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Entry version 137 (13 Feb 2019)
Sequence version 1 (01 Feb 1995)
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Protein

Adenylate cyclase type 8

Gene

Adcy8

Organism
Rattus norvegicus (Rat)
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:8163524, PubMed:24086669, PubMed:22494970, PubMed:21046358, PubMed:13680124, PubMed:25381556). 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:8163524). 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:21046358, PubMed:13680124, PubMed:25381556). 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 (PubMed:16741924).7 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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+1 Publication, Mn2+1 PublicationNote: Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro).By similarity

<p>This subsection of the ‘Function’ 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:8163524, PubMed:8557635, PubMed:19305019). 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 (PubMed:19158400, PubMed:11744699, PubMed:19171672, PubMed:22494970, PubMed:20410303). 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 (PubMed:20410303). 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 (PubMed:24086669, PubMed:25381556). Activated via stimulation of the GLP1R (PubMed:25381556). Synergistically activated by calcium/calmodulin and GNAS (PubMed:13680124). Stimulated by forskolin (PubMed:16186630, PubMed:13680124). Inhibited by PKA directly bound to AKAP5 at membrane raft (PubMed:22976297, PubMed:21771783). 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 (PubMed:16186630).14 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.18 mM for ATP (in the presence of 5.74 mM free Mg2+ and 1 muM exogenous calmodulin) (isoform 1)1 Publication
  2. KM=0.16 mM for ATP (in the presence of 5.74 mM free Mg2+ and 1 muM exogenous calmodulin) (isoform 2)1 Publication
  3. KM=2.10 mM for ATP (in the presence of 5.74 mM free Mg2+ and 1 muM exogenous calmodulin) (isoform 3)1 Publication
  4. KM=0.038 mM for ATP (in the presence of 0.23 mM free Mn2+ and 1 muM exogenous calmodulin) (isoform 1)1 Publication
  5. KM=0.025 mM for ATP (in the presence of 0.23 mM free Mn2+ and 1 muM exogenous calmodulin) (isoform 2)1 Publication
  6. KM=0.116 mM for ATP (in the presence of 0.23 mM free Mn2+ and 1 muM exogenous calmodulin) (isoform 3)1 Publication
  1. Vmax=7.4 nmol/min/mg enzyme (in the presence of 5.74 mM free Mg2+ and 1 muM exogenous calmodulin) (isoform 1)1 Publication
  2. Vmax=2 nmol/min/mg enzyme (in the presence of 5.74 mM free Mg2+ and 1 muM exogenous calmodulin) (isoform 2)1 Publication
  3. Vmax=1.5 nmol/min/mg enzyme (in the presence of 5.74 mM free Mg2+ and 1 muM exogenous calmodulin) (isoform 3)1 Publication
  4. Vmax=10.4 nmol/min/mg enzyme (in the presence of 0.23 mM free Mn2+ and 1 muM exogenous calmodulin) (isoform 1)1 Publication
  5. Vmax=3.5 nmol/min/mg enzyme (in the presence of 0.23 mM free Mn2+ and 1 muM exogenous calmodulin) (isoform 2)1 Publication
  6. Vmax=1.5 nmol/min/mg enzyme (in the presence of 0.23 mM free Mn2+ and 1 muM exogenous calmodulin) (isoform 3)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi416Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi416Magnesium 2; catalyticPROSITE-ProRule annotation1
Metal bindingi417Magnesium 2; via carbonyl oxygen; catalyticPROSITE-ProRule annotation1
Metal bindingi460Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi460Magnesium 2; catalyticPROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ 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 sitei504ATPBy similarity1
Binding sitei1031ATPBy similarity1
Binding sitei1153ATPBy 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>Sitei1196Essential for autoinhibition maintenance by promoting interaction of the N and C termini1 Publication1
Sitei1197Essential for autoinhibition maintenance1 Publication1
Sitei1200Essential for autoinhibition maintenance by promoting interaction of the N and C termini1 Publication1
Sitei1202Essential for CALM1 interaction1 Publication1
Sitei1204Essential for CALM1 interaction1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi416 – 421ATPBy similarity6
Nucleotide bindingi458 – 460ATPBy similarity3
Nucleotide bindingi1106 – 1108ATPBy similarity3
Nucleotide bindingi1113 – 1117ATPBy 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

