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Entry version 139 (12 Aug 2020)
Sequence version 1 (01 Nov 1997)
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Protein

Adenylate cyclase type 7

Gene

ADCY7

Organism
Bos taurus (Bovine)
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 transcript leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

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

Catalyzes the formation of cAMP in response to activation of G protein-coupled receptors. Functions in signaling cascades activated namely by thrombin and sphingosine 1-phosphate and mediates regulation of cAMP synthesis through synergistic action of the stimulatory G alpha protein with GNA13 (By similarity). Also, during inflammation, mediates zymosan-induced increase intracellular cAMP, leading to protein kinase A pathway activation in order to modulate innate immune responses through heterotrimeric G proteins G(12/13) (By similarity). Functions in signaling cascades activated namely by dopamine and C5 alpha chain and mediates regulation of cAMP synthesis through synergistic action of the stimulatory G protein with G beta:gamma complex (By similarity). Functions, through cAMP response regulation, to keep inflammation under control during bacterial infection by sensing the presence of serum factors, such as the bioactive lysophospholipid (LPA) that regulate LPS-induced TNF-alpha production. However, it is also required for the optimal functions of B and T cells during adaptive immune responses by regulating cAMP synthesis in both B and T cells (By similarity).By similarity

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

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

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

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

Activated by the G protein alpha subunit. Activated by the G protein beta and gamma subunit complex. Activated by GNA13 and GNA12. Ethanol and phorbol 12,13-dibutanoate significantly potentiate adenylate cyclase activity generated in response to the activation of the prostanoid receptor by the agonist prostaglandin E11- in a PKC-dependent manner (By similarity). Inhibited by lithium (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi284Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi284Magnesium 2; catalyticPROSITE-ProRule annotation1
Metal bindingi285Magnesium 2; via carbonyl oxygen; catalyticPROSITE-ProRule annotation1
Metal bindingi328Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi328Magnesium 2; catalyticPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei372ATPBy similarity1
Binding sitei929ATPBy similarity1
Binding sitei1055ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi284 – 289ATPBy similarity6
Nucleotide bindingi326 – 328ATPBy similarity3
Nucleotide bindingi1008 – 1010ATPBy similarity3
Nucleotide bindingi1015 – 1019ATPBy 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

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Adenylate cyclase type 7By similarity (EC:4.6.1.1)
Alternative name(s):
ATP pyrophosphate-lyase 7
Adenylate cyclase type VII
Adenylyl cyclase 7
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ADCY7By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBos taurus (Bovine)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9913 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaRuminantiaPecoraBovidaeBovinaeBos
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000009136 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

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

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 33CytoplasmicSequence analysisAdd BLAST33
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei34 – 54HelicalSequence analysisAdd BLAST21
Transmembranei63 – 83HelicalSequence analysisAdd BLAST21
Transmembranei95 – 120HelicalSequence analysisAdd BLAST26
Transmembranei125 – 145HelicalSequence analysisAdd BLAST21
Transmembranei150 – 170HelicalSequence analysisAdd BLAST21
Transmembranei176 – 196HelicalSequence analysisAdd BLAST21
Topological domaini197 – 594CytoplasmicSequence analysisAdd BLAST398
Transmembranei595 – 615HelicalSequence analysisAdd BLAST21
Transmembranei620 – 640HelicalSequence analysisAdd BLAST21
Transmembranei669 – 688HelicalSequence analysisAdd BLAST20
Transmembranei718 – 737HelicalSequence analysisAdd BLAST20
Transmembranei746 – 773HelicalSequence analysisAdd BLAST28
Transmembranei792 – 812HelicalSequence analysisAdd BLAST21
Topological domaini813 – 1078CytoplasmicSequence analysisAdd BLAST266

Keywords - Cellular componenti

Membrane

<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_00001957021 – 1078Adenylate cyclase type 7Add BLAST1078

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi701N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi776N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi781N-linked (GlcNAc...) asparagineSequence analysis1

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

Phosphorylated by PRKCD.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

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

More...
PaxDbi
Q29450

PRoteomics IDEntifications database

More...
PRIDEi
Q29450

<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

Found exclusively in the retinal pigment epithelium.

