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Entry version 166 (18 Sep 2019)
Sequence version 1 (01 Apr 1993)
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Protein

Adenylate cyclase type 6

Gene

Adcy6

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 the signaling molecule cAMP downstream of G protein-coupled receptors (PubMed:18071070, PubMed:24363043). Functions in signaling cascades downstream of beta-adrenergic receptors in the heart and in vascular smooth muscle cells (PubMed:18071070). Functions in signaling cascades downstream of the vasopressin receptor in the kidney and has a role in renal water reabsorption (PubMed:20466003, PubMed:20864687). Functions in signaling cascades downstream of PTH1R and plays a role in regulating renal phosphate excretion (PubMed:24854272). Functions in signaling cascades downstream of the VIP and SCT receptors in pancreas and contributes to the regulation of pancreatic amylase and fluid secretion (PubMed:23753526). Signaling mediates cAMP-dependent activation of protein kinase PKA and promotes increased phosphorylation of various proteins, including AKT (PubMed:18071070, PubMed:23753526). Plays a role in regulating cardiac sarcoplasmic reticulum Ca2+ uptake and storage, and is required for normal heart ventricular contractibility (PubMed:18071070). May contribute to normal heart function (PubMed:18071070, PubMed:20359598). Mediates vasodilatation after activation of beta-adrenergic receptors by isoproterenol (By similarity). Contributes to bone cell responses to mechanical stimuli (PubMed:20371630, PubMed:24277577).By similarity10 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+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_section">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

Activated by forskolin (PubMed:18071070, PubMed:20466003, PubMed:20864687, PubMed:23753526, PubMed:24363043). Inhibited by calcium ions, already at micromolar concentrations (PubMed:1379717, PubMed:18071070). Inhibited by adenosine, AMP and their analogs (By similarity). Activated by GNAS. Is further activated by the complex formed by GNB1 and GNG2 (By similarity). Phosphorylation by RAF1 results in its activation (By similarity).By similarity6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi382Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi382Magnesium 2; catalyticPROSITE-ProRule annotation1
Metal bindingi383Magnesium 2; via carbonyl oxygen; catalyticPROSITE-ProRule annotation1
Metal bindingi426Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi426Magnesium 2; catalyticPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei470ATPBy similarity1
Binding sitei1028ATPBy similarity1
Binding sitei1149ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi382 – 387ATPBy similarity6
Nucleotide bindingi424 – 426ATPBy similarity3
Nucleotide bindingi1102 – 1104ATPBy similarity3
Nucleotide bindingi1109 – 1113ATPBy 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-400042 Adrenaline,noradrenaline inhibits insulin secretion
R-MMU-418597 G alpha (z) signalling events
R-MMU-5610787 Hedgehog 'off' state

<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 6 (EC:4.6.1.16 Publications)
Alternative name(s):
ATP pyrophosphate-lyase 6
Adenylate cyclase type VI
Adenylyl cyclase 62 Publications
Short name:
AC62 Publications
Ca(2+)-inhibitable 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:Adcy6
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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

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

More...
MGIi
MGI:87917 Adcy6

<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 – 149CytoplasmicSequence analysisAdd BLAST149
<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>Transmembranei150 – 166HelicalSequence analysisAdd BLAST17
Transmembranei179 – 195HelicalSequence analysisAdd BLAST17
Transmembranei212 – 228HelicalSequence analysisAdd BLAST17
Transmembranei237 – 253HelicalSequence analysisAdd BLAST17
Transmembranei257 – 273HelicalSequence analysisAdd BLAST17
Transmembranei287 – 303HelicalSequence analysisAdd BLAST17
Topological domaini304 – 670CytoplasmicSequence analysisAdd BLAST367
Transmembranei671 – 688HelicalSequence analysisAdd BLAST18
Transmembranei699 – 715HelicalSequence analysisAdd BLAST17
Transmembranei740 – 756HelicalSequence analysisAdd BLAST17
Topological domaini757 – 816ExtracellularSequence analysisAdd BLAST60
Transmembranei817 – 833HelicalSequence analysisAdd BLAST17
Transmembranei836 – 852HelicalSequence analysisAdd BLAST17
Transmembranei894 – 910HelicalSequence analysisAdd BLAST17
Topological domaini911 – 1165CytoplasmicSequence analysisAdd BLAST255

