CACNA1S
entrez
779
canonical
uniprot
Q13698
canonical
ensembl
ENSG00000081248
resolver
ensp
ENSP00000355192
resolver
ensp
ENSP00000356307
resolver
enst
ENST00000362061
resolver
enst
ENST00000367338
resolver
genesymbol
CACNA1S
resolver
genesymbol_syn
CACH1
resolver
genesymbol_syn
CACN1
resolver
genesymbol_syn
CACNL1A3
resolver
hgnc
HGNC:1397
resolver
uniprot
A4IF51
resolver
uniprot
B1ALM2
resolver
uniprot
B1ALM3
resolver
uniprot
Q12896
resolver
uniprot
Q13934
resolver
uniprot_entry
B1ALM3_HUMAN
resolver
uniprot_entry
CAC1S_HUMAN
resolver
uniprot_sec
A4IF51
resolver
uniprot_sec
B1ALM2
resolver
uniprot_sec
Q12896
resolver
uniprot_sec
Q13934
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
MEPSSPQDEGLRKKQPKKPVPEILPRPPRALFCLTLENPLRKACISIVEWKPFETIILLTIFANCVALAVYLPMPEDDNNSLNLGLEKLEYFFLIVFSIEAAMKIIAYGFLFHQDAYLRSGWNVLDFTIVFLGVFTVILEQVNVIQSHTAPMSSKGAGLDVKALRAFRVLRPLRLVSGVPSLQVVLNSIFKAMLPLFHIALLVLFMVIIYAIIGLELFKGKMHKTCYFIGTDIVATVENEEPSPCARTGSGRRCTINGSECRGGWPGPNHGITHFDNFGFSMLTVYQCITMEGWTDVLYWVNDAIGNEWPWIYFVTLILLGSFFILNLVLGVLSGEFTKEREKAKSRGTFQKLREKQQLDEDLRGYMSWITQGEVMDVEDFREGKLSLDEGGSDTESLYEIAGLNKIIQFIRHWRQWNRIFRWKCHDIVKSKVFYWLVILIVALNTLSIASEHHNQPLWLTRLQDIANRVLLSLFTTEMLMKMYGLGLRQYFMSIFNRFDCFVVCSGILEILLVESGAMTPLGISVLRCIRLLRIFKITKYWTSLSNLVASLLNSIRSIASLLLLLFLFIVIFALLGMQLFGGRYDFEDTEVRRSNFDNFPQALISVFQVLTGEDWTSMMYNGIMAYGGPSYPGMLVCIYFIILFVCGNYILLNVFLAIAVDNLAEAESLTSAQKAKAEEKKRRKMSKGLPDKSEEEKSTMAKKLEQKPKGEGIPTTAKLKIDEFESNVNEVKDPYPSADFPGDDEEDEPEIPLSPRPRPLAELQLKEKAVPIPEASSFFIFSPTNKIRVLCHRIVNATWFTNFILLFILLSSAALAAEDPIRADSMRNQILKHFDIGFTSVFTVEIVLKMTTYGAFLHKGSFCRNYFNMLDLLVVAVSLISMGLESSAISVVKILRVLRVLRPLRAINRAKGLKHVVQCMFVAISTIGNIVLVTTLLQFMFACIGVQLFKGKFFRCTDLSKMTEEECRGYYYVYKDGDPMQIELRHREWVHSDFHFDNVLSAMMSLFTVSTFEGWPQLLYKAIDSNAEDVGPIYNNRVEMAIFFIIYIILIAFFMMNIFVGFVIVTFQEQGETEYKNCELDKNQRQCVQYALKARPLRCYIPKNPYQYQVWYIVTSSYFEYLMFALIMLNTICLGMQHYNQSEQMNHISDILNVAFTIIFTLEMILKLMAFKARGYFGDPWNVFDFLIVIGSIIDVILSEIDTFLASSGGLYCLGGGCGNVDPDESARISSAFFRLFRVMRLIKLLSRAEGVRTLLWTFIKSFQALPYVALLIVMLFFIYAVIGMQMFGKIALVDGTQINRNNNFQTFPQAVLLLFRCATGEAWQEILLACSYGKLCDPESDYAPGEEYTCGTNFAYYYFISFYMLCAFLVINLFVAVIMDNFDYLTRDWSILGPHHLDEFKAIWAEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKFCPHRVACKRLVGMNMPLNSDGTVTFNATLFALVRTALKIKTEGNFEQANEELRAIIKKIWKRTSMKLLDQVIPPIGDDEVTVGKFYATFLIQEHFRKFMKRQEEYYGYRPKKDIVQIQAGLRTIEEEAAPEICRTVSGDLAAEEELERAMVEAAMEEGIFRRTGGLFGQVDNFLERTNSLPPVMANQRPLQFAEIEMEEMESPVFLEDFPQDPRTNPLARANTNNANANVAYGNSNHSNSHVFSSVHYEREFPEETETPATRGRALGQPCRVLGPHSKPCVEMLKGLLTQRAMPRGQAPPAPCQCPRVESSMPEDRKSSTPGSLHEETPHSRSTRENTSRCSAPATALLIQKALVRGGLGTLAADANFIMATGQALADACQMEPEEVEIMATELLKGREAPEGMASSLGCLNLGSSLGSLDQHQGSQETLIPPRL
uniprot
proteins
disease_involvement
