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Q13698

- CAC1S_HUMAN

UniProt

Q13698 - CAC1S_HUMAN

Protein

Voltage-dependent L-type calcium channel subunit alpha-1S

Gene

CACNA1S

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 4 (14 Oct 2008)
      Previous versions | rss
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    Functioni

    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-1S gives 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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei292 – 2921Calcium ion selectivity and permeabilityBy similarity
    Sitei614 – 6141Calcium ion selectivity and permeabilityBy similarity
    Sitei1014 – 10141Calcium ion selectivity and permeabilityBy similarity
    Sitei1323 – 13231Calcium ion selectivity and permeabilityBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi1410 – 142112By similarityAdd
    BLAST

    GO - Molecular functioni

    1. high voltage-gated calcium channel activity Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. voltage-gated calcium channel activity Source: UniProtKB

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. calcium ion import Source: RefGenome
    3. calcium ion transport Source: UniProtKB
    4. endoplasmic reticulum organization Source: Ensembl
    5. extraocular skeletal muscle development Source: Ensembl
    6. membrane depolarization during action potential Source: RefGenome
    7. muscle contraction Source: UniProtKB
    8. myoblast fusion Source: Ensembl
    9. neuromuscular junction development Source: Ensembl
    10. skeletal muscle adaptation Source: Ensembl
    11. skeletal muscle fiber development Source: Ensembl
    12. skeletal system development Source: Ensembl
    13. striated muscle contraction Source: Ensembl

    Keywords - Molecular functioni

    Calcium channel, Ion channel, Voltage-gated channel

    Keywords - Biological processi

    Calcium transport, Ion transport, Transport

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_18312. NCAM1 interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:CACNA1S
    Synonyms:CACH1, CACN1, CACNL1A3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1397. CACNA1S.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. I band Source: UniProtKB
    3. plasma membrane Source: UniProtKB
    4. sarcoplasmic reticulum Source: Ensembl
    5. T-tubule Source: UniProtKB
    6. voltage-gated calcium channel complex Source: UniProtKB

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    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.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti528 – 5281R → G in HOKPP1. 1 Publication
    VAR_054953
    Natural varianti528 – 5281R → H in HOKPP1. 3 Publications
    VAR_001499
    Natural varianti900 – 9001R → S in HOKPP1. 1 Publication
    VAR_054954
    Natural varianti1239 – 12391R → G in HOKPP1. 3 Publications
    Corresponds to variant rs28930069 [ dbSNP | Ensembl ].
    VAR_001501
    Natural varianti1239 – 12391R → H in HOKPP1. 4 Publications
    Corresponds to variant rs28930068 [ dbSNP | Ensembl ].
    VAR_001502
    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.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1086 – 10861R → H in MHS5. 1 Publication
    Corresponds to variant rs1800559 [ dbSNP | Ensembl ].
    VAR_001500
    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.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi170400. phenotype.
    188580. phenotype.
    601887. phenotype.
    Orphaneti681. Hypokalemic periodic paralysis.
    423. Malignant hyperthermia.
    79102. Thyrotoxic periodic paralysis.
    PharmGKBiPA85.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 18731873Voltage-dependent L-type calcium channel subunit alpha-1SPRO_0000053943Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi79 – 791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi257 – 2571N-linked (GlcNAc...)Sequence Analysis
    Modified residuei687 – 6871Phosphoserine; by PKABy similarity
    Glycosylationi1141 – 11411N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1392 – 13921Phosphoserine; by PKASequence Analysis
    Modified residuei1617 – 16171PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylation by PKA activates the calcium channel.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ13698.
    PRIDEiQ13698.

    PTM databases

    PhosphoSiteiQ13698.

    Expressioni

    Tissue specificityi

    Skeletal muscle specific.

    Gene expression databases

    ArrayExpressiQ13698.
    BgeeiQ13698.
    CleanExiHS_CACNA1S.
    GenevestigatoriQ13698.

    Organism-specific databases

    HPAiCAB009507.
    HPA048892.
    HPA056815.

    Interactioni

    Subunit structurei

    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.By similarity

    Protein-protein interaction databases

    BioGridi107233. 3 interactions.
    IntActiQ13698. 2 interactions.
    MINTiMINT-7899448.
    STRINGi9606.ENSP00000355192.

