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Database: UniProt
Entry: CAC1S_HUMAN
LinkDB: CAC1S_HUMAN
Original site: CAC1S_HUMAN 
ID   CAC1S_HUMAN             Reviewed;        1873 AA.
AC   Q13698; A4IF51; B1ALM2; Q12896; Q13934;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 4.
DT   24-JAN-2024, entry version 226.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha-1S;
DE   AltName: Full=Calcium channel, L type, alpha-1 polypeptide, isoform 3, skeletal muscle;
DE   AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.1;
GN   Name=CACNA1S;
GN   Synonyms=CACH1, CACN1, CACNL1A3 {ECO:0000303|PubMed:7713519,
GN   ECO:0000303|PubMed:8838325};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS HIS-458 AND ASP-1840.
RC   TISSUE=Skeletal muscle;
RX   PubMed=7713519; DOI=10.1006/geno.1994.1677;
RA   Hogan K., Powers P.A., Gregg R.G.;
RT   "Cloning of the human skeletal muscle alpha 1 subunit of the
RT   dihydropyridine-sensitive L-type calcium channel (CACNL1A3).";
RL   Genomics 24:608-609(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASP-1840.
RX   PubMed=8838325; DOI=10.1006/geno.1996.0066;
RA   Hogan K., Gregg R.G., Powers P.A.;
RT   "The structure of the gene encoding the human skeletal muscle alpha 1
RT   subunit of the dihydropyridine-sensitive L-type calcium channel
RT   (CACNL1A3).";
RL   Genomics 31:392-394(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-1800.
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 788-830; 1019-1085 AND 1293-1318.
RX   PubMed=7916735; DOI=10.1006/geno.1993.1017;
RA   Gregg R.G., Couch F., Hogan K., Powers P.A.;
RT   "Assignment of the human gene for the alpha-1 subunit of the skeletal
RT   muscle DHP-sensitive calcium channel (CACNL1A3) to chromosome 1q31-q32.";
RL   Genomics 15:107-112(1993).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1200-1300, AND VARIANTS HOKPP1 GLY-1239 AND
RP   HIS-1239.
RX   PubMed=8004673; DOI=10.1016/0092-8674(94)90135-x;
RA   Ptacek L.J., Tawil R., Griggs R.C., Engel A.G., Layzer R.B., Kwiecinski H.,
RA   McManis P.G., Santiago L., Moore M., Fouad G., Bradley P., Leppert M.F.;
RT   "Dihydropyridine receptor mutations cause hypokalemic periodic paralysis.";
RL   Cell 77:863-868(1994).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1223-1413.
RA   Soldatov N.M.;
RT   "Human skeletal muscle L-type Ca2+ channel alpha 1S subunit gene shows
RT   splicing patterns similar to alpha 1C and alpha 1D genes in the region
RT   involved in hereditary disorders.";
RL   Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   INVOLVEMENT IN SUSCEPTIBILITY TO TTPP1.
RX   PubMed=15001631; DOI=10.1210/jc.2003-030924;
RA   Kung A.W., Lau K.S., Fong G.C., Chan V.;
RT   "Association of novel single nucleotide polymorphisms in the calcium
RT   channel alpha 1 subunit gene (Ca(v)1.1) and thyrotoxic periodic
RT   paralysis.";
RL   J. Clin. Endocrinol. Metab. 89:1340-1345(2004).
RN   [9] {ECO:0007744|PDB:2VAY}
RP   X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 1522-1542 IN COMPLEX WITH CALM.
RX   PubMed=19473981; DOI=10.1074/jbc.m109.013326;
RA   Halling D.B., Georgiou D.K., Black D.J., Yang G., Fallon J.L.,
RA   Quiocho F.A., Pedersen S.E., Hamilton S.L.;
RT   "Determinants in CaV1 channels that regulate the Ca2+ sensitivity of bound
RT   calmodulin.";
RL   J. Biol. Chem. 284:20041-20051(2009).
RN   [10] {ECO:0007744|PDB:6B27}
RP   X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 747-760 IN COMPLEX WITH STAC2,
RP   AND INTERACTION WITH STAC; STAC2 AND STAC3.
RX   PubMed=29078335; DOI=10.1073/pnas.1708852114;
RA   Wong King Yuen S.M., Campiglio M., Tung C.C., Flucher B.E., Van Petegem F.;
RT   "Structural insights into binding of STAC proteins to voltage-gated calcium
RT   channels.";
RL   Proc. Natl. Acad. Sci. U.S.A. 114:E9520-E9528(2017).
RN   [11]
RP   VARIANT HOKPP1 HIS-528.
RX   PubMed=7987325; DOI=10.1093/hmg/3.8.1415;
RA   Jurkatt-Rott K., Lehmann-Horn F., Elbaz A., Heine R., Gregg R.G., Hogan K.,
RA   Powers P.A., Lapie P., Vale-Santos J.E., Weissenbach J., Fontaine B.;
RT   "A calcium channel mutation causing hypokalemic periodic paralysis.";
RL   Hum. Mol. Genet. 3:1415-1419(1994).
RN   [12]
RP   SEQUENCE REVISION, VARIANT MHS5 HIS-1086, AND VARIANTS HIS-458 AND
RP   CYS-1539.
