Cacna1s
entrez
12292
canonical
uniprot
Q02789
canonical
ensembl
ENSMUSG00000026407
resolver
ensp
ENSMUSP00000107695
resolver
ensp
ENSMUSP00000107699
resolver
ensp
ENSMUSP00000125278
resolver
enst
ENSMUST00000160641
resolver
genesymbol
Cacna1s
resolver
genesymbol_syn
Cach1
resolver
genesymbol_syn
Cach1b
resolver
genesymbol_syn
Cacn1
resolver
genesymbol_syn
Cacnl1a3
resolver
uniprot
A0A8I4RSM0
resolver
uniprot
E9Q7B5
resolver
uniprot
E9QPX8
resolver
uniprot
F8VQE0
resolver
uniprot
Q3UPG8
resolver
uniprot
Q99240
resolver
uniprot_entry
A0A8I4RSM0_MOUSE
resolver
uniprot_entry
CAC1S_MOUSE
resolver
uniprot_sec
E9Q7B5
resolver
uniprot_sec
E9QPX8
resolver
uniprot_sec
F8VQE0
resolver
uniprot_sec
Q3UPG8
resolver
uniprot_sec
Q99240
resolver
activity_regulation
ACTIVITY REGULATION: Channel activity is blocked by dihydropyridines (DHP), phenylalkylamines, and by benzothiazepines. {ECO:0000250|UniProtKB:P07293}.
uniprot
proteins
amino_acid_sequence
MEPPSPQDEGLRKKQPKKPVPEILPRPPRALFCLTLQNPLRKACISIVEWKPFETIILLTIFANCVALAVYLPMPEDDNNTLNLGLEKLEYFFLIVFSIEAAMKIIAYGFLFHQDAYLRSGWNVLDFIIVFLGVFTVILEQVNIIQTNTAPMSSKGAGLDVKALRAFRVLRPLRLVSGVPSLQVVLNSIFKAMLPLFHIALLVLFMVIIYAIIGLELFKGKMHKTCYFIGTDIVATVENEKPSPCARTGSGRPCTINGSECRGGWPGPNHGITHFDNFGFSMLTVYQCISMEGWTDVLYWVNDAIGNEWPWIYFVTLILLGSFFILNLVLGVLSGEFTKEREKAKSRGTFQKLREKQQLEEDLRGYMSWITQGEVMDVDDLREGKLSLDEGGSDTESLYEIEGLNKIIQFIRHWRQWNRVFRWKCHDLVKSKVFYWLVILIVALNTLSIASEHHNQPLWLTHLQDVANRVLLTLFTIEMLMKMYGLGLRQYFMSIFNRFDCFVVCSGILEILLVESGAMSPLGISVLRCIRLLRLFKITKYWTSLSNLVASLLNSIRSIASLLLLLFLFIIIFALLGMQLFGGRYDFEDTEVRRSNFDNFPQALISVFQVLTGEDWNSVMYNGIMAYGGPTYPGVLVCIYFIILFVCGNYILLNVFLAIAVDNLAEAESLTSAQKAKAEERKRRKMSKGLPDKSEEERATVTKKLEQKSKGEGIPTTAKLKIDEFESNVNEVKDPYPSADFPGDDEEDEPEIPVSPRPRPLAELQLKEKAVPIPEASSFFIFSPTNKIRVLCHRIVNATWFTNFILLFILLSSAALAAEDPIRADSMRNQILEYFDYVFTAVFTVEIVLKMTTYGAFLHKGSFCRNYFNILDLLVVAVSLISMGLESSAISVVKILRVLRVLRPLRAINRAKGLKHVVQCVFVAIRTIGNIVLVTTLLQFMFACIGVQLFKGKFYSCNDLSKMTEEECRGYYYIYKDGDPTQIELRPRQWIHNDFHFDNVLSAMMSLFTVSTFEGWPQLLYKAIDSNEEDTGPVYNNRVEMAIFFIIYIILIAFFMMNIFVGFVIVTFQEQGETEYKNCELDKNQRQCVQYALKARPLRCYIPKNPYQYQVWYVVTSSYFEYLMFALIMLNTICLGMQHYNQSEQMNHISDILNVAFTIIFTLEMVLKLIAFKPRGYFGDPWNVFDFLIVIGSIIDVILSEIDTFLASSGGLYCLGGGCGNVDPDESARISSAFFRLFRVMRLVKLLNRAEGVRTLLWTFIKSFQALPYVALLIVMLFFIYAVIGMQMFGKIAMVDGTQINRNNNFQTFPQAVLLLFRCATGEAWQEILLACSYGKLCDPESDYAPGEEHTCGTNFAYYYFISFYMLCAFLIINLFVAVIMDNFDYLTRDWSILGPHHLDEFKAIWAEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKFCPHRVACKRLVGMNMPLNSDGTVTFNATLFALVRTALKIKTEGNFEQANEELRAIIKKIWKRTSMKLLDQVIPPIGDDEVTVGKFYATFLIQEHFRKFMKRQEEYYGYRPKKDTVQIQAGLRTIEEEAAPEIHRAISGDLTAEEELERAMVEAAMEEGIFRRTGGLFGQVDNFLERTNSLPPVMANQRPLQFAEIEMEELESPVFLEDFPQNPGTHPLARANTNNANANVAYGNSSHRNNPVFSSICYEREFLGEADMPVTREGPLSQPCRASGPHSRSHVDKLKRPMTQRGMPEGQVPPSPCQVTGAKAEHPVQKEGKGPTSRFLETPNSRNFEEHVPRNSAHRCTAPATAMLIQEALVRGGLDSLAADANFVMATGQALADACQMEPEEVEVAATELLKQESPEGGAVPWEP
uniprot
proteins
disease_involvement
DISEASE: Note=Defects in Cacna1s are the cause of muscular dysgenesis (MDG), a lethal autosomal recessive disorder in which there is total lack of excitation-contraction coupling in homozygotes, and which results in complete skeletal muscle paralysis. A single nucleotide deletion yields a protein with an altered and truncated C-terminus. {ECO:0000269|PubMed:1281468}.
uniprot
proteins
function
FUNCTION: Pore-forming, alpha-1S subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle. Calcium channels containing the alpha-1S subunit play an important role in excitation-contraction coupling in skeletal muscle via their interaction with RYR1, which triggers Ca(2+) release from the sarcplasmic reticulum and ultimately results in muscle contraction. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. {ECO:0000250|UniProtKB:P07293, ECO:0000250|UniProtKB:Q13698}.
