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Protein

Adenylate cyclase type 7

Gene

ADCY7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

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

Catalyzes the formation of cAMP in response to activation of G protein-coupled receptors (Probable). 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 (PubMed:23229509, PubMed:18541530). 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 (PubMed:23842570, PubMed:23229509). 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 similarity2 Publications3 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 ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activated by the G protein alpha subunit (PubMed:18541530). Activated by the G protein beta and gamma subunit complex (PubMed:23229509). Activated by GNA13 and GNA12 (PubMed:18541530). 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 (PubMed:12454008). Inhibited by lithium (By similarity).By similarity3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal 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 ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei372ATPBy similarity1
Binding sitei931ATPBy similarity1
Binding sitei1057ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi284 – 289ATPBy similarity6
Nucleotide bindingi326 – 328ATPBy similarity3
Nucleotide bindingi1010 – 1012ATPBy similarity3
Nucleotide bindingi1017 – 1021ATPBy 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

  • adenylate cyclase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionLyase
Biological processcAMP biosynthesis
LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-163359 Glucagon signaling in metabolic regulation
R-HSA-163615 PKA activation
R-HSA-164378 PKA activation in glucagon signalling
R-HSA-170660 Adenylate cyclase activating pathway
R-HSA-170670 Adenylate cyclase inhibitory pathway
R-HSA-418555 G alpha (s) signalling events
R-HSA-418594 G alpha (i) signalling events
R-HSA-418597 G alpha (z) signalling events
R-HSA-432040 Vasopressin regulates renal water homeostasis via Aquaporins
R-HSA-5610787 Hedgehog 'off' state

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P51828

<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 7Curated (EC:4.6.1.12 Publications)
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_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:ADCY7Imported
Synonyms:KIAA00371 Publication
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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 16

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000121281.12

Human Gene Nomenclature Database

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HGNCi
HGNC:238 ADCY7

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
600385 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P51828

<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; 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 – 33CytoplasmicSequence analysisAdd BLAST33
<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>Transmembranei34 – 54HelicalSequence analysisAdd BLAST21
Transmembranei63 – 83HelicalSequence analysisAdd BLAST21
Transmembranei95 – 117HelicalSequence analysisAdd BLAST23
Transmembranei122 – 142HelicalSequence analysisAdd BLAST21
Transmembranei147 – 167HelicalSequence 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
Transmembranei794 – 814HelicalSequence analysisAdd BLAST21
Topological domaini815 – 1080CytoplasmicSequence analysisAdd BLAST266

Keywords - Cellular componenti

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>Mutagenesisi477 – 482KMRASV → NAAIRS: Does not affect cAMP biosynthetic process in response to sphingosine 1-phosphate stimulation. Reduces by 40% cAMP biosynthetic process in response to C5 alpha chain stimulation. 1 Publication6
Mutagenesisi485 – 489TRYLE → NAAIR: Reduces cAMP biosynthetic process in response to C5 alpha chain stimulation and more severely in response to sphingosine 1-phosphate stimulation. 1 Publication5
Mutagenesisi491 – 496WGAARP → NAAIRS: Does not affect cAMP biosynthetic process in response to C5 alpha chain stimulation. Reduces by 40?60% cAMP biosynthetic process in response to sphingosine 1-phosphate stimulation. 1 Publication6
Mutagenesisi494 – 499ARPFAH → NAAIRS: Does not affect cAMP biosynthetic process in response to C5 alpha chain stimulation. Reduces by 40?60% cAMP biosynthetic process in response to sphingosine 1-phosphate stimulation. 1 Publication6
Mutagenesisi564 – 569SKSDDF → NAAIRS: Reduces cAMP biosynthetic process in response to C5 alpha chain stimulation and more severely in response to sphingosine 1-phosphate stimulation. 1 Publication6

Organism-specific databases

DisGeNET

More...
DisGeNETi
113

Open Targets

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OpenTargetsi
ENSG00000121281

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA28

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2097167

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
ADCY7

Domain mapping of disease mutations (DMDM)

More...
DMDMi
1706218

<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_00001957031 – 1080Adenylate cyclase type 7Add BLAST1080

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>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_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated by PRKCD.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P51828

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P51828

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

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PaxDbi
P51828

PeptideAtlas

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PeptideAtlasi
P51828

PRoteomics IDEntifications database

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PRIDEi
P51828

ProteomicsDB human proteome resource

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ProteomicsDBi
56430

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P51828

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

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PhosphoSitePlusi
P51828

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P51828

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000121281 Expressed in 215 organ(s), highest expression level in leukocyte

CleanEx database of gene expression profiles

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CleanExi
HS_ADCY7

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P51828 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P51828 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA041218
HPA048241