RX   PubMed=9199552; DOI=10.1086/515454;
RA   Monnier N., Procaccio V., Stieglitz P., Lunardi J.;
RT   "Malignant-hyperthermia susceptibility is associated with a mutation of the
RT   alpha-1-subunit of the human dihydropyridine-sensitive L-type voltage-
RT   dependent calcium-channel receptor in skeletal muscle.";
RL   Am. J. Hum. Genet. 60:1316-1325(1997).
RN   [13]
RP   INVOLVEMENT IN CMYP18, VARIANTS CMYP18 LYS-100; LEU-275; GLN-742; SER-742;
RP   VAL-1367 AND 1485-GLN--LEU-1873 DEL, CHARACTERIZATION OF VARIANTS CMYP18
RP   GLN-742; SER-742 AND VAL-1367, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=28012042; DOI=10.1007/s00401-016-1656-8;
RA   Schartner V., Romero N.B., Donkervoort S., Treves S., Munot P.,
RA   Pierson T.M., Dabaj I., Malfatti E., Zaharieva I.T., Zorzato F.,
RA   Abath Neto O., Brochier G., Lornage X., Eymard B., Taratuto A.L., Boehm J.,
RA   Gonorazky H., Ramos-Platt L., Feng L., Phadke R., Bharucha-Goebel D.X.,
RA   Sumner C.J., Bui M.T., Lacene E., Beuvin M., Labasse C., Dondaine N.,
RA   Schneider R., Thompson J., Boland A., Deleuze J.F., Matthews E.,
RA   Pakleza A.N., Sewry C.A., Biancalana V., Quijano-Roy S., Muntoni F.,
RA   Fardeau M., Boennemann C.G., Laporte J.;
RT   "Dihydropyridine receptor (DHPR, CACNA1S) congenital myopathy.";
RL   Acta Neuropathol. 133:517-533(2017).
RN   [14]
RP   VARIANTS HOKPP1 HIS-528; HIS-1239 AND GLY-1239.
RX   PubMed=18162704; DOI=10.3346/jkms.2007.22.6.946;
RA   Kim J.-B., Kim M.-H., Lee S.J., Kim D.-J., Lee B.C.;
RT   "The genotype and clinical phenotype of Korean patients with familial
RT   hypokalemic periodic paralysis.";
RL   J. Korean Med. Sci. 22:946-951(2007).
RN   [15]
RP   VARIANT HOKPP1 HIS-1239.
RX   PubMed=17418573; DOI=10.1016/j.nmd.2007.01.020;
RA   Houinato D., Laleye A., Adjien C., Adjagba M., Sternberg D., Hilbert P.,
RA   Vallat J.M., Darboux R.B., Funalot B., Avode D.G.;
RT   "Hypokalaemic periodic paralysis due to the CACNA1S R1239H mutation in a
RT   large African family.";
RL   Neuromuscul. Disord. 17:419-422(2007).
RN   [16]
RP   VARIANTS HOKPP1 GLY-528; HIS-528; SER-900; GLY-1239 AND HIS-1239.
RX   PubMed=19118277; DOI=10.1212/01.wnl.0000342387.65477.46;
RA   Matthews E., Labrum R., Sweeney M.G., Sud R., Haworth A., Chinnery P.F.,
RA   Meola G., Schorge S., Kullmann D.M., Davis M.B., Hanna M.G.;
RT   "Voltage sensor charge loss accounts for most cases of hypokalemic periodic
RT   paralysis.";
RL   Neurology 72:1544-1547(2009).
RN   [17]
RP   VARIANT CMYP18 HIS-789.
RX   PubMed=31227654; DOI=10.3233/jnd-190383;
RA   Yis U., Hiz S., Guenes S., Diniz G., Baydan F., Toepf A., Sonmezler E.,
RA   Lochmueller H., Horvath R., Oktay Y.;
RT   "Dihydropyridine Receptor Congenital Myopathy In A Consangineous Turkish
RT   Family.";
RL   J. Neuromuscul. Dis. 6:377-384(2019).
RN   [18]
RP   VARIANTS CMYP18 LYS-222 AND CYS-789.
RX   PubMed=33060286; DOI=10.1136/jmedgenet-2020-106901;
RA   Ravenscroft G., Clayton J.S., Faiz F., Sivadorai P., Milnes D.,
RA   Cincotta R., Moon P., Kamien B., Edwards M., Delatycki M., Lamont P.J.,
RA   Chan S.H., Colley A., Ma A., Collins F., Hennington L., Zhao T.,
RA   McGillivray G., Ghedia S., Chao K., O'Donnell-Luria A., Laing N.G.,
RA   Davis M.R.;
RT   "Neurogenetic fetal akinesia and arthrogryposis: genetics, expanding
RT   genotype-phenotypes and functional genomics.";
RL   J. Med. Genet. 58:609-618(2021).
CC   -!- FUNCTION: Pore-forming, alpha-1S subunit of the voltage-gated calcium
CC       channel that gives rise to L-type calcium currents in skeletal muscle.
CC       Calcium channels containing the alpha-1S subunit play an important role
CC       in excitation-contraction coupling in skeletal muscle via their
CC       interaction with RYR1, which triggers Ca(2+) release from the
CC       sarcoplasmic reticulum and ultimately results in muscle contraction.
