P84309 · ADCY5_MOUSE

  • Protein
    Adenylate cyclase type 5
  • Gene
    Adcy5
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. Mediates signaling downstream of ADRB1. Regulates the increase of free cytosolic Ca2+ in response to increased blood glucose levels and contributes to the regulation of Ca2+-dependent insulin secretion.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro).

Activity regulation

Activated by G(s) G alpha protein GNAS (By similarity).
Inhibited by G(i) G alpha protein GNAI1 (By similarity).
Activity is further increased by interaction with the G-protein beta and gamma subunit complex formed by GNB1 and GNG2 (By similarity).
Activated by forskolin (By similarity).
Is not activated by calmodulin. Inhibited by adenosine and ATP analogs (By similarity).
Inhibited by calcium ions, already at micromolar concentrations (By similarity).
Phosphorylation by RAF1 results in its activation (By similarity).

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site475Mg2+ 1 (UniProtKB | ChEBI); catalytic
Binding site475Mg2+ 2 (UniProtKB | ChEBI); catalytic
Binding site475-480ATP (UniProtKB | ChEBI)
Binding site476Mg2+ 2 (UniProtKB | ChEBI); catalytic
Binding site517-519ATP (UniProtKB | ChEBI)
Binding site519Mg2+ 1 (UniProtKB | ChEBI); catalytic
Binding site519Mg2+ 2 (UniProtKB | ChEBI); catalytic
Binding site563ATP (UniProtKB | ChEBI)
Binding site1124ATP (UniProtKB | ChEBI)
Binding site1198-1200ATP (UniProtKB | ChEBI)
Binding site1205-1209ATP (UniProtKB | ChEBI)
Binding site1245ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcilium
Cellular Componentendosome
Cellular Componentmembrane
Cellular Componentplasma membrane
Molecular Functionadenylate cyclase activity
Molecular Functionadenylate cyclase binding
Molecular FunctionATP binding
Molecular Functioncalcium- and calmodulin-responsive adenylate cyclase activity
Molecular Functionmetal ion binding
Molecular Functionscaffold protein binding
Biological Processadenylate cyclase-activating dopamine receptor signaling pathway
Biological Processadenylate cyclase-activating G protein-coupled receptor signaling pathway
Biological Processadenylate cyclase-inhibiting dopamine receptor signaling pathway
Biological Processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
Biological ProcesscAMP biosynthetic process
Biological Processcellular response to forskolin
Biological ProcessG protein-coupled adenosine receptor signaling pathway
Biological Processintracellular signal transduction
Biological Processlocomotory behavior
Biological Processneuromuscular process controlling balance
Biological Processpositive regulation of cytosolic calcium ion concentration
Biological Processregulation of insulin secretion involved in cellular response to glucose stimulus

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Adenylate cyclase type 5
  • EC number
  • Alternative names
    • ATP pyrophosphate-lyase 5
    • Adenylate cyclase type V
    • Adenylyl cyclase 5

Gene names

    • Name
      Adcy5

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P84309
  • Secondary accessions
    • Q3TU67
    • Q3UH09
    • Q5BL06

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Multi-pass membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-196Cytoplasmic
Transmembrane197-217Helical
Transmembrane243-263Helical
Transmembrane269-289Helical
Transmembrane300-320Helical
Transmembrane326-346Helical
Transmembrane375-395Helical
Topological domain396-763Cytoplasmic
Transmembrane764-784Helical
Transmembrane790-810Helical
Transmembrane837-857Helical
Topological domain858-910Extracellular
Transmembrane911-931Helical
Transmembrane936-956Helical
Transmembrane985-1005Helical
Topological domain1006-1262Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for chain, modified residue, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00001956951-1262Adenylate cyclase type 5
Modified residue23Omega-N-methylarginine
Modified residue97Phosphoserine
Modified residue156Phosphoserine
Glycosylation239N-linked (GlcNAc...) asparagine
Modified residue667Phosphoserine
Modified residue755Phosphoserine
Glycosylation834N-linked (GlcNAc...) asparagine
Glycosylation871N-linked (GlcNAc...) asparagine
Glycosylation888N-linked (GlcNAc...) asparagine
Glycosylation973N-linked (GlcNAc...) asparagine
Modified residue1012Phosphothreonine

