Reviewed,
UniProtKB/Swiss-Prot P97445 (CAC1A_MOUSE)
Last modified
June 16, 2009.
Version 87.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Voltage-dependent P/Q-type calcium channel subunit alpha-1A Alternative name(s): Voltage-gated calcium channel subunit alpha Cav2.1 Calcium channel, L type, alpha-1 polypeptide isoform 4 Brain calcium channel I Short name=BI | ||||
| 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 | 2368 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1A gives rise to P and/or Q-type calcium currents. P/Q-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by the funnel toxin (Ftx) and by the omega-agatoxin-IVA (omega-Aga-IVA). They are however insensitive to dihydropyridines (DHP), and omega-conotoxin-GVIA (omega-CTx-GVIA). |
| Subunit structure | Voltage-dependent calcium channels are multisubunit complexes, consisting of alpha-1, alpha-2, beta and delta subunits in a 1:1:1:1 ratio. The channel activity is directed by the pore-forming and voltage-sensitive alpha-1 subunit. In many cases, this subunit is sufficient to generate voltage-sensitive calcium channel activity. The auxiliary subunits beta and alpha-2/delta linked by a disulfide bridge regulate the channel activity. |
| Subcellular location | |
| Tissue specificity | Brain specific; mainly found in the cerebellum, olfactory bulb, cerebral cortex, hippocampus, and inferior colliculus. In the hippocampus, expression occurs in pyramidal and granule neurons, as well as in interneurons. Purkinje cells contain predominantly P-type VSCC, the Q-type being a prominent calcium current in cerebellar granule cells. |
| Domain | Each of the four internal repeats contains five hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one positively charged transmembrane segment (S4). S4 segments probably represent the voltage-sensor and are characterized by a series of positively charged amino acids at every third position. |
| Involvement in disease | Defects in Cacna1a are the cause of a delayed-onset, recessive neurological disorder seen in tottering (tg) mutants, resulting in ataxia, motor seizures and behavioral absence seizures resembling petit mal epilepsy (or absence epilepsy) in humans. There are two more alleles: leaner (tg(lA)), that is characterized by severe ataxia and frequent death past weaning, but no motor seizures; and rolling Nagoya (tg(rol)), that presents an intermediary phenotype, the ataxia being somewhat more severe that with tg, but without motors seizures. Selective degeneration of cerebellar Purkinje cells has been shown for all these types of mutants. |
| Sequence similarities | Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family. [View classification] |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 2368 | 2368 | Voltage-dependent P/Q-type calcium channel subunit alpha-1A | PRO_0000053917 | |||||
Regions | |||||||||
| Topological domain | 1 – 100 | 100 | Cytoplasmic Potential | ||||||
| Transmembrane | 101 – 119 | 19 | S1 of repeat I Potential | ||||||
| Topological domain | 120 – 138 | 19 | Extracellular Potential | ||||||
| Transmembrane | 139 – 156 | 18 | S2 of repeat I Potential | ||||||
| Topological domain | 157 – 168 | 12 | Cytoplasmic Potential | ||||||
| Transmembrane | 169 – 184 | 16 | S3 of repeat I Potential | ||||||
| Topological domain | 185 – 192 | 8 | Extracellular Potential | ||||||
| Transmembrane | 193 – 211 | 19 | S4 of repeat I Potential | ||||||