CC       Long-lasting (L-type) calcium channels belong to the 'high-voltage
CC       activated' (HVA) group. {ECO:0000269|PubMed:28012042}.
CC   -!- ACTIVITY REGULATION: Channel activity is blocked by dihydropyridines
CC       (DHP), phenylalkylamines, and by benzothiazepines.
CC       {ECO:0000250|UniProtKB:P07293}.
CC   -!- SUBUNIT: Component of a calcium channel complex consisting of a pore-
CC       forming alpha subunit (CACNA1S) and the ancillary subunits CACNB1 or
CC       CACNB2, CACNG1 and CACNA2D1. The channel complex contains alpha, beta,
CC       gamma and delta subunits in a 1:1:1:1 ratio, i.e. it contains either
CC       CACNB1 or CACNB2 (By similarity). CACNA1S channel activity is modulated
CC       by the auxiliary subunits (CACNB1 or CACNB2, CACNG1 and CACNA2D1).
CC       Interacts with DYSF and JSRP1 (By similarity). Interacts with RYR1 (By
CC       similarity). Interacts with STAC, STAC2 and STAC3 (via their SH3
CC       domains) (PubMed:29078335). Interacts with CALM (PubMed:19473981).
CC       {ECO:0000250|UniProtKB:P07293, ECO:0000250|UniProtKB:Q02789,
CC       ECO:0000269|PubMed:19473981, ECO:0000269|PubMed:29078335}.
CC   -!- INTERACTION:
CC       Q13698; Q9BWC9: CCDC106; NbExp=3; IntAct=EBI-5329490, EBI-711501;
CC       Q13698; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-5329490, EBI-3867333;
CC       Q13698; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-5329490, EBI-16439278;
CC       Q13698; Q86UT5: NHERF4; NbExp=3; IntAct=EBI-5329490, EBI-8744528;
CC       Q13698; Q04864-2: REL; NbExp=3; IntAct=EBI-5329490, EBI-10829018;
CC       Q13698; Q9H2K2: TNKS2; NbExp=2; IntAct=EBI-5329490, EBI-4398527;
CC   -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma, T-tubule
CC       {ECO:0000269|PubMed:28012042}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P07293}.
CC   -!- TISSUE SPECIFICITY: Skeletal muscle specific.
CC   -!- DOMAIN: Each of the four internal repeats contains five hydrophobic
CC       transmembrane segments (S1, S2, S3, S5, S6) and one positively charged
CC       transmembrane segment (S4). S4 segments probably represent the voltage-
CC       sensor and are characterized by a series of positively charged amino
CC       acids at every third position. {ECO:0000250|UniProtKB:P07293}.
CC   -!- DOMAIN: The loop between repeats II and III interacts with the
CC       ryanodine receptor, and is therefore important for calcium release from
CC       the endoplasmic reticulum necessary for muscle contraction.
CC       {ECO:0000250|UniProtKB:P07293}.
CC   -!- PTM: The alpha-1S subunit is found in two isoforms in the skeletal
CC       muscle: a minor form of 212 kDa containing the complete amino acid
CC       sequence, and a major form of 190 kDa derived from the full-length form
CC       by post-translational proteolysis close to Phe-1690.
CC       {ECO:0000250|UniProtKB:P07293}.
CC   -!- PTM: Phosphorylated. Phosphorylation by PKA activates the calcium
CC       channel. Both the minor and major forms are phosphorylated in vitro by
CC       PKA. Phosphorylation at Ser-1575 is involved in beta-adrenergic-
CC       mediated regulation of the channel. {ECO:0000250|UniProtKB:P07293}.
CC   -!- DISEASE: Periodic paralysis hypokalemic 1 (HOKPP1) [MIM:170400]: An
CC       autosomal dominant disorder manifested by episodic flaccid generalized
CC       muscle weakness associated with falls of serum potassium levels.
CC       {ECO:0000269|PubMed:17418573, ECO:0000269|PubMed:18162704,
CC       ECO:0000269|PubMed:19118277, ECO:0000269|PubMed:7987325,
CC       ECO:0000269|PubMed:8004673}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Malignant hyperthermia 5 (MHS5) [MIM:601887]: Autosomal
CC       dominant disorder that is potentially lethal in susceptible individuals
CC       on exposure to commonly used inhalational anesthetics and depolarizing
CC       muscle relaxants. {ECO:0000269|PubMed:9199552}. Note=Disease
CC       susceptibility is associated with variants affecting the gene
CC       represented in this entry.
CC   -!- DISEASE: Thyrotoxic periodic paralysis 1 (TTPP1) [MIM:188580]: A
CC       sporadic muscular disorder characterized by episodic weakness and
CC       hypokalemia during a thyrotoxic state. It is clinically similar to
CC       hereditary hypokalemic periodic paralysis, except for the fact that
CC       hyperthyroidism is an absolute requirement for disease manifestation.
CC       The disease presents with recurrent episodes of acute muscular weakness
CC       of the four extremities that vary in severity from paresis to complete
CC       paralysis. Attacks are triggered by ingestion of a high carbohydrate
CC       load or strenuous physical activity followed by a period of rest.
