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Q13698

- CAC1S_HUMAN

UniProt

Q13698 - CAC1S_HUMAN

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Protein
Voltage-dependent L-type calcium channel subunit alpha-1S
Gene
CACNA1S, CACH1, CACN1, CACNL1A3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 permeability By similarity
Sitei614 – 6141Calcium ion selectivity and permeability By similarity
Sitei1014 – 10141Calcium ion selectivity and permeability By similarity
Sitei1323 – 13231Calcium ion selectivity and permeability By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi1410 – 142112 By similarity
Add
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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5151Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei52 – 7019Helical; Name=S1 of repeat I; Reviewed prediction
Add
BLAST
Topological domaini71 – 8818Extracellular Reviewed prediction
Add
BLAST
Transmembranei89 – 10820Helical; Name=S2 of repeat I; Reviewed prediction
Add
BLAST
Topological domaini109 – 12012Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei121 – 13919Helical; Name=S3 of repeat I; Reviewed prediction
Add
BLAST
Topological domaini140 – 16021Extracellular Reviewed prediction
Add
BLAST
Transmembranei161 – 17919Helical; Name=S4 of repeat I; Reviewed prediction
Add
BLAST
Topological domaini180 – 19819Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei199 – 21820Helical; Name=S5 of repeat I; Reviewed prediction
Add
BLAST
Topological domaini219 – 30991Extracellular Reviewed prediction
Add
BLAST
Transmembranei310 – 33425Helical; Name=S6 of repeat I; Reviewed prediction
Add
BLAST
Topological domaini335 – 43298Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei433 – 45119Helical; Name=S1 of repeat II; Reviewed prediction
Add
BLAST
Topological domaini452 – 46615Extracellular Reviewed prediction
Add
BLAST
Transmembranei467 – 48620Helical; Name=S2 of repeat II; Reviewed prediction
Add
BLAST
Topological domaini487 – 4948Cytoplasmic Reviewed prediction
Transmembranei495 – 51319Helical; Name=S3 of repeat II; Reviewed prediction
Add
BLAST
Topological domaini514 – 52310Extracellular Reviewed prediction
Transmembranei524 – 54219Helical; Name=S4 of repeat II; Reviewed prediction
Add
BLAST
Topological domaini543 – 56119Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei562 – 58120Helical; Name=S5 of repeat II; Reviewed prediction
Add
BLAST
Topological domaini582 – 63655Extracellular Reviewed prediction
Add
BLAST
Transmembranei637 – 66125Helical; Name=S6 of repeat II; Reviewed prediction
Add
BLAST
Topological domaini662 – 799138Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei800 – 81819Helical; Name=S1 of repeat III; Reviewed prediction
Add
BLAST
Topological domaini819 – 83416Extracellular Reviewed prediction
Add
BLAST
Transmembranei835 – 85420Helical; Name=S2 of repeat III; Reviewed prediction
Add
BLAST
Topological domaini855 – 86612Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei867 – 88519Helical; Name=S3 of repeat III; Reviewed prediction
Add
BLAST
Topological domaini886 – 8927Extracellular Reviewed prediction
Transmembranei893 – 91119Helical; Name=S4 of repeat III; Reviewed prediction
Add
BLAST
Topological domaini912 – 93019Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei931 – 95020Helical; Name=S5 of repeat III; Reviewed prediction
Add
BLAST
Topological domaini951 – 104090Extracellular Reviewed prediction
Add
BLAST
Transmembranei1041 – 106525Helical; Name=S6 of repeat III; Reviewed prediction
Add
BLAST
Topological domaini1066 – 111853Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei1119 – 113719Helical; Name=S1 of repeat IV; Reviewed prediction
Add
BLAST
Topological domaini1138 – 115215Extracellular Reviewed prediction
Add
BLAST
Transmembranei1153 – 117220Helical; Name=S2 of repeat IV; Reviewed prediction
Add
BLAST
Topological domaini1173 – 11808Cytoplasmic Reviewed prediction
Transmembranei1181 – 119919Helical; Name=S3 of repeat IV; Reviewed prediction
Add
BLAST
Topological domaini1200 – 123132Extracellular Reviewed prediction
Add
BLAST
Transmembranei1232 – 125019Helical; Name=S4 of repeat IV; Reviewed prediction
Add
BLAST
Topological domaini1251 – 126919Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei1270 – 128920Helical; Name=S5 of repeat IV; Reviewed prediction
Add
BLAST
Topological domaini1290 – 135667Extracellular Reviewed prediction
Add
BLAST
Transmembranei1357 – 138125Helical; Name=S6 of repeat IV; Reviewed prediction
Add
BLAST
Topological domaini1382 – 1873492Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.5 Publications
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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.1 Publication
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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.1 Publication

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-1S
PRO_0000053943Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi79 – 791N-linked (GlcNAc...) Reviewed prediction
Glycosylationi257 – 2571N-linked (GlcNAc...) Reviewed prediction
Modified residuei687 – 6871Phosphoserine; by PKA By similarity
Glycosylationi1141 – 11411N-linked (GlcNAc...) Reviewed prediction
Modified residuei1392 – 13921Phosphoserine; by PKA Reviewed prediction
Modified residuei1617 – 16171Phosphoserine By 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.

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ13698.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati38 – 337300I
Add
BLAST
Repeati418 – 664247II
Add
BLAST
Repeati786 – 1068283III
Add
BLAST
Repeati1105 – 1384280IV
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni357 – 37418Binding to the beta subunit By similarity
Add
BLAST
Regioni988 – 107790Dihydropyridine binding By similarity
Add
BLAST
Regioni1337 – 140367Dihydropyridine binding By similarity
Add
BLAST
Regioni1349 – 139244Phenylalkylamine binding By similarity
Add
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

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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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261R → S in AAB37235. 1 Publication
Sequence conflicti265 – 2651W → C in AAA51902. 1 Publication
Sequence conflicti265 – 2651W → C in AAB37235. 1 Publication
Sequence conflicti574 – 5741A → R in AAA51902. 1 Publication
Sequence conflicti574 – 5741A → R in AAB37235. 1 Publication
Sequence conflicti627 – 6282YG → SS in AAA51902. 1 Publication
Sequence conflicti628 – 6281G → R in AAB37235. 1 Publication
Sequence conflicti916 – 9194Missing in AAB37235. 1 Publication
Sequence conflicti918 – 9192VQ → AR in AAA51902. 1 Publication
Sequence conflicti1180 – 11801D → N in AAA51902. 1 Publication
Sequence conflicti1180 – 11801D → N in AAB37235. 1 Publication
Sequence conflicti1294 – 12952LV → FE in AAA20531. 1 Publication
Sequence conflicti1318 – 13181R → RHA in AAB37235. 1 Publication
Sequence conflicti1472 – 14721R → G in AAB37235. 1 Publication
Sequence conflicti1510 – 15101I → M in AAB37235. 1 Publication
Sequence conflicti1532 – 15321H → D in AAB37235. 1 Publication
Sequence conflicti1671 – 16711G → A in AAA51902. 1 Publication
Sequence conflicti1671 – 16711G → A in AAB37235. 1 Publication
Sequence conflicti1710 – 17101V → S in AAA51902. 1 Publication
Sequence conflicti1815 – 18151A → G in AAA51902. 1 Publication
Sequence conflicti1815 – 18151A → G in AAB37235. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 153 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

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