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Entry version 151 (12 Aug 2020)
Sequence version 2 (03 Oct 2012)
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Protein

Adenylate cyclase type 8

Gene

Adcy8

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the formation of cAMP in response to calcium entry leadings to cAMP signaling activation that affect processes suche as synaptic plasticity and insulin secretion (PubMed:10864938, PubMed:25403481, PubMed:10482244, PubMed:14585998, PubMed:18448650). Plays a role in many brain functions, such as learning, memory, drug addiction, and anxiety modulation through regulation of synaptic plasticity by modulating long-term memory and long-term potentiation (LTP) through CREB transcription factor activity modulation (PubMed:10482244, PubMed:14585998, PubMed:18448650, PubMed:10864938, PubMed:12441059, PubMed:20638449, PubMed:27234425, PubMed:18222416). Plays a central role in insulin secretion by controlling glucose homeostasis through glucagon-like peptide 1 and glucose signaling pathway and maintains insulin secretion through calcium-dependent PKA activation leading to vesicle pool replenishment (PubMed:25403481). Also, allows PTGER3 to induce potentiation of PTGER4-mediated PLA2 secretion by switching from a negative to a positive regulation, during the IL1B induced-dedifferentiation of smooth muscle cells (By similarity).By similarity9 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

At rest, the N- and C-terminal domains interact, as part of a larger autoinhibitory complex, with calmodulin pre-associated at the N-terminal domain. Upon a calcium rise, calmodulin becomes calcium-saturated and subsequently binds to the C-terminal domain. Fully calcium-saturated calmodulin then leaves the N-terminal domain, binding solely to the C-terminal domain, and the whole autoinhibitory complex dissociates, resulting in activation of adenylate cyclase. As local calcium concentrations decrease, the calmodulin becomes calcium free and binds once more to the N-terminal domain, whereupon the whole system returns to rest with the re-association of the autoinhibitory complex (PubMed:14585998). In non-excitable cells, activated by capacitative calcium entry (CCE) through store-operated channels, namely through interaction with ORAI1 and STIM1; membrane raft and caveolae localization and membrane integrity are indispensable. CCE-mediated adenylate cyclase activity is decreased by AKAP5 and AKAP7. CCE-mediated adenylate cyclase activity is up-regulated by AKAP9 and the mitochondrially targeted AKAP1. In excitable cells, activated during membrane depolarization through L-type voltage-gated calcium channels (VGCC), leading to calcium entry; the L-type alpha subunit is sufficient. Activated via stimulation of the GLP1R. Synergistically activated by calcium/calmodulin and GNAS. Stimulated by forskolin. Inhibited by PKA directly bound to AKAP5 at membrane raft. Inhibition by acute activation of OPRM1 and activation by chronic activation of OPRM1 is mediated by pertussis toxin-sensitive G(i) and G(o) G alpha proteins and G beta-gamma dimer. Activity is inhibited by G beta-gamma dimer (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi417Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi417Magnesium 2; catalyticPROSITE-ProRule annotation1
Metal bindingi418Magnesium 2; via carbonyl oxygen; catalyticPROSITE-ProRule annotation1
Metal bindingi461Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi461Magnesium 2; catalyticPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei505ATPBy similarity1
Binding sitei1032ATPBy similarity1
Binding sitei1154ATPBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei1197Essential for autoinhibition maintenance by promoting interaction of the N and C terminiBy similarity1
Sitei1198Essential for autoinhibition maintenanceBy similarity1
Sitei1201Essential for autoinhibition maintenance by promoting interaction of the N and C terminiBy similarity1
Sitei1203Essential for CALM1 interactionBy similarity1
Sitei1205Essential for CALM1 interactionBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi417 – 422ATPBy similarity6
Nucleotide bindingi459 – 461ATPBy similarity3
Nucleotide bindingi1107 – 1109ATPBy similarity3
Nucleotide bindingi1114 – 1118ATPBy similarity5

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionLyase
Biological processcAMP biosynthesis
LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.6.1.1, 3474

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-163615, PKA activation
R-MMU-170660, Adenylate cyclase activating pathway
R-MMU-170670, Adenylate cyclase inhibitory pathway
R-MMU-418597, G alpha (z) signalling events
R-MMU-5610787, Hedgehog 'off' state
R-MMU-9664323, FCGR3A-mediated IL10 synthesis

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Adenylate cyclase type 8Curated (EC:4.6.1.1By similarity)
Alternative name(s):
ATP pyrophosphate-lyase 8
Adenylate cyclase type VIIIBy similarity
Adenylyl cyclase 8By similarity
Ca(2+)/calmodulin-activated adenylyl cyclase
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Adcy8Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 15