CC       Thyrotoxic periodic paralysis can occur in association with any cause
CC       of hyperthyroidism, but is most commonly associated with Graves
CC       disease. {ECO:0000269|PubMed:15001631}. Note=Disease susceptibility is
CC       associated with variants affecting the gene represented in this entry.
CC   -!- DISEASE: Congenital myopathy 18 (CMYP18) [MIM:620246]: A congenital
CC       myopathy of variable severity, ranging from severe fetal akinesia to
CC       milder forms of muscle weakness. Most affected individuals show delayed
CC       motor development with generalized hypotonia and progressive axial and
CC       limb muscle weakness beginning soon after birth or in infancy.
CC       Additional features may include swallowing difficulties, external
CC       ophthalmoplegia, ptosis, high-arched palate, and respiratory
CC       insufficiency. Muscle biopsy shows variable morphologic abnormalities,
CC       including alveolar changes in the intermyofibrillar network, fiber size
CC       variability, focal disorganization, internal nuclei, and dilated
CC       sarcoplasmic reticulum and T-tubules. CMYP18 inheritance is autosomal
CC       dominant or recessive. {ECO:0000269|PubMed:28012042,
CC       ECO:0000269|PubMed:31227654, ECO:0000269|PubMed:33060286}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC       1.A.1.11) family. CACNA1S subfamily. {ECO:0000305}.
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DR   EMBL; L33798; AAA51902.1; -; mRNA.
DR   EMBL; U30707; AAB37235.1; -; Genomic_DNA.
DR   EMBL; U30666; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30667; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30668; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30669; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30670; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30671; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30672; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30673; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30674; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30675; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30676; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30677; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30678; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30679; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30680; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30681; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30682; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30683; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30684; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30685; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30686; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30687; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30688; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30689; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30690; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30691; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30692; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30693; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30694; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30695; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30696; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30697; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30698; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30699; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30700; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30701; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30702; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30703; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30704; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30705; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; U30706; AAB37235.1; JOINED; Genomic_DNA.
DR   EMBL; AL358473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL139159; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC133671; AAI33672.1; -; mRNA.
DR   EMBL; M87486; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M87487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M87488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; U09784; AAA20531.1; -; mRNA.
DR   EMBL; Z50091; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z50092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z50093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS1407.1; -.
DR   PIR; A55645; A55645.
DR   PIR; I38611; I38611.
DR   RefSeq; NP_000060.2; NM_000069.2.
DR   PDB; 2VAY; X-ray; 1.94 A; B=1522-1542.
DR   PDB; 6B27; X-ray; 1.73 A; G/H/I/J/K/L=747-760.
DR   PDBsum; 2VAY; -.
DR   PDBsum; 6B27; -.
DR   AlphaFoldDB; Q13698; -.
DR   SMR; Q13698; -.
DR   BioGRID; 107233; 10.
DR   ComplexPortal; CPX-3192; Skeletal muscle VGCC complex.
DR   IntAct; Q13698; 9.
DR   MINT; Q13698; -.
DR   STRING; 9606.ENSP00000355192; -.
DR   BindingDB; Q13698; -.
DR   ChEMBL; CHEMBL3805; -.
DR   DrugBank; DB01118; Amiodarone.
DR   DrugBank; DB09229; Aranidipine.
DR   DrugBank; DB09231; Benidipine.
DR   DrugBank; DB13746; Bioallethrin.
DR   DrugBank; DB11148; Butamben.
DR   DrugBank; DB11093; Calcium citrate.
DR   DrugBank; DB11348; Calcium Phosphate.
DR   DrugBank; DB14481; Calcium phosphate dihydrate.
DR   DrugBank; DB09232; Cilnidipine.
DR   DrugBank; DB00568; Cinnarizine.
DR   DrugBank; DB04920; Clevidipine.
DR   DrugBank; DB04855; Dronedarone.
DR   DrugBank; DB06751; Drotaverine.
DR   DrugBank; DB09235; Efonidipine.
DR   DrugBank; DB00228; Enflurane.
DR   DrugBank; DB00153; Ergocalciferol.
DR   DrugBank; DB00898; Ethanol.
DR   DrugBank; DB01023; Felodipine.
DR   DrugBank; DB13961; Fish oil.
DR   DrugBank; DB00270; Isradipine.
DR   DrugBank; DB09236; Lacidipine.
DR   DrugBank; DB00825; Levomenthol.
DR   DrugBank; DB00653; Magnesium sulfate.
DR   DrugBank; DB09238; Manidipine.
DR   DrugBank; DB01388; Mibefradil.
DR   DrugBank; DB01110; Miconazole.
DR   DrugBank; DB00622; Nicardipine.
DR   DrugBank; DB01115; Nifedipine.
DR   DrugBank; DB06712; Nilvadipine.
DR   DrugBank; DB00393; Nimodipine.
DR   DrugBank; DB00401; Nisoldipine.
DR   DrugBank; DB01054; Nitrendipine.
DR   DrugBank; DB00252; Phenytoin.
DR   DrugBank; DB09090; Pinaverium.
DR   DrugBank; DB00243; Ranolazine.
DR   DrugBank; DB00421; Spironolactone.
DR   DrugBank; DB00273; Topiramate.
