Adenylate cyclase type 8

Details

Name
Adenylate cyclase type 8
Synonyms
  • 4.6.1.1
  • AC8
  • Adenylate cyclase type VIII
  • Adenylyl cyclase 8
  • ATP pyrophosphate-lyase 8
  • Ca(2+)/calmodulin-activated adenylyl cyclase
Gene Name
ADCY8
Organism
Humans
Amino acid sequence
>lcl|BSEQ0052750|Adenylate cyclase type 8
MELSDVRCLTGSEELYTIHPTPPAGDGRSASRPQRLLWQTAVRHITEQRFIHGHRGGSGS
GSGGSGKASDPAGGGPNHHAPQLSGDSALPLYSLGPGERAHSTCGTKVFPERSGSGSASG
SGGGGDLGFLHLDCAPSNSDFFLNGGYSYRGVIFPTLRNSFKSRDLERLYQRYFLGQRRK
SEVVMNVLDVLTKLTLLVLHLSLASAPMDPLKGILLGFFTGIEVVICALVVVRKDTTSHT
YLQYSGVVTWVAMTTQILAAGLGYGLLGDGIGYVLFTLFATYSMLPLPLTWAILAGLGTS
LLQVILQVVIPRLAVISINQVVAQAVLFMCMNTAGIFISYLSDRAQRQAFLETRRCVEAR
LRLETENQRQERLVLSVLPRFVVLEMINDMTNVEDEHLQHQFHRIYIHRYENVSILFADV
KGFTNLSTTLSAQELVRMLNELFARFDRLAHEHHCLRIKILGDCYYCVSGLPEPRQDHAH
CCVEMGLSMIKTIRYVRSRTKHDVDMRIGIHSGSVLCGVLGLRKWQFDVWSWDVDIANKL
ESGGIPGRIHISKATLDCLNGDYNVEEGHGKERNEFLRKHNIETYLIKQPEDSLLSLPED
IVKESVSSSDRRNSGATFTEGSWSPELPFDNIVGKQNTLAALTRNSINLLPNHLAQALHV
QSGPEEINKRIEHTIDLRSGDKLRREHIKPFSLMFKDSSLEHKYSQMRDEVFKSNLVCAF
IVLLFITAIQSLLPSSRVMPMTIQFSILIMLHSALVLITTAEDYKCLPLILRKTCCWINE
TYLARNVIIFASILINFLGAILNILWCDFDKSIPLKNLTFNSSAVFTDICSYPEYFVFTG
VLAMVTCAVFLRLNSVLKLAVLLIMIAIYALLTETVYAGLFLRYDNLNHSGEDFLGTKEV
SLLLMAMFLLAVFYHGQQLEYTARLDFLWRVQAKEEINEMKELREHNENMLRNILPSHVA
RHFLEKDRDNEELYSQSYDAVGVMFASIPGFADFYSQTEMNNQGVECLRLLNEIIADFDE
LLGEDRFQDIEKIKTIGSTYMAVSGLSPEKQQCEDKWGHLCALADFSLALTESIQEINKH
SFNNFELRIGISHGSVVAGVIGAKKPQYDIWGKTVNLASRMDSTGVSGRIQVPEETYLIL
KDQGFAFDYRGEIYVKGISEQEGKIKTYFLLGRVQPNPFILPPRRLPGQYSLAAVVLGLV
QSLNRQRQKQLLNENNNTGIIKGHYNRRTLLSPSGTEPGAQAEGTDKSDLP
Number of residues
1251
Molecular Weight
140120.79
Theoretical pI
Not Available
GO Classification
Functions
actin binding / adenylate cyclase activity / ATP binding / calcium- and calmodulin-responsive adenylate cyclase activity / calmodulin binding / metal ion binding / protein dimerization activity / protein heterodimerization activity / protein homodimerization activity / protein phosphatase 2A binding
Processes
activation of protein kinase A activity / adenylate cyclase-activating G protein-coupled receptor signaling pathway / cAMP biosynthetic process / cellular response to calcium ion / cellular response to forskolin / cellular response to glucagon stimulus / cellular response to glucose stimulus / cellular response to morphine / G protein-coupled opioid receptor signaling pathway / glucose homeostasis / glucose mediated