  • actin binding Source: UniProtKB
  • adenylate cyclase activity Source: GO_Central
  • ATP binding Source: UniProtKB-KW
  • calcium- and calmodulin-responsive adenylate cyclase activity Source: UniProtKB
  • calmodulin binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • phosphatase binding Source: UniProtKB
  • protein C-terminus binding Source: RGD
  • protein dimerization activity Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein N-terminus binding Source: RGD
  • protein phosphatase 2A binding Source: UniProtKB

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 5301

<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_and_taxonomy_section">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:4.6.1.12 Publications)
Alternative name(s):
ATP pyrophosphate-lyase 8
Adenylate cyclase type VIIIBy similarity
Adenylyl cyclase 81 Publication
Ca(2+)/calmodulin-activated adenylyl cyclase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
2036 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_location_section">'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 – 179CytoplasmicSequence analysisAdd BLAST179
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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>Transmembranei180 – 200HelicalSequence analysisAdd BLAST21
Transmembranei209 – 229HelicalSequence analysisAdd BLAST21
Transmembranei244 – 264HelicalSequence analysisAdd BLAST21
Transmembranei271 – 291HelicalSequence analysisAdd BLAST21
Transmembranei293 – 313HelicalSequence analysisAdd BLAST21
Transmembranei318 – 338HelicalSequence analysisAdd BLAST21
Topological domaini339 – 712CytoplasmicSequence analysisAdd BLAST374
Transmembranei713 – 733HelicalSequence analysisAdd BLAST21
Transmembranei735 – 755HelicalSequence analysisAdd BLAST21
Transmembranei784 – 804HelicalSequence analysisAdd BLAST21
Transmembranei828 – 848HelicalSequence analysisAdd BLAST21
Transmembranei858 – 878HelicalSequence analysisAdd BLAST21
Transmembranei891 – 911HelicalSequence analysisAdd BLAST21
Topological domaini912 – 1248CytoplasmicSequence analysisAdd BLAST337

