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)

Entry name
ADCY7
UniProt ID
EVMP confidence score
0.50
Supporting publications (n)
1
Transmembrane count
12
Protein classification
EnzymesMetabolic proteinsPredicted intracellular proteinsPredicted membrane proteins
EVMP confidence score

Annotation confidence score; open for threshold definitions.

Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information13
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 (4)
EnzymesMetabolic proteinsPredicted intracellular proteinsPredicted membrane proteins
Protein Function (3)
  • 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 (2)
AC7KIAA0037
Gene Description
Adenylate cyclase 7
Chromosome
16
Position
50246137-50318135
Supporting publications (n)
1
EVMP confidence score
0.50
Fluorescence & Localization1
ADCY7 fluorescence
Function & Pathway7
Protein Function (3)
  • Enzymes
  • Predicted intracellular proteins
  • ENZYME proteins:Lyases
Mediation Categories (5)
Clinical-translation mediationFusion and delivery mediationImmune mediationMetabolism mediationReceptor-signaling mediation
Relations & Evidence16

Ligand-Receptor Signaling (14)

14 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
transmembranetransmembraneOmniPathNoNoNoNoNo
cell_surfacecell_surfaceSurfaceomeNoNoNoNoNo
cell_surfacecell_surfaceOmniPathNoNoNoNoNo
transmembranetransmembrane_predictedPhobiusNoNoNoNoNo
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Regulatory Interaction Network (1)

1 record.

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

Isolation & Detection Technology (1)

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
PRotein Organic Solvent Precipitation;Differential UltracentrifugationMass spectrometry132384937
Sequence, Structure & Domains9

Sequences

Length
1,080
Mass
120,308
Sequence
MPAKGRYFLNEGEEGPDQDALYEKYQLTSQHGPLLLTLLLVAATACVALIIIAFSQGDPSRHQAILGMAFLVLAVFAALSVLMYVECLLRRWLRALALLTWACLVALGYVLVFDAWTKAACAWEQVPFFLFIVFVVYTLLPFSMRGAVAVGAVSTASHLLVLGSLMGGFTTPSVRVGLQLLANAVIFLCGNLTGAFHKHQMQDASRDLFTYTVKCIQIRRKLRIEKRQQENLLLSVLPAHISMGMKLAIIERLKEHGDRRCMPDNNFHSLYVKRHQNVSILYADIVGFTQLASDCSPKELVVVLNELFGKFDQIAKANECMRIKILGDCYYCVSGLPVSLPTHARNCVKMGLDMCQAIKQVREATGVDINMRVGIHSGNVLCGVIGLRKWQYDVWSHDVSLANRMEAAGVPGRVHITEATLKHLDKAYEVEDGHGQQRDPYLKEMNIRTYLVIDPRSQQPPPPSQHLPRPKGDAALKMRASVRMTRYLESWGAARPFAHLNHRESVSSGETHVPNGRRPKSVPQRHRRTPDRSMSPKGRSEDDSYDDEMLSAIEGLSSTRPCCSKSDDFYTFGSIFLEKGFEREYRLAPIPRARHDFACASLIFVCILLVHVLLMPRTAALGVSFGLVACVLGLVLGLCFATKFSRCCPARGTLCTISERVETQPLLRLTLAVLTIGSLLTVAIINLPLMPFQVPELPVGNETGLLAASSKTRALCEPLPYYTCSCVLGFIACSVFLRMSLEPKVVLLTVALVAYLVLFNLSPCWQWDCCGQGLGNLTKPNGTTSGTPSCSWKDLKTMTNFYLVLFYITLLTLSRQIDYYCRLDCLWKKKFKKEHEEFETMENVNRLLLENVLPAHVAAHFIGDKLNEDWYHQSYDCVCVMFASVPDFKVFYTECDVNKEGLECLRLLNEIIADFDELLLKPKFSGVEKIKTIGSTYMAAAGLSVASGHENQELERQHAHIGVMVEFSIALMSKLDGINRHSFNSFRLRVGINHGPVIAGVIGARKPQYDIWGNTVNVASRMESTGELGKIQVTEETCTILQGLGYSCECRGLINVKGKGELRTYFVCTDTAKFQGLGLN

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 Relevance1
Supporting Publications1
PMIDTitleAbstract
27821849Detailed Analysis of Protein Topology of Extracellular Vesicles-Evidence of Unconventional Membrane Protein Orientation.No abstract available