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1341110, Adcy8

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 180CytoplasmicSequence analysisAdd BLAST180
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei181 – 201HelicalSequence analysisAdd BLAST21
Transmembranei210 – 230HelicalSequence analysisAdd BLAST21
Transmembranei245 – 265HelicalSequence analysisAdd BLAST21
Transmembranei272 – 292HelicalSequence analysisAdd BLAST21
Transmembranei294 – 314HelicalSequence analysisAdd BLAST21
Transmembranei319 – 339HelicalSequence analysisAdd BLAST21
Topological domaini340 – 713CytoplasmicSequence analysisAdd BLAST374
Transmembranei714 – 734HelicalSequence analysisAdd BLAST21
Transmembranei736 – 756HelicalSequence analysisAdd BLAST21
Transmembranei785 – 805HelicalSequence analysisAdd BLAST21
Transmembranei829 – 849HelicalSequence analysisAdd BLAST21
Transmembranei859 – 879HelicalSequence analysisAdd BLAST21
Transmembranei892 – 912HelicalSequence analysisAdd BLAST21
Topological domaini913 – 1249CytoplasmicSequence analysisAdd BLAST337

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Coated pit, Cytoplasmic vesicle, Membrane, Synapse

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Adcy8 knockout mice are fertile and seem normal. However mice reveal a tendency for both male and female to be somewhat smaller from day of life 45 and 30 respectively while food intake is normal. From there, females remain 10-15% smaller. In contrast, male transiently grew more slowly between day of life 45 and 92, after which point differences are not significant. Mice are less nervous.1 Publication

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001957061 – 1249Adenylate cyclase type 8Add BLAST1249

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei55Omega-N-methylarginineCombined sources1
Modified residuei612PhosphoserineCombined sources1
Modified residuei622PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi815N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi819N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi886N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated by PKA; mediates inhibition of adenylate cyclase activity at membrane raft; does not influence either CALM1 or PPP2CA interaction with ADCY8.By similarity
N-glycosylated; N-glycosylation is responsible for raft-targeting; is not necessary for CCE-stimulated adenylate cyclase activity.By similarity

Keywords - PTMi

Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P97490

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P97490

PeptideAtlas

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PeptideAtlasi
P97490

PRoteomics IDEntifications database

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PRIDEi
P97490

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

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GlyGeni
P97490, 3 sites

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P97490

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P97490

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Abundantly expressed within the olfactory bulb, thalamus, habenula, CA1 region of the hippocampus, and hypothalamus (PubMed:10864938). Strongly expressed in pyramidal cells of CA1 and weakly in CA3 and the dentate gyrus. Strongly and homogeneously expressed in all cell layers of the anterior cingulate cortex (ACC). Widely expressed in the insular cortex. Weakly expressed in the spinal dorsal horn (PubMed:12441059). Abundantly present in the CA1/CA2 region in the hippocampus neonatal and intensifies by adulthood. Weakly expressed in the cerebellum at postnatal day 7 and decreased further by postnatal day 14 (PubMed:17335981).3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000022376, Expressed in stomach and 191 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P97490, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P97490, MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; via transmembrane domain (PubMed:19158400). Monomer (PubMed:19158400). Heterodimer. Oligemer; via transmembrane domain.

Interacts with PRKAR2A and AKAP5; inhibits adenylate cyclase activity through PKA phosphorylation.

Interacts with PPP2CA and PPP2R1A; does not mediate the inhibitory effects of PKA on adenylate cyclase activity; interaction is dependent of catalytically active PPP2CA; antagonizes interaction with calmodulin.

Interacts with AKAP5 (palmitoylated form); promotes the phosphorylation of ADCY8 after store-operated calcium entry (SOCE) stimulation at membrane raft.

Interacts with ORAI1; interaction is calcium store depletion independent; interaction occurs in membrane raft; interaction increases markedly after store depletion; positively regulates SOCE-induced adenylate cyclase activity; contributes to the targeting of ADCY8 to discrete regions of the plasma membrane that are shielded from other calcium events.

Interacts with STIM1.

Interacts with actin; interaction is calcium independent; interaction is affected by calcium-calmodulin; interaction controls the distribution and regulation of ADCY8.

Interacts with calmodulin; at rest, interacts via N-terminal domain; upon a calcium rise, calmodulin becomes calcium-saturated and subsequently binds to the C-terminal domain forming an autoinhibitory complex; fully calcium-saturated calmodulin leaves the N-terminal domain, binding solely to the C-terminal domain leading to dissociation of autoinhibitory complex and resulting in activation of adenylate cyclase; antagonizes interaction with PPP2CA; interaction is calcium dependent.

Interacts with PPP2R5D (By similarity).