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Coated pit, Cytoplasmic vesicle, Membrane, Postsynaptic cell 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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1 – 106Missing : Does not affect adenylate cyclase activity in response to calcium in vitro. Reduces adenylate cyclase activity in response to capacitative calcium entry (CCE). Reduces colocalization with actin. Does not improve the distribution of the actin cytoskeleton at the plasma membrane. 1 PublicationAdd BLAST106
Mutagenesisi38 – 40WQT → AAA: Does not interacts with CALM1; when associated with 49-A--A-51. Interacts with PPP2CA; when associated with 49-A--A-51. Greatly reduces CCE-stimulated adenylate cyclase activity; when associated with 49-A--A-51. Does not affect caveolar localization; when associated with 49-A--A-51. Does not affect calcium/calmodulin stimulated adenylate cyclase activity; when associated with 49-A--A-51. Decreases calcium/calmodulin stimulated adenylate cyclase activity; when associated with 49-A--A-51; A-1197; A-1198 and A-1202. 3 Publications3
Mutagenesisi49 – 51RFI → AAA: Does not interacts with CALM1; when associated with 38-A--A-40. Interacts with PPP2CA; when associated with 38-A--A-40. Greatly reduces CCE-stimulated adenylate cyclase activity; when associated with 38-A--A-40. Does not affect caveolar localization; when associated with 38-A--A-40.Does not affect calcium/calmodulin stimulated adenylate cyclase activity; when associated with 38-A--A-40. Decreases calcium/calmodulin stimulated adenylate cyclase activity; when associated with 38-A--A-40; A-1197; A-1198 and A-1202. 3 Publications3
Mutagenesisi66S → A: Decraeses significantly the stimulatoty effect of PKA inhibitor on calcium-stimulated adenylate cyclase activity. 1 Publication1
Mutagenesisi112S → A: Loses the stimulatoty effect of PKA inhibitor on calcium-stimulated adenylate cyclase activity. 1 Publication1
Mutagenesisi112S → D: Insensitive to the stimulatory effect of PKA inhibitor on calcium-stimulated adenylate cyclase activity. 1 Publication1
Mutagenesisi178S → A: Does not affect the stimulatoty effect of PKA inhibitor on calcium-stimulated adenylate cyclase activity. 1 Publication1
Mutagenesisi416D → N: Loses adenylate cyclase activity in response to calcium. 1 Publication1
Mutagenesisi432L → A: Does not affect dimerization; when associated with A-439. Dramatically reduces the levels of the N-glycosylated monomeric species; when associated with A-439. Loss of calcium- and calmodulin-responsive adenylate cyclase activity; when associated with A-439. Affects membrane raft localization; when associated with A-439. 1 Publication1
Mutagenesisi439L → A: Does not affect dimerization. Does not affect dimerization;when associated with A-432. Does not affect dimerization;when associated with A-446 and A-432. Does not affect dimerization;when associated with A-432; A-446 and A-453. Dramatically reduces the levels of the N-glycosylated monomeric species. Dramatically reduces the levels of the N-glycosylated monomeric species; when associated with A-432.Dramatically reduces the levels of the N-glycosylated monomeric species; when associated with A-446 and A-432. Dramatically reduces the levels of the N-glycosylated monomeric species; when associated with A-453; A-432 and A-446. Loss of calcium- and calmodulin-responsive adenylate cyclase activity. Loss of calcium- and calmodulin-responsive adenylate cyclase activity; when associated with A-432. Loss of calcium- and calmodulin-responsive adenylate cyclase activity; when associated with A-446 and A-432. Loss of calcium- and calmodulin-responsive adenylate cyclase activity; when associated with A-453; A-432 and A-446. Affects membrane raft localization. Affects membrane raft localization; when associated with A-432. Affects membrane raft localization; when associated with A-446 and A-432. Affects membrane raft localization; when associated with A-439; A-432 and A-446. 1 Publication1
Mutagenesisi446L → A: Does not affect dimerization; when associated with A-439 and A-432. Dramatically reduces the levels of the N-glycosylated monomeric species; when associated with A-439 and A-432. Loss of calcium- and calmodulin-responsive adenylate cyclase activity; when associated with A-439 and A-432. Affects membrane raft localization; when associated with A-439 and A-432. 1 Publication1
Mutagenesisi453L → A: Does not affect dimerization; when associated with A-439; A-432 and A-446. Dramatically reduces the levels of the N-glycosylated monomeric species; when associated with A-439; A-432 and A-446. Loss of calcium- and calmodulin-responsive adenylate cyclase activity; when associated with A-439; A-432 and A-446. Affects membrane raft localization; when associated with A-439; A-432 and A-446. 1 Publication1
Mutagenesisi611S → A: Does not affect the stimulatoty effect of PKA inhibitoron calcium-stimulated adenylate cyclase activity. 1 Publication1
