Reviewed,
UniProtKB/Swiss-Prot O55017 (CAC1B_MOUSE)
Last modified
January 19, 2010.
Version 100.
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 N-type calcium channel subunit alpha-1B Alternative name(s): Voltage-gated calcium channel subunit alpha Cav2.2 Calcium channel, L type, alpha-1 polypeptide isoform 5 Brain calcium channel III Short name=BIII | ||||
| 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 | 2327 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-1B gives rise to N-type calcium currents. N-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by omega-conotoxin-GVIA (omega-CTx-GVIA) and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to dihydropyridines (DHP), and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing alpha-1B subunit may play a role in directed migration of immature neurons. |
| Subunit structure | Multisubunit complex 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. Interacts with RIMS1 and RIMBP2 By similarity. Ref.3 |
| Subcellular location | |
| Tissue specificity | Widespread expression throughout the brain. Highest levels in pyramidal cell layers C1, C2 and C3 of the hippocampus, in the dentate gyrus, in the cortex layers 2 et 4, in the subiculum and the habenula. |
| 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. |
| Post-translational modification | Phosphorylated in vitro by CaM-kinase II, PKA, PKC and CGPK By similarity. Ref.4 Ref.5 |
| Sequence similarities | Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family. [View classification] Contains 1 EF-hand domain. |
| Sequence caution | The sequence AAB60437.1 differs from that shown. Reason: Frameshift at positions 1924, 1934, 2121 and 2127. |
Ontologies
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform NB1 (identifier: O55017-1) 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 NB2 (identifier: O55017-2) The sequence of this isoform differs from the canonical sequence as follows: 756-756: A → AFVKQTRGTVSRSSSVSSVNSP |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 2327 | 2327 | Voltage-dependent N-type calcium channel subunit alpha-1B | PRO_0000053922 | |||||
Regions | |||||||||
| Topological domain | 1 – 95 | 95 | Cytoplasmic Potential | ||||||
| Transmembrane | 96 – 114 | 19 | S1 of repeat I Potential | ||||||
| Topological domain | 115 – 133 | 19 | Extracellular Potential | ||||||
| Transmembrane | 134 – 151 | 18 | S2 of repeat I Potential | ||||||
| Topological domain | 152 – 164 | 13 | Cytoplasmic Potential | ||||||
| Transmembrane | 165 – 179 | 15 | S3 of repeat I Potential | ||||||
| Topological domain | 180 – 186 | 7 | Extracellular Potential | ||||||
| Transmembrane | 187 – 205 | 19 | S4 of repeat I Potential | ||||||
| Topological domain | 206 – 225 | 20 | Cytoplasmic Potential | ||||||
| Transmembrane | 226 – 245 | 20 | S5 of repeat I Potential | ||||||
| Topological domain | 246 – 331 | 86 | Extracellular Potential | ||||||
| Transmembrane | 332 – 356 | 25 | S6 of repeat I Potential | ||||||
| Topological domain | 357 – 482 | 126 | Cytoplasmic Potential | ||||||
| Transmembrane | 483 – 502 | 20 | S1 of repeat II Potential | ||||||
| Topological domain | 503 – 516 | 14 | Extracellular Potential | ||||||
| Transmembrane | 517 – 536 | 20 | S2 of repeat II Potential | ||||||
| Topological domain | 537 – 544 | 8 | Cytoplasmic Potential | ||||||
| Transmembrane | 545 – 563 | 19 | S3 of repeat II Potential | ||||||
| Topological domain | 564 – 574 | 11 | Extracellular Potential | ||||||
| Transmembrane | 575 – 592 | 18 | S4 of repeat II Potential | ||||||
| Topological domain | 593 – 611 | 19 | Cytoplasmic Potential | ||||||
| Transmembrane | 612 – 631 | 20 | S5 of repeat II Potential | ||||||
| Topological domain | 632 – 684 | 53 | Extracellular Potential | ||||||
| Transmembrane | 685 – 709 | 25 | S6 of repeat II Potential | ||||||
| Topological domain | 710 – 1134 | 425 | Cytoplasmic Potential | ||||||
| Transmembrane | 1135 – 1158 | 24 | S1 of repeat III Potential | ||||||
| Topological domain | 1159 – 1175 | 17 | Extracellular Potential | ||||||
