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Q13698 (CAC1S_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Voltage-dependent L-type calcium channel subunit alpha-1S
Alternative name(s):
Calcium channel, L type, alpha-1 polypeptide, isoform 3, skeletal muscle
Voltage-gated calcium channel subunit alpha Cav1.1
Gene names
Name:CACNA1S
Synonyms:CACH1, CACN1, CACNL1A3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1873 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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-1Sgives 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 structure

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 DYSF and JSRP1. Interacts with RYR1 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.

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.

Post-translational modification

Phosphorylation by PKA activates the calcium channel By similarity.

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6 Ref.9 Ref.11 Ref.12 Ref.13

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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.10

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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.8

Sequence similarities

Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family. CACNA1S subfamily. [View classification]

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   Molecular functionCalcium channel
Ion channel
Voltage-gated channel
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Traceable author statement. Source: Reactome

calcium ion import

Inferred from Biological aspect of Ancestor. Source: RefGenome

calcium ion transport

Inferred from direct assay PubMed 9852570. Source: UniProtKB

endoplasmic reticulum organization

Inferred from electronic annotation. Source: Ensembl

extraocular skeletal muscle development

Inferred from electronic annotation. Source: Ensembl

membrane depolarization during action potential

Inferred from Biological aspect of Ancestor. Source: RefGenome

muscle contraction

Inferred from mutant phenotype Ref.12. Source: UniProtKB

myoblast fusion

Inferred from electronic annotation. Source: Ensembl

neuromuscular junction development

Inferred from electronic annotation. Source: Ensembl

skeletal muscle adaptation

Inferred from electronic annotation. Source: Ensembl

skeletal muscle fiber development

Inferred from electronic annotation. Source: Ensembl

skeletal system development

Inferred from electronic annotation. Source: Ensembl

striated muscle contraction

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentI band

Inferred from direct assay PubMed 11206130. Source: UniProtKB

T-tubule

Inferred from direct assay PubMed 17204937. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 11206130. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 11206130. Source: UniProtKB

sarcoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

voltage-gated calcium channel complex

Inferred from direct assay PubMed 9852570. Source: UniProtKB

   Molecular_functionhigh voltage-gated calcium channel activity

Inferred from direct assay PubMed 9852570. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

voltage-gated calcium channel activity

Inferred from direct assay PubMed 9852570. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18731873Voltage-dependent L-type calcium channel subunit alpha-1S
PRO_0000053943

