapproved, withdrawnunknownDetails