Cacna1s
entrez
682930
canonical
uniprot
Q02485
canonical
ensembl
ENSRNOG00000046231
resolver
ensp
ENSRNOP00000067264
resolver
genesymbol
Cacna1s
resolver
genesymbol_syn
Cach1
resolver
genesymbol_syn
Cacn1
resolver
genesymbol_syn
Cacnl1a3
resolver
genesymbol_syn
Cchl1a3
resolver
uniprot
B3XZL8
resolver
uniprot
P70484
resolver
uniprot
Q01553
resolver
uniprot
Q62817
resolver
uniprot_entry
CAC1S_RAT
resolver
uniprot_sec
B3XZL8
resolver
uniprot_sec
P70484
resolver
uniprot_sec
Q01553
resolver
uniprot_sec
Q62817
resolver
activity_regulation
ACTIVITY REGULATION: Channel activity is blocked by dihydropyridines (DHP), phenylalkylamines, and by benzothiazepines. {ECO:0000250|UniProtKB:P07293, ECO:0000305}.
uniprot
proteins
amino_acid_sequence
MEPSSPQDEGLRKKQPKKPVPEILPRPPRALFCLTLQNPLRKACISVVEWKPFETIILLTIFANCVALAVYLPMPEDDNNTLNLGLEKLEYFFLIVFSIEAAMKIIAYGFLFHQDAYLRSGWNVLDFIIVFLGVFTAILEQVNIIQTNTAPMSSKGAGLDVKALRAFRVLRPLRLVSGVPSLQVVLNSIFKAMLPLFHIALLVLFMVIIYAIIGLELFKGKMHKTCYFIGTDIVATVENEKPSPCARTGSGRPCTINGSECRGGWPGPNHGITHFDNFGFSMLTVYQCISMEGWTDVLYWVNDAIGNEWPWIYFVTLILLGSFFILNLVLGVLSGEFTKEREKAKSRGTFQKLREKQQLEEDLRGYMSWITQGEVMDVDDLREGKLSLDEGGSDTESLYEIEGLNKIIQFIRHWRQWNRVFRWKCHDLVKSKVFYWLVILIVALNTLSIASEHHNQPLWLTHLQDVANRVLLALFTIEMLMKMYGLGLRQYFMSIFNRFDCFVVCSGILEILLVESGAMTPLGISVLRCIRLLRLFKITKYWTSLSNLVASLLNSIRSIASLLLLLFLFMIIFALLGMQLFGGRYDFEDTEVRRSNFDNFPQALISVFQVLTGEDWNSVMYNGIMAYGGPSYPGVLVCIYFIILFVCGNYILLNVFLAIAVDNLAEAESLTSAQKAKAEERKRRKMSRGLPDKSEEERSTMTKKLEQKPKGEGIPTTAKLKIDEFESNVNEVKDPYPSADFPGDDEEDEPEIPASPRPRPLAELQLKEKAVPIPEASSFFIFSPTNKIRVLCHRIVNATWFTNFILLFILLSSAALAAEDPIRADSMRNQILEYFDYVFTAVFTVEIVLKMTTYGAFLHKGSFCRNYFNILDLLVVAVSLISMGLESSAISVVKILRVLRVLRPLRAINRAKGLKHVVQCVFVAIRTIGNIVLVTTLLQFMFACIGVQLFKGKFYSCNDLSKMTEEECRGYYYIYKDGDPTQIELRPRQWIHNDFHFDNVLSAMMSLFTVSTFEGWPQLLYKAIDSNEEDTGPVYNNRVEMAIFFIIYIILIAFFMMNIFVGFVIVTFQEQGETEYKNCELDKNQRQCVQYALKARPLRCYIPKNPYQYQVWYVVTSSYFEYLMFALIMLNTICLGMQHYNQSEQMNHISDILNVAFTIIFTLEMILKLIAFKPRGYFGDPWNVFDFLIVIGSIIDVILSEIDTLLASSGGLYCLGGGCGNVDPDESARISSAFFRLFRVMRLIKLLSRAEGVRTLLWTFIKSFQALPYVALLIVMLFFIYAVIGMQMFGKIAMVDGTQINRNNNFQTFPQAVLLLFRCATGEAWQEILLACSYGKRCDPESDYAPGEEYACGTNFAYYYFISFYMLCAFLIINLFVAVIMDNFDYLTRDWSILGPHHLDEFKAIWAEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKFCPHRVACKRLVGMNMPLNSDGTVTFNATLFALVRTALKIKTEGNFEQANEELRAIIKKIWKRTSMKLLDQVIPPIGDDEVTVGKFYATFLIQEHFRKFMKRQEEYYGYRPKKDTVQIQAGLRTIEEEAAPEIHRAISGDLTAEEELERAMVEAAMEEGIFRRTGGLFGQVDNFLERTNSLPPVMANQRPLQFAEMEMEELESPVFLEDFPQNPGTHPLARANTNNANANVAYGNSSHRNSPVFSSIRYERELLEEAGRPVTREGPFSQPCSVSGVNSRSHVDKLERQMSQRRMPKGQVPPSPCQLSQEKHPVHEEGKGPRSWSTETSDSESFEERVPRNSAHKCTAPATTMLIQEALVRGGLDSLAADANFVMATGQALADACQMEPEEVEVAATELLKRESPKGGAMPREP
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:0000269|PubMed:20101487}.
uniprot
proteins
mass_dalton
210396
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
1279681
uniprot
proteins
pubmed
1335956
uniprot
proteins
pubmed
20101487
uniprot
proteins
pubmed
2174428
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
7479909
uniprot
proteins
sequence_length
1850
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