P54282 (CAC1A_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 114.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Voltage-dependent P/Q-type calcium channel subunit alpha-1A Alternative name(s): Brain calcium channel I Short name=BI Calcium channel, L type, alpha-1 polypeptide, isoform 4 Rat brain class A Short name=RBA-I Voltage-gated calcium channel subunit alpha Cav2.1 | ||||
| Gene names |
| ||||
| Organism | Rattus norvegicus (Rat) [Reference proteome] | ||||
| 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 | 2212 AA. |
| Sequence status | Complete. |
| 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. Interact (via C-terminal CDB motif) with CABP1 in the pre- and postsynaptic membranes. |
| Subcellular location | |
| Tissue specificity | Brain specific. Purkinje cells contain predominantly P-type VSCC, the Q-type being a prominent calcium current in cerebellar granule cells. Also found in heart, in kidney distal convoluted tubule (DCT), and in pituitary. |
| 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. |
| Sequence similarities | Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family. CACNA1A subfamily. [View classification] |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| Rims1 | Q9JIR4 | 4 | EBI-3507416,EBI-3507436 |
Alternative products
| This entry describes 4 isoforms produced by alternative splicing. [Align] [Select] Note: Additional isoforms seem to exist. | ||||||
| Isoform 1 (identifier: P54282-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: P54282-2) Also known as: RKC8; The sequence of this isoform differs from the canonical sequence as follows: 1602-1602: G → GNP | ||||||
| Isoform 3 (identifier: P54282-3) Also known as: RBA-65; The sequence of this isoform is not available. | ||||||
| Isoform 4 (identifier: P54282-4) The sequence of this isoform is not available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 2212 | 2212 | Voltage-dependent P/Q-type calcium channel subunit alpha-1A | PRO_0000053919 | |||||
Regions | |||||||||
| Topological domain | 1 – 100 | 100 | Cytoplasmic Potential | ||||||
| Transmembrane | 101 – 119 | 19 | Helical; Name=S1 of repeat I; Potential | ||||||
| Topological domain | 120 – 138 | 19 | Extracellular Potential | ||||||
| Transmembrane | 139 – 156 | 18 | Helical; Name=S2 of repeat I; Potential | ||||||
| Topological domain | 157 – 168 | 12 | Cytoplasmic Potential | ||||||
| Transmembrane | 169 – 184 | 16 | Helical; Name=S3 of repeat I; Potential | ||||||
| Topological domain | 185 – 192 | 8 | Extracellular Potential | ||||||
| Transmembrane | 193 – 211 | 19 | Helical; Name=S4 of repeat I; Potential | ||||||
| Topological domain | 212 – 230 | 19 | Cytoplasmic Potential | ||||||
| Transmembrane | 231 – 250 | 20 | Helical; Name=S5 of repeat I; Potential | ||||||
| Topological domain | 251 – 337 | 87 | Extracellular Potential | ||||||
| Transmembrane | 338 – 362 | 25 | Helical; Name=S6 of repeat I; Potential | ||||||
| Topological domain | 363 – 489 | 127 | Cytoplasmic Potential | ||||||
| Transmembrane | 490 – 509 | 20 | Helical; Name=S1 of repeat II; Potential | ||||||
| Topological domain | 510 – 523 | 14 | Extracellular Potential | ||||||
| Transmembrane | 524 – 543 | 20 | Helical; Name=S2 of repeat II; Potential | ||||||
| Topological domain | 544 – 551 | 8 | Cytoplasmic Potential | ||||||
| Transmembrane | 552 – 570 | 19 | Helical; Name=S3 of repeat II; Potential | ||||||
| Topological domain | 571 – 580 | 10 | Extracellular Potential | ||||||
| Transmembrane | 581 – 599 | 19 | Helical; Name=S4 of repeat II; Potential | ||||||
| Topological domain | 600 – 618 | 19 | Cytoplasmic Potential | ||||||
| Transmembrane | 619 – 638 | 20 | Helical; Name=S5 of repeat II; Potential | ||||||
| Topological domain | 639 – 691 | 53 | Extracellular Potential | ||||||
| Transmembrane | 692 – 716 | 25 | Helical; Name=S6 of repeat II; Potential | ||||||
| Topological domain | 717 – 1190 | 474 | Cytoplasmic Potential | ||||||
| Transmembrane | 1191 – 1214 | 24 | Helical; Name=S1 of repeat III; Potential | ||||||
| Topological domain | 1215 – 1231 | 17 | Extracellular Potential | ||||||
| Transmembrane | 1232 – 1251 | 20 | Helical; Name=S2 of repeat III; Potential | ||||||
| Topological domain | 1252 – 1258 | 7 | Cytoplasmic Potential | ||||||
| Transmembrane | 1259 – 1282 | 24 | Helical; Name=S3 of repeat III; Potential | ||||||
| Topological domain | 1283 – 1293 | 11 | Extracellular Potential | ||||||
| Transmembrane | 1294 – 1311 | 18 | Helical; Name=S4 of repeat III; Potential | ||||||
| Topological domain | 1312 – 1330 | 19 | Cytoplasmic Potential | ||||||
| Transmembrane | 1331 – 1350 | 20 | Helical; Name=S5 of repeat III; Potential | ||||||
| Topological domain | 1351 – 1437 | 87 | Extracellular Potential | ||||||
| Transmembrane | 1438 – 1462 | 25 | Helical; Name=S6 of repeat III; Potential | ||||||
| Topological domain | 1463 – 1518 | 56 | Cytoplasmic Potential | ||||||