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, Membrane

<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

Mutant mice are born at the expected Mendelian rate, present no obvious phenotype and are fertile (PubMed:18071070, PubMed:20466003, PubMed:23753526, PubMed:24277577). Their hearts display a decrease in left ventricular pressure, both at the basal level and after activation of beta-adrenergic receptors (PubMed:18071070). Besides, their hearts show defects in sarcoplasmic Ca2+ uptake and storage, and decreased levels of protein phosphorylation (PubMed:18071070). Male mice show increased mortality after transversal aortic constriction (PubMed:20359598). In contrast, female mice do not show increased mortality after transversal aortic constriction, and develop less heart hypertrophy and fibrosis than wild-type (PubMed:20359598). Compared to wild-type, mutant mice drink more and produce greater volumes of urine with decreased osmolarity, but there is no difference in the total quantity of excreted urinary solutes and no difference in blood plasma composition (PubMed:20466003, PubMed:20864687). The impaired urinary water homeostasis is due to retention of AQP2 in intracellular vesicles and decreased AQP2 levels at the cell membrane (PubMed:20466003). Mutant mice display increased urinary inorganic phosphate excretion, but normal plasma phosphate levels (PubMed:24854272). Mutant mice display increased plasma levels of PTH and FGF23, the two principal regulators of urinary phosphate excretion (PubMed:24854272). Mutant mice display no obvious skeleton defects, but display less bone formation after load stress than wild-type (PubMed:24277577). Mutant mice lacking both Adcy6 and Pkd1 survive longer and have less severe polycystic kidney disease than mice lacking only Pkd1 (PubMed:24158982).8 Publications

<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_00001957001 – 1165Adenylate cyclase type 6Add BLAST1165

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 residuei53PhosphoserineBy similarity1
<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>Glycosylationi277N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei553PhosphoserineBy similarity1
Modified residuei573PhosphoserineCombined sources1
Modified residuei659PhosphoserineBy similarity1
Glycosylationi790N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi875N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei916PhosphothreonineBy similarity1

<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

Phosphorylation by RAF1 increases enzyme activity. Phosphorylation by PKA on Ser-659 inhibits the GNAS-mediated increase in catalytic activity. Phosphorylation by PKC on Ser-553, Ser-659 and Thr-916 inhibits catalytic activity.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q01341

MaxQB - The MaxQuant DataBase

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MaxQBi
Q01341

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

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PaxDbi
Q01341

PRoteomics IDEntifications database

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PRIDEi
Q01341

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q01341

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

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PhosphoSitePlusi
Q01341

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q01341

<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

Detected in kidney tubules (PubMed:20466003). Detected in primary bone cells with osteocyte morphology (PubMed:24277577). Detected in heart (at protein level) (PubMed:18071070). Highly expressed in heart (PubMed:1379717, PubMed:18071070). Detected in kidney, pancreas acini and ducts (PubMed:23753526). Expressed in cochlear outer and inner hair cells (PubMed:17567809). Weakly detectable in brain, intestine, lung and spleen (PubMed:1379717).6 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

In the inner ear, between 16 dpc and P1, present along the sterocilia of outer hair cells, but almost undetectable in inner hair cell hair bundle. From P3 onward, expression in outer hair cell bundles is restricted to their base and it is also expressed at the base of inner hair cell stereocilia.1 Publication

<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

Part of a complex containing AKAP5, ADCY5, PDE4C and PKD2 (PubMed:21670265).

Interacts with RAF1.

Interacts (via cytoplasmic N-terminus) with GNAS, GNB1 and GNG2 (By similarity).

By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000093939

<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

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

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SMRi
Q01341

Database of comparative protein structure models

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ModBasei
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

<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.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
COG2114 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000006941

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q01341

KEGG Orthology (KO)

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KOi
K08046

Database of Orthologous Groups

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OrthoDBi
215180at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q01341

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

More...
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>. 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_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 has 1 described isoform and 5 potential isoforms that are computationally mapped.Show allAlign All