Mutagenesisi814N → Q: Does not affect deglycosylation. Does not affect plasma membrane targeting; when associated with Q-818 and A-885. Affects membrane raft localization; when associated with Q-818 and A-885. Does not affect CCE-stimulated adenylate cyclase activity; when associated with Q-818 and A-885. 1 Publication1
Mutagenesisi818N → Q: Does not affect deglycosylation. Does not affect plasma membrane targeting; when associated with Q-814 and A-885. Affects membrane raft localization; when associated with Q-814 and A-885. Does not affect CCE-stimulated adenylate cyclase activity; when associated with Q-814 and A-885. 1 Publication1
Mutagenesisi852S → A: Does not affect the stimulatoty effect of PKA inhibitoron calcium-stimulated adenylate cyclase activity. 1 Publication1
Mutagenesisi885N → E: Does not affect deglycosylation. Does not affect plasma membrane targeting; when associated with Q-814 and A-818. Affects membrane raft localization; when associated with Q-814 and A-818. Does not affect CCE-stimulated adenylate cyclase activity; when associated with Q-814 and A-818. 1 Publication1
Mutagenesisi1120S → A: Does not affect the stimulatoty effect of PKA inhibitor on calcium-stimulated adenylate cyclase activity. 1 Publication1
Mutagenesisi1196L → A: Consistently high basal adenylate cyclase activity; when associated with A-1200. Does not affect calmodulin binding; when associated with A-1200. 1 Publication1
Mutagenesisi1197V → A: Does not affect calcium activated adenylate cyclase; when associated with A-1198. Does not affect calcium activated adenylate cyclase; when associated with A-1198 and A-1202.Decreases calcium/calmodulin stimulated adenylate cyclase activity; when associated with 49-A--A-51; 38-A--A-40; A-1198 and A-1202. Has an elevated basal activity; when associated with A-1198. Has an elevated basal activity; when associated with A-1198 and A-1202. Does not affect calmodulin binding; when associated with A-1198. Does not affect calmodulin binding; when associated with A-1198 and A-1202. 1 Publication1
Mutagenesisi1197V → N: Does not affect calcium activated adenylate cyclase. Significant high basal adenylate cyclase activity. Significant high basal adenylate cyclase activity; when associated with Q-1202. 1 Publication1
Mutagenesisi1198Q → A: Does not affect calcium activated adenylate cyclase; when associated with A-1197. Does not affect calcium activated adenylate cyclase; when associated with A-1197 and A-1202. Decreases calcium/calmodulin stimulated adenylate cyclase activity; when associated with 49-A--A-51; 38-A--A-40; A-1197 and A-1202. Has an elevated basal activity; when associated with A-1197. Has an elevated basal activity; when associated with A-1197 and A-1202. Does not affect calmodulin binding; when associated with A-1197. Does not affect calmodulin binding; when associated with A-1197 and A-1202. 1 Publication1
Mutagenesisi1198Q → K: Does not affect calcium activated adenylate cyclase. 1 Publication1
Mutagenesisi1199S → D: Increase CCE -stimulated adenylate cyclase. Has an high basal activity. 1 Publication1
Mutagenesisi1200L → A: Consistently high basal adenylate cyclase activity; when associated with A-1196. Does not affect calmodulin binding; when associated with A-1196. 1 Publication1
Mutagenesisi1202R → A: Does not affect calcium activated adenylate cyclase; when associated with A-1197 and A-1198. Decreases calcium/calmodulin stimulated adenylate cyclase activity; when associated with 49-A--A-51; 38-A--A-40; A-1197 and A-1198. Has an elevated basal activity; when associated with A-1197 and A-1198. Does not affect calmodulin binding; when associated with A-1197 and A-1198. 1 Publication1
Mutagenesisi1202R → E: Does not affect calcium activated adenylate cyclase; when associated with E-1204. Greatly diminishes calmodulin binding; when associated with E-1204. 1 Publication1
Mutagenesisi1202R → Q: Does not affect calcium activated adenylate cyclase. Increases slightly basal adenylate cyclase activity but not significantly, and retains an appreciable calcium regulation. Significant high basal adenylate cyclase activity; when associated with N-1197. 1 Publication1
Mutagenesisi1204R → E: Does not affect calcium activated adenylate cyclase; when associated with E-1202. Greatly diminishes calmodulin binding; when associated with E-1202. 1 Publication1
Mutagenesisi1206K → E: Does not affect calcium activated adenylate cyclase. Does not affect calmodulin binding. 1 Publication1
Mutagenesisi1208L → E: Does not affect calcium activated adenylate cyclase; when associated with E-1209. Does not affect calmodulin binding; when associated with E-1209. 1 Publication1
Mutagenesisi1209L → E: Does not affect calcium activated adenylate cyclase; when associated with E-1208. Does not affect calmodulin binding; when associated with E-1208. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2095179

