Protein detail

ADCY7

Adenylate cyclase type 7 (EC 4.6.1.1) (ATP pyrophosphate-lyase 7) (Adenylate cyclase type VII) (Adenylyl cyclase 7) (Cyclic di-AMP synthase ADCY7) (EC 2.7.7.85)

Protein symbol
ADCY7
UniProt ID
EVMP score
0.50
Frequency
1
Transmembrane count
12
Protein classification
EnzymesMetabolic proteinsPredicted intracellular proteinsPredicted membrane proteins
EVMP score: annotation confidence score.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information
Protein Names
Adenylate cyclase type 7 (EC 4.6.1.1) (ATP pyrophosphate-lyase 7) (Adenylate cyclase type VII) (Adenylyl cyclase 7) (Cyclic di-AMP synthase ADCY7) (EC 2.7.7.85)
Protein Class
EnzymesMetabolic proteinsPredicted intracellular proteinsPredicted membrane proteins
Protein Function
  • Enzymes
  • Predicted intracellular proteins
  • ENZYME proteins:Lyases
Transmembrane
34..54; Helical; 63..83; Helical; 95..117; Helical; 122..142; Helical; 147..167; Helical; 176..196; Helical; 595..615; Helical; 620..640; Helical; 669..688; Helical; 718..737; Helical; 746..773; Helical; 794..814; Helical
Transmembrane Count
12
Entrez Gene Symbol
Gene Synonym
AC7KIAA0037
Gene Description
Adenylate cyclase 7
Chromosome
16
Position
50246137-50318135
Frequency
1
EVMP Score
0.50
Fluorescence & Localization
Function & Pathway
Protein Function
  • Enzymes
  • Predicted intracellular proteins
  • ENZYME proteins:Lyases
KEGG
Reactome
Mediation Categories
Clinical-translation mediationFusion and delivery mediationImmune mediationMetabolism mediationReceptor-signaling mediation
Relations & Evidence

Enzyme-Mediated Modification

0 records.

Ligand-Receptor Signaling

14 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
transmembranetransmembraneOmniPathNoNoNoNoNo
cell_surfacecell_surfaceSurfaceomeNoNoNoNoNo
cell_surfacecell_surfaceOmniPathNoNoNoNoNo
transmembranetransmembrane_predictedPhobiusNoNoNoNoNo
Page 2 of 2Previous

Regulatory Interaction Network

1 record.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
KPCDQ05655ADCY7P51828YesYesNoPhosphoPointSIGNORHPRDSPIKE_LCSPIKESIGNOR:12454008SPIKE_LC:17185372HPRD:12454008SPIKE:17185372

Protein Complex Composition

0 records.

Isolation & Detection Technology

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
PRotein Organic Solvent Precipitation;Differential UltracentrifugationMass spectrometry132384937
Sequence, Structure & Domains

Sequences

Length
1,080
Mass
120,308
Sequence
MPAKGRYFLNEGEEGPDQDALYEKYQLTSQHGPLLLTLLLVAATACVALIIIAFSQGDPSRHQAILGMAFLVLAVFAALSVLMYVECLLRRWLRALALLTWACLVALGYVLVFDAWTKAACAWEQVPFFLFIVFVVYTLLPFSMRGAVAVGAVSTASHLLVLGSLMGGFTTPSVRVGLQLLANAVIFLCGNLTGAFHKHQMQDASRDLFTYTVKCIQIRRKLRIEKRQQENLLLSVLPAHISMGMKLAIIERLKEHGDRRCMPDNNFHSLYVKRHQNVSILYADIVGFTQLASDCSPKELVVVLNELFGKFDQIAKANECMRIKILGDCYYCVSGLPVSLPTHARNCVKMGLDMCQAIKQVREATGVDINMRVGIHSGNVLCGVIGLRKWQYDVWSHDVSLANRMEAAGVPGRVHITEATLKHLDKAYEVEDGHGQQRDPYLKEMNIRTYLVIDPRSQQPPPPSQHLPRPKGDAALKMRASVRMTRYLESWGAARPFAHLNHRESVSSGETHVPNGRRPKSVPQRHRRTPDRSMSPKGRSEDDSYDDEMLSAIEGLSSTRPCCSKSDDFYTFGSIFLEKGFEREYRLAPIPRARHDFACASLIFVCILLVHVLLMPRTAALGVSFGLVACVLGLVLGLCFATKFSRCCPARGTLCTISERVETQPLLRLTLAVLTIGSLLTVAIINLPLMPFQVPELPVGNETGLLAASSKTRALCEPLPYYTCSCVLGFIACSVFLRMSLEPKVVLLTVALVAYLVLFNLSPCWQWDCCGQGLGNLTKPNGTTSGTPSCSWKDLKTMTNFYLVLFYITLLTLSRQIDYYCRLDCLWKKKFKKEHEEFETMENVNRLLLENVLPAHVAAHFIGDKLNEDWYHQSYDCVCVMFASVPDFKVFYTECDVNKEGLECLRLLNEIIADFDELLLKPKFSGVEKIKTIGSTYMAAAGLSVASGHENQELERQHAHIGVMVEFSIALMSKLDGINRHSFNSFRLRVGINHGPVIAGVIGARKPQYDIWGNTVNVASRMESTGELGKIQVTEETCTILQGLGYSCECRGLINVKGKGELRTYFVCTDTAKFQGLGLN

3D Structural Models

Domain & Motif Annotations

Compositional Bias
515..529; Basic 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)
279..406; Guanylate cyclase 1; 879..1023; Guanylate cyclase 2
Region
454..474; Disordered; 477..482; Mediates regulation of adenylate cyclase activity by C5 alpha-induced G- beta and gamma pathway; 491..499; Mediates regulation of adenylate cyclase activity by sphingosine 1-phosphate-induced G alpha 13 pathway; 504..546; Disordered; 506..584; Modulates adenylate cyclase activity by modulating the binding of G(s)alpha to the high-affinity G(s)alpha binding site in 7C1a/7C2
Protein Families
Adenylyl cyclase class-4/guanylyl cyclase family
Sequence Similarities
Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
Clinical Relevance