<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

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
106626, 3 interactors

Protein interaction database and analysis system

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IntActi
P51828, 3 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000254235

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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P51828

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

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SMRi
P51828

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini279 – 406Guanylate cyclase 1PROSITE-ProRule annotationAdd BLAST128
Domaini879 – 1023Guanylate cyclase 2PROSITE-ProRule annotationAdd BLAST145

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 pathway1 Publication6
Regioni491 – 499Mediates regulation of adenylate cyclase activity by sphingosine 1-phosphate-induced G alpha 13 pathway1 Publication9
Regioni506 – 584Modulates adenylate cyclase activity by modulating the binding of G(s)alpha to the high-affinity G(s)alpha binding site in 7C1a/7C21 PublicationAdd 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

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eggNOGi
KOG3619 Eukaryota
COG2114 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000159096

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000006941

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG050458

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P51828

KEGG Orthology (KO)

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KOi
K08047

Identification of Orthologs from Complete Genome Data

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OMAi
TNFYLVL

Database of Orthologous Groups

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OrthoDBi
EOG091G05JR

Database for complete collections of gene phylogenies

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PhylomeDBi
P51828

TreeFam database of animal gene trees

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TreeFami
TF313845

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.70.1230, 2 hits

Integrated resource of protein families, domains and functional sites

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

Pfam protein domain database

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

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF039050 Ade_cyc, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00044 CYCc, 2 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF55073 SSF55073, 2 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00452 GUANYLATE_CYCLASE_1, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>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 6 potential isoforms that are computationally mapped.Show allAlign All

P51828-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPAKGRYFLN EGEEGPDQDA LYEKYQLTSQ HGPLLLTLLL VAATACVALI
60 70 80 90 100
IIAFSQGDPS RHQAILGMAF LVLAVFAALS VLMYVECLLR RWLRALALLT
110 120 130 140 150
WACLVALGYV LVFDAWTKAA CAWEQVPFFL FIVFVVYTLL PFSMRGAVAV
160 170 180 190 200
GAVSTASHLL VLGSLMGGFT TPSVRVGLQL LANAVIFLCG NLTGAFHKHQ
210 220 230 240 250
MQDASRDLFT YTVKCIQIRR KLRIEKRQQE NLLLSVLPAH ISMGMKLAII
260 270 280 290 300
ERLKEHGDRR CMPDNNFHSL YVKRHQNVSI LYADIVGFTQ LASDCSPKEL
310 320 330 340 350
VVVLNELFGK FDQIAKANEC MRIKILGDCY YCVSGLPVSL PTHARNCVKM
360 370 380 390 400
GLDMCQAIKQ VREATGVDIN MRVGIHSGNV LCGVIGLRKW QYDVWSHDVS
410 420 430 440 450
LANRMEAAGV PGRVHITEAT LKHLDKAYEV EDGHGQQRDP YLKEMNIRTY
460 470 480 490 500
LVIDPRSQQP PPPSQHLPRP KGDAALKMRA SVRMTRYLES WGAARPFAHL
510 520 530 540 550
NHRESVSSGE THVPNGRRPK SVPQRHRRTP DRSMSPKGRS EDDSYDDEML
560 570 580 590 600
SAIEGLSSTR PCCSKSDDFY TFGSIFLEKG FEREYRLAPI PRARHDFACA
610 620 630 640 650
SLIFVCILLV HVLLMPRTAA LGVSFGLVAC VLGLVLGLCF ATKFSRCCPA
660 670 680 690 700
RGTLCTISER VETQPLLRLT LAVLTIGSLL TVAIINLPLM PFQVPELPVG
710 720 730 740 750
NETGLLAASS KTRALCEPLP YYTCSCVLGF IACSVFLRMS LEPKVVLLTV
760 770 780 790 800
ALVAYLVLFN LSPCWQWDCC GQGLGNLTKP NGTTSGTPSC SWKDLKTMTN
810 820 830 840 850
FYLVLFYITL LTLSRQIDYY CRLDCLWKKK FKKEHEEFET MENVNRLLLE
860 870 880 890 900
NVLPAHVAAH FIGDKLNEDW YHQSYDCVCV MFASVPDFKV FYTECDVNKE
910 920 930 940 950
GLECLRLLNE IIADFDELLL KPKFSGVEKI KTIGSTYMAA AGLSVASGHE
960 970 980 990 1000
NQELERQHAH IGVMVEFSIA LMSKLDGINR HSFNSFRLRV GINHGPVIAG
1010 1020 1030 1040 1050
VIGARKPQYD IWGNTVNVAS RMESTGELGK IQVTEETCTI LQGLGYSCEC
1060 1070 1080
RGLINVKGKG ELRTYFVCTD TAKFQGLGLN
Length:1,080
Mass (Da):120,308
Last modified:October 1, 1996 - 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:iE33951621E281242
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 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F5H4D1F5H4D1_HUMAN
Adenylate cyclase type 7
ADCY7
734Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H3BQ93H3BQ93_HUMAN
Adenylate cyclase type 7
ADCY7
530Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F5H699F5H699_HUMAN
Adenylate cyclase type 7
ADCY7
433Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
I3L3Q5I3L3Q5_HUMAN
Adenylate cyclase type 7
ADCY7
81Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H3BMA5H3BMA5_HUMAN
Adenylate cyclase type 7
ADCY7
108Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
I3L2Y1I3L2Y1_HUMAN
Adenylate cyclase type 7
ADCY7
17Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<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 BAA05021 differs from that shown. Reason: Erroneous initiation.Curated

