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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

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

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
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.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.
397755. Periodic paralysis with transient compartment-like syndrome.
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

BgeeiQ13698.
CleanExiHS_CACNA1S.
ExpressionAtlasiQ13698. baseline and differential.
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 – 153614Combined sources
Helixi1538 – 15414Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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.
GeneTreeiENSGT00760000118827.
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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        10         20         30         40         50
MEPSSPQDEG LRKKQPKKPV PEILPRPPRA LFCLTLENPL RKACISIVEW
60 70 80 90 100
KPFETIILLT IFANCVALAV YLPMPEDDNN SLNLGLEKLE YFFLIVFSIE
110 120 130 140 150
AAMKIIAYGF LFHQDAYLRS GWNVLDFTIV FLGVFTVILE QVNVIQSHTA
160 170 180 190 200
PMSSKGAGLD VKALRAFRVL RPLRLVSGVP SLQVVLNSIF KAMLPLFHIA
210 220 230 240 250
LLVLFMVIIY AIIGLELFKG KMHKTCYFIG TDIVATVENE EPSPCARTGS
260 270 280 290 300
GRRCTINGSE CRGGWPGPNH GITHFDNFGF SMLTVYQCIT MEGWTDVLYW
310 320 330 340 350
VNDAIGNEWP WIYFVTLILL GSFFILNLVL GVLSGEFTKE REKAKSRGTF
360 370 380 390 400
QKLREKQQLD EDLRGYMSWI TQGEVMDVED FREGKLSLDE GGSDTESLYE
410 420 430 440 450
IAGLNKIIQF IRHWRQWNRI FRWKCHDIVK SKVFYWLVIL IVALNTLSIA
460 470 480 490 500
SEHHNQPLWL TRLQDIANRV LLSLFTTEML MKMYGLGLRQ YFMSIFNRFD
510 520 530 540 550
CFVVCSGILE ILLVESGAMT PLGISVLRCI RLLRIFKITK YWTSLSNLVA
560 570 580 590 600
SLLNSIRSIA SLLLLLFLFI VIFALLGMQL FGGRYDFEDT EVRRSNFDNF
610 620 630 640 650
PQALISVFQV LTGEDWTSMM YNGIMAYGGP SYPGMLVCIY FIILFVCGNY
660 670 680 690 700
ILLNVFLAIA VDNLAEAESL TSAQKAKAEE KKRRKMSKGL PDKSEEEKST
710 720 730 740 750
MAKKLEQKPK GEGIPTTAKL KIDEFESNVN EVKDPYPSAD FPGDDEEDEP
760 770 780 790 800
EIPLSPRPRP LAELQLKEKA VPIPEASSFF IFSPTNKIRV LCHRIVNATW
810 820 830 840 850
FTNFILLFIL LSSAALAAED PIRADSMRNQ ILKHFDIGFT SVFTVEIVLK
860 870 880 890 900
MTTYGAFLHK GSFCRNYFNM LDLLVVAVSL ISMGLESSAI SVVKILRVLR
910 920 930 940 950
VLRPLRAINR AKGLKHVVQC MFVAISTIGN IVLVTTLLQF MFACIGVQLF
960 970 980 990 1000
KGKFFRCTDL SKMTEEECRG YYYVYKDGDP MQIELRHREW VHSDFHFDNV
1010 1020 1030 1040 1050
LSAMMSLFTV STFEGWPQLL YKAIDSNAED VGPIYNNRVE MAIFFIIYII
1060 1070 1080 1090 1100
LIAFFMMNIF VGFVIVTFQE QGETEYKNCE LDKNQRQCVQ YALKARPLRC
1110 1120 1130 1140 1150
YIPKNPYQYQ VWYIVTSSYF EYLMFALIML NTICLGMQHY NQSEQMNHIS
1160 1170 1180 1190 1200
DILNVAFTII FTLEMILKLM AFKARGYFGD PWNVFDFLIV IGSIIDVILS
1210 1220 1230 1240 1250
EIDTFLASSG GLYCLGGGCG NVDPDESARI SSAFFRLFRV MRLIKLLSRA
1260 1270 1280 1290 1300
EGVRTLLWTF IKSFQALPYV ALLIVMLFFI YAVIGMQMFG KIALVDGTQI
1310 1320 1330 1340 1350
NRNNNFQTFP QAVLLLFRCA TGEAWQEILL ACSYGKLCDP ESDYAPGEEY
1360 1370 1380 1390 1400
TCGTNFAYYY FISFYMLCAF LVINLFVAVI MDNFDYLTRD WSILGPHHLD
1410 1420 1430 1440 1450
EFKAIWAEYD PEAKGRIKHL DVVTLLRRIQ PPLGFGKFCP HRVACKRLVG
1460 1470 1480 1490 1500
MNMPLNSDGT VTFNATLFAL VRTALKIKTE GNFEQANEEL RAIIKKIWKR
1510 1520 1530 1540 1550
TSMKLLDQVI PPIGDDEVTV GKFYATFLIQ EHFRKFMKRQ EEYYGYRPKK
1560 1570 1580 1590 1600
DIVQIQAGLR TIEEEAAPEI CRTVSGDLAA EEELERAMVE AAMEEGIFRR
1610 1620 1630 1640 1650
TGGLFGQVDN FLERTNSLPP VMANQRPLQF AEIEMEEMES PVFLEDFPQD
1660 1670 1680 1690 1700
PRTNPLARAN TNNANANVAY GNSNHSNSHV FSSVHYEREF PEETETPATR
1710 1720 1730 1740 1750
GRALGQPCRV LGPHSKPCVE MLKGLLTQRA MPRGQAPPAP CQCPRVESSM
1760 1770 1780 1790 1800
PEDRKSSTPG SLHEETPHSR STRENTSRCS APATALLIQK ALVRGGLGTL
1810 1820 1830 1840 1850
AADANFIMAT GQALADACQM EPEEVEIMAT ELLKGREAPE GMASSLGCLN
1860 1870
LGSSLGSLDQ HQGSQETLIP PRL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 CHEMBL2095229.
DrugBanki DB00381. Amlodipine.
DB00568. Cinnarizine.
DB04920. Clevidipine.
DB04855. Dronedarone.
DB01023. Felodipine.
DB00270. Isradipine.
DB00653. Magnesium Sulfate.
DB01115. Nifedipine.
DB06712. Nilvadipine.
DB00393. Nimodipine.
DB00401. Nisoldipine.
DB01054. Nitrendipine.
DB00421. Spironolactone.
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.
397755. Periodic paralysis with transient compartment-like syndrome.
79102. Thyrotoxic periodic paralysis.
PharmGKBi PA85.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1226.
GeneTreei ENSGT00760000118827.
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

Bgeei Q13698.
CleanExi HS_CACNA1S.
ExpressionAtlasi Q13698. baseline and differential.
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: November 26, 2014
This is version 156 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