| Topological domain | 212 – 230 | 19 | Cytoplasmic Potential | ||||||
| Transmembrane | 231 – 250 | 20 | S5 of repeat I Potential | ||||||
| Topological domain | 251 – 337 | 87 | Extracellular Potential | ||||||
| Transmembrane | 338 – 362 | 25 | S6 of repeat I Potential | ||||||
| Topological domain | 363 – 489 | 127 | Cytoplasmic Potential | ||||||
| Transmembrane | 490 – 509 | 20 | S1 of repeat II Potential | ||||||
| Topological domain | 510 – 523 | 14 | Extracellular Potential | ||||||
| Transmembrane | 524 – 543 | 20 | S2 of repeat II Potential | ||||||
| Topological domain | 544 – 551 | 8 | Cytoplasmic Potential | ||||||
| Transmembrane | 552 – 570 | 19 | S3 of repeat II Potential | ||||||
| Topological domain | 571 – 580 | 10 | Extracellular Potential | ||||||
| Transmembrane | 581 – 599 | 19 | S4 of repeat II Potential | ||||||
| Topological domain | 600 – 618 | 19 | Cytoplasmic Potential | ||||||
| Transmembrane | 619 – 638 | 20 | S5 of repeat II Potential | ||||||
| Topological domain | 639 – 691 | 53 | Extracellular Potential | ||||||
| Transmembrane | 692 – 716 | 25 | S6 of repeat II Potential | ||||||
| Topological domain | 717 – 1190 | 474 | Cytoplasmic Potential | ||||||
| Transmembrane | 1191 – 1214 | 24 | S1 of repeat III Potential | ||||||
| Topological domain | 1215 – 1231 | 17 | Extracellular Potential | ||||||
| Transmembrane | 1232 – 1251 | 20 | S2 of repeat III Potential | ||||||
| Topological domain | 1252 – 1258 | 7 | Cytoplasmic Potential | ||||||
| Transmembrane | 1259 – 1282 | 24 | S3 of repeat III Potential | ||||||
| Topological domain | 1283 – 1293 | 11 | Extracellular Potential | ||||||
| Transmembrane | 1294 – 1311 | 18 | S4 of repeat III Potential | ||||||
| Topological domain | 1312 – 1330 | 19 | Cytoplasmic Potential | ||||||
| Transmembrane | 1331 – 1350 | 20 | S5 of repeat III Potential | ||||||
| Topological domain | 1351 – 1437 | 87 | Extracellular Potential | ||||||
| Transmembrane | 1438 – 1462 | 25 | S6 of repeat III Potential | ||||||
| Topological domain | 1463 – 1518 | 56 | Cytoplasmic Potential | ||||||
| Transmembrane | 1519 – 1537 | 19 | S1 of repeat IV Potential | ||||||
| Topological domain | 1538 – 1551 | 14 | Extracellular Potential | ||||||
| Transmembrane | 1552 – 1573 | 22 | S2 of repeat IV Potential | ||||||
| Topological domain | 1574 – 1580 | 7 | Cytoplasmic Potential | ||||||
| Transmembrane | 1581 – 1600 | 20 | S3 of repeat IV Potential | ||||||
| Topological domain | 1601 – 1607 | 7 | Extracellular Potential | ||||||
| Transmembrane | 1608 – 1626 | 19 | S4 of repeat IV Potential | ||||||
| Topological domain | 1627 – 1645 | 19 | Cytoplasmic Potential | ||||||
| Transmembrane | 1646 – 1665 | 20 | S5 of repeat IV Potential | ||||||
| Topological domain | 1666 – 1737 | 72 | Extracellular Potential | ||||||
| Transmembrane | 1738 – 1763 | 26 | S6 of repeat IV Potential | ||||||
| Topological domain | 1764 – 2368 | 605 | Cytoplasmic Potential | ||||||
| Repeat | 65 – 365 | 301 | I | ||||||
| Repeat | 475 – 719 | 245 | II | ||||||
| Repeat | 1182 – 1465 | 284 | III | ||||||
| Repeat | 1502 – 1765 | 264 | IV | ||||||
| Calcium binding | 1791 – 1802 | 12 | By similarity | ||||||
| Region | 385 – 402 | 18 | Binding to the beta subunit By similarity | ||||||
| Compositional bias | 729 – 734 | 6 | Poly-Glu | ||||||
| Compositional bias | 1155 – 1158 | 4 | Poly-Glu | ||||||
Sites | |||||||||
| Site | 320 | 1 | Calcium ion selectivity and permeability By similarity | ||||||