    Structurei

    Secondary structure

    1
    1873
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1523 – 153614
    Helixi1538 – 15414

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VAYX-ray1.94B1522-1542[»]
    ProteinModelPortaliQ13698.
    SMRiQ13698. Positions 89-333, 348-374, 434-669, 795-1064, 1114-1382, 1465-1542.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13698.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 5151CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini71 – 8818ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini109 – 12012CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini140 – 16021ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini180 – 19819CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini219 – 30991ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini335 – 43298CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini452 – 46615ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini487 – 4948CytoplasmicSequence Analysis
    Topological domaini514 – 52310ExtracellularSequence Analysis
    Topological domaini543 – 56119CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini582 – 63655ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini662 – 799138CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini819 – 83416ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini855 – 86612CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini886 – 8927ExtracellularSequence Analysis
    Topological domaini912 – 93019CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini951 – 104090ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1066 – 111853CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1138 – 115215ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1173 – 11808CytoplasmicSequence Analysis
    Topological domaini1200 – 123132ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1251 – 126919CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1290 – 135667ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1382 – 1873492CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei52 – 7019Helical; Name=S1 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei89 – 10820Helical; Name=S2 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei121 – 13919Helical; Name=S3 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei161 – 17919Helical; Name=S4 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei199 – 21820Helical; Name=S5 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei310 – 33425Helical; Name=S6 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei433 – 45119Helical; Name=S1 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei467 – 48620Helical; Name=S2 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei495 – 51319Helical; Name=S3 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei524 – 54219Helical; Name=S4 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei562 – 58120Helical; Name=S5 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei637 – 66125Helical; Name=S6 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei800 – 81819Helical; Name=S1 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei835 – 85420Helical; Name=S2 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei867 – 88519Helical; Name=S3 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei893 – 91119Helical; Name=S4 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei931 – 95020Helical; Name=S5 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1041 – 106525Helical; Name=S6 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1119 – 113719Helical; Name=S1 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1153 – 117220Helical; Name=S2 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1181 – 119919Helical; Name=S3 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1232 – 125019Helical; Name=S4 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1270 – 128920Helical; Name=S5 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1357 – 138125Helical; Name=S6 of repeat IVSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati38 – 337300IAdd
    BLAST
    Repeati418 – 664247IIAdd
    BLAST
    Repeati786 – 1068283IIIAdd
    BLAST
    Repeati1105 – 1384280IVAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni357 – 37418Binding to the beta subunitBy similarityAdd
    BLAST
    Regioni988 – 107790Dihydropyridine bindingBy similarityAdd
    BLAST
    Regioni1337 – 140367Dihydropyridine bindingBy similarityAdd
    BLAST
    Regioni1349 – 139244Phenylalkylamine bindingBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi562 – 5687Poly-Leu

    Domaini

    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.

    Sequence similaritiesi

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1226.
    HOGENOMiHOG000231529.
    HOVERGENiHBG050763.
    InParanoidiQ13698.
    KOiK04857.
    OMAiMGFESST.
    PhylomeDBiQ13698.
    TreeFamiTF312805.

