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UniProtKB - Q03343 (ADCY6_RAT)

Entry version 172 (02 Jun 2021)
Sequence version 1 (01 Oct 1993)
Previous versions | rss
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Protein

Adenylate cyclase type 6

Gene

Adcy6

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 the signaling molecule cAMP downstream of G protein-coupled receptors (PubMed:1409703, PubMed:15385642, PubMed:17110384, PubMed:21606183).

Functions in signaling cascades downstream of beta-adrenergic receptors in the heart and in vascular smooth muscle cells (PubMed:21606183).

Functions in signaling cascades downstream of the vasopressin receptor in the kidney and has a role in renal water reabsorption. Functions in signaling cascades downstream of PTH1R and plays a role in regulating renal phosphate excretion. Functions in signaling cascades downstream of the VIP and SCT receptors in pancreas and contributes to the regulation of pancreatic amylase and fluid secretion (By similarity).

Signaling mediates cAMP-dependent activation of protein kinase PKA (PubMed:21606183).

This promotes increased phosphorylation of various proteins, including AKT. Plays a role in regulating cardiac sarcoplasmic reticulum Ca2+ uptake and storage, and is required for normal heart ventricular contractibility. May contribute to normal heart function (By similarity).

Mediates vasodilatation after activation of beta-adrenergic receptors by isoproterenol (By similarity).

Contributes to bone cell responses to mechanical stimuli (By similarity).

By similarity4 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+2 PublicationsNote: 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:9391159). Inhibited by calcium ions, already at micromolar concentrations (By similarity). Inhibited by adenosine, AMP and their analogs (By similarity). Activated by GNAS (PubMed:9391159, PubMed:17110384). Is further activated by the complex formed by GNB1 and GNG2 (PubMed:17110384). Phosphorylation by RAF1 results in its activation (PubMed:15385642).By similarity2 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 sitei1029ATPBy similarity1
Binding sitei1150ATPBy 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 bindingi1103 – 1105ATPBy similarity3
Nucleotide bindingi1110 – 1114ATPBy 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-RNO-163615, PKA activation
R-RNO-170660, Adenylate cyclase activating pathway
R-RNO-170670, Adenylate cyclase inhibitory pathway
R-RNO-400042, Adrenaline,noradrenaline inhibits insulin secretion
R-RNO-418597, G alpha (z) signalling events
R-RNO-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:4.6.1.15 Publications)
Alternative name(s):
ATP pyrophosphate-lyase 6
Adenylate cyclase type VI
Short name:
ACVI
Adenylyl cyclase 6
Short name:
AC61 Publication
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>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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<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		2035, 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

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 – 671CytoplasmicSequence analysisAdd BLAST368
Transmembranei672 – 689HelicalSequence analysisAdd BLAST18
Transmembranei700 – 716HelicalSequence analysisAdd BLAST17
Transmembranei741 – 757HelicalSequence analysisAdd BLAST17
Topological domaini758 – 817ExtracellularSequence analysisAdd BLAST60
Transmembranei818 – 834HelicalSequence analysisAdd BLAST17
Transmembranei837 – 853HelicalSequence analysisAdd BLAST17
Transmembranei895 – 911HelicalSequence analysisAdd BLAST17
Topological domaini912 – 1166CytoplasmicSequence 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

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>Mutagenesisi311S → A: No effect on phosphorylation by PKC. 1 Publication1
Mutagenesisi554S → A: Reduces phosphorylation by PKC and PKC-mediated inhibition. 1 Publication1
Mutagenesisi660S → A: Abolishes phosphorylation by PKA and PKA-mediated down-regulation of enzyme activity. 1 Publication1
Mutagenesisi660S → A: Reduces phosphorylation by PKC and PKC-mediated inhibition. 1 Publication1
Mutagenesisi917T → A: Reduces phosphorylation by PKC, abolishes PKC-mediated inhibition. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2095179

DrugCentral

More...DrugCentrali		Q03343

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001957011 – 1166Adenylate cyclase type 6Add BLAST1166

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 residuei53PhosphoserineCombined sources1
Modified residuei554Phosphoserine; by PKC; in vitro1 Publication1
Modified residuei574PhosphoserineCombined sources1
Modified residuei660Phosphoserine; by PKA; in vitro1 Publication1
Modified residuei660Phosphoserine; by PKC; in vitro1 Publication1
<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>Glycosylationi791N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi876N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei917Phosphothreonine; by PKC; in vitro1 Publication1

<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 (PubMed:15385642). Phosphorylation by PKA on Ser-660 inhibits the GNAS-mediated increase in catalytic activity (PubMed:9391159). Phosphorylation by PKC on Ser-554, Ser-660 and Thr-917 inhibits catalytic activity (PubMed:11877398).3 Publications

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

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

More...PaxDbi		Q03343

PRoteomics IDEntifications database

More...PRIDEi		Q03343

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		Q03343, 2 sites

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q03343

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

More...PhosphoSitePlusi		Q03343

SwissPalm database of S-palmitoylation events

More...SwissPalmi		Q03343

<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 brain and kidney (PubMed:1409703). Detected in vascular smooth muscle cells (PubMed:21606183).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

Part of a complex containing AKAP5, ADCY5, PDE4C and PKD2 (By similarity).

Interacts with RAF1 (PubMed:15385642).