DR   DrugBank; DB09089; Trimebutine.
DR   DrugBank; DB00661; Verapamil.
DR   DrugCentral; Q13698; -.
DR   GuidetoPHARMACOLOGY; 528; -.
DR   TCDB; 1.A.1.11.32; the voltage-gated ion channel (vic) superfamily.
DR   GlyCosmos; Q13698; 3 sites, No reported glycans.
DR   GlyGen; Q13698; 5 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q13698; -.
DR   PhosphoSitePlus; Q13698; -.
DR   BioMuta; CACNA1S; -.
DR   DMDM; 209572767; -.
DR   jPOST; Q13698; -.
DR   MassIVE; Q13698; -.
DR   PaxDb; 9606-ENSP00000355192; -.
DR   PeptideAtlas; Q13698; -.
DR   Antibodypedia; 4015; 200 antibodies from 32 providers.
DR   DNASU; 779; -.
DR   Ensembl; ENST00000362061.4; ENSP00000355192.3; ENSG00000081248.12.
DR   GeneID; 779; -.
DR   KEGG; hsa:779; -.
DR   MANE-Select; ENST00000362061.4; ENSP00000355192.3; NM_000069.3; NP_000060.2.
DR   UCSC; uc001gvv.4; human.
DR   AGR; HGNC:1397; -.
DR   CTD; 779; -.
DR   DisGeNET; 779; -.
DR   GeneCards; CACNA1S; -.
DR   GeneReviews; CACNA1S; -.
DR   HGNC; HGNC:1397; CACNA1S.
DR   HPA; ENSG00000081248; Group enriched (skeletal muscle, tongue).
DR   MalaCards; CACNA1S; -.
DR   MIM; 114208; gene.
DR   MIM; 170400; phenotype.
DR   MIM; 188580; phenotype.
DR   MIM; 601887; phenotype.
DR   MIM; 620246; phenotype.
DR   neXtProt; NX_Q13698; -.
DR   OpenTargets; ENSG00000081248; -.
DR   Orphanet; 681; Hypokalemic periodic paralysis.
DR   Orphanet; 423; Malignant hyperthermia of anesthesia.
DR   Orphanet; 397755; Periodic paralysis with transient compartment-like syndrome.
DR   Orphanet; 79102; Thyrotoxic periodic paralysis.
DR   PharmGKB; PA85; -.
DR   VEuPathDB; HostDB:ENSG00000081248; -.
DR   eggNOG; KOG2301; Eukaryota.
DR   GeneTree; ENSGT00940000158289; -.
DR   InParanoid; Q13698; -.
DR   OMA; WFENLED; -.
DR   OrthoDB; 1110761at2759; -.
DR   PhylomeDB; Q13698; -.
DR   TreeFam; TF312805; -.
DR   PathwayCommons; Q13698; -.
DR   Reactome; R-HSA-419037; NCAM1 interactions.
DR   SignaLink; Q13698; -.
DR   SIGNOR; Q13698; -.
DR   BioGRID-ORCS; 779; 24 hits in 1160 CRISPR screens.
DR   ChiTaRS; CACNA1S; human.
DR   EvolutionaryTrace; Q13698; -.
DR   GeneWiki; Cav1.1; -.
DR   GenomeRNAi; 779; -.
DR   Pharos; Q13698; Tclin.
DR   PRO; PR:Q13698; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q13698; Protein.
DR   Bgee; ENSG00000081248; Expressed in gluteal muscle and 83 other cell types or tissues.
DR   ExpressionAtlas; Q13698; baseline and differential.
DR   Genevisible; Q13698; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0031674; C:I band; IDA:UniProtKB.
DR   GO; GO:1990454; C:L-type voltage-gated calcium channel complex; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0030315; C:T-tubule; IDA:UniProtKB.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:UniProtKB.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0140677; F:molecular function activator activity; EXP:DisProt.
DR   GO; GO:0036094; F:small molecule binding; EXP:DisProt.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:UniProtKB.
DR   GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; NAS:ComplexPortal.
DR   GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
DR   GO; GO:0071313; P:cellular response to caffeine; ISS:UniProtKB.
DR   GO; GO:0007029; P:endoplasmic reticulum organization; IEA:Ensembl.
DR   GO; GO:0002074; P:extraocular skeletal muscle development; IEA:Ensembl.
DR   GO; GO:0006936; P:muscle contraction; IMP:UniProtKB.
DR   GO; GO:0007520; P:myoblast fusion; IEA:Ensembl.
DR   GO; GO:0007528; P:neuromuscular junction development; IEA:Ensembl.
DR   GO; GO:0045933; P:positive regulation of muscle contraction; NAS:ComplexPortal.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:UniProtKB.
DR   GO; GO:0043501; P:skeletal muscle adaptation; IEA:Ensembl.
DR   GO; GO:0048741; P:skeletal muscle fiber development; IEA:Ensembl.
DR   GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
DR   GO; GO:0006941; P:striated muscle contraction; IEA:Ensembl.
DR   DisProt; DP01103; -.
DR   Gene3D; 1.10.287.70; -; 4.
DR   Gene3D; 6.10.250.2180; -; 1.
DR   Gene3D; 6.10.250.2500; -; 1.