uniprot
proteins
mass_dalton
210320
uniprot
proteins
post_translational_modification
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. {ECO:0000250|UniProtKB:P07293}.; PTM: Phosphorylated. Phosphorylation by PKA activates the calcium channel. Both the minor and major forms are phosphorylated in vitro by PKA. Phosphorylation at Ser-1575 is involved in beta-adrenergic-mediated regulation of the channel. {ECO:0000250|UniProtKB:P07293}.
uniprot
proteins
protein_family
CACNA1S subfamily
uniprot
proteins
protein_family
Calcium channel alpha-1 subunit (TC 1.A.1.11) family
uniprot
proteins
pubmed
1281468
uniprot
proteins
pubmed
12871958
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16550931
uniprot
proteins
pubmed
16638807
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
2173707
uniprot
proteins
pubmed
28351836
uniprot
proteins
pubmed
29467163
uniprot
proteins
sequence_length
1852
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:P07293}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P07293}.
uniprot
proteins
transmembrane_region
TRANSMEM 52..70; /note="Helical; Name=S1 of repeat I"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 86..106; /note="Helical; Name=S2 of repeat I"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 116..136; /note="Helical; Name=S3 of repeat I"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 161..179; /note="Helical; Name=S4 of repeat I"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 197..218; /note="Helical; Name=S5 of repeat I"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 310..330; /note="Helical; Name=S6 of repeat I"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 433..451; /note="Helical; Name=S1 of repeat II"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 463..483; /note="Helical; Name=S2 of repeat II"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 495..514; /note="Helical; Name=S3 of repeat II"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 524..542; /note="Helical; Name=S4 of repeat II"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 562..581; /note="Helical; Name=S5 of repeat II"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 634..653; /note="Helical; Name=S6 of repeat II"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 800..818; /note="Helical; Name=S1 of repeat III"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 831..850; /note="Helical; Name=S2 of repeat III"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 867..885; /note="Helical; Name=S3 of repeat III"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 893..911; /note="Helical; Name=S4 of repeat III"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 931..950; /note="Helical; Name=S5 of repeat III"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1039..1060; /note="Helical; Name=S6 of repeat III"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1119..1140; /note="Helical; Name=S1 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1149..1170; /note="Helical; Name=S2 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1181..1200; /note="Helical; Name=S3 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1232..1250; /note="Helical; Name=S4 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1269..1289; /note="Helical; Name=S5 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1357..1381; /note="Helical; Name=S6 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P07293
uniprot
proteins