    Family and domain databases

    Gene3Di1.20.120.350. 4 hits.
    InterProiIPR027359. Channel_four-helix_dom.
    IPR005821. Ion_trans_dom.
    IPR014873. VDCC_a1su_IQ.
    IPR005450. VDCC_L_a1ssu.
    IPR005446. VDCC_L_a1su.
    IPR002077. VDCCAlpha1.
    [Graphical view]
    PfamiPF08763. Ca_chan_IQ. 1 hit.
    PF00520. Ion_trans. 4 hits.
    [Graphical view]
    PRINTSiPR00167. CACHANNEL.
    PR01630. LVDCCALPHA1.
    PR01634. LVDCCALPHA1S.
    SMARTiSM01062. Ca_chan_IQ. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q13698-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEPSSPQDEG LRKKQPKKPV PEILPRPPRA LFCLTLENPL RKACISIVEW     50
    KPFETIILLT IFANCVALAV YLPMPEDDNN SLNLGLEKLE YFFLIVFSIE 100
    AAMKIIAYGF LFHQDAYLRS GWNVLDFTIV FLGVFTVILE QVNVIQSHTA 150
    PMSSKGAGLD VKALRAFRVL RPLRLVSGVP SLQVVLNSIF KAMLPLFHIA 200
    LLVLFMVIIY AIIGLELFKG KMHKTCYFIG TDIVATVENE EPSPCARTGS 250
    GRRCTINGSE CRGGWPGPNH GITHFDNFGF SMLTVYQCIT MEGWTDVLYW 300
    VNDAIGNEWP WIYFVTLILL GSFFILNLVL GVLSGEFTKE REKAKSRGTF 350
    QKLREKQQLD EDLRGYMSWI TQGEVMDVED FREGKLSLDE GGSDTESLYE 400
    IAGLNKIIQF IRHWRQWNRI FRWKCHDIVK SKVFYWLVIL IVALNTLSIA 450
    SEHHNQPLWL TRLQDIANRV LLSLFTTEML MKMYGLGLRQ YFMSIFNRFD 500
    CFVVCSGILE ILLVESGAMT PLGISVLRCI RLLRIFKITK YWTSLSNLVA 550
    SLLNSIRSIA SLLLLLFLFI VIFALLGMQL FGGRYDFEDT EVRRSNFDNF 600
    PQALISVFQV LTGEDWTSMM YNGIMAYGGP SYPGMLVCIY FIILFVCGNY 650
    ILLNVFLAIA VDNLAEAESL TSAQKAKAEE KKRRKMSKGL PDKSEEEKST 700
    MAKKLEQKPK GEGIPTTAKL KIDEFESNVN EVKDPYPSAD FPGDDEEDEP 750
    EIPLSPRPRP LAELQLKEKA VPIPEASSFF IFSPTNKIRV LCHRIVNATW 800
    FTNFILLFIL LSSAALAAED PIRADSMRNQ ILKHFDIGFT SVFTVEIVLK 850
    MTTYGAFLHK GSFCRNYFNM LDLLVVAVSL ISMGLESSAI SVVKILRVLR 900
    VLRPLRAINR AKGLKHVVQC MFVAISTIGN IVLVTTLLQF MFACIGVQLF 950
    KGKFFRCTDL SKMTEEECRG YYYVYKDGDP MQIELRHREW VHSDFHFDNV 1000
    LSAMMSLFTV STFEGWPQLL YKAIDSNAED VGPIYNNRVE MAIFFIIYII 1050
    LIAFFMMNIF VGFVIVTFQE QGETEYKNCE LDKNQRQCVQ YALKARPLRC 1100
    YIPKNPYQYQ VWYIVTSSYF EYLMFALIML NTICLGMQHY NQSEQMNHIS 1150
    DILNVAFTII FTLEMILKLM AFKARGYFGD PWNVFDFLIV IGSIIDVILS 1200
    EIDTFLASSG GLYCLGGGCG NVDPDESARI SSAFFRLFRV MRLIKLLSRA 1250
    EGVRTLLWTF IKSFQALPYV ALLIVMLFFI YAVIGMQMFG KIALVDGTQI 1300
    NRNNNFQTFP QAVLLLFRCA TGEAWQEILL ACSYGKLCDP ESDYAPGEEY 1350
    TCGTNFAYYY FISFYMLCAF LVINLFVAVI MDNFDYLTRD WSILGPHHLD 1400
    EFKAIWAEYD PEAKGRIKHL DVVTLLRRIQ PPLGFGKFCP HRVACKRLVG 1450
    MNMPLNSDGT VTFNATLFAL VRTALKIKTE GNFEQANEEL RAIIKKIWKR 1500
    TSMKLLDQVI PPIGDDEVTV GKFYATFLIQ EHFRKFMKRQ EEYYGYRPKK 1550
    DIVQIQAGLR TIEEEAAPEI CRTVSGDLAA EEELERAMVE AAMEEGIFRR 1600
    TGGLFGQVDN FLERTNSLPP VMANQRPLQF AEIEMEEMES PVFLEDFPQD 1650
    PRTNPLARAN TNNANANVAY GNSNHSNSHV FSSVHYEREF PEETETPATR 1700
    GRALGQPCRV LGPHSKPCVE MLKGLLTQRA MPRGQAPPAP CQCPRVESSM 1750
    PEDRKSSTPG SLHEETPHSR STRENTSRCS APATALLIQK ALVRGGLGTL 1800
    AADANFIMAT GQALADACQM EPEEVEIMAT ELLKGREAPE GMASSLGCLN 1850
    LGSSLGSLDQ HQGSQETLIP PRL 1873
    Length:1,873
    Mass (Da):212,350
    Last modified:October 14, 2008 - v4