| Transmembrane | 1176 – 1195 | 20 | S2 of repeat III Potential | ||||||
| Topological domain | 1196 – 1203 | 8 | Cytoplasmic Potential | ||||||
| Transmembrane | 1204 – 1226 | 23 | S3 of repeat III Potential | ||||||
| Topological domain | 1227 – 1241 | 15 | Extracellular Potential | ||||||
| Transmembrane | 1242 – 1256 | 15 | S4 of repeat III Potential | ||||||
| Topological domain | 1257 – 1277 | 21 | Cytoplasmic Potential | ||||||
| Transmembrane | 1278 – 1297 | 20 | S5 of repeat III Potential | ||||||
| Topological domain | 1298 – 1383 | 86 | Extracellular Potential | ||||||
| Transmembrane | 1384 – 1408 | 25 | S6 of repeat III Potential | ||||||
| Topological domain | 1409 – 1465 | 57 | Cytoplasmic Potential | ||||||
| Transmembrane | 1466 – 1484 | 19 | S1 of repeat IV Potential | ||||||
| Topological domain | 1485 – 1498 | 14 | Extracellular Potential | ||||||
| Transmembrane | 1499 – 1518 | 20 | S2 of repeat IV Potential | ||||||
| Topological domain | 1519 – 1527 | 9 | Cytoplasmic Potential | ||||||
| Transmembrane | 1528 – 1546 | 19 | S3 of repeat IV Potential | ||||||
| Topological domain | 1547 – 1554 | 8 | Extracellular Potential | ||||||
| Transmembrane | 1555 – 1573 | 19 | S4 of repeat IV Potential | ||||||
| Topological domain | 1574 – 1592 | 19 | Cytoplasmic Potential | ||||||
| Transmembrane | 1593 – 1612 | 20 | S5 of repeat IV Potential | ||||||
| Topological domain | 1613 – 1674 | 62 | Extracellular Potential | ||||||
| Transmembrane | 1675 – 1694 | 20 | S6 of repeat IV Potential | ||||||
| Topological domain | 1695 – 2327 | 633 | Cytoplasmic Potential | ||||||
| Repeat | 82 – 359 | 278 | I | ||||||
| Repeat | 468 – 712 | 245 | II | ||||||
| Repeat | 1126 – 1412 | 287 | III | ||||||
| Repeat | 1449 – 1702 | 254 | IV | ||||||
| Domain | 1715 – 1750 | 36 | EF-hand | ||||||
| Nucleotide binding | 451 – 458 | 8 | ATP Potential | ||||||
| Calcium binding | 1728 – 1739 | 12 | By similarity | ||||||
| Region | 379 – 396 | 18 | Binding to the beta subunit By similarity | ||||||
| Compositional bias | 2040 – 2044 | 5 | Poly-His | ||||||
| Compositional bias | 2106 – 2110 | 5 | Poly-Ser | ||||||
Sites | |||||||||
| Site | 314 | 1 | Calcium ion selectivity and permeability By similarity | ||||||
| Site | 663 | 1 | Calcium ion selectivity and permeability By similarity | ||||||
| Site | 1358 | 1 | Calcium ion selectivity and permeability By similarity | ||||||
| Site | 1646 | 1 | Calcium ion selectivity and permeability By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 455 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 745 | 1 | Phosphoserine Ref.5 | ||||||
| Modified residue | 783 | 1 | Phosphoserine Ref.4 Ref.5 | ||||||
| Modified residue | 1710 | 1 | Phosphoserine; by PKA Potential | ||||||
| Modified residue | 1959 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2244 | 1 | Phosphoserine Ref.5 | ||||||
| Glycosylation | 256 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1554 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1666 | 1 | N-linked (GlcNAc...) Potential | ||||||
Natural variations | |||||||||
| Alternative sequence | 756 | 1 | A → AFVKQTRGTVSRSSSVSSVN SP in isoform NB2. | VSP_000883 | |||||
| Natural variant | 414 | 1 | D → DA | ||||||
Experimental info | |||||||||
| Sequence conflict | 238 | 1 | A → G in AAB60437. Ref.2 | ||||||
| Sequence conflict | 645 | 1 | N → I in AAB60437. Ref.2 | ||||||
| Sequence conflict | 757 – 759 | 3 | RQQ → QE in AAB60437. Ref.2 | ||||||
| Sequence conflict | 880 | 1 | A → P in AAB60437. Ref.2 | ||||||
| Sequence conflict | 1128 | 1 | L → F in AAB60437. Ref.2 | ||||||
| Sequence conflict | 1173 | 1 | K → E in AAB60437. Ref.2 | ||||||
| Sequence conflict | 1185 | 1 | F → C in AAB60437. Ref.2 | ||||||
| Sequence conflict | 1227 – 1230 | 4 | Missing in AAB60437. Ref.2 | ||||||
| Sequence conflict | 1388 | 1 | F → L in AAB60437. Ref.2 | ||||||
| Sequence conflict | 1549 | 1 | A → AET in AAB60437. Ref.2 | ||||||
| Sequence conflict | 1615 | 1 | I → S in AAB60437. Ref.2 | ||||||
