[1]
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NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Skeletal muscle;
DOI=10.1038/328313a0; PubMed=3037387 [NCBI, ExPASy, EBI, Israel, Japan]
Tanabe T.,
Takeshima H.,
Mikami A.,
Flockerzi V.,
Takahashi H.,
Kangawa K.,
Kojima M.,
Matsuo H.,
Hirose T.,
Numa S.;
"Primary structure of the receptor for calcium channel blockers from skeletal muscle.";
Nature 328:313-318(1987).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Skeletal muscle;
PubMed=2458626 [NCBI, ExPASy, EBI, Israel, Japan]
Ellis S.B.,
Williams M.E.,
Ways N.R.,
Brenner R.,
Sharp A.H.,
Leung A.T.,
Campbell K.P.,
McKenna E.,
Koch W.J.,
Hui A.,
Schwartz A.,
Harpold M.M.;
"Sequence and expression of mRNAs encoding the alpha 1 and alpha 2 subunits of a DHP-sensitive calcium channel.";
Science 241:1661-1664(1988).
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[3]
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BETA-SUBUNIT BINDING DOMAIN.
DOI=10.1038/368067a0; PubMed=7509046 [NCBI, ExPASy, EBI, Israel, Japan]
Pragnell M.,
de Waard M.,
Mori Y.,
Tanabe T.,
Snutch T.P.,
Campbell K.P.;
"Calcium channel beta-subunit binds to a conserved motif in the I-II cytoplasmic linker of the alpha 1-subunit.";
Nature 368:67-70(1994).
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[4]
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PHENYLALKYLAMINE-BINDING SITE.
PubMed=2174553 [NCBI, ExPASy, EBI, Israel, Japan]
Striessnig J.,
Glossmann H.,
Catterall W.A.;
"Identification of a phenylalkylamine binding region within the alpha 1 subunit of skeletal muscle Ca2+ channels.";
Proc. Natl. Acad. Sci. U.S.A. 87:9108-9112(1990).
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[5]
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DIHYDROPYRIDINE-BINDING SITE.
PubMed=1656465 [NCBI, ExPASy, EBI, Israel, Japan]
Nakayama H.,
Taki M.,
Striessnig J.,
Glossmann H.,
Catterall W.A.,
Kanaoka Y.;
"Identification of 1,4-dihydropyridine binding regions within the alpha 1 subunit of skeletal muscle Ca2+ channels by photoaffinity labeling with diazipine.";
Proc. Natl. Acad. Sci. U.S.A. 88:9203-9207(1991).
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[6]
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DIHYDROPYRIDINE-BINDING SITE.
PubMed=1660150 [NCBI, ExPASy, EBI, Israel, Japan]
Striessnig J.,
Murphy B.J.,
Catterall W.A.;
"Dihydropyridine receptor of L-type Ca2+ channels: identification of binding domains for [3H](+)-PN200-110 and [3H]azidopine within the alpha 1 subunit.";
Proc. Natl. Acad. Sci. U.S.A. 88:10769-10773(1991).
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[7]
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PHOSPHORYLATION AT SER-687 AND SER-1617.
PubMed=2844809 [NCBI, ExPASy, EBI, Israel, Japan]
Roehrkasten A.,
Meyer H.E.,
Nastainczyk W.,
Sieber M.,
Hofmann F.;
"CAMP-dependent protein kinase rapidly phosphorylates serine-687 of the skeletal muscle receptor for calcium channel blockers.";
J. Biol. Chem. 263:15325-15329(1988).
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[8]
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PHOSPHORYLATION BY PKA.
PubMed=2549550 [NCBI, ExPASy, EBI, Israel, Japan]
Nunoki K.,
Florio V.,
Catterall W.A.;
"Activation of purified calcium channels by stoichiometric protein phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 86:6816-6820(1989).
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[9]
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STRUCTURE BY NMR OF 671-690.
DOI=10.1074/jbc.275.16.11631; PubMed=10766780 [NCBI, ExPASy, EBI, Israel, Japan]
Casarotto M.G.,
Gibson F.,
Pace S.M.,
Curtis S.M.,
Mulcair M.,
Dulhunty A.F.;
"A structural requirement for activation of skeletal ryanodine receptors by peptides of the dihydropyridine receptor II-III loop.";
J. Biol. Chem. 275:11631-11637(2000).
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[10]
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X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 34-415 IN COMPLEX WITH CACNA1S.
DOI=10.1016/S0896-6273(04)00250-8; PubMed=15134636 [NCBI, ExPASy, EBI, Israel, Japan]
Opatowsky Y.,
Chen C.-C.,
Campbell K.P.,
Hirsch J.A.;
"Structural analysis of the voltage-dependent calcium channel beta subunit functional core and its complex with the alpha1 interaction domain.";
Neuron 42:387-399(2004).
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- 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-1S gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the "high-voltage activated" (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to omega-conotoxin-GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing the alpha-1S subunit play an important role in excitation-contraction coupling in skeletal muscle.
- SUBUNIT: 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. An additional gamma subunit is present only in skeletal muscle L-type channel. Interacts with JSRP1 (By similarity).
- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
- TISSUE SPECIFICITY: Skeletal muscle specific.
- 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.
- DOMAIN: The loop between repeats II and III interacts with the ryanodine receptor, and is therefore important for calcium release from the endoplasmic reticulum necessary for muscle contraction.
- PTM: The alpha-1S subunit is found in two isoforms in the skeletal muscle: a minor form of 212 kDa containing the complete amino acid sequence, and a major form of 190 kDa derived from the full-length form by post-translational proteolysis close to Phe-1690.
- PTM: Both the minor and major forms are phosphorylated in vitro by PKA. Phosphorylation by PKA activates the calcium channel.
- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family [view classification].
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