Regions

Topological domain1 – 5151Cytoplasmic Potential
Transmembrane52 – 7019Helical; Name=S1 of repeat I; Potential
Topological domain71 – 8818Extracellular Potential
Transmembrane89 – 10820Helical; Name=S2 of repeat I; Potential
Topological domain109 – 12012Cytoplasmic Potential
Transmembrane121 – 13919Helical; Name=S3 of repeat I; Potential
Topological domain140 – 16021Extracellular Potential
Transmembrane161 – 17919Helical; Name=S4 of repeat I; Potential
Topological domain180 – 19819Cytoplasmic Potential
Transmembrane199 – 21820Helical; Name=S5 of repeat I; Potential
Topological domain219 – 30991Extracellular Potential
Transmembrane310 – 33425Helical; Name=S6 of repeat I; Potential
Topological domain335 – 43298Cytoplasmic Potential
Transmembrane433 – 45119Helical; Name=S1 of repeat II; Potential
Topological domain452 – 46615Extracellular Potential
Transmembrane467 – 48620Helical; Name=S2 of repeat II; Potential
Topological domain487 – 4948Cytoplasmic Potential
Transmembrane495 – 51319Helical; Name=S3 of repeat II; Potential
Topological domain514 – 52310Extracellular Potential
Transmembrane524 – 54219Helical; Name=S4 of repeat II; Potential
Topological domain543 – 56119Cytoplasmic Potential
Transmembrane562 – 58120Helical; Name=S5 of repeat II; Potential
Topological domain582 – 63655Extracellular Potential
Transmembrane637 – 66125Helical; Name=S6 of repeat II; Potential
Topological domain662 – 799138Cytoplasmic Potential
Transmembrane800 – 81819Helical; Name=S1 of repeat III; Potential
Topological domain819 – 83416Extracellular Potential
Transmembrane835 – 85420Helical; Name=S2 of repeat III; Potential
Topological domain855 – 86612Cytoplasmic Potential
Transmembrane867 – 88519Helical; Name=S3 of repeat III; Potential
Topological domain886 – 8927Extracellular Potential
Transmembrane893 – 91119Helical; Name=S4 of repeat III; Potential
Topological domain912 – 93019Cytoplasmic Potential
Transmembrane931 – 95020Helical; Name=S5 of repeat III; Potential
Topological domain951 – 104090Extracellular Potential
Transmembrane1041 – 106525Helical; Name=S6 of repeat III; Potential
Topological domain1066 – 111853Cytoplasmic Potential
Transmembrane1119 – 113719Helical; Name=S1 of repeat IV; Potential
Topological domain1138 – 115215Extracellular Potential
Transmembrane1153 – 117220Helical; Name=S2 of repeat IV; Potential
Topological domain1173 – 11808Cytoplasmic Potential
Transmembrane1181 – 119919Helical; Name=S3 of repeat IV; Potential
Topological domain1200 – 123132Extracellular Potential
Transmembrane1232 – 125019Helical; Name=S4 of repeat IV; Potential
Topological domain1251 – 126919Cytoplasmic Potential
Transmembrane1270 – 128920Helical; Name=S5 of repeat IV; Potential
Topological domain1290 – 135667Extracellular Potential
Transmembrane1357 – 138125Helical; Name=S6 of repeat IV; Potential
Topological domain1382 – 1873492Cytoplasmic Potential
Repeat38 – 337300I
Repeat418 – 664247II
Repeat786 – 1068283III
Repeat1105 – 1384280IV
Calcium binding1410 – 142112 By similarity
Region357 – 37418Binding to the beta subunit By similarity
Region988 – 107790Dihydropyridine binding By similarity
Region1337 – 140367Dihydropyridine binding By similarity
Region1349 – 139244Phenylalkylamine binding By similarity
Compositional bias562 – 5687Poly-Leu

Sites

Site2921Calcium ion selectivity and permeability By similarity
Site6141Calcium ion selectivity and permeability By similarity
Site10141Calcium ion selectivity and permeability By similarity
Site13231Calcium ion selectivity and permeability By similarity

Amino acid modifications

Modified residue6871Phosphoserine; by PKA By similarity
Modified residue13921Phosphoserine; by PKA Potential
Modified residue16171Phosphoserine By similarity
Glycosylation791N-linked (GlcNAc...) Potential
Glycosylation2571N-linked (GlcNAc...) Potential
Glycosylation11411N-linked (GlcNAc...) Potential

Natural variations

Natural variant691A → G.
Corresponds to variant rs12406479 [ dbSNP | Ensembl ].
VAR_046970
Natural variant4581L → H. Ref.1 Ref.10
Corresponds to variant rs12742169 [ dbSNP | Ensembl ].
VAR_001498
Natural variant5281R → G in HOKPP1. Ref.13
VAR_054953
Natural variant5281R → H in HOKPP1. Ref.9 Ref.11 Ref.13
VAR_001499
Natural variant9001R → S in HOKPP1. Ref.13
VAR_054954
Natural variant10861R → H in MHS5. Ref.10
Corresponds to variant rs1800559 [ dbSNP | Ensembl ].
VAR_001500
Natural variant12391R → G in HOKPP1. Ref.6 Ref.11 Ref.13
Corresponds to variant rs28930069 [ dbSNP | Ensembl ].
VAR_001501
Natural variant12391R → H in HOKPP1. Ref.6 Ref.11 Ref.12 Ref.13
Corresponds to variant rs28930068 [ dbSNP | Ensembl ].
VAR_001502
Natural variant15391R → C. Ref.10
Corresponds to variant rs3850625 [ dbSNP | Ensembl ].
VAR_001503
Natural variant16581R → H.
Corresponds to variant rs13374149 [ dbSNP | Ensembl ].
VAR_046971
Natural variant18001L → S. Ref.4
Corresponds to variant rs12139527 [ dbSNP | Ensembl ].
VAR_046972
Natural variant18401E → D. Ref.1 Ref.2
Corresponds to variant rs1042379 [ dbSNP | Ensembl ].
VAR_046973

