Protein detail

ADCY9

Adenylate cyclase type 9 (EC 4.6.1.1) (ATP pyrophosphate-lyase 9) (Adenylate cyclase type IX) (ACIX) (Adenylyl cyclase 9) (AC9)

Protein symbol
ADCY9
UniProt ID
EVMP score
0.50
Frequency
5
Transmembrane count
12
Protein classification
EnzymesMetabolic proteinsPredicted intracellular proteinsPredicted membrane proteins
Basic Information
Protein Names
Adenylate cyclase type 9 (EC 4.6.1.1) (ATP pyrophosphate-lyase 9) (Adenylate cyclase type IX) (ACIX) (Adenylyl cyclase 9) (AC9)
Protein Class
EnzymesMetabolic proteinsPredicted intracellular proteinsPredicted membrane proteins
Protein Function
  • Enzymes
  • Predicted intracellular proteins
  • ENZYME proteins:Lyases
Transmembrane
118..138; Helical; 142..162; Helical; 172..192; Helical; 216..235; Helical; 242..259; Helical; 281..301; Helical; 787..807; Helical; 819..839; Helical; 868..888; Helical; 892..912; Helical; 921..941; Helical; 976..996; Helical
Transmembrane Count
12
Entrez Gene Symbol
Gene Synonym
AC9
Gene Description
Adenylate cyclase 9
Chromosome
16
Position
3953387-4116442
Frequency
5
EVMP Score
0.50
Fluorescence & Localization
Tissue SpecificintestineCell SpecificColonocytes
Function & Pathway
Protein Function
  • Enzymes
  • Predicted intracellular proteins
  • ENZYME proteins:Lyases
KEGG
Reactome
Mediation Categories
Clinical-translation mediationFusion and delivery mediationMetabolism mediationReceptor-signaling mediation
Relations & Evidence

Enzyme-Mediated Modification

2 records.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
ADCY9CDK2P24941S610phosphorylationKEAKEA:17570479
ADCY9MAPK9P45984S610phosphorylationKEAKEA:17570479

Ligand-Receptor Signaling

22 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
transmembranetransmembraneUniProt_keywordNoNoNoNoNo
transmembranetransmembraneLOCATENoNoNoNoNo
transmembranetransmembraneRamilowski_locationNoNoNoNoNo
transmembranetransmembraneOmniPathNoNoNoNoNo
plasma_membraneplasma_membraneUniProt_locationNoNoNoNoNo
plasma_membraneplasma_membraneOmniPathNoNoNoNoNo
cell_surfacecell_surfaceSurfaceomeNoNoNoNoNo
cell_surfacecell_surfaceOmniPathNoNoNoNoNo
receptorreceptorscConnectNoYesNoNoNo
receptorreceptoriTALKNoYesNoNoNo
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Regulatory Interaction Network

4 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
GNAS3O95467ADCY9O60503YesYesNoCellTalkDBFantom5_LRdbiTALKKEGG-MEDICUStalklrSIGNORACSNWangLRdbSTRING_talklrEMBRACEACSN:9228084SIGNOR:29292367ACSN:21406690CellTalkDB:32196115
ALEXP84996ADCY9O60503YesYesNoCellTalkDBFantom5_LRdbiTALKKEGG-MEDICUStalklrSIGNORACSNWangLRdbSTRING_talklrEMBRACEACSN:9228084SIGNOR:29292367ACSN:21406690CellTalkDB:32196115
GNAS2P63092ADCY9O60503YesYesNoCellTalkDBFantom5_LRdbiTALKKEGG-MEDICUStalklrSIGNORACSNWangLRdbSTRING_talklrEMBRACEACSN:9228084SIGNOR:29292367ACSN:21406690CellTalkDB:32196115
GNAS1Q5JWF2ADCY9O60503YesYesNoCellTalkDBFantom5_LRdbiTALKKEGG-MEDICUStalklrSIGNORACSNWangLRdbSTRING_talklrEMBRACEACSN:9228084SIGNOR:29292367ACSN:21406690CellTalkDB:32196115