Q01341-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSWFSGLLVP KVDERKTAWG ERNGQKRPRH ANRASGFCAP RYMSCLKNAE
60 70 80 90 100
PPSPTPAAHT RCPWQDEAFI RRAGPGRGVE LGLRSVALGF DDTEVTTPMG
110 120 130 140 150
TAEVAPDTSP RSGPSCWHRL VQVFQSKQFR SAKLERLYQR YFFQMNQSSL
160 170 180 190 200
TLLMAVLVLL MAVLLTFHAA PAQPQPAYVA LLTCASVLFV VLMVVCNRHS
210 220 230 240 250
FRQDSMWVVS YVVLGILAAV QVGGALAANP HSPSAGLWCP VFFVYITYTL
260 270 280 290 300
LPIRMRAAVL SGLGLSTLHL ILAWQLNSSD PFLWKQLGAN VVLFLCTNAI
310 320 330 340 350
GVCTHYPAEV SQRQAFQETR GYIQARLHLQ HENRQQERLL LSVLPQHVAM
360 370 380 390 400
EMKEDINTKK EDMMFHKIYI QKHDNVSILF ADIEGFTSLA SQCTAQELVM
410 420 430 440 450
TLNELFARFD KLAAENHCLR IKILGDCYYC VSGLPEARAD HAHCCVEMGV
460 470 480 490 500
DMIEAISLVR EVTGVNVNMR VGIHSGRVHC GVLGLRKWQF DVWSNDVTLA
510 520 530 540 550
NHMEAGGGRR IHITRATLQY LNGDYEVEPG RGGERNAYLK EQCIETFLIL
560 570 580 590 600
GASQKRKEEK AMLAKLQRTR ANSMEGLMPR WVPDRAFSRT KDSKAFRQMG
610 620 630 640 650
IDDSSKDNRG AQDALNPEDE VDEFLGRAID ARSIDQLRKD HVRRFLLTFQ
660 670 680 690 700
REDLEKKYSR KVDPRFGAYV ACALLVFCFI CFIQLLVFPY STLILGIYAA
710 720 730 740 750
IFLLLLVTVL ICAVCSCGSF FPKALQRLSR NIVRSRVHST AVGIFSVLLV
760 770 780 790 800
FISAIANMFT CNHTPIRTCA ARMLNLTPAD VTACHLQQLN YSLGLDAPLC
810 820 830 840 850
EGTAPTCSFP EYFVGNVLLS LLASSVFLHI SSIGKLAMTF ILGFTYLVLL
860 870 880 890 900
LLGPPAAIFD NYDLLLGVHG LASSNETFDG LDCPAVGRVA LKYMTPVILL
910 920 930 940 950
VFALALYLHA QQVESTARLD FLWKLQATGE KEEMEELQAY NRRLLHNILP
960 970 980 990 1000
KDVAAHFLAR ERRNDELYYQ SCECVAVMFA SIANFSEFYV ELEANNEGVE
1010 1020 1030 1040 1050
CLRLLNEIIA DFDEIISEER FRQLEKIKTI GSTYMAASGL NASTYDQVGR
1060 1070 1080 1090 1100
SHITALADYA MRLMEQMKHI NEHSFNNFQM KIGLNMGPVV AGVIGARKPQ
1110 1120 1130 1140 1150
YDIWGNTVNV SSRMDSTGVP DRIQVTTDLY QVLAAKGYQL ECRGVVKVKG
1160
KGEMTTYFLN GGPSS
Length:1,165
Mass (Da):130,319
Last modified:April 1, 1993 - 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:i24EE1BB45DF1E87E
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 are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F8VQ52F8VQ52_MOUSE
Adenylate cyclase
Adcy6
1,168Annotation score:

Annotation score:4 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>
A0A2I3BRC5A0A2I3BRC5_MOUSE
Adenylate cyclase
Adcy6 mCG_18405
1,166Annotation 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>
A0A2I3BRS6A0A2I3BRS6_MOUSE
Adenylate cyclase type 6
Adcy6
524Annotation score:

Annotation score:2 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>
A0A2I3BQ20A0A2I3BQ20_MOUSE
Adenylate cyclase type 6
Adcy6
194Annotation score:

Annotation score:1 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>
A0A2I3BS04A0A2I3BS04_MOUSE
Adenylate cyclase type 6
Adcy6
43Annotation score:

Annotation score:1 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 conflicti47K → N in AAA37182 (PubMed:1332848).Curated1
Sequence conflicti76G → A in AAA37182 (PubMed:1332848).Curated1
Sequence conflicti508 – 509GR → RAG in AAA37182 (PubMed:1332848).Curated2
Sequence conflicti737V → G in AAA37182 (PubMed:1332848).Curated1
Sequence conflicti881L → Q in AAA37182 (PubMed:1332848).Curated1
Sequence conflicti990V → M in AAA37182 (PubMed:1332848).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

More...
DDBJi
Links Updated
M93422 mRNA Translation: AAA37174.1
M96653 mRNA Translation: AAA37182.1

Protein sequence database of the Protein Information Resource

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PIRi
A49201

NCBI Reference Sequences

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RefSeqi
NP_031431.2, NM_007405.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
11512

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:11512

<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
M93422 mRNA Translation: AAA37174.1
M96653 mRNA Translation: AAA37182.1
PIRiA49201
RefSeqiNP_031431.2, NM_007405.2

3D structure databases

SMRiQ01341
ModBaseiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000093939

PTM databases

iPTMnetiQ01341
PhosphoSitePlusiQ01341
SwissPalmiQ01341

Proteomic databases

jPOSTiQ01341
MaxQBiQ01341
PaxDbiQ01341
PRIDEiQ01341

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
11512

Genome annotation databases

GeneIDi11512
KEGGimmu:11512

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
112
MGIiMGI:87917 Adcy6

Phylogenomic databases

eggNOGiKOG3619 Eukaryota
COG2114 LUCA
HOGENOMiHOG000006941
InParanoidiQ01341
KOiK08046
OrthoDBi215180at2759
PhylomeDBiQ01341

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-400042 Adrenaline,noradrenaline inhibits insulin secretion
R-MMU-418597 G alpha (z) signalling events
R-MMU-5610787 Hedgehog 'off' state

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Adcy6 mouse

Protein Ontology

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PROi
PR:Q01341

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

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

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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 nameiADCY6_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: Q01341
<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: April 1, 1993
Last sequence update: April 1, 1993
Last modified: September 18, 2019
This is version 166 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
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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