<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

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9913.ENSBTAP00000008153

<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
Q29450

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>Regioni477 – 482Mediates regulation of adenylate cyclase activity by C5 alpha-induced G- beta and gamma pathwayBy similarity6
Regioni491 – 499Mediates regulation of adenylate cyclase activity by sphingosine 1-phosphate-induced G alpha 13 pathwayBy similarity9
Regioni506 – 584Modulates adenylate cyclase activity by modulating the binding of G(s)alpha to the high-affinity G(s)alpha binding site in 7C1a/7C2By similarityAdd BLAST79

<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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_001072_2_5_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q29450

KEGG Orthology (KO)

More...
KOi
K08047

Database of Orthologous Groups

More...
OrthoDBi
363718at2759

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
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, 1 hit
PS50125, GUANYLATE_CYCLASE_2, 2 hits

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

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

Q29450-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPAKGRYFLN EGEEGPDQDA LYEKYRLTSQ HGPLLLMLLL VAIAACTTLI
60 70 80 90 100
VITFSYGDPS RHRAVLGTAF FTLAMFVLLY ALVYVECLDR RGLRISALLI
110 120 130 140 150
WGCLVTLGYV LVFDFDSPRK DTLCLWGRCP SSSFVVFVVY TLLPFSMWGA
160 170 180 190 200
VTAGLVSSIS HLLVLAMHQE DFTSPVGLKL LATAVVFVCG NLTGAFHKHH
210 220 230 240 250
MQDASHDLFT YTVKCIQIRR KLRIEKRQQE NLLLSVLPAH ISMGMKLAII
260 270 280 290 300
ERLKERGDRR YLPDNNFHNL YVKRHQNVSI LYADIVGFTR LASDCSPKEL
310 320 330 340 350
VVVLNELFGK FDQIAKANEC MRIKILGDCY YCVSGLPVSL PNHARNCVKM
360 370 380 390 400
GLDMCEAIKQ VREATGVDIS MRVGIHSGNV LCGVIGLRKW QYDVWSHDVS
410 420 430 440 450
LANRMEAAGV PGRVHITEAT LKHLDKAYEV EDGHGQQRDP YLKEMNIRTY
460 470 480 490 500
LVIDPRSQQP PQPSQHNSKN KGNATLKMRA SVRMTRYLES WGAARPFAHL
510 520 530 540 550
NQRESVSSSE TLVSHGRRPK AVPLRRHRTP DRSASPKGRS EDDSYDDEML
560 570 580 590 600
SAIEGLSSTR PCCSKSDDFS TFGSIFLEKG FEREYRLAPI PRVRYYFACA
610 620 630 640 650
SLVFVCILLI HVLLLYSMKT LGVSFGLVAC VLGLVLGLCF ADVFLRCCPA
660 670 680 690 700
LGKLRAIAES VETQPLLRVS LAILTIGSLL VIAVVNLPLM PFRDRGLTAG
710 720 730 740 750
NETGLRAVSG WEMSPCYLLP YYTCSCILAF IACSVFLRMS LELKVVLLTV
760 770 780 790 800
ALVAYLVLFN VYPSWQWDCC GHSLGNLTGT NGTLSSSSCS WHLKTMTNFY
810 820 830 840 850
LVLFYTTLIM LSRQIDYYCR LDCLWKKKFK KEHEEFETME NVNRLLLENV
860 870 880 890 900
LPAHVAAHFI GDKLNEDWYH QSYDCVCVMF ASVPDFKVFY TECDVNKEGL
910 920 930 940 950
ECLRLLNEII ADFDELLLKP KFSGVEKIKT IGSTYMAAAG LSVPSGPENQ
960 970 980 990 1000
DLERQHAHIG IMVEFSTALM SKLDGINRHS FNSFRLRVGI NHGPVIAGVI
1010 1020 1030 1040 1050
GARKPQYDIW GNTVNVASRM ESTGELGKIQ VTEETCTILQ GLGYSCECRG
1060 1070
LIDVKGKGEL RTYFVCTDTA KFQGLGLN
Length:1,078
Mass (Da):120,820
Last modified:November 1, 1997 - 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:i50E89BF08E37FCBB
GO

<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 CAA89894 differs from that shown. Reason: Erroneous initiation.Curated

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
Z49806 mRNA Translation: CAA89894.1 Different initiation.

NCBI Reference Sequences

More...
RefSeqi
NP_776655.1, NM_174230.2
XP_005218501.1, XM_005218444.3

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
281603

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bta:281603

<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
Z49806 mRNA Translation: CAA89894.1 Different initiation.
RefSeqiNP_776655.1, NM_174230.2
XP_005218501.1, XM_005218444.3

3D structure databases

SMRiQ29450
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000008153

Proteomic databases

PaxDbiQ29450
PRIDEiQ29450

Genome annotation databases

GeneIDi281603
KEGGibta:281603

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
113

Phylogenomic databases

eggNOGiKOG3619, Eukaryota
HOGENOMiCLU_001072_2_5_1
InParanoidiQ29450
KOiK08047
OrthoDBi363718at2759
TreeFamiTF313845

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, 1 hit
PS50125, GUANYLATE_CYCLASE_2, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiADCY7_BOVIN
<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: Q29450
Secondary accession number(s): O02856
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: August 12, 2020
This is version 139 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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