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

By similarity1 Publication

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

Protein interaction database and analysis system

More...IntActi		Q03343, 2 interactors

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000016624

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q03343

<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

More...SMRi		Q03343

Database of comparative protein structure models

More...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

More...eggNOGi		KOG3619, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q03343

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q03343

Family and domain databases

Conserved Domains Database

More...CDDi		cd07302, CHD, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.70.1230, 2 hits

Integrated resource of protein families, domains and functional sites

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

Pfam protein domain database

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

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF039050, Ade_cyc, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00044, CYCc, 2 hits

Superfamily database of structural and functional annotation

More...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 2 potential isoforms that are computationally mapped.Show allAlign All

Q03343-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSWFSGLLVP KVDERKTAWG ERNGQKRPRQ ATRARGFCAP RYMSCLKNVE 
        60         70         80         90        100
PPSPTPAART RCPWQDEAFI RRAGPGRGVK LGLRSVALGF DDTEVTTPMG 
       110        120        130        140        150
TAEVAPDTSP RSGPSCWHRL AQVFQSKQFR SAKLERLYQR YFFQMNQSSL 
       160        170        180        190        200
TLLMAVLVLL MAVLLTFHAA PALPQPAYVA LLTCASVLFV VLMVVCNRHS 
       210        220        230        240        250
FRQDSMWVVS YVVLGILAAV QVGGALAANP RSPSAGLWCP VFFVYITYTL 
       260        270        280        290        300
LPIRMRAAVL SGLGLSTLHL ILAWHLNNGD 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
NHMEAGGRAG RIHITRATLQ YLNGDYEVEP GRGGERNGYL KEQCIETFLI 
       560        570        580        590        600
LGASQKRKEE KAMLVKLQRT RANSMEGLMP RWVPDRAFSR TKDSKAFRQM 
       610        620        630        640        650
GIDDSSKENR GAQDALNPED EVDEFLGRAI DARSIDQLRK DHVRRFLLTF 
       660        670        680        690        700
QREDLEKKYS RKVDPRFGAY VACALLVFCF ICFIQFLVFP HSALILGIYA 
       710        720        730        740        750
GIFLLLLVTV LICAVCSCGS FFPNALQRLS RSIVRSRVHS TAVGVFSVLL 
       760        770        780        790        800
VFISAIANMF TCSHTPLRTC AARMLNLTPS DVTACHLRQI NYSLGLEAPL 
       810        820        830        840        850
CEGTAPTCSF PEYFVGSVLL SLLASSVFLH ISSIGKLVMT FVLGFIYLLL 
       860        870        880        890        900
LLLGPPATIF DNYDLLLSVH GLASSNETFD GLDCPAVGRV ALKYMTPVIL 
       910        920        930        940        950
LVFALALYLH AQQVESTARL DFLWKLQATG EKEEMEELQA YNRRLLHNIL 
       960        970        980        990       1000
PKDVAAHFLA RERRNDELYY QSCECVAVMF ASIANFSEFY VELEANNEGV 
      1010       1020       1030       1040       1050
ECLRLLNEII ADFDEIISEE RFRQLEKIKT IGSTYMAASG LNASTYDQVG 
      1060       1070       1080       1090       1100
RSHITALADY AMRLMEQMKH INEHSFNNFQ MKIGLNMGPV VAGVIGARKP 
      1110       1120       1130       1140       1150
QYDIWGNTVN VSSRMDSTGV PDRIQVTTDL YQVLAAKGYQ LECRGVVKVK 
      1160 
GKGEMTTYFL NGGPSS
Length:1,166
Mass (Da):130,506
Last modified:October 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:i5042C650546E4E79
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2K429A0A0G2K429_RAT
Adenylate cyclase type 6
Adcy6 rCG_50695
1,180Annotation 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>
F1LSD1F1LSD1_RAT
Adenylate cyclase type 6
Adcy6 rCG_50695
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>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA40678 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

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 conflicti80K → E in AAA40678 (PubMed:1409703).Curated1
Sequence conflicti130R → P in AAA40678 (PubMed:1409703).Curated1
Sequence conflicti538G → A in AAA40678 (PubMed:1409703).Curated1
Sequence conflicti790I → L in AAA40678 (PubMed:1409703).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
L01115 mRNA Translation: AAA40676.1
M96160 mRNA Translation: AAA40678.1 Different initiation.

Protein sequence database of the Protein Information Resource

More...PIRi		A47202

NCBI Reference Sequences

More...RefSeqi		NP_036953.4, NM_012821.4

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		25289

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:25289

UCSC genome browser

More...UCSCi		RGD:2035, rat

<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
L01115 mRNA Translation: AAA40676.1
M96160 mRNA Translation: AAA40678.1 Different initiation.
PIRiA47202
RefSeqiNP_036953.4, NM_012821.4

3D structure databases

SMRiQ03343
ModBaseiSearch...

Protein-protein interaction databases

IntActiQ03343, 2 interactors
STRINGi10116.ENSRNOP00000016624

Chemistry databases

BindingDBiQ03343
ChEMBLiCHEMBL2095179
DrugCentraliQ03343

PTM databases

GlyGeniQ03343, 2 sites
iPTMnetiQ03343
PhosphoSitePlusiQ03343
SwissPalmiQ03343

Proteomic databases

PaxDbiQ03343
PRIDEiQ03343

Genome annotation databases

GeneIDi25289
KEGGirno:25289
UCSCiRGD:2035, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		112
RGDi2035, Adcy6

Phylogenomic databases

eggNOGiKOG3619, Eukaryota
InParanoidiQ03343
PhylomeDBiQ03343

Enzyme and pathway databases

ReactomeiR-RNO-163615, PKA activation
R-RNO-170660, Adenylate cyclase activating pathway
R-RNO-170670, Adenylate cyclase inhibitory pathway
R-RNO-400042, Adrenaline,noradrenaline inhibits insulin secretion
R-RNO-418597, G alpha (z) signalling events
R-RNO-5610787, Hedgehog 'off' state

Miscellaneous databases

Protein Ontology

More...PROi		PR:Q03343

Family and domain databases

CDDicd07302, CHD, 1 hit
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

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_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: Q03343
<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: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 2, 2021
This is version 172 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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