Protein detail

ADCY5

Adenylate cyclase type 5 (EC 4.6.1.1) (ATP pyrophosphate-lyase 5) (Adenylate cyclase type V) (Adenylyl cyclase 5) (AC5)

Protein symbol
ADCY5
UniProt ID
EVMP score
0.50
Frequency
1
Transmembrane count
12
Protein classification
Disease related genesEnzymesHuman disease related genesMetabolic 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 5 (EC 4.6.1.1) (ATP pyrophosphate-lyase 5) (Adenylate cyclase type V) (Adenylyl cyclase 5) (AC5)
Protein Class
Disease related genesEnzymesHuman disease related genesMetabolic proteinsPredicted membrane proteins
Protein Function
  • Disease related genes
  • Enzymes
  • Human disease related genes:Nervous system diseases:Other nervous and sensory system diseases
  • ENZYME proteins:Lyases
Transmembrane
196..216; Helical; 242..262; Helical; 268..288; Helical; 299..319; Helical; 325..345; Helical; 374..394; Helical; 770..790; Helical; 792..812; Helical; 836..856; Helical; 910..930; Helical; 935..955; Helical; 984..1004; Helical
Transmembrane Count
12
Entrez Gene Symbol
Gene Synonym
AC5
Gene Description
Adenylate cyclase 5
Chromosome
3
Position
123282296-123449090
Frequency
1
EVMP Score
0.50
Fluorescence & Localization
Function & Pathway
Protein Function
  • Disease related genes
  • Enzymes
  • Human disease related genes:Nervous system diseases:Other nervous and sensory system diseases
  • ENZYME proteins:Lyases
KEGG
Reactome
Mediation Categories
Clinical-translation mediationFusion and delivery mediationMetabolism mediationReceptor-signaling mediation
Relations & Evidence

Enzyme-Mediated Modification

0 records.

Ligand-Receptor Signaling

21 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
receptorreceptorOmniPathNoYesNoNoNo
extracellularextracellularOmniPathNoNoNoNoNo
intracellularintracellularLOCATENoNoNoNoNo
intracellularintracellularComPPINoNoNoNoNo
intracellularintracellularGO_IntercellNoNoNoNoNo
intracellularintracellularOmniPathNoNoNoNoNo
cell_surface_enzymecell_surface_enzymeSurfaceomeYesNoNoNoNo
cell_surface_enzymecell_surface_enzymeOmniPathYesNoNoNoNo
transmembranetransmembraneUniProt_locationNoNoNoNoNo
transmembranetransmembraneUniProt_topologyNoNoNoNoNo
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Regulatory Interaction Network

8 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
ADCY5O95622CAMPP49913YesYesNoWangCui2007SignaLink3TCRcuration_SignaLink3SignaLink3:23109003SignaLink3:15539636SignaLink3:16460834SignaLink3:7935349
GNAI1P63096ADCY5O95622YesNoYesKEGG-MEDICUSSIGNORHPRDSignaLink3WangTCRcuration_SignaLink3SIGNOR:8119955SignaLink3:7935349SignaLink3:23109003SignaLink3:11376933HPRD:9748257SignaLink3:15539636SignaLink3:16460834
GNAI2P04899ADCY5O95622YesNoYesKEGG-MEDICUSSIGNORSignaLink3WangTCRcuration_SignaLink3SIGNOR:8119955SignaLink3:7935349SignaLink3:23109003SignaLink3:11376933SignaLink3:15539636SignaLink3:16460834
GNAI3P08754ADCY5O95622YesNoYesKEGG-MEDICUSSIGNORCui2007SignaLink3CA1WangTCRcuration_SignaLink3SIGNOR:8119955SignaLink3:7935349SignaLink3:23109003SignaLink3:11376933SignaLink3:16460834SignaLink3:15539636CA1:8327893
GNAZP19086ADCY5O95622YesNoYesWangCui2007SIGNORCA1SIGNOR:7829508CA1:7829508
GNALP38405ADCY5O95622YesYesNoWangSIGNORSIGNOR:21303898
COMPLEX:P59768_P62873ADCY5O95622YesNoYesSIGNORSIGNOR:9707174
GNB5O14775ADCY5O95622YesYesYesSIGNORSIGNOR:21303898

Protein Complex Composition

1 record.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
ADCY5O956222PDBPDB:8sl4

Isolation & Detection Technology

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationSize Exclusion ChromatographyMass spectrometryMass spectrometry|FACSFACSR Sequencing140689422
Sequence, Structure & Domains

Sequences

Length
1,261
Mass
138,908
Sequence
MSGSKSVSPPGYAAQKTAAPAPRGGPEHRSAWGEADSRANGYPHAPGGSARGSTKKPGGAVTPQQQQRLASRWRSDDDDDPPLSGDDPLAGGFGFSFRSKSAWQERGGDDCGRGSRRQRRGAASGGSTRAPPAGGGGGSAAAAASAGGTEVRPRSVEVGLEERRGKGRAADELEAGAVEGGEGSGDGGSSADSGSGAGPGAVLSLGACCLALLQIFRSKKFPSDKLERLYQRYFFRLNQSSLTMLMAVLVLVCLVMLAFHAARPPLQLPYLAVLAAAVGVILIMAVLCNRAAFHQDHMGLACYALIAVVLAVQVVGLLLPQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSALHLAIALRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGDYEVEPGCGGERNAYLKEHSIETFLILRCTQKRKEEKAMIAKMNRQRTNSIGHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDKNAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLTFREPDLEKKYSKQVDDRFGAYVACASLVFLFICFVQITIVPHSIFMLSFYLTCSLLLTLVVFVSVIYSCVKLFPSPLQTLSRKIVRSKMNSTLVGVFTITLVFLAAFVNMFTCNSRDLLGCLAQEHNISASQVNACHVAESAVNYSLGDEQGFCGSPWPNCNFPEYFTYSVLLSLLACSVFLQISCIGKLVLMLAIELIYVLIVEVPGVTLFDNADLLVTANAIDFFNNGTSQCPEHATKVALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKLQATEEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIISEDRFRQLEKIKTIGSTYMAASGLNDSTYDKVGKTHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNGGPPLS
Alternative Products
Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O95622-1; Sequence=Displayed; Name=2; IsoId=O95622-2; Sequence=VSP_042914, VSP_042915
Alternative Sequence
1..28; MSGSKSVSPPGYAAQKTAAPAPRGGPEH -> MKSQKEGCCSRGDLSIQTGPGGEWAPRR (in isoform 2); 29..378; Missing (in isoform 2)

3D Structural Models

3D Structure
Electron microscopy (2)

Domain & Motif Annotations

Compositional Bias
25..37; Basic and acidic residues; 121..132; Low complexity; 151..171; Basic and acidic residues; 178..188; Gly 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)
469..596; Guanylate cyclase 1; 1071..1210; Guanylate cyclase 2
Region
1..195; Disordered
Protein Families
Adenylyl cyclase class-4/guanylyl cyclase family
Sequence Similarities
Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
Clinical Relevance
Disease Involvement
Disease variantIntellectual disability