Post-translational modification

Phosphorylated by RAF1.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Interacts with GNAS, GNB1 and GNG2 (By similarity).
Part of a complex containing AKAP5, ADCY6, PDE4C and PKD2 (PubMed:21670265).
Interacts with RAF1 (By similarity).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, compositional bias, domain, coiled coil.

TypeIDPosition(s)Description
Region1-194Disordered
Compositional bias50-71Polar residues
Compositional bias104-118Basic and acidic residues
Compositional bias156-172Basic and acidic residues
Domain470-597Guanylate cyclase 1
Coiled coil1019-1045
Domain1072-1211Guanylate cyclase 2

Domain

The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain.

Sequence similarities

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

P84309-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    1,262
  • Mass (Da)
    139,122
  • Last updated
    2007-01-09 v2
  • Checksum
    342966E7CA67E28D
MSGSKSVSPPGYAAQTAASPAPRGGPEHRAAWGEADSRANGYPHAPGGSTRGSTKRSGGAVTPQQQQRLASRWRGGDDDEDPPLSGDDPLAGGFGFSFRSKSAWQERGGDDGGRGSRRQRRGAAGGGSTRAPPAGGSGSSAAAAAAAGGTEVRPRSVELGLEERRGKGRAAEELEPGTGIVEDGDGSEDGGSSVASGSGTGAVLSLGACCLALLQIFRSKKFPSDKLERLYQRYFFRLNQSSLTMLMAVLVLVCLVMLAFHAARPPLQIAYLAVLAAAVGVILIMAVLCNRAAFHQDHMGLACYALIAVVLAVQVVGLLLPQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSALHLAISLHTNSQDQFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGDYEVEPGCGGDRNAYLKEHSIETFLILSCTQKRKEEKAMIAKMNRQRTNSIGHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDKNAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLTFREPDLEKKYSKQVDDRFGAYVACASLVFLFICFVQITIVPHSLFMLSFYLSCFLLLALVVFVSVIYACVKLFPTPLQTLSRKIVRSKKNSTLVGVFTITLVFLSAFVNMFMCNSKNLVGCLAEEHNITVNQVNACHVMESAFNYSLGDEQGFCGSPQPNCNFPEYFTYSVLLSLLACSVFLQISCIGKLVLMLAIEFIYVLIVEVPGVTLFDNADLLVTANAIDFSNNGTSQCPEHATKVALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKLQATEEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIISEDRFRQLEKIKTIGSTYMAASGLNDSTYDKAGKTHIKAIADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNGGPPLS

P84309-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1259-1262: PPLS → LGHDGVVGKLKAGLGVSMELKGLLFHCGEVTPPHNVWGTGTGRRVACAILSPHLHAQRQCPVRETGLLTREARGHQARSSGSEQKKIFIK

Features

Showing features for sequence conflict, compositional bias, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict25in Ref. 2; AAH90846
Compositional bias50-71Polar residues
Compositional bias104-118Basic and acidic residues
Compositional bias156-172Basic and acidic residues
Sequence conflict686in Ref. 1; BAE28048
Sequence conflict924in Ref. 2; AAH90846
Alternative sequenceVSP_0222241259-1262in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK147649
EMBL· GenBank· DDBJ
BAE28048.1
EMBL· GenBank· DDBJ
mRNA
AK160942
EMBL· GenBank· DDBJ
BAE36104.1
EMBL· GenBank· DDBJ
mRNA
BC035550
EMBL· GenBank· DDBJ
-mRNA No translation available.
BC090846
EMBL· GenBank· DDBJ
AAH90846.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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