DR   Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 4.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005450; VDCC_L_a1ssu.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR45628; VOLTAGE-DEPENDENT CALCIUM CHANNEL TYPE A SUBUNIT ALPHA-1; 1.
DR   PANTHER; PTHR45628:SF9; VOLTAGE-DEPENDENT L-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1S; 1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01630; LVDCCALPHA1.
DR   PRINTS; PR01634; LVDCCALPHA1S.
DR   SMART; SM01062; Ca_chan_IQ; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Calcium channel; Calcium transport;
KW   Calmodulin-binding; Cell membrane; Disease variant; Disulfide bond;
KW   Glycoprotein; Ion channel; Ion transport; Membrane; Metal-binding;
KW   Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..1873
FT                   /note="Voltage-dependent L-type calcium channel subunit
FT                   alpha-1S"
FT                   /id="PRO_0000053943"
FT   TOPO_DOM        1..51
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        52..70
FT                   /note="Helical; Name=S1 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        71..85
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        86..106
FT                   /note="Helical; Name=S2 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        107..115
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        116..136
FT                   /note="Helical; Name=S3 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        137..160
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        161..179
FT                   /note="Helical; Name=S4 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        180..196
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        197..218
FT                   /note="Helical; Name=S5 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        219..279
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        280..301
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        302..309
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        310..330
FT                   /note="Helical; Name=S6 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        331..432
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        433..451
FT                   /note="Helical; Name=S1 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        452..462
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        463..483
FT                   /note="Helical; Name=S2 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        484..494
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        495..514
FT                   /note="Helical; Name=S3 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        515..523
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        524..542
FT                   /note="Helical; Name=S4 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        543..561
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        562..581
FT                   /note="Helical; Name=S5 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        582..601
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        602..623
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        624..633
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        634..653
FT                   /note="Helical; Name=S6 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        654..799
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        800..818
FT                   /note="Helical; Name=S1 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        819..830
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        831..850
FT                   /note="Helical; Name=S2 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        851..866
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        867..885
FT                   /note="Helical; Name=S3 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        886..892
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        893..911
FT                   /note="Helical; Name=S4 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        912..930
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        931..950
FT                   /note="Helical; Name=S5 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        951..1000
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        1001..1021
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        1022..1038
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1039..1060
FT                   /note="Helical; Name=S6 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        1061..1118
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1119..1140
FT                   /note="Helical; Name=S1 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        1141..1148
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1149..1170
FT                   /note="Helical; Name=S2 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        1171..1180
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1181..1200
FT                   /note="Helical; Name=S3 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        1201..1231
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1232..1250
FT                   /note="Helical; Name=S4 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        1251..1268
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1269..1289
FT                   /note="Helical; Name=S5 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        1290..1311
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        1312..1330
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        1331..1356
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1357..1381
FT                   /note="Helical; Name=S6 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   TOPO_DOM        1382..1873
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REPEAT          38..337
