Reviewed,
UniProtKB/Swiss-Prot O88444 (ADCY1_MOUSE)
Last modified
January 19, 2010.
Version 78.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Adenylate cyclase type 1 EC=4.6.1.1 Alternative name(s): Adenylate cyclase type I ATP pyrophosphate-lyase 1 Adenylyl cyclase 1 Ca(2+)/calmodulin-activated adenylyl cyclase | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 1118 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | This is a calmodulin-sensitive adenylyl cyclase. May be involved in regulatory processes in the central nervous system. It may play a role in memory acquisition and learning By similarity. |
| Catalytic activity | ATP = 3',5'-cyclic AMP + diphosphate. |
| Cofactor | Binds 2 magnesium ions per subunit By similarity. |
| Enzyme regulation | Activated by calcium/calmodulin. Inhibited by the G protein beta and gamma subunit complex By similarity. |
| Subcellular location | |
| Sequence similarities | Belongs to the adenylyl cyclase class-4/guanylyl cyclase family. Contains 2 guanylate cyclase domains. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1118 | 1118 | Adenylate cyclase type 1 | PRO_0000195683 | |||||
Regions | |||||||||
| Topological domain | 1 – 62 | 62 | Cytoplasmic Potential | ||||||
| Transmembrane | 63 – 83 | 21 | Potential | ||||||
| Transmembrane | 87 – 107 | 21 | Potential | ||||||
| Transmembrane | 124 – 144 | 21 | Potential | ||||||
| Transmembrane | 157 – 177 | 21 | Potential | ||||||
| Transmembrane | 182 – 202 | 21 | Potential | ||||||
| Transmembrane | 213 – 233 | 21 | Potential | ||||||
| Topological domain | 234 – 609 | 376 | Cytoplasmic Potential | ||||||
| Transmembrane | 610 – 630 | 21 | Potential | ||||||
| Transmembrane | 634 – 654 | 21 | Potential | ||||||
| Transmembrane | 673 – 693 | 21 | Potential | ||||||
| Transmembrane | 724 – 744 | 21 | Potential | ||||||
| Transmembrane | 752 – 772 | 21 | Potential | ||||||
| Transmembrane | 774 – 793 | 20 | Potential | ||||||
| Topological domain | 794 – 1118 | 325 | Cytoplasmic Potential | ||||||
| Region | 492 – 519 | 28 | Interaction with calmodulin By similarity | ||||||
| Region | 1023 – 1046 | 24 | Interaction with calmodulin By similarity | ||||||
Sites | |||||||||
| Metal binding | 307 | 1 | Magnesium 1 By similarity | ||||||
| Metal binding | 307 | 1 | Magnesium 2 By similarity | ||||||
| Metal binding | 308 | 1 | Magnesium 2; via carbonyl oxygen By similarity | ||||||
| Metal binding | 351 | 1 | Magnesium 1 By similarity | ||||||
| Metal binding | 351 | 1 | Magnesium 2 By similarity | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 703 | 1 | N-linked (GlcNAc...) Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 147 – 155 | 9 | SSAGGAMGS → ALQEAQWAR in AAC29478. Ref.2 | ||||||
| Sequence conflict | 234 | 1 | T → A in AAC29478. Ref.2 | ||||||
| Sequence conflict | 270 | 1 | L → M in AAC29478. Ref.2 | ||||||
| Sequence conflict | 319 | 1 | T → K in AAC29478. Ref.2 | ||||||
| Sequence conflict | 466 | 1 | R → K in AAC29478. Ref.2 | ||||||
| Sequence conflict | 523 | 1 | F → I in AAC29478. Ref.2 | ||||||
| Sequence conflict | 542 | 1 | S → T in AAC29478. Ref.2 | ||||||
| Sequence conflict | 549 | 1 | S → T in AAC29478. Ref.2 | ||||||
| Sequence conflict | 570 | 1 | R → L in AAC29478. Ref.2 | ||||||
| Sequence conflict | 598 | 1 | Q → R in AAC29478. Ref.2 | ||||||
| Sequence conflict | 692 | 1 | G → V in AAC29478. Ref.2 | ||||||
| Sequence conflict | 697 | 1 | A → S in AAC29478. Ref.2 | ||||||
| Sequence conflict | 707 | 1 | V → L in AAC29478. Ref.2 | ||||||
| Sequence conflict | 713 | 1 | G → C in AAC29478. Ref.2 | ||||||
| Sequence conflict | 720 – 721 | 2 | AL → GP in AAC29478. Ref.2 | ||||||
| Sequence conflict | 774 – 776 | 3 | VGG → AMGA in AAC29478. Ref.2 | ||||||
| Sequence conflict | 867 – 869 | 3 | GVM → AVL in AAC29478. Ref.2 | ||||||
| Sequence conflict | 938 | 1 | R → K in AAC29478. Ref.2 | ||||||
| Sequence conflict | 991 | 1 | R → C in AAC29478. Ref.2 | ||||||
| Sequence conflict | 1020 | 1 | T → I in AAC29478. Ref.2 | ||||||
| Sequence conflict | 1030 | 1 | C → S in AAC29478. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J. |
| [2] | "Loss of adenylyl cyclase I activity disrupts patterning of mouse somatosensory cortex." Abdel-Majid R.M., Leong W.L., Schalkwyk L.C., Smallman D.S., Wong S.T., Storm D.R., Fine A., Dobson M.J., Guernsey D.L., Neumann P.E. Nat. Genet. 19:289-291(1998) [PubMed: 9662407] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 100-1050. Strain: C57BL/6J. Tissue: Brain. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AL669838 Genomic DNA. Translation: CAI25155.1. AF053980 mRNA. Translation: AAC29478.1. |
| IPI | IPI00130949. |
| RefSeq | NP_033752.1. |
| UniGene | Mm.259733 |
3D structure databases | |
| SMR | O88444. Positions 287-476, 858-1053. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | O88444. |
PTM databases | |
| PhosphoSite | O88444. |
Proteomic databases | |
| PRIDE | O88444. |
Genome annotation databases | |
| Ensembl | ENSMUST00000020706; ENSMUSP00000020706; ENSMUSG00000020431; Mus musculus. [Genome view] |
| GeneID | 432530. |
| KEGG | mmu:432530. |
| UCSC | uc007hzf.1. mouse. |
Organism-specific databases | |
| CTD | 432530. |
| MGI | MGI:99677. Adcy1. |
Phylogenomic databases | |
| eggNOG | roNOG09082. |
| HOGENOM | HBG445220. |
| HOVERGEN | O88444. |
| InParanoid | O88444. |
| OMA | KCISSHL. |
| OrthoDB | EOG99PDHQ. |
| PhylomeDB | O88444. |
Enzyme and pathway databases | |
| BRENDA | 4.6.1.1. 244. |
Gene expression databases | |
| ArrayExpress | O88444. |
| Bgee | O88444. |
| CleanEx | MM_ADCY1. |
| Genevestigator | O88444. |
| GermOnline | ENSMUSG00000020431. Mus musculus. |
Family and domain databases | |
| InterPro | IPR001054. A/G_cyclase. IPR018297. A/G_cyclase_CS. [Graphical view] |
| Gene3D | G3DSA:3.30.70.1230. A/G_cyclase. 2 hits. |
| Pfam | 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... |
Other Resources | |
| NextBio | 407738. |
| SOURCE | Search... |
Entry information
| Entry name | ADCY1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: O88444 Secondary accession number(s): Q5SS89 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