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
D25538 mRNA Translation: BAA05021.2 Different initiation.
AC007597 Genomic DNA No translation available.
BC126271 mRNA Translation: AAI26272.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS10741.1

Protein sequence database of the Protein Information Resource

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PIRi
PN0453

NCBI Reference Sequences

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RefSeqi
NP_001105.1, NM_001114.4
XP_016878384.1, XM_017022895.1

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.513578

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000254235; ENSP00000254235; ENSG00000121281
ENST00000394697; ENSP00000378187; ENSG00000121281

Database of genes from NCBI RefSeq genomes

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GeneIDi
113

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:113

UCSC genome browser

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UCSCi
uc002egd.3 human

<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
D25538 mRNA Translation: BAA05021.2 Different initiation.
AC007597 Genomic DNA No translation available.
BC126271 mRNA Translation: AAI26272.1
CCDSiCCDS10741.1
PIRiPN0453
RefSeqiNP_001105.1, NM_001114.4
XP_016878384.1, XM_017022895.1
UniGeneiHs.513578

3D structure databases

ProteinModelPortaliP51828
SMRiP51828
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106626, 3 interactors
IntActiP51828, 3 interactors
STRINGi9606.ENSP00000254235

Chemistry databases

ChEMBLiCHEMBL2097167

PTM databases

iPTMnetiP51828
PhosphoSitePlusiP51828
SwissPalmiP51828

Polymorphism and mutation databases

BioMutaiADCY7
DMDMi1706218

Proteomic databases

EPDiP51828
MaxQBiP51828
PaxDbiP51828
PeptideAtlasiP51828
PRIDEiP51828
ProteomicsDBi56430

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000254235; ENSP00000254235; ENSG00000121281
ENST00000394697; ENSP00000378187; ENSG00000121281
GeneIDi113
KEGGihsa:113
UCSCiuc002egd.3 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
113
DisGeNETi113
EuPathDBiHostDB:ENSG00000121281.12

GeneCards: human genes, protein and diseases

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GeneCardsi
ADCY7
HGNCiHGNC:238 ADCY7
HPAiHPA041218
HPA048241
MIMi600385 gene
neXtProtiNX_P51828
OpenTargetsiENSG00000121281
PharmGKBiPA28

Human Unidentified Gene-Encoded large proteins database

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HUGEi
Search...

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3619 Eukaryota
COG2114 LUCA
GeneTreeiENSGT00940000159096
HOGENOMiHOG000006941
HOVERGENiHBG050458
InParanoidiP51828
KOiK08047
OMAiTNFYLVL
OrthoDBiEOG091G05JR
PhylomeDBiP51828
TreeFamiTF313845

Enzyme and pathway databases

ReactomeiR-HSA-163359 Glucagon signaling in metabolic regulation
R-HSA-163615 PKA activation
R-HSA-164378 PKA activation in glucagon signalling
R-HSA-170660 Adenylate cyclase activating pathway
R-HSA-170670 Adenylate cyclase inhibitory pathway
R-HSA-418555 G alpha (s) signalling events
R-HSA-418594 G alpha (i) signalling events
R-HSA-418597 G alpha (z) signalling events
R-HSA-432040 Vasopressin regulates renal water homeostasis via Aquaporins
R-HSA-5610787 Hedgehog 'off' state
SIGNORiP51828

Miscellaneous databases

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

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ChiTaRSi
ADCY7 human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
ADCY7

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
113

Protein Ontology

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PROi
PR:P51828

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000121281 Expressed in 215 organ(s), highest expression level in leukocyte
CleanExiHS_ADCY7
ExpressionAtlasiP51828 baseline and differential
GenevisibleiP51828 HS

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

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ProtoNeti
Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiADCY7_HUMAN
<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: P51828
Secondary accession number(s): A0AVA6
<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, 1996
Last sequence update: October 1, 1996
Last modified: December 5, 2018
This is version 160 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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