Experimental info

Sequence conflict261R → S in AAB37235. Ref.2
Sequence conflict2651W → C in AAA51902. Ref.1
Sequence conflict2651W → C in AAB37235. Ref.2
Sequence conflict5741A → R in AAA51902. Ref.1
Sequence conflict5741A → R in AAB37235. Ref.2
Sequence conflict627 – 6282YG → SS in AAA51902. Ref.1
Sequence conflict6281G → R in AAB37235. Ref.2
Sequence conflict916 – 9194Missing in AAB37235. Ref.2
Sequence conflict918 – 9192VQ → AR in AAA51902. Ref.1
Sequence conflict11801D → N in AAA51902. Ref.1
Sequence conflict11801D → N in AAB37235. Ref.2
Sequence conflict1294 – 12952LV → FE in AAA20531. Ref.6
Sequence conflict13181R → RHA in AAB37235. Ref.2
Sequence conflict14721R → G in AAB37235. Ref.2
Sequence conflict15101I → M in AAB37235. Ref.2
Sequence conflict15321H → D in AAB37235. Ref.2
Sequence conflict16711G → A in AAA51902. Ref.1
Sequence conflict16711G → A in AAB37235. Ref.2
Sequence conflict17101V → S in AAA51902. Ref.1
Sequence conflict18151A → G in AAA51902. Ref.1
Sequence conflict18151A → G in AAB37235. Ref.2

Secondary structure

..... 1873
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q13698 [UniParc].

Last modified October 14, 2008. Version 4.
Checksum: 7B7446727E578913

FASTA1,873212,350
        10         20         30         40         50         60 
MEPSSPQDEG LRKKQPKKPV PEILPRPPRA LFCLTLENPL RKACISIVEW KPFETIILLT 

        70         80         90        100        110        120 
IFANCVALAV YLPMPEDDNN SLNLGLEKLE YFFLIVFSIE AAMKIIAYGF LFHQDAYLRS 

       130        140        150        160        170        180 
GWNVLDFTIV FLGVFTVILE QVNVIQSHTA PMSSKGAGLD VKALRAFRVL RPLRLVSGVP 

       190        200        210        220        230        240 
SLQVVLNSIF KAMLPLFHIA LLVLFMVIIY AIIGLELFKG KMHKTCYFIG TDIVATVENE 

       250        260        270        280        290        300 
EPSPCARTGS GRRCTINGSE CRGGWPGPNH GITHFDNFGF SMLTVYQCIT MEGWTDVLYW 

       310        320        330        340        350        360 
VNDAIGNEWP WIYFVTLILL GSFFILNLVL GVLSGEFTKE REKAKSRGTF QKLREKQQLD 

       370        380        390        400        410        420 
EDLRGYMSWI TQGEVMDVED FREGKLSLDE GGSDTESLYE IAGLNKIIQF IRHWRQWNRI 

       430        440        450        460        470        480 
FRWKCHDIVK SKVFYWLVIL IVALNTLSIA SEHHNQPLWL TRLQDIANRV LLSLFTTEML 

       490        500        510        520        530        540 
MKMYGLGLRQ YFMSIFNRFD CFVVCSGILE ILLVESGAMT PLGISVLRCI RLLRIFKITK 

       550        560        570        580        590        600 
YWTSLSNLVA SLLNSIRSIA SLLLLLFLFI VIFALLGMQL FGGRYDFEDT EVRRSNFDNF 