signaling pathway / intracellular signal transduction / learning or memory / locomotory behavior / long-term memory / memory / neuroinflammatory response / positive regulation of CREB transcription factor activity / positive regulation of cytosolic calcium ion concentration / positive regulation of insulin secretion involved in cellular response to glucose stimulus / positive regulation of long-term synaptic depression / positive regulation of long-term synaptic potentiation / positive regulation of synaptic plasticity / protein complex oligomerization / protein homooligomerization / regulation of cellular response to stress / regulation of cytosolic calcium ion concentration / regulation of insulin secretion / signal transduction
Components
apical plasma membrane / axon / basolateral plasma membrane / caveola / clathrin-coated pit / clathrin-coated vesicle membrane / dendrite / excitatory synapse / glutamatergic synapse / hippocampal mossy fiber to CA3 synapse / integral component of plasma membrane / integral component of presynaptic membrane / membrane / membrane raft / neuronal cell body membrane / plasma membrane / plasma membrane raft / postsynaptic density / presynaptic active zone / Schaffer collateral - CA1 synapse
General Function
Catalyzes the formation of cAMP in response to calcium entry leadings to cAMP signaling activation that affect processes suche as synaptic plasticity and insulin secretion. Plays a role in many brain functions, such as learning, memory, drug addiction, and anxiety modulation through regulation of synaptic plasticity by modulating long-term memory and long-term potentiation (LTP) through CREB transcription factor activity modulation. Plays a central role in insulin secretion by controlling glucose homeostasis through glucagon-like peptide 1 and glucose signaling pathway and maintains insulin secretion through calcium-dependent PKA activation leading to vesicle pool replenishment. Also, allows PTGER3 to induce potentiation of PTGER4-mediated PLA2 secretion by switching from a negative to a positive regulation, during the IL1B induced-dedifferentiation of smooth muscle cells.
Specific Function
Actin binding
Pfam Domain Function
Transmembrane Regions
183-203 212-232 247-267 274-294 296-316 321-341 716-736 738-758 787-807 831-851 861-881 894-914
Cellular Location
Cell membrane
Gene sequence
>lcl|BSEQ0052751|Adenylate cyclase type 8 (ADCY8)