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001957071 – 1248Adenylate cyclase type 8Add BLAST1248

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-methylarginineBy similarity1
Modified residuei611PhosphoserineBy similarity1
Modified residuei621PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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>Glycosylationi814N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi818N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi885N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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 ADCY8.2 Publications
Isoform 1: N-glycosylated; N-glycosylation is responsible for raft-targeting; is not necessary for CCE-stimulated adenylate cyclase activity.2 Publications
Isoform 3: N-glycosylated; N-glycosylation is responsible for raft-targeting; is not necessary for CCE-stimulated adenylate cyclase activity.2 Publications

Keywords - PTMi

Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

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

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PaxDbi
P40146

PRoteomics IDEntifications database

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PRIDEi
P40146

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P40146

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

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PhosphoSitePlusi
P40146

<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

Brain (PubMed:13680124, PubMed:8557635). Expressed in insulin-producing cells (PubMed:13680124).2 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Reduces by glucose (PubMed:21046358). Up-regulated during vascular smooth muscle cell de-differentiation by IL1B (PubMed:16741924).2 Publications

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; via transmembrane domain (PubMed:19158400, PubMed:11856299). Monomer (PubMed:19158400). Heterodimer (PubMed:11856299). Oligemer; via transmembrane domain (PubMed:11856299). Interacts with PRKAR2A and AKAP5; inhibits adenylate cyclase activity through PKA phosphorylation (PubMed:22976297). 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 (PubMed:22976297, PubMed:16258073). Interacts with AKAP5 (palmitoylated form); promotes the phosphorylation of ADCY8 after store-operated calcium entry (SOCE) stimulation at membrane raft (PubMed:21771783, PubMed:20410303). 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 (PubMed:22494970). Interacts with STIM1 (PubMed:22494970). Interacts with actin; interaction is calcium independent; interaction is affected by calcium-calmodulin; interaction controls the distribution and regulation of ADCY8 (PubMed:22399809). 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 (PubMed:19305019, PubMed:16258073, PubMed:22399809). Interacts with PPP2R5D (PubMed:22976297).9 Publications

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

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STRINGi
10116.ENSRNOP00000006789

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P40146

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P40146

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<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 – 179Involved in ORAI1, STIM1, PPP2CA and PPP2R1A interaction3 PublicationsAdd BLAST179
Regioni1 – 106Involved in AKAP5 and PRKAR2A interaction1 PublicationAdd BLAST106
Regioni1106 – 1248Involved in CALM1 interaction1 PublicationAdd BLAST143
Regioni1197 – 1212Required for both calcium stimulation and maintenance of autoinhibition1 PublicationAdd 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 interaction1 Publication3
Motifi49 – 51Essential for CALM1 interaction1 Publication3

<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 (PubMed:11856299). 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 (PubMed:19305019).By similarity2 Publications

<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
COG2114 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000006941

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG050458

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P40146

KEGG Orthology (KO)

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KOi
K08048

Database of Orthologous Groups

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OrthoDBi
107368at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P40146

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

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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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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 describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 4 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: P40146-1) [UniParc]FASTAAdd to basket
Also known as: VIII-A1 Publication

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MELSDVHCLS GSEELYTIHP TPPAADGGSG SRPQRLLWQT AVRHITEQRF
60 70 80 90 100
IHGHRGGGGG GSRKASNPAG SGPNHHAPQL SSDSVLPLYS LGSGERAHNT
110 120 130 140 150
GGTKVFPERS GSGSASGSGG GGDLGFLHLD CAPSNSDFFL NGGYSYRGVI
160 170 180 190 200
FPTLRNSFKS RDLERLYQRY FLGQRRKSEV VMNVLDVLTK LTLLVLHLSL
210 220 230 240 250
ASAPMDPLKG ILLGFFTGIE VVICALVVVR KDTTSHTYLQ YSGVVTWVAM
260 270 280 290 300
TTQILAAGLG YGLLGDGIGY VLFTLFATYS MLPLPLTWAI LAGLGTSLLQ
310 320 330 340 350
VTLQVLIPRL AVFSINQVLA QVVLFMCMNT AGIFISYLSD RAQRQAFLET
360 370 380 390 400
RRCVEARLRL ETENQRQERL VLSVLPRFVV LEMINDMTNV EDEHLQHQFH
410 420 430 440 450
RIYIHRYENV SILFADVKGF TNLSTTLSAQ ELVRMLNELF ARFDRLAHEH
460 470 480 490 500
HCLRIKILGD CYYCVSGLPE PRQDHAHCCV EMGLSMIKTI RFVRSRTKHD
510 520 530 540 550
VDMRIGIHSG SVLCGVLGLR KWQFDVWSWD VDIANKLESG GIPGRIHISK
560 570 580 590 600
ATLDCLSGDY NVEEGHGKER NEFLRKHNIE TYLIKQPEES LLSLPEDIVK
610 620 630 640 650
ESVSCSDRRN SGATFTEGSW SPELPFDNIV GKQNTLAALT RNSINLLPNH
660 670 680 690 700
LAQALHVQSG PEEINKRIEH TIDLRSGDKL RREHIKPFSL MFKDSSLEHK
710 720 730 740 750
YSQMRDEVFK SNLVCAFIVL LFITAIQSLL PSSRLMPMTI QFSILIMLHS
760 770 780 790 800
ALVLITTAED YKCLPLILRK TCCWINETYL ARNVIIFASI LINFLGAVIN
810 820 830 840 850
ILWCDFDKSI PLKNLTFNSS AVFTDICSYP EYFVFTGVLA MVTCAVFLRL
860 870 880 890 900
NSVLKLAVLL IMIAIYALLT ETIYAGLFLS YDNLNHSGED FLGTKEASLL
910 920 930 940 950
LMAMFLLAVF YHGQQLEYTA RLDFLWRVQA KEEINEMKDL REHNENMLRN
960 970 980 990 1000
ILPGHVARHF LEKDRDNEEL YSQSYDAVGV MFASIPGFAD FYSQTEMNNQ
1010 1020 1030 1040 1050
GVECLRLLNE IIADFDELLG EDRFQDIEKI KTIGSTYMAV SGLSPEKQQC
1060 1070 1080 1090 1100
EDKWGHLCAL ADFSLALTES IQEINKHSFN NFELRIGISH GSVVAGVIGA
1110 1120 1130 1140 1150
KKPQYDIWGK TVNLASRMDS TGVSGRIQVP EETYLILKDQ GFAFDYRGEI
1160 1170 1180 1190 1200
YVKGISEQEG KIKTYFLLGR VQPNPFILPP RRLPGQYSLA AVVLGLVQSL
1210 1220 1230 1240
NRQRQKQLLN ENSNSGIIKS HYNRRTLLTP SGPEPGAQAE GTDKSDLP
Length:1,248
Mass (Da):139,823
Last modified:February 1, 1995 - v1
<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:i0171A3CEED034961
GO
Isoform 2 (identifier: P40146-2) [UniParc]FASTAAdd to basket
Also known as: VIII-B1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     802-831: Missing.

