Q9VW60 · ADCY2_DROME

Function

function

Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling.

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).

Features

Showing features for binding site.

113071002003004005006007008009001,0001,1001,2001,300
TypeIDPosition(s)Description
Binding site322Mg2+ 1 (UniProtKB | ChEBI); catalytic
Binding site322Mg2+ 2 (UniProtKB | ChEBI); catalytic
Binding site322-327ATP (UniProtKB | ChEBI)
Binding site323Mg2+ 2 (UniProtKB | ChEBI); catalytic
Binding site364-366ATP (UniProtKB | ChEBI)
Binding site366Mg2+ 1 (UniProtKB | ChEBI); catalytic
Binding site366Mg2+ 2 (UniProtKB | ChEBI); catalytic
Binding site410ATP (UniProtKB | ChEBI)
Binding site1162ATP (UniProtKB | ChEBI)
Binding site1242-1244ATP (UniProtKB | ChEBI)
Binding site1249-1253ATP (UniProtKB | ChEBI)
Binding site1289ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentplasma membrane
Molecular Functionadenylate cyclase activity
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Biological Processadenylate cyclase-activating G protein-coupled receptor signaling pathway
Biological Processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
Biological ProcesscAMP biosynthetic process
Biological Processinstar larval or pupal development
Biological Processintracellular signal transduction
Biological Processnegative regulation of multicellular organism growth
Biological Processresponse to starvation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Adenylate cyclase type 2
  • EC number
  • Alternative names
    • ATP pyrophosphate-lyase 2
    • Adenylyl cyclase 76E

Gene names

    • Name
      Ac76E
    • ORF names
      CG7978

Organism names

  • Taxonomic identifier
  • Strains
    • Canton-S
    • Berkeley
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora

Accessions

  • Primary accession
    Q9VW60
  • Secondary accessions
    • O77247
    • Q8MRK9

Proteomes

Organism-specific databases

Subcellular Location

Membrane
; Multi-pass membrane protein
Cell membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane, topological domain.

Type
IDPosition(s)Description
Transmembrane85-105Helical
Transmembrane113-133Helical
Transmembrane137-157Helical
Transmembrane178-198Helical
Transmembrane211-231Helical
Topological domain232-828Cytoplasmic
Transmembrane829-849Helical
Transmembrane851-871Helical
Transmembrane900-920Helical
Transmembrane963-983Helical
Transmembrane987-1007Helical
Transmembrane1024-1044Helical
Topological domain1045-1307Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for chain, glycosylation.

Type
IDPosition(s)Description
ChainPRO_00001957131-1307Adenylate cyclase type 2
Glycosylation934N-linked (GlcNAc...) asparagine
Glycosylation941N-linked (GlcNAc...) asparagine
Glycosylation948N-linked (GlcNAc...) asparagine
Glycosylation1019N-linked (GlcNAc...) asparagine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain317-444Guanylate cyclase 1
Region510-540Disordered
Compositional bias515-532Basic and acidic residues
Region579-633Disordered
Compositional bias594-617Basic and acidic residues
Compositional bias647-670Polar residues
Region647-693Disordered
Domain1110-1255Guanylate 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

  • Sequence status
    Complete
  • Length
    1,307
  • Mass (Da)
    142,817
  • Last updated
    2002-10-01 v3
  • Checksum
    D7EE45CF93F80161
MVNHNAETAKTGNGTNATANLIVKADGNATQPKAMTSSAARMNDALSASLADLSEQENGTTAEDIHLNDLYTRYRQRLRKSLFRSGLLTSLLACVVSIIIGIVYGQHLVQTMLLVLAALISGSILTALQFPAVLSSPAAALAFAIVTTFSLGTIAAITGDELAPLPMYALFLCIHSMLPISWPVSVVLALFMTAIHIVYRIGTSPDYAPNLPMLFGEIVMLASASVSGLYYRIMSDAAHNRTVDGTRTGIEQRVKLECEREQQEQLLLSVIPAYIAAEVKRSIMLKMADACQRAGGQASTSATRFHELHVQRHTNVTILFADIVNFTPLSSSLTASDLVKTLNDLFGRFDQIAQENQCLRIKILGDCYYCVSGLPISRPQHATNCVNMGLQMIDAIRHVREATGINVDMRIGIHTGNVLCGVLGLRKWQFDVWSDDVTLANHMESGGVAGRVHITKQTLDFLGDKFEVEQGEGGNRDAYLADHKVESYLIVPPKPAYTYSVPRVVECIEQNDPSPTTEETKEIKETDQSHEATDVADVLLPVTVAPPPAIVDEKMSPTSINSQEAPLHAPLASAASMSIKELSEEEDEADEATAVTEPLMHRDQDGKNDKEPKANGGHRGSGDSAASESVAKSAALSLPADDLLSMSGSESGISNSGAQAQSSNPASVTPTAAAPAGGAASNSLTVAEAPERSRRKLSVQGLMSFADRRRSSGAFIEGRKLSIHSGESFRSHAGHVTRNRPSSKMTKYVECWGADRPFANIAESKLVKNIGLASIAMIESNLLPPERKCFNFNFFGPPTELKPFTMWYRNTPREAMYRAQPDTHFRFDLICAFVLFLSLAVVQLIVIELNLALLGSLLASFVSLALFLYLSNMSVPDVHASTTERNGPGQVVASSRYLRLAMFVVVNILISSCAVFSVINYTVPDGVSKEPSSNQTILESNFSSVFVNSTLEDVQLWEIDYAIPIAPVFLYCCAISLAAISAFLRSGFILKLIAMLVAVIAQVTVLGYSDLFEMYNDANITHGLPLEIKGFLLLLVIILVLHTLDRQGEYVARTDFLWKAKLKVEQEEVETMRGINKILLENILPAHVATHFLHLERSTELYHESYSCVAVMFASIPNYKEFYDETDVNKQGLECLRLLNEIICDFDKLLLKPKFSGIEKIKTIASTYMCASGLRPGKEDGATDEKRTEEHNVVILVEFAIALMSILDSINRESFQRFRLRIGLNHGPVIAGVIGAQKPQYDIWSNTVNVASRMDSCGVMGRLQTTENTAKILMTAGYECECRGLTYVKGKGNLVTYFVKTPFDGKL

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
M9NDD2M9NDD2_DROMEAc76E1312

Sequence caution

The sequence AAM50201.1 differs from that shown. Reason: Erroneous initiation

Features

Showing features for compositional bias, sequence conflict.

Type
IDPosition(s)Description
Compositional bias515-532Basic and acidic residues
Sequence conflict538in Ref. 1; AAC62509
Compositional bias594-617Basic and acidic residues
Compositional bias647-670Polar residues
Sequence conflict679in Ref. 1; AAC62509
Sequence conflict1037in Ref. 1; AAC62509
Sequence conflict1183in Ref. 4; AAM50201

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF093454
EMBL· GenBank· DDBJ
AAC62509.1
EMBL· GenBank· DDBJ
mRNA
AE014296
EMBL· GenBank· DDBJ
AAF49089.3
EMBL· GenBank· DDBJ
Genomic DNA
AY119547
EMBL· GenBank· DDBJ
AAM50201.1
EMBL· GenBank· DDBJ
mRNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

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