ATGGAGCTCTCCGATGTGCGCTGCCTTACAGGCAGCGAGGAACTCTACACCATCCACCCG
ACGCCCCCGGCCGGCGACGGCAGGAGCGCCTCCCGGCCGCAGCGGCTGCTGTGGCAGACG
GCGGTGCGACACATCACGGAGCAGCGCTTCATTCACGGGCACCGGGGAGGCAGCGGCAGC
GGGAGTGGAGGCTCGGGCAAAGCCTCGGACCCTGCGGGCGGCGGCCCCAACCACCACGCG
CCGCAGCTGTCAGGCGACTCGGCGCTGCCCCTCTACTCGCTGGGCCCGGGAGAGCGAGCG
CACAGCACCTGCGGCACCAAAGTCTTCCCGGAACGCAGCGGGAGCGGCAGTGCCAGCGGC
AGCGGAGGCGGGGGCGACCTGGGCTTCCTGCACCTTGACTGTGCCCCTAGCAACTCGGAT
TTCTTTCTTAATGGGGGCTATAGCTACCGAGGGGTCATTTTCCCCACCCTGCGCAACTCC
TTCAAATCTCGGGATTTGGAACGCCTCTACCAGCGCTATTTCTTGGGCCAAAGGCGCAAA
TCGGAAGTGGTGATGAACGTGCTGGACGTGCTGACCAAACTCACTCTCTTGGTCCTACAC
TTGAGCCTGGCCTCGGCCCCCATGGACCCGCTCAAGGGCATCCTGCTGGGCTTCTTCACC
GGCATTGAGGTAGTGATCTGCGCCCTGGTGGTGGTCAGGAAGGACACCACCTCCCACACG
TACCTGCAGTACAGCGGCGTGGTCACCTGGGTGGCCATGACCACCCAGATCCTGGCAGCA
GGCCTCGGCTACGGGCTCCTGGGCGACGGCATAGGCTACGTGCTCTTCACGCTCTTCGCC
ACCTACAGTATGCTGCCGCTGCCGCTCACCTGGGCCATCCTGGCCGGCCTGGGCACCTCG
CTGCTGCAGGTCATCCTCCAAGTGGTCATACCCCGGCTGGCGGTCATTTCCATCAACCAG
GTTGTGGCCCAGGCAGTGCTATTCATGTGTATGAACACAGCTGGAATCTTCATCAGTTAC
CTGTCAGACCGGGCCCAGCGCCAAGCTTTCCTGGAGACTCGGAGGTGTGTGGAGGCCAGG
CTGCGCCTGGAGACAGAGAACCAAAGACAGGAGCGGCTCGTGCTTTCTGTGCTCCCCCGG
TTTGTTGTCCTGGAAATGATCAACGACATGACCAATGTGGAAGATGAGCACCTGCAGCAC
CAGTTCCATCGGATCTACATCCATCGCTATGAGAACGTCAGTATTCTTTTTGCAGATGTT
AAAGGATTTACCAACCTCTCCACGACCTTGTCTGCTCAGGAGCTGGTCAGGATGCTCAAC
GAGCTCTTTGCCAGATTTGATCGACTGGCCCATGAGCATCACTGCCTTCGTATTAAAATC
CTGGGGGACTGCTACTACTGCGTGTCTGGACTTCCTGAGCCCCGCCAGGACCATGCCCAC
TGCTGTGTTGAAATGGGTCTCAGCATGATCAAAACCATCAGGTATGTGCGGTCAAGGACA
AAACACGATGTTGACATGAGGATTGGAATCCACTCCGGCTCGGTGCTGTGCGGTGTTTTG
GGACTAAGGAAGTGGCAGTTTGATGTCTGGTCTTGGGATGTGGATATTGCAAACAAACTC
GAATCTGGAGGAATCCCTGGGAGGATTCACATTTCCAAAGCCACGCTGGACTGTCTCAAC
GGTGACTATAACGTGGAAGAGGGCCATGGTAAAGAGAGGAATGAATTCCTGAGGAAGCAT
AATATCGAAACTTACTTAATTAAGCAGCCTGAGGACAGTCTGCTGTCCTTGCCTGAAGAT
ATCGTCAAGGAGTCAGTGAGCTCCTCAGACCGGAGAAACAGTGGGGCCACATTCACTGAA
GGATCCTGGAGCCCTGAACTGCCCTTTGATAATATCGTGGGGAAACAGAATACTCTGGCT
GCCCTAACAAGAAATTCAATAAATCTGCTTCCAAACCATCTTGCACAAGCTTTGCATGTC
CAGTCTGGGCCTGAGGAAATTAACAAGAGAATAGAACATACCATCGACTTGCGGAGTGGC
GATAAATTGAGAAGAGAGCATATCAAGCCATTCTCACTGATGTTTAAAGACTCCAGCCTG
GAGCACAAGTATTCTCAAATGAGGGATGAAGTGTTCAAGTCAAACTTGGTCTGTGCATTT
ATCGTTCTTCTATTTATCACGGCAATACAAAGTTTGCTTCCTTCTTCAAGAGTGATGCCA
ATGACCATCCAGTTCTCCATTCTGATTATGCTGCACTCGGCTCTGGTCCTCATCACCACA
GCAGAGGATTATAAATGTTTGCCCCTCATCCTCCGGAAAACTTGCTGTTGGATTAATGAG
ACCTATTTGGCCCGGAACGTCATCATCTTTGCATCCATTTTGATTAATTTCCTGGGTGCC