Protein Complex Composition

2 records.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
ADCY9NEMP1RGPD6RGPD8O14524O14715O60503Q996660:0:0:0hu.MAP2
ADCY9AREGO60503P155140:0hu.MAP2

Isolation & Detection Technology

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationMass spectrometry131805958
Sequence, Structure & Domains

Sequences

Length
1,353
Mass
150,701
Sequence
MASPPHQQLLHHHSTEVSCDSSGDSNSVRVKINPKQLSSNSHPKHCKYSISSSCSSSGDSGGVPRRVGGGGRLRRQKKLPQLFERASSRWWDPKFDSVNLEEACLERCFPQTQRRFRYALFYIGFACLLWSIYFAVHMRSRLIVMVAPALCFLLVCVGFFLFTFTKLYARHYAWTSLALTLLVFALTLAAQFQVLTPVSGRGDSSNLTATARPTDTCLSQVGSFSMCIEVLFLLYTVMHLPLYLSLCLGVAYSVLFETFGYHFRDEACFPSPGAGALHWELLSRGLLHGCIHAIGVHLFVMSQVRSRSTFLKVGQSIMHGKDLEVEKALKERMIHSVMPRIIADDLMKQGDEESENSVKRHATSSPKNRKKKSSIQKAPIAFRPFKMQQIEEVSILFADIVGFTKMSANKSAHALVGLLNDLFGRFDRLCEETKCEKISTLGDCYYCVAGCPEPRADHAYCCIEMGLGMIKAIEQFCQEKKEMVNMRVGVHTGTVLCGILGMRRFKFDVWSNDVNLANLMEQLGVAGKVHISEATAKYLDDRYEMEDGKVIERLGQSVVADQLKGLKTYLISGQRAKESRCSCAEALLSGFEVIDGSQVSSGPRGQGTASSGNVSDLAQTVKTFDNLKTCPSCGITFAPKSEAGAEGGAPQNGCQDEHKNSTKASGGPNPKTQNGLLSPPQEEKLTNSQTSLCEILQEKGRWAGVSLDQSALLPLRFKNIREKTDAHFVDVIKEDSLMKDYFFKPPINQFSLNFLDQELERSYRTSYQEEVIKNSPVKTFASPTFSSLLDVFLSTTVFLTLSTTCFLKYEAATVPPPPAALAVFSAALLLEVLSLAVSIRMVFFLEDVMACTKRLLEWIAGWLPRHCIGAILVSLPALAVYSHVTSEYETNIHFPVFTGSAALIAVVHYCNFCQLSSWMRSSLATVVGAGPLLLLYVSLCPDSSVLTSPLDAVQNFSSERNPCNSSVPRDLRRPASLIGQEVVLVFFLLLLLVWFLNREFEVSYRLHYHGDVEADLHRTKIQSMRDQADWLLRNIIPYHVAEQLKVSQTYSKNHDSGGVIFASIVNFSEFYEENYEGGKECYRVLNELIGDFDELLSKPDYSSIEKIKTIGATYMAASGLNTAQAQDGSHPQEHLQILFEFAKEMMRVVDDFNNNMLWFNFKLRVGFNHGPLTAGVIGTTKLLYDIWGDTVNIASRMDTTGVECRIQVSEESYRVLSKMGYDFDYRGTVNVKGKGQMKTYLYPKCTDHRVIPQHQLSISPDIRVQVDGSIGRSPTDEIANLVPSVQYVDKTSLGSDSSTQAKDAHLSPKRPWKEPVKAEERGRFGKAIEKDDCDETGIEEANELTKLNVSKSV

3D Structural Models

3D Structure
Electron microscopy (6)

Domain & Motif Annotations

Compositional Bias
16..27; Polar residues; 49..66; Low complexity; 359..374; Basic residues; 1292..1301; Polar residues; 1302..1326; Basic and acidic residues
Domain (CC)
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.
Domain (FT)
394..521; Guanylate cyclase 1; 1058..1198; Guanylate cyclase 2
Region
1..27; Disordered; 49..71; Disordered; 349..375; Disordered; 642..684; Disordered; 1292..1326; Disordered
Protein Families
Adenylyl cyclase class-4/guanylyl cyclase family
Sequence Similarities
Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
Clinical Relevance