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Entry version 147 (18 Sep 2019)
Sequence version 2 (12 Apr 2005)
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Protein

Adenylate cyclase type 1

Gene

Adcy1

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 in response to G-protein signaling. Mediates responses to increased cellular Ca2+/calmodulin levels (PubMed:9662407, PubMed:7816821). May be involved in regulatory processes in the central nervous system (PubMed:9662407). May play a role in memory and learning (PubMed:7816821). Plays a role in the regulation of the circadian rhythm of daytime contrast sensitivity probably by modulating the rhythmic synthesis of cyclic AMP in the retina (PubMed:24048828).3 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 calcium/calmodulin (PubMed:9662407). Activated by forskolin. Activated by the G protein alpha subunit GNAS. Inhibited by the G protein beta and gamma subunit complex. Inhibited by the ATP analogs adenosine, 2'-deoxyadenosine and 2'-deoxy-3'-AMP.By similarity1 Publication

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 bindingi307Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi307Magnesium 2; catalyticPROSITE-ProRule annotation1
Metal bindingi308Magnesium 2; via carbonyl oxygen; catalyticPROSITE-ProRule annotation1
Metal bindingi351Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi351Magnesium 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 sitei395ATPBy similarity1
Binding sitei919ATPBy similarity1
Binding sitei1043ATPBy 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 bindingi307 – 312ATPBy similarity6
Nucleotide bindingi349 – 351ATPBy similarity3
Nucleotide bindingi996 – 998ATPBy similarity3
Nucleotide bindingi1003 – 1007ATPBy 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 functionCalmodulin-binding, Lyase
Biological processBiological rhythms, cAMP biosynthesis
LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.6.1.1 3474

Reactome - a knowledgebase of biological pathways and processes

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

<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 1 (EC:4.6.1.11 Publication)
Alternative name(s):
ATP pyrophosphate-lyase 1
Adenylate cyclase type I
Adenylyl cyclase 1
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:Adcy1
<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: Chromosome 11

Organism-specific databases

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

More...
MGIi
MGI:99677 Adcy1

<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 – 62CytoplasmicSequence analysisAdd BLAST62
<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>Transmembranei63 – 83HelicalSequence analysisAdd BLAST21
Transmembranei87 – 107HelicalSequence analysisAdd BLAST21
Transmembranei124 – 144HelicalSequence analysisAdd BLAST21
Transmembranei157 – 177HelicalSequence analysisAdd BLAST21
Transmembranei182 – 202HelicalSequence analysisAdd BLAST21
Transmembranei213 – 233HelicalSequence analysisAdd BLAST21
Topological domaini234 – 609CytoplasmicSequence analysisAdd BLAST376
Transmembranei610 – 630HelicalSequence analysisAdd BLAST21
Transmembranei634 – 654HelicalSequence analysisAdd BLAST21
Transmembranei673 – 693HelicalSequence analysisAdd BLAST21
Transmembranei724 – 744HelicalSequence analysisAdd BLAST21
Transmembranei752 – 772HelicalSequence analysisAdd BLAST21
Transmembranei774 – 793HelicalSequence analysisAdd BLAST20
Topological domaini794 – 1118CytoplasmicSequence analysisAdd BLAST325

Keywords - Cellular componenti

Cell membrane, Cytoplasm, 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

Mice appear grossly normal and healthy, but have decreased levels of calmodulin-sensitive adenylyl cyclase activity in the brain (PubMed:7816821). They show impaired spatial memory (PubMed:7816821). Mice show a significant reduction in daytime contrast sensitivity (PubMed:24048828).2 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_00001956831 – 1118Adenylate cyclase type 1Add BLAST1118

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 residuei550PhosphoserineCombined 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>Glycosylationi703N-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

N-glycosylated.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
O88444

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

More...
PaxDbi
O88444

PeptideAtlas

More...
PeptideAtlasi
O88444

PRoteomics IDEntifications database

More...
PRIDEi
O88444

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O88444

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

More...
PhosphoSitePlusi
O88444

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
O88444

<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

Expressed throughout inner ear development.1 Publication

<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

Expression in the retina oscillates in a circadian manner.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000020431 Expressed in 227 organ(s), highest expression level in cerebellum

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
O88444 MM

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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_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

Interacts with CALM.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000020706

<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
O88444

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

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>Regioni492 – 519Interaction with calmodulinBy similarityAdd BLAST28
Regioni1023 – 1046Interaction with calmodulinBy similarityAdd BLAST24

<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 modules have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two modules.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
COG2114 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000154872

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000006941

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O88444

KEGG Orthology (KO)

More...
KOi
K08041

Identification of Orthologs from Complete Genome Data

More...
OMAi
KYKQIER

Database of Orthologous Groups

More...
OrthoDBi
594476at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O88444

TreeFam database of animal gene trees

More...
TreeFami
TF313845

Family and domain databases

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
IPR029787 Nucleotide_cyclase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF16214 AC_N, 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>Sequencei

<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.