FT                   /note="I"
FT                   /evidence="ECO:0000305"
FT   REPEAT          418..664
FT                   /note="II"
FT                   /evidence="ECO:0000305"
FT   REPEAT          786..1068
FT                   /note="III"
FT                   /evidence="ECO:0000305"
FT   REPEAT          1105..1384
FT                   /note="IV"
FT                   /evidence="ECO:0000305"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          357..374
FT                   /note="Binding to the beta subunit"
FT                   /evidence="ECO:0000250|UniProtKB:Q02789"
FT   REGION          675..717
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          731..757
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          747..760
FT                   /note="Interaction with STAC, STAC2 and STAC3 (via SH3
FT                   domains)"
FT                   /evidence="ECO:0000269|PubMed:29078335"
FT   REGION          988..1077
FT                   /note="Dihydropyridine binding"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   REGION          1337..1403
FT                   /note="Dihydropyridine binding"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   REGION          1349..1391
FT                   /note="Phenylalkylamine binding"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   REGION          1522..1542
FT                   /note="Interaction with calmodulin"
FT                   /evidence="ECO:0000269|PubMed:19473981"
FT   REGION          1731..1780
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           290..293
FT                   /note="Selectivity filter of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   MOTIF           612..615
FT                   /note="Selectivity filter of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   MOTIF           1012..1015
FT                   /note="Selectivity filter of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   MOTIF           1321..1324
FT                   /note="Selectivity filter of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        675..710
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1748..1772
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         292
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   BINDING         614
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   BINDING         1014
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   MOD_RES         393
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q02789"
FT   MOD_RES         397
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q02789"
FT   MOD_RES         687
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   MOD_RES         1575
FT                   /note="Phosphoserine; by PKA and CAMK2"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   MOD_RES         1617
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   CARBOHYD        79
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        226..254
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   DISULFID        245..261
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   DISULFID        957..968
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   DISULFID        1338..1352
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   VARIANT         69
FT                   /note="A -> G (in dbSNP:rs12406479)"
FT                   /id="VAR_046970"
FT   VARIANT         100
FT                   /note="E -> K (in CMYP18; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:28012042"
FT                   /id="VAR_088226"
FT   VARIANT         222
FT                   /note="M -> K (in CMYP18; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:33060286"
FT                   /id="VAR_088227"
FT   VARIANT         275
FT                   /note="F -> L (in CMYP18)"
FT                   /evidence="ECO:0000269|PubMed:28012042"
FT                   /id="VAR_088228"
FT   VARIANT         458
FT                   /note="L -> H (in dbSNP:rs12742169)"
FT                   /evidence="ECO:0000269|PubMed:7713519,
FT                   ECO:0000269|PubMed:9199552"
FT                   /id="VAR_001498"
FT   VARIANT         528
FT                   /note="R -> G (in HOKPP1; dbSNP:rs80338778)"
FT                   /evidence="ECO:0000269|PubMed:19118277"
FT                   /id="VAR_054953"
FT   VARIANT         528
FT                   /note="R -> H (in HOKPP1; dbSNP:rs80338777)"
FT                   /evidence="ECO:0000269|PubMed:18162704,
FT                   ECO:0000269|PubMed:19118277, ECO:0000269|PubMed:7987325"
FT                   /id="VAR_001499"
FT   VARIANT         742
FT                   /note="P -> Q (in CMYP18; decreased protein abundance)"
FT                   /evidence="ECO:0000269|PubMed:28012042"
FT                   /id="VAR_088229"
FT   VARIANT         742
FT                   /note="P -> S (in CMYP18; decreased protein abundance)"
FT                   /evidence="ECO:0000269|PubMed:28012042"
FT                   /id="VAR_088230"
FT   VARIANT         789
FT                   /note="R -> C (in CMYP18; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:33060286"
FT                   /id="VAR_088231"
FT   VARIANT         789
FT                   /note="R -> H (in CMYP18; uncertain significance;
FT                   dbSNP:rs1157720606)"
FT                   /evidence="ECO:0000269|PubMed:31227654"
FT                   /id="VAR_088232"
FT   VARIANT         900
FT                   /note="R -> S (in HOKPP1)"
FT                   /evidence="ECO:0000269|PubMed:19118277"
FT                   /id="VAR_054954"
FT   VARIANT         1086
FT                   /note="R -> H (in MHS5; dbSNP:rs1800559)"
FT                   /evidence="ECO:0000269|PubMed:9199552"
FT                   /id="VAR_001500"
FT   VARIANT         1239
FT                   /note="R -> G (in HOKPP1; dbSNP:rs28930069)"
FT                   /evidence="ECO:0000269|PubMed:18162704,
FT                   ECO:0000269|PubMed:19118277, ECO:0000269|PubMed:8004673"
FT                   /id="VAR_001501"