| Sequence conflict | 1636 | 1 | L → I in AAB60437. Ref.2 | ||||||
| Sequence conflict | 1657 | 1 | G → D in AAB60437. Ref.2 | ||||||
| Sequence conflict | 1802 – 1837 | 36 | Missing in AAB60437. Ref.2 | ||||||
| Sequence conflict | 1942 | 1 | A → G in AAB60437. Ref.2 | ||||||
| Sequence conflict | 1949 | 1 | G → D in AAB60437. Ref.2 | ||||||
| Sequence conflict | 1963 | 1 | A → L in AAB60437. Ref.2 | ||||||
| Sequence conflict | 1979 | 1 | E → D in AAB60437. Ref.2 | ||||||
| Sequence conflict | 1994 | 1 | P → L in AAB60437. Ref.2 | ||||||
| Sequence conflict | 2021 | 1 | H → D in AAB60437. Ref.2 | ||||||
| Sequence conflict | 2075 | 1 | A → AA in AAB60437. Ref.2 | ||||||
| Sequence conflict | 2141 | 1 | T → A in AAB60437. Ref.2 | ||||||
| Sequence conflict | 2168 | 1 | S → I in AAB60437. Ref.2 | ||||||
| Sequence conflict | 2309 | 1 | S → N in AAB60437. Ref.2 | ||||||
| Sequence conflict | 2313 | 1 | R → G in AAB60437. Ref.2 | ||||||
| Sequence conflict | 2316 | 1 | H → A in AAB60437. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Nucleotide sequence polymorphism of mouse alpha1 B." Hong T., Birnbaumer L. Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6. Tissue: Brain. |
| [2] | "Molecular cloning of a murine N-type calcium channel alpha 1 subunit. Evidence for isoforms, brain distribution, and chromosomal localization." Coppola T., Waldmann R., Borsotto M., Heurteaux C., Romey G., Mattei M.-G., Lazdunski M. FEBS Lett. 338:1-5(1994) [PubMed: 8307146] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS NB1 AND NB2). Tissue: Neuroblastoma. |
| [3] | "Direct interaction of the Rab3 effector RIM with Ca2+ channels, SNAP-25, and synaptotagmin." Coppola T., Magnin-Luethi S., Perret-Menoud V., Gattesco S., Schiavo G., Regazzi R. J. Biol. Chem. 276:32756-32762(2001) [PubMed: 11438518] [Abstract] Cited for: INTERACTION WITH RIMS1. Tissue: Brain. |
| [4] | "Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed: 16452087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, MASS SPECTROMETRY. Tissue: Brain. |
| [5] | "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-745; SER-783 AND SER-2244, MASS SPECTROMETRY. Tissue: Brain cortex. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF042317 mRNA. Translation: AAB97840.1. U04999 mRNA. Translation: AAB60437.1. Frameshift. |
| IPI | IPI00115062. IPI00466672. |
| PIR | S41080. |
| RefSeq | NP_001035993.1. |
| UniGene | Mm.4424 |
3D structure databases | |
| SMR | O55017. Positions 1138-1214. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | O55017. |
Protein family/group databases | |
| TCDB | 1.A.1.11.9. voltage-gated ion channel (VIC) superfamily. |
PTM databases | |
| PhosphoSite | O55017. |
Proteomic databases | |
| PRIDE | O55017. |
Genome annotation databases | |
| Ensembl | ENSMUST00000041342; ENSMUSP00000037416; ENSMUSG00000004113; Mus musculus. [Genome view] ENSMUST00000093372; ENSMUSP00000091064; ENSMUSG00000004113; Mus musculus. [Genome view] |
| GeneID | 12287. |
| KEGG | mmu:12287. |
| UCSC | uc008ipe.1. mouse. uc008ipf.1. mouse. |
Organism-specific databases | |
| CTD | 12287. |
| MGI | MGI:88296. Cacna1b. |
Phylogenomic databases | |
| HOVERGEN | O55017. |
Gene expression databases | |
| ArrayExpress | O55017. |
| Bgee | O55017. |
| Genevestigator | O55017. |
| GermOnline | ENSMUSG00000004113. Mus musculus. |
Family and domain databases | |
| InterPro | IPR018249. EF_HAND_2. IPR005821. Ion_trans. IPR014873. VDCC_a1su_IQ. IPR005447. VDCC_N_a1su. IPR002077. VDCCAlpha1. [Graphical view] |
| PANTHER | PTHR10037:SF58. NVDCCAlpha1. 1 hit. |
| Pfam | PF08763. Ca_chan_IQ. 1 hit. PF00520. Ion_trans. 4 hits. [Graphical view] |
| PRINTS | PR00167. CACHANNEL. PR01631. NVDCCALPHA1. |
| PROSITE | PS50222. EF_HAND_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 280760. |
| SOURCE | Search... |
Entry information
| Entry name | CAC1B_MOUSE | ||||||||
| Accession | Primary (citable) accession number: O55017 Secondary accession number(s): Q60609 | ||||||||
| 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


