Protein detail

ADCY8

Adenylate cyclase type 8 (EC 4.6.1.1) (ATP pyrophosphate-lyase 8) (Adenylate cyclase type VIII) (Adenylyl cyclase 8) (AC8) (Ca(2+)/calmodulin-activated adenylyl cyclase)

Entry name
ADCY8
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 8 (EC 4.6.1.1) (ATP pyrophosphate-lyase 8) (Adenylate cyclase type VIII) (Adenylyl cyclase 8) (AC8) (Ca(2+)/calmodulin-activated adenylyl cyclase)
Protein Class (4)
EnzymesMetabolic proteinsPredicted intracellular proteinsPredicted membrane proteins
Protein Function (3)
  • Enzymes
  • Predicted intracellular proteins
  • ENZYME proteins:Lyases
Transmembrane
183..203; Helical; 212..232; Helical; 247..267; Helical; 274..294; Helical; 296..316; Helical; 321..341; Helical; 716..736; Helical; 738..758; Helical; 787..807; Helical; 831..851; Helical; 861..881; Helical; 894..914; Helical
Transmembrane Count
12
Entrez Gene Symbol
Gene Synonym (3)
AC8ADCY3HBAC1
Gene Description
Adenylate cyclase 8
Chromosome
8
Position
130780301-131040909
Supporting publications (n)
1
EVMP confidence score
0.50
Fluorescence & Localization4
ADCY8 fluorescence
Cell SpecificNeutrophil progenitorsSecretome LocationIntracellular and membraneSecretome FunctionEnzyme
Function & Pathway7
Protein Function (3)
  • Enzymes
  • Predicted intracellular proteins
  • ENZYME proteins:Lyases
Mediation Categories (4)
Clinical-translation mediationFusion and delivery mediationMetabolism mediationReceptor-signaling mediation
Relations & Evidence20

Ligand-Receptor Signaling (19)

19 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
receptorreceptorCellTalkDBNoYesNoNoNo
receptorreceptorOmniPathNoYesNoNoNo
intracellularintracellularComPPINoNoNoNoNo
intracellularintracellularGO_IntercellNoNoNoNoNo
intracellularintracellularUniProt_locationNoNoNoNoNo
intracellularintracellularOmniPathNoNoNoNoNo
transmembranetransmembraneUniProt_locationNoNoNoNoNo
transmembranetransmembraneUniProt_topologyNoNoNoNoNo
transmembranetransmembraneUniProt_keywordNoNoNoNoNo
transmembranetransmembraneLOCATENoNoNoNoNo
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Isolation & Detection Technology (1)

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Polymer PrecipitationWestern blotting138731868
Sequence, Structure & Domains9

Sequences

Length
1,251
Mass
140,122
Sequence
MELSDVRCLTGSEELYTIHPTPPAGDGRSASRPQRLLWQTAVRHITEQRFIHGHRGGSGSGSGGSGKASDPAGGGPNHHAPQLSGDSALPLYSLGPGERAHSTCGTKVFPERSGSGSASGSGGGGDLGFLHLDCAPSNSDFFLNGGYSYRGVIFPTLRNSFKSRDLERLYQRYFLGQRRKSEVVMNVLDVLTKLTLLVLHLSLASAPMDPLKGILLGFFTGIEVVICALVVVRKDTTSHTYLQYSGVVTWVAMTTQILAAGLGYGLLGDGIGYVLFTLFATYSMLPLPLTWAILAGLGTSLLQVILQVVIPRLAVISINQVVAQAVLFMCMNTAGIFISYLSDRAQRQAFLETRRCVEARLRLETENQRQERLVLSVLPRFVVLEMINDMTNVEDEHLQHQFHRIYIHRYENVSILFADVKGFTNLSTTLSAQELVRMLNELFARFDRLAHEHHCLRIKILGDCYYCVSGLPEPRQDHAHCCVEMGLSMIKTIRYVRSRTKHDVDMRIGIHSGSVLCGVLGLRKWQFDVWSWDVDIANKLESGGIPGRIHISKATLDCLNGDYNVEEGHGKERNEFLRKHNIETYLIKQPEDSLLSLPEDIVKESVSSSDRRNSGATFTEGSWSPELPFDNIVGKQNTLAALTRNSINLLPNHLAQALHVQSGPEEINKRIEHTIDLRSGDKLRREHIKPFSLMFKDSSLEHKYSQMRDEVFKSNLVCAFIVLLFITAIQSLLPSSRVMPMTIQFSILIMLHSALVLITTAEDYKCLPLILRKTCCWINETYLARNVIIFASILINFLGAILNILWCDFDKSIPLKNLTFNSSAVFTDICSYPEYFVFTGVLAMVTCAVFLRLNSVLKLAVLLIMIAIYALLTETVYAGLFLRYDNLNHSGEDFLGTKEVSLLLMAMFLLAVFYHGQQLEYTARLDFLWRVQAKEEINEMKELREHNENMLRNILPSHVARHFLEKDRDNEELYSQSYDAVGVMFASIPGFADFYSQTEMNNQGVECLRLLNEIIADFDELLGEDRFQDIEKIKTIGSTYMAVSGLSPEKQQCEDKWGHLCALADFSLALTESIQEINKHSFNNFELRIGISHGSVVAGVIGAKKPQYDIWGKTVNLASRMDSTGVSGRIQVPEETYLILKDQGFAFDYRGEIYVKGISEQEGKIKTYFLLGRVQPNPFILPPRRLPGQYSLAAVVLGLVQSLNRQRQKQLLNENNNTGIIKGHYNRRTLLSPSGTEPGAQAEGTDKSDLP

Domain & Motif Annotations

Compositional Bias
56..76; Gly residues
Motif
38..40; Essential for CALM1 interaction; 49..51; Essential for CALM1 interaction
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. The two transmembrane clusters are necessary and suficient for the plasma membrane targeting and oligomers assembly. The N-terminal and C-terminal domains interact at rest as part of a larger autoinhibitory complex, with calmodulin pre-associated at the N-terminal domain; the binding is specifically inhibited by fully calcium-saturated calmodulin, resulting in activation of AC8..
Region
1..182; Involved in ORAI1, STIM1, PPP2CA and PPP2R1A interaction; 1..109; Involved in AKAP5 and PRKAR2A interaction; 50..92; Disordered; 1109..1251; Involved in CALM1 interaction; 1200..1215; Required for both calcium stimulation and maintenance of autoinhibition; 1223..1251; Disordered
Protein Families
Adenylyl cyclase class-4/guanylyl cyclase family
Sequence Similarities
Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
Clinical Relevance2
Supporting Publications1
PMIDTitleAbstract
32384937Alzheimer's disease progression characterized by alterations in the molecular profiles and biogenesis of brain extracellular vesicles.No abstract available