       610        620        630        640        650        660 
PQALISVFQV LTGEDWTSMM YNGIMAYGGP SYPGMLVCIY FIILFVCGNY ILLNVFLAIA 

       670        680        690        700        710        720 
VDNLAEAESL TSAQKAKAEE KKRRKMSKGL PDKSEEEKST MAKKLEQKPK GEGIPTTAKL 

       730        740        750        760        770        780 
KIDEFESNVN EVKDPYPSAD FPGDDEEDEP EIPLSPRPRP LAELQLKEKA VPIPEASSFF 

       790        800        810        820        830        840 
IFSPTNKIRV LCHRIVNATW FTNFILLFIL LSSAALAAED PIRADSMRNQ ILKHFDIGFT 

       850        860        870        880        890        900 
SVFTVEIVLK MTTYGAFLHK GSFCRNYFNM LDLLVVAVSL ISMGLESSAI SVVKILRVLR 

       910        920        930        940        950        960 
VLRPLRAINR AKGLKHVVQC MFVAISTIGN IVLVTTLLQF MFACIGVQLF KGKFFRCTDL 

       970        980        990       1000       1010       1020 
SKMTEEECRG YYYVYKDGDP MQIELRHREW VHSDFHFDNV LSAMMSLFTV STFEGWPQLL 

      1030       1040       1050       1060       1070       1080 
YKAIDSNAED VGPIYNNRVE MAIFFIIYII LIAFFMMNIF VGFVIVTFQE QGETEYKNCE 

      1090       1100       1110       1120       1130       1140 
LDKNQRQCVQ YALKARPLRC YIPKNPYQYQ VWYIVTSSYF EYLMFALIML NTICLGMQHY 

      1150       1160       1170       1180       1190       1200 
NQSEQMNHIS DILNVAFTII FTLEMILKLM AFKARGYFGD PWNVFDFLIV IGSIIDVILS 

      1210       1220       1230       1240       1250       1260 
EIDTFLASSG GLYCLGGGCG NVDPDESARI SSAFFRLFRV MRLIKLLSRA EGVRTLLWTF 

      1270       1280       1290       1300       1310       1320 
IKSFQALPYV ALLIVMLFFI YAVIGMQMFG KIALVDGTQI NRNNNFQTFP QAVLLLFRCA 

      1330       1340       1350       1360       1370       1380 
TGEAWQEILL ACSYGKLCDP ESDYAPGEEY TCGTNFAYYY FISFYMLCAF LVINLFVAVI 

      1390       1400       1410       1420       1430       1440 
MDNFDYLTRD WSILGPHHLD EFKAIWAEYD PEAKGRIKHL DVVTLLRRIQ PPLGFGKFCP 

      1450       1460       1470       1480       1490       1500 
HRVACKRLVG MNMPLNSDGT VTFNATLFAL VRTALKIKTE GNFEQANEEL RAIIKKIWKR 

      1510       1520       1530       1540       1550       1560 
TSMKLLDQVI PPIGDDEVTV GKFYATFLIQ EHFRKFMKRQ EEYYGYRPKK DIVQIQAGLR 

      1570       1580       1590       1600       1610       1620 
TIEEEAAPEI CRTVSGDLAA EEELERAMVE AAMEEGIFRR TGGLFGQVDN FLERTNSLPP 

      1630       1640       1650       1660       1670       1680 
VMANQRPLQF AEIEMEEMES PVFLEDFPQD PRTNPLARAN TNNANANVAY GNSNHSNSHV 

      1690       1700       1710       1720       1730       1740 
FSSVHYEREF PEETETPATR GRALGQPCRV LGPHSKPCVE MLKGLLTQRA MPRGQAPPAP 

      1750       1760       1770       1780       1790       1800 
CQCPRVESSM PEDRKSSTPG SLHEETPHSR STRENTSRCS APATALLIQK ALVRGGLGTL 