| Site | 670 | 1 | Calcium ion selectivity and permeability By similarity | ||||||
| Site | 1411 | 1 | Calcium ion selectivity and permeability By similarity | ||||||
| Site | 1707 | 1 | Calcium ion selectivity and permeability By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 752 | 1 | Phosphoserine Ref.3 | ||||||
| Modified residue | 1981 | 1 | Phosphoserine Ref.3 | ||||||
| Modified residue | 2027 | 1 | Phosphotyrosine Ref.3 | ||||||
| Modified residue | 2220 | 1 | Phosphoserine Ref.3 | ||||||
| Modified residue | 2273 | 1 | Phosphoserine Ref.3 | ||||||
| Glycosylation | 285 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1607 | 1 | N-linked (GlcNAc...) Potential | ||||||
Natural variations | |||||||||
| Natural variant | 649 | 1 | P → L in tg. Ref.2 | ||||||
Experimental info | |||||||||
| Sequence conflict | 79 | 1 | S → P in AAC52940. Ref.2 | ||||||
| Sequence conflict | 82 | 1 | L → F in AAC52940. Ref.2 | ||||||
| Sequence conflict | 884 | 1 | P → L in AAC52940. Ref.2 | ||||||
| Sequence conflict | 888 | 1 | E → D in AAW56205. Ref.1 | ||||||
| Sequence conflict | 1083 | 1 | N → D in AAC52940. Ref.2 | ||||||
| Sequence conflict | 1349 | 1 | L → F in AAC52940. Ref.2 | ||||||
| Sequence conflict | 1373 | 1 | L → F in AAC52940. Ref.2 | ||||||
| Sequence conflict | 2161 | 1 | P → PH in AAW56205. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Molecular identity of P-type calcium current in Purkinje neurons." Richards K.S., Swensen A.M., Lipscombe D. Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Swiss Webster. Tissue: Brain. |
| [2] | "Absence epilepsy in tottering mutant mice is associated with calcium channel defects." Fletcher C.F., Lutz C.M., O'Sullivan T.N., Shaughnessy J.D. Jr., Hawkes R., Frankel W.N., Copeland N.G., Jenkins N.A. Cell 87:607-617(1996) [PubMed: 8929530] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 49-2212, VARIANT TG LEU-649. Strain: DBA/2J. |
| [3] | "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-752; SER-1981; TYR-2027; SER-2220 AND SER-2273, MASS SPECTROMETRY. Tissue: Brain cortex. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AY714490 mRNA. Translation: AAW56205.1. U76716 mRNA. Translation: AAC52940.1. | |
| IPI | IPI00408646. |
| RefSeq | NP_031604.3. |
| UniGene | Mm.334658 |
3D structure databases | |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | P97445. |
Genome annotation databases | |
| Ensembl | ENSMUSG00000034656. Mus musculus. [Contig view] |
| GeneID | 12286. |
| KEGG | mmu:12286. |
Organism-specific databases | |
| MGI | MGI:109482. Cacna1a. |
Phylogenomic databases | |
| HOGENOM | P97445. |
| HOVERGEN | P97445. |
| OMA | P97445. ALYNEMD. |
Gene expression databases | |
| ArrayExpress | P97445. |
| Bgee | P97445. |
| GermOnline | ENSMUSG00000034656. Mus musculus. |
Family and domain databases | |
| InterPro | IPR017956. AT_hook_DNA-bd_CS. IPR005821. Ion_trans. IPR014873. VDCC_a1su_IQ. IPR005448. VDCC_P/Q_a1su. IPR002077. VDCCAlpha1. [Graphical view] |
| PANTHER | PTHR10037:SF59. PQVDCCAlpha1. 1 hit. |
| Pfam | PF08763. Ca_chan_IQ. 1 hit. PF00520. Ion_trans. 4 hits. [Graphical view] |
| PRINTS | PR00167. CACHANNEL. PR01632. PQVDCCALPHA1. |
| SMART | SM00384. AT_hook. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 280756. |
| SOURCE | Search... |
Entry information
| Entry name | CAC1A_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P97445 Secondary accession number(s): Q2TPN3 | ||||||||
| 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