By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
197977, 4 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P97490

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000023007

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
P97490, protein

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 180Involved in ORAI1, STIM1, PPP2CA and PPP2R1A interactionBy similarityAdd BLAST180
Regioni1 – 107Involved in AKAP5 and PRKAR2A interactionBy similarityAdd BLAST107
Regioni1107 – 1249Involved in CALM1 interactionBy similarityAdd BLAST143
Regioni1198 – 1213Required for both calcium stimulation and maintenance of autoinhibitionBy similarityAdd BLAST16

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi38 – 40Essential for CALM1 interactionBy similarity3
Motifi49 – 51Essential for CALM1 interactionBy similarity3

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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.By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3619, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000158742

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_001072_3_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P97490

KEGG Orthology (KO)

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KOi
K08048

Identification of Orthologs from Complete Genome Data

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OMAi
AYQRYSH

Database of Orthologous Groups

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OrthoDBi
107368at2759

TreeFam database of animal gene trees

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TreeFami
TF313845

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.70.1230, 2 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR001054, A/G_cyclase
IPR018297, A/G_cyclase_CS
IPR032628, AC_N
IPR030672, Adcy
IPR009398, Adcy_conserved_dom
IPR029787, Nucleotide_cyclase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF16214, AC_N, 1 hit
PF06327, DUF1053, 1 hit
PF00211, Guanylate_cyc, 2 hits

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF039050, Ade_cyc, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00044, CYCc, 2 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF55073, SSF55073, 2 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00452, GUANYLATE_CYCLASE_1, 2 hits
PS50125, GUANYLATE_CYCLASE_2, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P97490-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MELSDVHCLS GSEELYTIQP TPPAGDDGSG SRPQRLLWQT AVRHITEQRF
60 70 80 90 100
IHGHRGGGGG GVSRKASNPA GSGPNHHAPQ LSSDSVLPLY SLGPGERAHN
110 120 130 140 150
TGGTKVFPER SGSGSASGSG GGGDLGFLHL DCAPSNSDFF LNGGYSYRGV
160 170 180 190 200
IFPTLRNSFK SRDLERLYQR YFLGQRRKSE VVMNVLDVLT KLTLLVLHLS
210 220 230 240 250
LASAPMDPLK GILLGFFTGI EVVICALVVV RKDNTSHTYL QYSGVVTWVA
260 270 280 290 300
MTTQILAAGL GYGLLGDGIG YVLFTLFATY SMLPLPLTWA ILAGLGTSLL
310 320 330 340 350
QVTLQVLIPR LAVFSINQVL AQVVLFMCMN TAGIFISYLS DRAQRQAFLE
360 370 380 390 400
TRRCVEARLR LETENQRQER LVLSVLPRFV VLEMINDMTN VEDEHLQHQF
410 420 430 440 450
HRIYIHRYEN VSILFADVKG FTNLSTTLSA QELVRMLNEL FARFDRLAHE
460 470 480 490 500
HHCLRIKILG DCYYCVSGLP EPRRDHAHCC VEMGLSMIKT IRFVRSRTKH
510 520 530 540 550
DVDMRIGIHS GSVLCGVLGL RKWQFDVWSW DVDIANKLES GGIPGRIHIS
560 570 580 590 600
KATLDCLNGD YNVEEGHGKE RNEFLRKHNI ETYLIKQPEE SLLCLPEDIV
610 620 630 640 650
KESVSCSDRR NSGATFTEGS WSPELPFDNI VGKQNTLAAL TRNSINLLPN
660 670 680 690 700
HLAQALHVQS GPEEINKRIE HTIDLRSGDK LRREHIKPFS LMFKDSSLEH
710 720 730 740 750
KYSQMRDEVF KSNLVCAFIV LLFITAIQSL LPSSRLMPMT IQFSILIMLH
760 770 780 790 800
SALVLITTAE DYKCLPLILR KTCCWINETY LARNVIIFAS ILINFLGAVL
810 820 830 840 850
NILWCDFDKS IPLKNLTFNS SAVFTDICSY PEYFVFTGVL AMVTCAVFLR
860 870 880 890 900
LNSVLKLAVL LIMIAIYALL TETIYAGLFL SYDNLNHSGE DFLGTKEASL
910 920 930 940 950
LLMAMFLLAV FYHGQQLEYT ARLDFLWRVQ AKEEINEMKE LREHNENMLR
960 970 980 990 1000
NILPSHVARH FLEKDRDNEE LYSQSYDAVG VMFASIPGFA DFYSQTEMNN
1010 1020 1030 1040 1050
QGVECLRLLN EIIADFDELL GEDRFQDIEK IKTIGSTYMA VSGLSPEKQQ
1060 1070 1080 1090 1100
CEDKWGHLCA LADFSLALTE SIQEINKHSF NNFELRIGIS HGSVVAGVIG
1110 1120 1130 1140 1150
AKKPQYDIWG KTVNLASRMD STGVSGRIQV PEETYLILKD QGFAFDYRGE
1160 1170 1180 1190 1200
IYVKGISEQE GKIKTYFLLG RVQPNPFILP PRRLPGQYSL AAVVLGLVQS
1210 1220 1230 1240
LNRQRQKQLL NENSNSGIIK SHYNRRTLLT PSGPEPGAQA EGTDKSDLP
Length:1,249
Mass (Da):140,095
Last modified:October 3, 2012 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i26103B6E0DB9C701
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A2I3BQ46A0A2I3BQ46_MOUSE
Adenylate cyclase type 8
Adcy8
1,219Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti24A → V in AAB41885 (Ref. 1) Curated1
Sequence conflicti59G → C in AAB41885 (Ref. 1) Curated1
Sequence conflicti849L → V in AAB41885 (Ref. 1) Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
U85021 mRNA Translation: AAB41885.1
AC116996 Genomic DNA No translation available.
AC160934 Genomic DNA No translation available.
CH466545 Genomic DNA Translation: EDL29360.1
CH466545 Genomic DNA Translation: EDL29361.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS27506.1