Show »
Length:1,218
Mass (Da):136,386
Checksum:i64B7D3DF627B46C3
GO
Isoform 3 (identifier: P40146-3) [UniParc]FASTAAdd to basket
Also known as: VIII-c1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     635-700: Missing.

Note: EC50 is approximately 4 times more sensitive to stimulation by calcium/calmodulin than isoform 1 and 2.1 Publication
Show »
Length:1,182
Mass (Da):132,274
Checksum:i127B9DEB37BC883C
GO
Isoform 4 (identifier: P40146-4) [UniParc]FASTAAdd to basket
Also known as: VIII-D1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     635-700: Missing.
     802-831: Missing.

Show »
Length:1,152
Mass (Da):128,837
Checksum:i4BB59B79F7CA4298
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
G3V6N0G3V6N0_RAT
Adenylate cyclase
Adcy8 rCG_60206
1,248Annotation 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>

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_059986635 – 700Missing in isoform 3 and isoform 4. 2 PublicationsAdd BLAST66
Alternative sequenceiVSP_059987802 – 831Missing in isoform 2 and isoform 4. 2 PublicationsAdd BLAST30

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
L26986 mRNA Translation: AAA20504.1

Protein sequence database of the Protein Information Resource

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PIRi
A53588

NCBI Reference Sequences

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RefSeqi
NP_058838.1, NM_017142.1 [P40146-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Rn.10382

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
29241

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:29241

UCSC genome browser

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UCSCi
RGD:2036 rat [P40146-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
L26986 mRNA Translation: AAA20504.1
PIRiA53588
RefSeqiNP_058838.1, NM_017142.1 [P40146-1]
UniGeneiRn.10382

3D structure databases

ProteinModelPortaliP40146
SMRiP40146
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000006789

Chemistry databases

ChEMBLiCHEMBL2095179

PTM databases

iPTMnetiP40146
PhosphoSitePlusiP40146

Proteomic databases

PaxDbiP40146
PRIDEiP40146

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29241
KEGGirno:29241
UCSCiRGD:2036 rat [P40146-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
114
RGDi2036 Adcy8

Phylogenomic databases

eggNOGiKOG3619 Eukaryota
COG2114 LUCA
HOGENOMiHOG000006941
HOVERGENiHBG050458
InParanoidiP40146
KOiK08048
OrthoDBi107368at2759
PhylomeDBiP40146

Enzyme and pathway databases

BRENDAi4.6.1.1 5301

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P40146

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...

<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_RAT
<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: P40146
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: February 13, 2019
This is version 137 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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