O88444-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAGAPRGQGG GGGAGEPGGA ERAAGPGGRR GFRACGEEFA CPELEALFRG
60 70 80 90 100
YTLRLEQAAT LKALAVLSLL AGALALAELL GAPGPAPGLA KGSHPVHCIL
110 120 130 140 150
FLALFVVTNV RSLQVSQLQQ VGQLALFFSL TFALLCCPFA LGGPARSSAG
160 170 180 190 200
GAMGSTVAEQ GVWQLLLVTF VSYALLPVRS LLAIGFGLVV AASHLLVTAA
210 220 230 240 250
LVPAKRPRLW RTLGANALLF FGVNMYGVFV RILTERSQRK AFLQARNCIE
260 270 280 290 300
DRLRLEDENE KQERLLMSLL PRNVAMEMKE DFLKPPERIF HKIYIQRHDN
310 320 330 340 350
VSILFADIVG FTGLASQCTA QELVKLLNEL FGKFDELATE NHCRRIKILG
360 370 380 390 400
DCYYCVSGLT QPKTDHAHCC VEMGLDMIDT ITSVAEATEV DLNMRVGLHT
410 420 430 440 450
GRVLCGVLGL RKWQYDVWSN DVTLANVMEA AGLPGKVHIT KTTLACLNGD
460 470 480 490 500
YEVEPGHGHE RNTFLRTHNI ETFFIVPSHR RKIFPGLILS DIKPAKRMKF
510 520 530 540 550
KTVCYLLVQL MHCRKMFKAE IPFSNVMTCE DDDKRRALRT ASEKLRNRSS
560 570 580 590 600
FSTNVVYTTP GTRVNRYISR LLEARQTELE MADLNFFTLK YKHVEREQKY
610 620 630 640 650
HQLQDEYFTS AVVLALILAA LFGLIYLLVI PQSVAVLLLL VFSICFLVAC
660 670 680 690 700
TLYLHITRVQ CFPGCLTIQI RTALCVFIVV LIYSVAQGCV VGCLPWAWSS
710 720 730 740 750
QSNSSLVVLA AGGRRTVLPA LPCESAHHAL LCCLVGTLPL AIFLRVSSLP
760 770 780 790 800
KMILLSGLTT SYILVLELSG YTKVGGGALS GRSYEPIMAI LLFSCTLALH
810 820 830 840 850
ARQVDVRLRL DYLWAAQAEE ERDDMERVKL DNKRILFNLL PAHVAQHFLM
860 870 880 890 900
SNPRNMDLYY QSYSQVGVMF ASIPNFNDFY IELDGNNMGV ECLRLLNEII
910 920 930 940 950
ADFDELMDKD FYKDLEKIKT IGSTYMAAVG LAPTAGTRAK KSISSHLCTL
960 970 980 990 1000
ADFAIDMFDV LDEINYQSYN DFVLRVGINV GPVVAGVIGA RRPQYDIWGN
1010 1020 1030 1040 1050
TVNVASRMDS TGVQGRIQVT EEVHRLLKRC SYQFVCRGKV SVKGKGEMLT
1060 1070 1080 1090 1100
YFLEGRTDGN SSHGRTFRLE RRMCPYGRGG GQARRPPLCP AAGPPVRPGL
1110
PPAPTSQYLS STAAGKEA
Length:1,118
Mass (Da):123,373
Last modified:April 12, 2005 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iCEFAFF3940B22277
GO

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 conflicti147 – 155SSAGGAMGS → ALQEAQWAR in AAC29478 (PubMed:9662407).Curated9
Sequence conflicti234T → A in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti270L → M in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti319T → K in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti466R → K in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti523F → I in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti542S → T in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti549S → T in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti570R → L in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti598Q → R in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti692G → V in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti697A → S in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti707V → L in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti713G → C in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti720 – 721AL → GP in AAC29478 (PubMed:9662407).Curated2
Sequence conflicti774 – 776VGG → AMGA in AAC29478 (PubMed:9662407).Curated3
Sequence conflicti867 – 869GVM → AVL in AAC29478 (PubMed:9662407).Curated3
Sequence conflicti938R → K in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti991R → C in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti1020T → I in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti1030C → S in AAC29478 (PubMed:9662407).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AL669838 Genomic DNA No translation available.
AF053980 mRNA Translation: AAC29478.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS24426.1

NCBI Reference Sequences

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RefSeqi
NP_033752.1, NM_009622.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000020706; ENSMUSP00000020706; ENSMUSG00000020431

Database of genes from NCBI RefSeq genomes

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GeneIDi
432530

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:432530

UCSC genome browser

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UCSCi
uc007hzf.1 mouse

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL669838 Genomic DNA No translation available.
AF053980 mRNA Translation: AAC29478.1
CCDSiCCDS24426.1
RefSeqiNP_033752.1, NM_009622.1

3D structure databases

SMRiO88444
ModBaseiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000020706

PTM databases

iPTMnetiO88444
PhosphoSitePlusiO88444
SwissPalmiO88444

Proteomic databases

MaxQBiO88444
PaxDbiO88444
PeptideAtlasiO88444
PRIDEiO88444

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020706; ENSMUSP00000020706; ENSMUSG00000020431
GeneIDi432530
KEGGimmu:432530
UCSCiuc007hzf.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
107
MGIiMGI:99677 Adcy1

Phylogenomic databases

eggNOGiKOG3619 Eukaryota
COG2114 LUCA
GeneTreeiENSGT00940000154872
HOGENOMiHOG000006941
InParanoidiO88444
KOiK08041
OMAiKYKQIER
OrthoDBi594476at2759
PhylomeDBiO88444
TreeFamiTF313845

Enzyme and pathway databases

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

Miscellaneous databases

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

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ChiTaRSi
Adcy1 mouse

Protein Ontology

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PROi
PR:O88444

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000020431 Expressed in 227 organ(s), highest expression level in cerebellum
GenevisibleiO88444 MM

Family and domain databases

Gene3Di3.30.70.1230, 2 hits
InterProiView protein in InterPro
IPR001054 A/G_cyclase
IPR018297 A/G_cyclase_CS
IPR032628 AC_N
IPR030672 Adcy
IPR029787 Nucleotide_cyclase
PfamiView protein in Pfam
PF16214 AC_N, 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

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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 nameiADCY1_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: O88444
Secondary accession number(s): Q5SS89
<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: December 21, 2004
Last sequence update: April 12, 2005
Last modified: September 18, 2019
This is version 147 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

Keywords - Technical termi

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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