    Checksum:i7B7446727E578913
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 261R → S in AAB37235. (PubMed:8838325)Curated
    Sequence conflicti265 – 2651W → C in AAA51902. (PubMed:7713519)Curated
    Sequence conflicti265 – 2651W → C in AAB37235. (PubMed:8838325)Curated
    Sequence conflicti574 – 5741A → R in AAA51902. (PubMed:7713519)Curated
    Sequence conflicti574 – 5741A → R in AAB37235. (PubMed:8838325)Curated
    Sequence conflicti627 – 6282YG → SS in AAA51902. (PubMed:7713519)Curated
    Sequence conflicti628 – 6281G → R in AAB37235. (PubMed:8838325)Curated
    Sequence conflicti916 – 9194Missing in AAB37235. (PubMed:8838325)Curated
    Sequence conflicti918 – 9192VQ → AR in AAA51902. (PubMed:7713519)Curated
    Sequence conflicti1180 – 11801D → N in AAA51902. (PubMed:7713519)Curated
    Sequence conflicti1180 – 11801D → N in AAB37235. (PubMed:8838325)Curated
    Sequence conflicti1294 – 12952LV → FE in AAA20531. (PubMed:8004673)Curated
    Sequence conflicti1318 – 13181R → RHA in AAB37235. (PubMed:8838325)Curated
    Sequence conflicti1472 – 14721R → G in AAB37235. (PubMed:8838325)Curated
    Sequence conflicti1510 – 15101I → M in AAB37235. (PubMed:8838325)Curated
    Sequence conflicti1532 – 15321H → D in AAB37235. (PubMed:8838325)Curated
    Sequence conflicti1671 – 16711G → A in AAA51902. (PubMed:7713519)Curated
    Sequence conflicti1671 – 16711G → A in AAB37235. (PubMed:8838325)Curated
    Sequence conflicti1710 – 17101V → S in AAA51902. (PubMed:7713519)Curated
    Sequence conflicti1815 – 18151A → G in AAA51902. (PubMed:7713519)Curated
    Sequence conflicti1815 – 18151A → G in AAB37235. (PubMed:8838325)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti69 – 691A → G.
    Corresponds to variant rs12406479 [ dbSNP | Ensembl ].
    VAR_046970
    Natural varianti458 – 4581L → H.2 Publications
    Corresponds to variant rs12742169 [ dbSNP | Ensembl ].
    VAR_001498
    Natural varianti528 – 5281R → G in HOKPP1. 1 Publication
    VAR_054953
    Natural varianti528 – 5281R → H in HOKPP1. 3 Publications
    VAR_001499
    Natural varianti900 – 9001R → S in HOKPP1. 1 Publication
    VAR_054954
    Natural varianti1086 – 10861R → H in MHS5. 1 Publication
    Corresponds to variant rs1800559 [ dbSNP | Ensembl ].
    VAR_001500
    Natural varianti1239 – 12391R → G in HOKPP1. 3 Publications
    Corresponds to variant rs28930069 [ dbSNP | Ensembl ].
    VAR_001501
    Natural varianti1239 – 12391R → H in HOKPP1. 4 Publications
    Corresponds to variant rs28930068 [ dbSNP | Ensembl ].
    VAR_001502
    Natural varianti1539 – 15391R → C.1 Publication
    Corresponds to variant rs3850625 [ dbSNP | Ensembl ].
    VAR_001503
    Natural varianti1658 – 16581R → H.
    Corresponds to variant rs13374149 [ dbSNP | Ensembl ].
    VAR_046971
    Natural varianti1800 – 18001L → S.1 Publication
    Corresponds to variant rs12139527 [ dbSNP | Ensembl ].
    VAR_046972
    Natural varianti1840 – 18401E → D.2 Publications
    Corresponds to variant rs1042379 [ dbSNP | Ensembl ].
    VAR_046973