NCBI Reference Sequences

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RefSeqi
NP_033753.2, NM_009623.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000023007; ENSMUSP00000023007; ENSMUSG00000022376

Database of genes from NCBI RefSeq genomes

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GeneIDi
11514

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:11514

UCSC genome browser

More...
UCSCi
uc007vzo.1, mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U85021 mRNA Translation: AAB41885.1
AC116996 Genomic DNA No translation available.
AC160934 Genomic DNA No translation available.
CH466545 Genomic DNA Translation: EDL29360.1
CH466545 Genomic DNA Translation: EDL29361.1
CCDSiCCDS27506.1
RefSeqiNP_033753.2, NM_009623.2

3D structure databases

Database of comparative protein structure models

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ModBasei
Search...

SWISS-MODEL Interactive Workspace

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SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

BioGRIDi197977, 4 interactors
CORUMiP97490
STRINGi10090.ENSMUSP00000023007

PTM databases

GlyGeniP97490, 3 sites
iPTMnetiP97490
PhosphoSitePlusiP97490

Proteomic databases

MaxQBiP97490
PaxDbiP97490
PeptideAtlasiP97490
PRIDEiP97490

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
4355, 215 antibodies

Genome annotation databases

EnsembliENSMUST00000023007; ENSMUSP00000023007; ENSMUSG00000022376
GeneIDi11514
KEGGimmu:11514
UCSCiuc007vzo.1, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
114
MGIiMGI:1341110, Adcy8

Phylogenomic databases

eggNOGiKOG3619, Eukaryota
GeneTreeiENSGT00940000158742
HOGENOMiCLU_001072_3_0_1
InParanoidiP97490
KOiK08048
OMAiAYQRYSH
OrthoDBi107368at2759
TreeFamiTF313845

Enzyme and pathway databases

BRENDAi4.6.1.1, 3474
ReactomeiR-MMU-163615, PKA activation
R-MMU-170660, Adenylate cyclase activating pathway
R-MMU-170670, Adenylate cyclase inhibitory pathway
R-MMU-418597, G alpha (z) signalling events
R-MMU-5610787, Hedgehog 'off' state
R-MMU-9664323, FCGR3A-mediated IL10 synthesis

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
11514, 0 hits in 18 CRISPR screens

Protein Ontology

More...
PROi
PR:P97490
RNActiP97490, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000022376, Expressed in stomach and 191 other tissues
ExpressionAtlasiP97490, baseline and differential
GenevisibleiP97490, MM

Family and domain databases

Gene3Di3.30.70.1230, 2 hits
InterProiView protein in InterPro
IPR001054, A/G_cyclase
IPR018297, A/G_cyclase_CS
IPR032628, AC_N
IPR030672, Adcy
IPR009398, Adcy_conserved_dom
IPR029787, Nucleotide_cyclase
PfamiView protein in Pfam
PF16214, AC_N, 1 hit
PF06327, DUF1053, 1 hit
PF00211, Guanylate_cyc, 2 hits
PIRSFiPIRSF039050, Ade_cyc, 1 hit
SMARTiView protein in SMART
SM00044, CYCc, 2 hits
SUPFAMiSSF55073, SSF55073, 2 hits
PROSITEiView protein in PROSITE
PS00452, GUANYLATE_CYCLASE_1, 2 hits
PS50125, GUANYLATE_CYCLASE_2, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiADCY8_MOUSE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P97490
Secondary accession number(s): G3X8V9
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 3, 2012
Last modified: August 12, 2020
This is version 151 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families
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