Reviewed,
UniProtKB/Swiss-Prot P26770 (ADCY4_RAT)
Last modified
June 16, 2009.
Version 73.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Adenylate cyclase type 4 EC=4.6.1.1 Alternative name(s): Adenylate cyclase type IV ATP pyrophosphate-lyase 4 Adenylyl cyclase 4 | ||
| Gene names |
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| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 1064 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | This is a membrane-bound, calmodulin-insensitive adenylyl cyclase. |
| Catalytic activity | ATP = 3',5'-cyclic AMP + diphosphate. |
| Cofactor | Binds 2 magnesium ions per subunit By similarity. |
| Enzyme regulation | Insensitive to calcium/calmodulin. Stimulated by the G protein beta and gamma subunit complex. |
| Subcellular location | |
| Tissue specificity | Widely distributed. |
| Sequence similarities | Belongs to the adenylyl cyclase class-4/guanylyl cyclase family. Contains 2 guanylate cyclase domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | cAMP biosynthesis |
| Cellular component | Membrane |
| Domain | Repeat Transmembrane |
| Ligand | ATP-binding Magnesium Metal-binding Nucleotide-binding |
| Molecular function | Lyase |
| PTM | Glycoprotein |
| Gene Ontology (GO) | |
| Biological process | cAMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW intracellular signaling cascade Ref.1Inferred from direct assay. Source: RGD |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylate cyclase activity Ref.1Inferred from direct assay. Source: RGD magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1064 | 1064 | Adenylate cyclase type 4 | PRO_0000195692 | |||||
Regions | |||||||||
| Topological domain | 1 – 28 | 28 | Cytoplasmic Potential | ||||||
| Transmembrane | 29 – 50 | 22 | Potential | ||||||
| Transmembrane | 61 – 80 | 20 | Potential | ||||||
| Transmembrane | 94 – 117 | 24 | Potential | ||||||
| Transmembrane | 120 – 138 | 19 | Potential | ||||||
| Transmembrane | 141 – 162 | 22 | Potential | ||||||
| Transmembrane | 170 – 190 | 21 | Potential | ||||||
| Topological domain | 191 – 582 | 392 | Cytoplasmic Potential | ||||||
| Transmembrane | 583 – 604 | 22 | Potential | ||||||
| Transmembrane | 608 – 630 | 23 | Potential | ||||||
| Transmembrane | 661 – 684 | 24 | Potential | ||||||
| Topological domain | 685 – 707 | 23 | Extracellular Potential | ||||||
| Transmembrane | 708 – 733 | 26 | Potential | ||||||
| Transmembrane | 741 – 761 | 21 | Potential | ||||||
| Transmembrane | 788 – 804 | 17 | Potential | ||||||
| Topological domain | 805 – 1064 | 260 | Cytoplasmic Potential | ||||||
Sites | |||||||||
| Metal binding | 278 | 1 | Magnesium 1 By similarity | ||||||
| Metal binding | 278 | 1 | Magnesium 2 By similarity | ||||||
| Metal binding | 279 | 1 | Magnesium 2; via carbonyl oxygen By similarity | ||||||
| Metal binding | 322 | 1 | Magnesium 1 By similarity | ||||||
| Metal binding | 322 | 1 | Magnesium 2 By similarity | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 694 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 701 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| [1] | "Cloning and expression of a widely distributed (type IV) adenylyl cyclase." Gao B., Gilman A.G. Proc. Natl. Acad. Sci. U.S.A. 88:10178-10182(1991) [PubMed: 1946437] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis. |
Cross-references
Sequence databases | |
|---|---|
| M80633 mRNA. Translation: AAA40665.1. | |
| IPI | IPI00339145. |
| PIR | A41542. |
| UniGene | Rn.1904 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1CJK based on UniProtKB P26769. |
| SMR | P26770. Positions 854-1053. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | P26770. |
Genome annotation databases | |
| Ensembl | ENSRNOG00000020401. Rattus norvegicus. [Contig view] |
Organism-specific databases | |
| RGD | 2034. Adcy4. |
Phylogenomic databases | |
| HOVERGEN | P26770. |
Enzyme and pathway databases | |
| BRENDA | 4.6.1.1. 248. |
Gene expression databases | |
| ArrayExpress | P26770. |
| GermOnline | ENSRNOG00000020401. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR001054. A/G_cyclase. IPR018297. A/G_cyclase_CS. IPR009398. Aden_cycl-like. [Graphical view] |
| Gene3D | G3DSA:3.30.70.1230. A/G_cyclase. 2 hits. |
| Pfam | PF06327. DUF1053. 1 hit. PF00211. Guanylate_cyc. 2 hits. [Graphical view] |
| SMART | SM00044. CYCc. 2 hits. [Graphical view] |
| PROSITE | PS00452. GUANYLATE_CYCLASE_1. 2 hits. PS50125. GUANYLATE_CYCLASE_2. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ADCY4_RAT | ||||||||
| Accession | Primary (citable) accession number: P26770 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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