DISEASE: Periodic paralysis hypokalemic 1 (HOKPP1) [MIM:170400]: An autosomal dominant disorder manifested by episodic flaccid generalized muscle weakness associated with falls of serum potassium levels. {ECO:0000269|PubMed:17418573, ECO:0000269|PubMed:18162704, ECO:0000269|PubMed:19118277, ECO:0000269|PubMed:7987325, ECO:0000269|PubMed:8004673}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Malignant hyperthermia 5 (MHS5) [MIM:601887]: Autosomal dominant disorder that is potentially lethal in susceptible individuals on exposure to commonly used inhalational anesthetics and depolarizing muscle relaxants. {ECO:0000269|PubMed:9199552}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Thyrotoxic periodic paralysis 1 (TTPP1) [MIM:188580]: A sporadic muscular disorder characterized by episodic weakness and hypokalemia during a thyrotoxic state. It is clinically similar to hereditary hypokalemic periodic paralysis, except for the fact that hyperthyroidism is an absolute requirement for disease manifestation. The disease presents with recurrent episodes of acute muscular weakness of the four extremities that vary in severity from paresis to complete paralysis. Attacks are triggered by ingestion of a high carbohydrate load or strenuous physical activity followed by a period of rest. Thyrotoxic periodic paralysis can occur in association with any cause of hyperthyroidism, but is most commonly associated with Graves disease. {ECO:0000269|PubMed:15001631}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Congenital myopathy 18 (CMYO18) [MIM:620246]: A congenital myopathy of variable severity, ranging from severe fetal akinesia to milder forms of muscle weakness. Most affected individuals show delayed motor development with generalized hypotonia and progressive axial and limb muscle weakness beginning soon after birth or in infancy. Additional features may include swallowing difficulties, external ophthalmoplegia, ptosis, high-arched palate, and respiratory insufficiency. Muscle biopsy shows variable morphologic abnormalities, including alveolar changes in the intermyofibrillar network, fiber size variability, focal disorganization, internal nuclei, and dilated sarcoplasmic reticulum and T-tubules. CMYO18 inheritance is autosomal dominant or recessive. {ECO:0000269|PubMed:28012042, ECO:0000269|PubMed:31227654, ECO:0000269|PubMed:33060286}. Note=The disease is caused by variants affecting the gene represented in this entry.
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 sarcoplasmic reticulum and ultimately results in muscle contraction. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. {ECO:0000269|PubMed:28012042}.
uniprot
proteins
mass_dalton
212350
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
15001631
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17418573
uniprot
proteins
pubmed
18162704
uniprot
proteins
pubmed
19118277
uniprot
proteins
pubmed
19473981
uniprot
proteins
pubmed
28012042
uniprot
proteins
pubmed
29078335
uniprot
proteins
pubmed
31227654
uniprot
proteins
pubmed
33060286
uniprot
proteins
pubmed
7713519
uniprot
proteins
pubmed
7916735
uniprot
proteins
pubmed
7987325
uniprot
proteins
pubmed
8004673
uniprot
proteins
pubmed
8838325
uniprot
proteins
pubmed
9199552
uniprot
proteins
sequence_length
1873
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane, sarcolemma, T-tubule {ECO:0000269|PubMed:28012042}; 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