      1810       1820       1830       1840       1850       1860 
AADANFIMAT GQALADACQM EPEEVEIMAT ELLKGREAPE GMASSLGCLN LGSSLGSLDQ 

      1870 
HQGSQETLIP PRL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of the human skeletal muscle alpha 1 subunit of the dihydropyridine-sensitive L-type calcium channel (CACNL1A3)."
Hogan K., Powers P.A., Gregg R.G.
Genomics 24:608-609(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS HIS-458 AND ASP-1840.
Tissue: Skeletal muscle.
[2]"The structure of the gene encoding the human skeletal muscle alpha 1 subunit of the dihydropyridine-sensitive L-type calcium channel (CACNL1A3)."
Hogan K., Gregg R.G., Powers P.A.
Genomics 31:392-394(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ASP-1840.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-1800.
[5]"Assignment of the human gene for the alpha-1 subunit of the skeletal muscle DHP-sensitive calcium channel (CACNL1A3) to chromosome 1q31-q32."
Gregg R.G., Couch F., Hogan K., Powers P.A.
Genomics 15:107-112(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 788-830; 1019-1085 AND 1293-1318.
[6]"Dihydropyridine receptor mutations cause hypokalemic periodic paralysis."
Ptacek L.J., Tawil R., Griggs R.C., Engel A.G., Layzer R.B., Kwiecinski H., McManis P.G., Santiago L., Moore M., Fouad G., Bradley P., Leppert M.F.
Cell 77:863-868(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1200-1300, VARIANTS HOKPP1 GLY-1239 AND HIS-1239.
[7]"Human skeletal muscle L-type Ca2+ channel alpha 1S subunit gene shows splicing patterns similar to alpha 1C and alpha 1D genes in the region involved in hereditary disorders."
Soldatov N.M.
Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1223-1413.
[8]"Association of novel single nucleotide polymorphisms in the calcium channel alpha 1 subunit gene (Ca(v)1.1) and thyrotoxic periodic paralysis."
Kung A.W., Lau K.S., Fong G.C., Chan V.
J. Clin. Endocrinol. Metab. 89:1340-1345(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO TTPP1.
[9]"A calcium channel mutation causing hypokalemic periodic paralysis."
Jurkatt-Rott K., Lehmann-Horn F., Elbaz A., Heine R., Gregg R.G., Hogan K., Powers P.A., Lapie P., Vale-Santos J.E., Weissenbach J., Fontaine B.
Hum. Mol. Genet. 3:1415-1419(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HOKPP1 HIS-528.
[10]"Malignant-hyperthermia susceptibility is associated with a mutation of the alpha-1-subunit of the human dihydropyridine-sensitive L-type voltage-dependent calcium-channel receptor in skeletal muscle."
Monnier N., Procaccio V., Stieglitz P., Lunardi J.
Am. J. Hum. Genet. 60:1316-1325(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION, VARIANT MHS5 HIS-1086, VARIANTS HIS-458 AND CYS-1539.
[11]"The genotype and clinical phenotype of Korean patients with familial hypokalemic periodic paralysis."
Kim J.-B., Kim M.-H., Lee S.J., Kim D.-J., Lee B.C.
J. Korean Med. Sci. 22:946-951(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HOKPP1 HIS-528; HIS-1239 AND GLY-1239.
[12]"Hypokalaemic periodic paralysis due to the CACNA1S R1239H mutation in a large African family."
Houinato D., Laleye A., Adjien C., Adjagba M., Sternberg D., Hilbert P., Vallat J.M., Darboux R.B., Funalot B., Avode D.G.
Neuromuscul. Disord. 17:419-422(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HOKPP1 HIS-1239.
[13]"Voltage sensor charge loss accounts for most cases of hypokalemic periodic paralysis."
Matthews E., Labrum R., Sweeney M.G., Sud R., Haworth A., Chinnery P.F., Meola G., Schorge S., Kullmann D.M., Davis M.B., Hanna M.G.
Neurology 72:1544-1547(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HOKPP1 GLY-528; HIS-528; SER-900; GLY-1239 AND HIS-1239.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L33798 mRNA. Translation: AAA51902.1.
U30707 expand/collapse EMBL AC list , U30666, U30667, U30668, U30669, U30670, U30671, U30672, U30673, U30674, U30675, U30676, U30677, U30678, U30679, U30680, U30681, U30682, U30683, U30684, U30685, U30686, U30687, U30688, U30689, U30690, U30691, U30692, U30693, U30694, U30695, U30696, U30697, U30698, U30699, U30700, U30701, U30702, U30703, U30704, U30705, U30706 Genomic DNA. Translation: AAB37235.1.
AL358473, AL139159 Genomic DNA. Translation: CAI12386.1.
AL139159, AL358473 Genomic DNA. Translation: CAI23207.1.
BC133671 mRNA. Translation: AAI33672.1.
M87486 Genomic DNA. No translation available.
M87487 Genomic DNA. No translation available.
M87488 Genomic DNA. No translation available.
U09784 mRNA. Translation: AAA20531.1.
Z50091 Genomic DNA. No translation available.
Z50092 Genomic DNA. No translation available.
Z50093 Genomic DNA. No translation available.
CCDSCCDS1407.1.
PIRA55645.
I38611.
RefSeqNP_000060.2. NM_000069.2.
UniGeneHs.1294.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VAYX-ray1.94B1522-1542[»]
ProteinModelPortalQ13698.
SMRQ13698. Positions 89-333, 348-374, 434-669, 795-1064, 1114-1382, 1465-1542.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107233. 3 interactions.
IntActQ13698. 2 interactions.
MINTMINT-7899448.
STRING9606.ENSP00000355192.