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L33798 mRNA. Translation: AAA51902.1.
    U30707
    , 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.
    CCDSiCCDS1407.1.
    PIRiA55645.
    I38611.
    RefSeqiNP_000060.2. NM_000069.2.
    UniGeneiHs.1294.

    Genome annotation databases

    EnsembliENST00000362061; ENSP00000355192; ENSG00000081248.
    GeneIDi779.
    KEGGihsa:779.
    UCSCiuc001gvv.3. human.

    Polymorphism databases

    DMDMi209572767.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L33798 mRNA. Translation: AAA51902.1 .
    U30707
    , 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.
    CCDSi CCDS1407.1.
    PIRi A55645.
    I38611.
    RefSeqi NP_000060.2. NM_000069.2.
    UniGenei Hs.1294.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2VAY X-ray 1.94 B 1522-1542 [» ]
    ProteinModelPortali Q13698.
    SMRi Q13698. Positions 89-333, 348-374, 434-669, 795-1064, 1114-1382, 1465-1542.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107233. 3 interactions.
    IntActi Q13698. 2 interactions.
    MINTi MINT-7899448.
    STRINGi 9606.ENSP00000355192.

    Chemistry

    BindingDBi Q13698.
    ChEMBLi CHEMBL2363032.
    DrugBanki DB00653. Magnesium Sulfate.
    DB00661. Verapamil.
    GuidetoPHARMACOLOGYi 528.

    PTM databases

    PhosphoSitei Q13698.

    Polymorphism databases

    DMDMi 209572767.

    Proteomic databases

    PaxDbi Q13698.
    PRIDEi Q13698.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000362061 ; ENSP00000355192 ; ENSG00000081248 .
    GeneIDi 779.
    KEGGi hsa:779.
    UCSCi uc001gvv.3. human.

    Organism-specific databases

    CTDi 779.
    GeneCardsi GC01M201008.
    GeneReviewsi CACNA1S.
    H-InvDB HIX0028855.
    HGNCi HGNC:1397. CACNA1S.
    HPAi CAB009507.
    HPA048892.
    HPA056815.
    MIMi 114208. gene.
    170400. phenotype.
    188580. phenotype.
    601887. phenotype.
    neXtProti NX_Q13698.
    Orphaneti 681. Hypokalemic periodic paralysis.
    423. Malignant hyperthermia.
    79102. Thyrotoxic periodic paralysis.
    PharmGKBi PA85.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1226.
    HOGENOMi HOG000231529.
    HOVERGENi HBG050763.
    InParanoidi Q13698.
    KOi K04857.
    OMAi MGFESST.
    PhylomeDBi Q13698.
    TreeFami TF312805.

    Enzyme and pathway databases

    Reactomei REACT_18312. NCAM1 interactions.

    Miscellaneous databases

    EvolutionaryTracei Q13698.
    GeneWikii Cav1.1.
    GenomeRNAii 779.
    NextBioi 3148.
    PROi Q13698.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13698.
    Bgeei Q13698.
    CleanExi HS_CACNA1S.
    Genevestigatori Q13698.

    Family and domain databases

    Gene3Di 1.20.120.350. 4 hits.
    InterProi IPR027359. Channel_four-helix_dom.
    IPR005821. Ion_trans_dom.
    IPR014873. VDCC_a1su_IQ.
    IPR005450. VDCC_L_a1ssu.
    IPR005446. VDCC_L_a1su.
    IPR002077. VDCCAlpha1.
    [Graphical view ]
    Pfami PF08763. Ca_chan_IQ. 1 hit.
    PF00520. Ion_trans. 4 hits.
    [Graphical view ]
    PRINTSi PR00167. CACHANNEL.
    PR01630. LVDCCALPHA1.
    PR01634. LVDCCALPHA1S.
    SMARTi SM01062. Ca_chan_IQ. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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.

    Entry informationi

    Entry nameiCAC1S_HUMAN
    AccessioniPrimary (citable) accession number: Q13698
    Secondary accession number(s): A4IF51
    , B1ALM2, Q12896, Q13934
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: October 14, 2008
    Last modified: October 1, 2014
    This is version 154 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3