ATCTTAAATATCCTGTGGTGTGATTTTGACAAGTCGATACCCTTGAAGAACCTGACTTTC
AATTCCTCAGCTGTGTTTACAGATATCTGCTCCTACCCAGAGTACTTTGTCTTCACGGGG
GTGTTGGCCATGGTGACCTGTGCAGTTTTCCTCCGGCTGAACTCCGTCCTGAAGCTGGCA
GTGCTGCTGATCATGATTGCCATCTATGCCCTGCTCACTGAGACCGTCTACGCAGGCCTC
TTTCTGCGTTATGACAACCTCAACCACAGTGGAGAAGATTTCCTGGGGACCAAGGAGGTA
TCACTGCTACTGATGGCCATGTTCCTCCTGGCTGTGTTCTACCATGGACAGCAGCTGGAG
TACACAGCCCGCCTGGACTTCCTTTGGCGAGTACAGGCCAAAGAGGAGATCAATGAGATG
AAGGAGCTGAGGGAACACAATGAGAACATGCTCCGGAATATCTTACCCAGCCATGTGGCC
CGCCATTTCCTAGAGAAGGACCGAGACAATGAGGAGCTGTATTCTCAATCCTATGATGCT
GTTGGGGTGATGTTTGCCTCCATCCCAGGATTTGCGGACTTTTACTCTCAGACTGAAATG
AATAACCAGGGAGTGGAATGCCTGCGCTTGCTCAATGAGATCATTGCTGACTTCGATGAG
TTGCTTGGTGAAGACCGATTTCAAGACATTGAAAAGATTAAGACCATTGGCAGCACCTAC
ATGGCCGTGTCAGGCCTGTCACCTGAAAAACAGCAATGTGAAGACAAGTGGGGACATTTG
TGTGCTCTGGCTGACTTCTCACTCGCCCTGACAGAAAGCATACAGGAGATCAACAAGCAT
TCATTCAACAATTTTGAACTCCGGATTGGCATCAGCCACGGCTCAGTGGTAGCTGGCGTT
ATCGGCGCTAAGAAACCACAGTATGACATTTGGGGCAAAACTGTGAACCTGGCAAGCCGA
ATGGACAGCACGGGGGTTAGTGGCCGGATCCAAGTCCCAGAGGAGACCTATCTCATCCTG
AAGGACCAGGGCTTTGCCTTTGATTACCGAGGGGAGATCTATGTGAAGGGTATCAGTGAA
CAGGAAGGAAAAATCAAAACGTACTTTCTTCTGGGAAGAGTCCAACCCAACCCATTCATC
TTGCCCCCAAGAAGACTGCCTGGGCAGTACTCCCTGGCCGCGGTTGTCCTGGGACTTGTC
CAGTCCCTCAATAGGCAAAGGCAGAAGCAGCTACTCAATGAGAACAACAACACAGGAATC
ATCAAGGGTCATTACAACCGGCGGACTTTGTTGTCACCCAGCGGCACAGAGCCTGGAGCC
CAGGCTGAAGGCACCGACAAATCTGATTTGCCATAA
Chromosome Location
8
Locus
8q24.22
External Identifiers
ResourceLink
UniProtKB IDP40145
UniProtKB Entry NameADCY8_HUMAN
HGNC IDHGNC:239
General References
  1. Defer N, Marinx O, Stengel D, Danisova A, Iourgenko V, Matsuoka I, Caput D, Hanoune J: Molecular cloning of the human type VIII adenylyl cyclase. FEBS Lett. 1994 Aug 29;351(1):109-13. [Article]
  2. Parma J, Stengel D, Gannage MH, Poyard M, Barouki R, Hanoune J: Sequence of a human brain adenylyl cyclase partial cDNA: evidence for a consensus cyclase specific domain. Biochem Biophys Res Commun. 1991 Aug 30;179(1):455-62. [Article]
  3. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [Article]
  4. Raoux M, Vacher P, Papin J, Picard A, Kostrzewa E, Devin A, Gaitan J, Limon I, Kas MJ, Magnan C, Lang J: Multilevel control of glucose homeostasis by adenylyl cyclase 8. Diabetologia. 2015 Apr;58(4):749-57. doi: 10.1007/s00125-014-3445-z. Epub 2014 Nov 19. [Article]
  5. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02587Colforsinexperimental, investigationalyesactivatorDetails