| Transmembrane | 1519 – 1537 | 19 | Helical; Name=S1 of repeat IV; Potential | ||||||
| Topological domain | 1538 – 1551 | 14 | Extracellular Potential | ||||||
| Transmembrane | 1552 – 1573 | 22 | Helical; Name=S2 of repeat IV; Potential | ||||||
| Topological domain | 1574 – 1580 | 7 | Cytoplasmic Potential | ||||||
| Transmembrane | 1581 – 1600 | 20 | Helical; Name=S3 of repeat IV; Potential | ||||||
| Topological domain | 1601 – 1607 | 7 | Extracellular Potential | ||||||
| Transmembrane | 1608 – 1626 | 19 | Helical; Name=S4 of repeat IV; Potential | ||||||
| Topological domain | 1627 – 1645 | 19 | Cytoplasmic Potential | ||||||
| Transmembrane | 1646 – 1665 | 20 | Helical; Name=S5 of repeat IV; Potential | ||||||
| Topological domain | 1666 – 1737 | 72 | Extracellular Potential | ||||||
| Transmembrane | 1738 – 1763 | 26 | Helical; Name=S6 of repeat IV; Potential | ||||||
| Topological domain | 1764 – 2212 | 449 | Cytoplasmic Potential | ||||||
| Repeat | 87 – 365 | 279 | 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 | 13 – 20 | 8 | Poly-Gly | ||||||
| Compositional bias | 729 – 734 | 6 | Poly-Glu | ||||||
| Compositional bias | 1155 – 1158 | 4 | Poly-Glu | ||||||
| Compositional bias | 2162 – 2171 | 10 | Poly-His | ||||||
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 | 1600 | 1 | Binds to omega-Aga-IVA By similarity | ||||||
| Site | 1707 | 1 | Calcium ion selectivity and permeability By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 752 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1773 | 1 | Phosphoserine; by PKA Potential | ||||||
| Modified residue | 1981 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2027 | 1 | Phosphotyrosine By similarity | ||||||
| Glycosylation | 285 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1607 | 1 | N-linked (GlcNAc...) Potential | ||||||
Natural variations | |||||||||
| Alternative sequence | 1602 | 1 | G → GNP in isoform 2. | VSP_000881 | |||||
Sequences
| ||||||||||||||||||||||||||||||||||||
References
| [1] | "Primary structure of a calcium channel that is highly expressed in the rat cerebellum." Starr T.V.B., Prystay W., Snutch T.P. Proc. Natl. Acad. Sci. U.S.A. 88:5621-5625(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Brain. |
| [2] | "Molecular characterization and nephron distribution of a family of transcripts encoding the pore-forming subunit of Ca2+ channels in the kidney." Yu A.S.L., Hebert S.C., Brenner B.M., Lytton J. Proc. Natl. Acad. Sci. U.S.A. 89:10494-10498(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1354-1659 (ISOFORM 2). Tissue: Kidney. |
| [3] | "Rat brain expresses a heterogeneous family of calcium channels." Snutch T.P., Leonard J.P., Gilbert M.M., Lester H.A., Davidson N. Proc. Natl. Acad. Sci. U.S.A. 87:3391-3395(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1435-1667 (ISOFORM 3). |
| [4] | "Differential modulation of Ca(v)2.1 channels by calmodulin and Ca2+-binding protein 1." Lee A., Westenbroek R.E., Haeseleer F., Palczewski K., Scheuer T., Catterall W.A. Nat. Neurosci. 5:210-217(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CABP1. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M64373 mRNA. Translation: AAA40806.1. M99222 mRNA. Translation: AAA40896.1. |
| IPI | IPI00211870. IPI00231785. |
| PIR | A41098. |
| RefSeq | NP_037050.2. NM_012918.3. |
| UniGene | Rn.87769. |
3D structure databases | |
| ProteinModelPortal | P54282. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-29638N. |
| IntAct | P54282. 2 interactions. |
Protein family/group databases | |
| TCDB | 1.A.1.11.8. voltage-gated ion channel (VIC) superfamily. |
PTM databases | |
| PhosphoSite | P54282. |
Proteomic databases | |
| PaxDb | P54282. |
| PRIDE | P54282. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 25398. |
| KEGG | rno:25398. |
Organism-specific databases | |
| CTD | 773. |
| RGD | 2244. Cacna1a. |
Phylogenomic databases | |
| eggNOG | COG1226. |
| HOGENOM | HOG000231530. |
| HOVERGEN | HBG050763. |
| KO | K04344. |
| OrthoDB | EOG48KR9C. |
Gene expression databases | |
| ArrayExpress | P54282. |
| Genevestigator | P54282. |
Family and domain databases | |
| Gene3D | 1.20.120.350. 4 hits. |
| InterPro | IPR005821. Ion_trans_dom. IPR027359. K_channel_four-helix_dom. IPR014873. VDCC_a1su_IQ. IPR005448. VDCC_P/Q_a1su. IPR002077. VDCCAlpha1. [Graphical view] |
| PANTHER | PTHR10037:SF59. PTHR10037:SF59. 1 hit. |
| Pfam | PF08763. Ca_chan_IQ. 1 hit. PF00520. Ion_trans. 4 hits. [Graphical view] |
| PRINTS | PR00167. CACHANNEL. PR01632. PQVDCCALPHA1. |
| SMART | SM01062. Ca_chan_IQ. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| BindingDB | P54282. |
| ChEMBL | CHEMBL4417. |
| NextBio | 13949997. |
Entry information
| Entry name | CAC1A_RAT | ||||||||
| Accession | Primary (citable) accession number: P54282 Secondary accession number(s): Q01541 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