FT   VARIANT         1239
FT                   /note="R -> H (in HOKPP1; dbSNP:rs28930068)"
FT                   /evidence="ECO:0000269|PubMed:17418573,
FT                   ECO:0000269|PubMed:18162704, ECO:0000269|PubMed:19118277,
FT                   ECO:0000269|PubMed:8004673"
FT                   /id="VAR_001502"
FT   VARIANT         1367
FT                   /note="L -> V (in CMYP18; uncertain significance; patient
FT                   myotubes show decreased depolarization-induced release of
FT                   sequestered calcium ion into cytosol compared to control)"
FT                   /evidence="ECO:0000269|PubMed:28012042"
FT                   /id="VAR_088233"
FT   VARIANT         1485..1873
FT                   /note="Missing (in CMYP18)"
FT                   /evidence="ECO:0000269|PubMed:28012042"
FT                   /id="VAR_088234"
FT   VARIANT         1539
FT                   /note="R -> C (in dbSNP:rs3850625)"
FT                   /evidence="ECO:0000269|PubMed:9199552"
FT                   /id="VAR_001503"
FT   VARIANT         1658
FT                   /note="R -> H (in dbSNP:rs13374149)"
FT                   /id="VAR_046971"
FT   VARIANT         1800
FT                   /note="L -> S (in dbSNP:rs12139527)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_046972"
FT   VARIANT         1840
FT                   /note="E -> D (in dbSNP:rs1042379)"
FT                   /evidence="ECO:0000269|PubMed:7713519,
FT                   ECO:0000269|PubMed:8838325"
FT                   /id="VAR_046973"
FT   CONFLICT        26
FT                   /note="R -> S (in Ref. 2; AAB37235)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        265
FT                   /note="W -> C (in Ref. 1; AAA51902 and 2; AAB37235)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        574
FT                   /note="A -> R (in Ref. 1; AAA51902 and 2; AAB37235)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        627..628
FT                   /note="YG -> SS (in Ref. 1; AAA51902)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        628
FT                   /note="G -> R (in Ref. 2; AAB37235)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        916..919
FT                   /note="Missing (in Ref. 2; AAB37235)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        918..919
FT                   /note="VQ -> AR (in Ref. 1; AAA51902)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1180
FT                   /note="D -> N (in Ref. 1; AAA51902 and 2; AAB37235)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1294..1295
FT                   /note="LV -> FE (in Ref. 6; AAA20531)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1318
FT                   /note="R -> RHA (in Ref. 2; AAB37235)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1472
FT                   /note="R -> G (in Ref. 2; AAB37235)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1510
FT                   /note="I -> M (in Ref. 2; AAB37235)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1532
FT                   /note="H -> D (in Ref. 2; AAB37235)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1671
FT                   /note="G -> A (in Ref. 1; AAA51902 and 2; AAB37235)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1710
FT                   /note="V -> S (in Ref. 1; AAA51902)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1815
FT                   /note="A -> G (in Ref. 1; AAA51902 and 2; AAB37235)"
FT                   /evidence="ECO:0000305"
FT   HELIX           1523..1536
FT                   /evidence="ECO:0007829|PDB:2VAY"
FT   HELIX           1538..1541
FT                   /evidence="ECO:0007829|PDB:2VAY"
SQ   SEQUENCE   1873 AA;  212350 MW;  7B7446727E578913 CRC64;
     MEPSSPQDEG LRKKQPKKPV PEILPRPPRA LFCLTLENPL RKACISIVEW KPFETIILLT
     IFANCVALAV YLPMPEDDNN SLNLGLEKLE YFFLIVFSIE AAMKIIAYGF LFHQDAYLRS
     GWNVLDFTIV FLGVFTVILE QVNVIQSHTA PMSSKGAGLD VKALRAFRVL RPLRLVSGVP
     SLQVVLNSIF KAMLPLFHIA LLVLFMVIIY AIIGLELFKG KMHKTCYFIG TDIVATVENE
     EPSPCARTGS GRRCTINGSE CRGGWPGPNH GITHFDNFGF SMLTVYQCIT MEGWTDVLYW
     VNDAIGNEWP WIYFVTLILL GSFFILNLVL GVLSGEFTKE REKAKSRGTF QKLREKQQLD
     EDLRGYMSWI TQGEVMDVED FREGKLSLDE GGSDTESLYE IAGLNKIIQF IRHWRQWNRI
     FRWKCHDIVK SKVFYWLVIL IVALNTLSIA SEHHNQPLWL TRLQDIANRV LLSLFTTEML
     MKMYGLGLRQ YFMSIFNRFD CFVVCSGILE ILLVESGAMT PLGISVLRCI RLLRIFKITK
     YWTSLSNLVA SLLNSIRSIA SLLLLLFLFI VIFALLGMQL FGGRYDFEDT EVRRSNFDNF
     PQALISVFQV LTGEDWTSMM YNGIMAYGGP SYPGMLVCIY FIILFVCGNY ILLNVFLAIA
     VDNLAEAESL TSAQKAKAEE KKRRKMSKGL PDKSEEEKST MAKKLEQKPK GEGIPTTAKL
     KIDEFESNVN EVKDPYPSAD FPGDDEEDEP EIPLSPRPRP LAELQLKEKA VPIPEASSFF
     IFSPTNKIRV LCHRIVNATW FTNFILLFIL LSSAALAAED PIRADSMRNQ ILKHFDIGFT
     SVFTVEIVLK MTTYGAFLHK GSFCRNYFNM LDLLVVAVSL ISMGLESSAI SVVKILRVLR
     VLRPLRAINR AKGLKHVVQC MFVAISTIGN IVLVTTLLQF MFACIGVQLF KGKFFRCTDL
     SKMTEEECRG YYYVYKDGDP MQIELRHREW VHSDFHFDNV LSAMMSLFTV STFEGWPQLL
     YKAIDSNAED VGPIYNNRVE MAIFFIIYII LIAFFMMNIF VGFVIVTFQE QGETEYKNCE
     LDKNQRQCVQ YALKARPLRC YIPKNPYQYQ VWYIVTSSYF EYLMFALIML NTICLGMQHY
     NQSEQMNHIS DILNVAFTII FTLEMILKLM AFKARGYFGD PWNVFDFLIV IGSIIDVILS
     EIDTFLASSG GLYCLGGGCG NVDPDESARI SSAFFRLFRV MRLIKLLSRA EGVRTLLWTF
     IKSFQALPYV ALLIVMLFFI YAVIGMQMFG KIALVDGTQI NRNNNFQTFP QAVLLLFRCA
     TGEAWQEILL ACSYGKLCDP ESDYAPGEEY TCGTNFAYYY FISFYMLCAF LVINLFVAVI
     MDNFDYLTRD WSILGPHHLD EFKAIWAEYD PEAKGRIKHL DVVTLLRRIQ PPLGFGKFCP
     HRVACKRLVG MNMPLNSDGT VTFNATLFAL VRTALKIKTE GNFEQANEEL RAIIKKIWKR
     TSMKLLDQVI PPIGDDEVTV GKFYATFLIQ EHFRKFMKRQ EEYYGYRPKK DIVQIQAGLR
     TIEEEAAPEI CRTVSGDLAA EEELERAMVE AAMEEGIFRR TGGLFGQVDN FLERTNSLPP
     VMANQRPLQF AEIEMEEMES PVFLEDFPQD PRTNPLARAN TNNANANVAY GNSNHSNSHV
     FSSVHYEREF PEETETPATR GRALGQPCRV LGPHSKPCVE MLKGLLTQRA MPRGQAPPAP
     CQCPRVESSM PEDRKSSTPG SLHEETPHSR STRENTSRCS APATALLIQK ALVRGGLGTL
     AADANFIMAT GQALADACQM EPEEVEIMAT ELLKGREAPE GMASSLGCLN LGSSLGSLDQ
     HQGSQETLIP PRL
//
DBGET integrated database retrieval system