Chemistry

BindingDBQ13698.
ChEMBLCHEMBL2363032.
DrugBankDB00653. Magnesium Sulfate.
DB00661. Verapamil.
GuidetoPHARMACOLOGY528.

PTM databases

PhosphoSiteQ13698.

Polymorphism databases

DMDM209572767.

Proteomic databases

PaxDbQ13698.
PRIDEQ13698.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000362061; ENSP00000355192; ENSG00000081248.
GeneID779.
KEGGhsa:779.
UCSCuc001gvv.3. human.

Organism-specific databases

CTD779.
GeneCardsGC01M201008.
GeneReviewsCACNA1S.
H-InvDBHIX0028855.
HGNCHGNC:1397. CACNA1S.
HPACAB009507.
HPA048892.
HPA056815.
MIM114208. gene.
170400. phenotype.
188580. phenotype.
601887. phenotype.
neXtProtNX_Q13698.
Orphanet681. Hypokalemic periodic paralysis.
423. Malignant hyperthermia.
79102. Thyrotoxic periodic paralysis.
PharmGKBPA85.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1226.
HOGENOMHOG000231529.
HOVERGENHBG050763.
InParanoidQ13698.
KOK04857.
OMAMGFESST.
PhylomeDBQ13698.
TreeFamTF312805.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.

Gene expression databases

ArrayExpressQ13698.
BgeeQ13698.
CleanExHS_CACNA1S.
GenevestigatorQ13698.

Family and domain databases

Gene3D1.20.120.350. 4 hits.
InterProIPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005450. VDCC_L_a1ssu.
IPR005446. VDCC_L_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PfamPF08763. Ca_chan_IQ. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSPR00167. CACHANNEL.
PR01630. LVDCCALPHA1.
PR01634. LVDCCALPHA1S.
SMARTSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ13698.
GeneWikiCav1.1.
GenomeRNAi779.
NextBio3148.
PROQ13698.
SOURCESearch...

Entry information

Entry nameCAC1S_HUMAN
AccessionPrimary (citable) accession number: Q13698
Secondary accession number(s): A4IF51 expand/collapse secondary AC list , B1ALM2, Q12896, Q13934
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: October 14, 2008
Last modified: July 9, 2014
This is version 152 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM