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Protein

Voltage-dependent P/Q-type calcium channel subunit alpha-1A

Gene

CACNA1A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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-1A gives rise to P and/or Q-type calcium currents. P/Q-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by the funnel toxin (Ftx) and by the omega-agatoxin-IVA (omega-Aga-IVA). They are however insensitive to dihydropyridines (DHP), and omega-conotoxin-GVIA (omega-CTx-GVIA).

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei318Calcium ion selectivity and permeabilityBy similarity1
Sitei668Calcium ion selectivity and permeabilityBy similarity1
Sitei1460Calcium ion selectivity and permeabilityBy similarity1
Sitei1649Binds to omega-Aga-IVABy similarity1
Sitei1756Calcium ion selectivity and permeabilityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi1840 – 1851By similarityAdd BLAST12

GO - Molecular functioni

  • calcium channel activity Source: Reactome
  • high voltage-gated calcium channel activity Source: GO_Central
  • metal ion binding Source: UniProtKB-KW
  • syntaxin binding Source: UniProtKB
  • voltage-gated calcium channel activity Source: UniProtKB

GO - Biological processi

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

BioCyciZFISH:ENSG00000141837-MONOMER.
ReactomeiR-HSA-112308. Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels.
R-HSA-422356. Regulation of insulin secretion.

Protein family/group databases

TCDBi1.A.1.11.27. the voltage-gated ion channel (vic) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Voltage-dependent P/Q-type calcium channel subunit alpha-1A
Alternative name(s):
Brain calcium channel I
Short name:
BI
Calcium channel, L type, alpha-1 polypeptide isoform 4
Voltage-gated calcium channel subunit alpha Cav2.1
Gene namesi
Name:CACNA1A
Synonyms:CACH4, CACN3, CACNL1A4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:1388. CACNA1A.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 98CytoplasmicSequence analysisAdd BLAST98
Transmembranei99 – 117Helical; Name=S1 of repeat ISequence analysisAdd BLAST19
Topological domaini118 – 135ExtracellularSequence analysisAdd BLAST18
Transmembranei136 – 155Helical; Name=S2 of repeat ISequence analysisAdd BLAST20
Topological domaini156 – 167CytoplasmicSequence analysisAdd BLAST12
Transmembranei168 – 185Helical; Name=S3 of repeat ISequence analysisAdd BLAST18
Topological domaini186 – 190ExtracellularSequence analysis5
Transmembranei191 – 209Helical; Name=S4 of repeat ISequence analysisAdd BLAST19
Topological domaini210 – 228CytoplasmicSequence analysisAdd BLAST19
Transmembranei229 – 248Helical; Name=S5 of repeat ISequence analysisAdd BLAST20
Topological domaini249 – 335ExtracellularSequence analysisAdd BLAST87
Transmembranei336 – 360Helical; Name=S6 of repeat ISequence analysisAdd BLAST25
Topological domaini361 – 487CytoplasmicSequence analysisAdd BLAST127
Transmembranei488 – 506Helical; Name=S1 of repeat IISequence analysisAdd BLAST19
Topological domaini507 – 521ExtracellularSequence analysisAdd BLAST15
Transmembranei522 – 541Helical; Name=S2 of repeat IISequence analysisAdd BLAST20
Topological domaini542 – 549CytoplasmicSequence analysis8
Transmembranei550 – 568Helical; Name=S3 of repeat IISequence analysisAdd BLAST19
Topological domaini569 – 578ExtracellularSequence analysis10
Transmembranei579 – 597Helical; Name=S4 of repeat IISequence analysisAdd BLAST19
Topological domaini598 – 616CytoplasmicSequence analysisAdd BLAST19
Transmembranei617 – 636Helical; Name=S5 of repeat IISequence analysisAdd BLAST20
Topological domaini637 – 689ExtracellularSequence analysisAdd BLAST53
Transmembranei690 – 714Helical; Name=S6 of repeat IISequence analysisAdd BLAST25
Topological domaini715 – 1242CytoplasmicSequence analysisAdd BLAST528
Transmembranei1243 – 1261Helical; Name=S1 of repeat IIISequence analysisAdd BLAST19
Topological domaini1262 – 1277ExtracellularSequence analysisAdd BLAST16
Transmembranei1278 – 1297Helical; Name=S2 of repeat IIISequence analysisAdd BLAST20
Topological domaini1298 – 1309CytoplasmicSequence analysisAdd BLAST12
Transmembranei1310 – 1328Helical; Name=S3 of repeat IIISequence analysisAdd BLAST19
Topological domaini1329 – 1339ExtracellularSequence analysisAdd BLAST11
Transmembranei1340 – 1358Helical; Name=S4 of repeat IIISequence analysisAdd BLAST19
Topological domaini1359 – 1377CytoplasmicSequence analysisAdd BLAST19
Transmembranei1378 – 1397Helical; Name=S5 of repeat IIISequence analysisAdd BLAST20
Topological domaini1398 – 1484ExtracellularSequence analysisAdd BLAST87
Transmembranei1485 – 1509Helical; Name=S6 of repeat IIISequence analysisAdd BLAST25
Topological domaini1510 – 1564CytoplasmicSequence analysisAdd BLAST55
Transmembranei1565 – 1593Helical; Name=S1 of repeat IVSequence analysisAdd BLAST29
Topological domaini1594 – 1598ExtracellularSequence analysis5
Transmembranei1599 – 1618Helical; Name=S2 of repeat IVSequence analysisAdd BLAST20
Topological domaini1619 – 1626CytoplasmicSequence analysis8
Transmembranei1627 – 1645Helical; Name=S3 of repeat IVSequence analysisAdd BLAST19
Topological domaini1646 – 1652ExtracellularSequence analysis7
Transmembranei1653 – 1671Helical; Name=S4 of repeat IVSequence analysisAdd BLAST19
Topological domaini1672 – 1690CytoplasmicSequence analysisAdd BLAST19
Transmembranei1691 – 1710Helical; Name=S5 of repeat IVSequence analysisAdd BLAST20
Topological domaini1711 – 1782ExtracellularSequence analysisAdd BLAST72
Transmembranei1783 – 1807Helical; Name=S6 of repeat IVSequence analysisAdd BLAST25
Topological domaini1808 – 2505CytoplasmicSequence analysisAdd BLAST698

GO - Cellular componenti

  • cell projection Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • dendrite Source: Ensembl
  • integral component of membrane Source: UniProtKB
  • neuronal cell body Source: Ensembl
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • presynapse Source: GOC
  • voltage-gated calcium channel complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Spinocerebellar ataxia 6 (SCA6)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionSpinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA6 is an autosomal dominant cerebellar ataxia (ADCA), mainly caused by expansion of a CAG repeat in the coding region of CACNA1A. There seems to be a correlation between the repeat number and earlier onset of the disorder.
See also OMIM:183086
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_043825293G → R in EA2 and SCA6. 2 PublicationsCorresponds to variant rs121908215dbSNPEnsembl.1
Natural variantiVAR_063685405A → T in SCA6. 1 PublicationCorresponds to variant rs121908245dbSNPEnsembl.1
Natural variantiVAR_0636911664R → Q in SCA6. 1 PublicationCorresponds to variant rs121908247dbSNPEnsembl.1
Migraine, familial hemiplegic, 1 (FHM1)6 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA subtype of migraine with aura associated with ictal hemiparesis and, in some families, cerebellar ataxia and atrophy. Migraine is a disabling symptom complex of periodic headaches, usually temporal and unilateral. Headaches are often accompanied by irritability, nausea, vomiting and photophobia, preceded by constriction of the cranial arteries. Migraine with aura is characterized by recurrent attacks of reversible neurological symptoms (aura) that precede or accompany the headache. Aura may include a combination of sensory disturbances, such as blurred vision, hallucinations, vertigo, numbness and difficulty in concentrating and speaking.
See also OMIM:141500
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001491192R → Q in FHM1. 1 PublicationCorresponds to variant rs121908211dbSNPEnsembl.1
Natural variantiVAR_043820195R → K in FHM1. 1 PublicationCorresponds to variant rs121908222dbSNPEnsembl.1
Natural variantiVAR_043821218S → L in FHM1. 1 PublicationCorresponds to variant rs121908225dbSNPEnsembl.1
Natural variantiVAR_043826583R → Q in FHM1. 1 PublicationCorresponds to variant rs121908217dbSNPEnsembl.1
Natural variantiVAR_001492666T → M in FHM1 and EA2. 3 PublicationsCorresponds to variant rs121908212dbSNPEnsembl.1
Natural variantiVAR_001493714V → A in FHM1. 1 PublicationCorresponds to variant rs121908213dbSNPEnsembl.1
Natural variantiVAR_043827715D → E in FHM1. 1 PublicationCorresponds to variant rs121908218dbSNPEnsembl.1
Natural variantiVAR_0438291335K → E in FHM1. 1 PublicationCorresponds to variant rs121908223dbSNPEnsembl.1
Natural variantiVAR_0438301346R → Q in FHM1; with progressive cerebellar ataxia. 2 PublicationsCorresponds to variant rs121908230dbSNPEnsembl.1
Natural variantiVAR_0438311384Y → C in FHM1. 1 PublicationCorresponds to variant rs121908219dbSNPEnsembl.1
Natural variantiVAR_0438331456V → L in FHM1. 1 PublicationCorresponds to variant rs121908237dbSNPEnsembl.1
Natural variantiVAR_0438381667R → W in FHM1. 1 PublicationCorresponds to variant rs121908220dbSNPEnsembl.1
Natural variantiVAR_0438391683W → R in FHM1. 1 PublicationCorresponds to variant rs121908221dbSNPEnsembl.1
Natural variantiVAR_0637061695V → I in FHM1. 1 PublicationCorresponds to variant rs121908224dbSNPEnsembl.1
Natural variantiVAR_0014941810I → L in FHM1. 1 PublicationCorresponds to variant rs121908214dbSNPEnsembl.1
Episodic ataxia 2 (EA2)13 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disorder characterized by acetozolamide-responsive attacks of ataxia, migraine-like symptoms, interictal nystagmus, and cerebellar atrophy.
See also OMIM:108500
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_063683248Y → C in EA2. 1 PublicationCorresponds to variant rs121908238dbSNPEnsembl.1
Natural variantiVAR_043822253H → Y in EA2. 1 PublicationCorresponds to variant rs121908228dbSNPEnsembl.1
Natural variantiVAR_043823256C → R in EA2. 1 PublicationCorresponds to variant rs121908231dbSNPEnsembl.1
Natural variantiVAR_043824287C → Y in EA2. 1 PublicationCorresponds to variant rs121908236dbSNPEnsembl.1
Natural variantiVAR_043825293G → R in EA2 and SCA6. 2 PublicationsCorresponds to variant rs121908215dbSNPEnsembl.1
Natural variantiVAR_067342388E → K in EA2. 1 Publication1
Natural variantiVAR_063684389L → F in EA2. 1 PublicationCorresponds to variant rs121908239dbSNPEnsembl.1
Natural variantiVAR_063687501T → M in EA2. 1 PublicationCorresponds to variant rs121908240dbSNPEnsembl.1
Natural variantiVAR_063688638G → D in EA2; reduces P/Q current densities. 1 PublicationCorresponds to variant rs121908246dbSNPEnsembl.1
Natural variantiVAR_001492666T → M in FHM1 and EA2. 3 PublicationsCorresponds to variant rs121908212dbSNPEnsembl.1
Natural variantiVAR_063689798M → T in EA2. 1 PublicationCorresponds to variant rs121908241dbSNPEnsembl.1
Natural variantiVAR_063690897P → R in EA2. 1 PublicationCorresponds to variant rs121908242dbSNPEnsembl.1
Natural variantiVAR_0438321403F → C in EA2; loss of function. 1 PublicationCorresponds to variant rs121908227dbSNPEnsembl.1
Natural variantiVAR_0438341482G → R in EA2. 1 PublicationCorresponds to variant rs121908232dbSNPEnsembl.1
Natural variantiVAR_0438351490F → S in EA2. 1 PublicationCorresponds to variant rs121908233dbSNPEnsembl.1
Natural variantiVAR_0438361493V → I in EA2. 1 PublicationCorresponds to variant rs121908234dbSNPEnsembl.1
Natural variantiVAR_0438371661R → H in EA2. 1 PublicationCorresponds to variant rs121908216dbSNPEnsembl.1
Natural variantiVAR_0636921679R → C in EA2. 1 PublicationCorresponds to variant rs121908243dbSNPEnsembl.1
Natural variantiVAR_0438401736H → L in EA2. 1 PublicationCorresponds to variant rs121908229dbSNPEnsembl.1
Natural variantiVAR_0438411756E → K in EA2. 1 PublicationCorresponds to variant rs121908226dbSNPEnsembl.1
Natural variantiVAR_0636931869C → R in EA2. 1 PublicationCorresponds to variant rs121908244dbSNPEnsembl.1
Natural variantiVAR_0438422135R → C in EA2. 1 PublicationCorresponds to variant rs121908235dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Neurodegeneration, Spinocerebellar ataxia

Organism-specific databases

DisGeNETi773.
MalaCardsiCACNA1A.
MIMi108500. phenotype.
141500. phenotype.
183086. phenotype.
OpenTargetsiENSG00000141837.
Orphaneti2131. Alternating hemiplegia of childhood.
71518. Benign paroxysmal torticollis of infancy.
569. Familial or sporadic hemiplegic migraine.
97. Familial paroxysmal ataxia.
98758. Spinocerebellar ataxia type 6.
PharmGKBiPA26007.

Chemistry databases

ChEMBLiCHEMBL4266.
DrugBankiDB01244. Bepridil.
DB00836. Loperamide.
DB00230. Pregabalin.
DB00421. Spironolactone.
DB00661. Verapamil.

Polymorphism and mutation databases

BioMutaiCACNA1A.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000539161 – 2505Voltage-dependent P/Q-type calcium channel subunit alpha-1AAdd BLAST2505

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi283N-linked (GlcNAc...)Sequence analysis1
Modified residuei409PhosphothreonineBy similarity1
Modified residuei448PhosphoserineBy similarity1
Modified residuei451PhosphoserineBy similarity1
Modified residuei750PhosphoserineBy similarity1
Modified residuei753PhosphoserineBy similarity1
Modified residuei790PhosphoserineBy similarity1
Modified residuei1085PhosphoserineBy similarity1
Modified residuei1094PhosphoserineBy similarity1
Modified residuei1822Phosphoserine; by PKASequence analysis1
Modified residuei1984PhosphothreonineBy similarity1
Modified residuei2047PhosphoserineBy similarity1
Modified residuei2065PhosphoserineBy similarity1
Modified residuei2077PhosphoserineBy similarity1
Modified residuei2079PhosphoserineBy similarity1
Modified residuei2120PhosphoserineBy similarity1
Modified residuei2140PhosphoserineBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiO00555.
PaxDbiO00555.
PeptideAtlasiO00555.
PRIDEiO00555.

PTM databases

iPTMnetiO00555.
PhosphoSitePlusiO00555.

Expressioni

Tissue specificityi

Brain specific; mainly found in cerebellum, cerebral cortex, thalamus and hypothalamus. Expressed in the small cell lung carcinoma cell line SCC-9. No expression in heart, kidney, liver or muscle. Purkinje cells contain predominantly P-type VSCC, the Q-type being a prominent calcium current in cerebellar granule cells.1 Publication

Gene expression databases

BgeeiENSG00000141837.
ExpressionAtlasiO00555. baseline and differential.
GenevisibleiO00555. HS.

Organism-specific databases

HPAiHPA064258.

Interactioni

Subunit structurei

Voltage-dependent calcium channels are multisubunit complexes, 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. Interact (via C-terminal CDB motif) with CABP1 in the pre- and postsynaptic membranes.

Binary interactionsi

WithEntry#Exp.IntActNotes
ABI1Q8IZP02EBI-766279,EBI-375446
ADGRL1O949102EBI-766279,EBI-3389315
AMIGO2Q86SJ22EBI-766279,EBI-3866830
ARHGAP22Q7Z5H32EBI-766279,EBI-3866859
CSNK2BP678702EBI-766279,EBI-348169
DNAJB5O759532EBI-766279,EBI-5655937
GRNP287992EBI-766279,EBI-747754
HIVEP1P158222EBI-766279,EBI-722264
LTBP4Q8N2S12EBI-766279,EBI-947718
MATN2O003392EBI-766279,EBI-949020
MEGF6O750952EBI-766279,EBI-947597
MEGF8Q7Z7M02EBI-766279,EBI-947617
PUF60Q9UHX12EBI-766279,EBI-1053259
RBM12BQ8IXT52EBI-766279,EBI-3044077
TSPOAP1O951532EBI-766279,EBI-5915931
TUBB2BQ9BVA12EBI-766279,EBI-355665
UQCRC2P226952EBI-766279,EBI-1051424
YLPM1P497502EBI-766279,EBI-712871

GO - Molecular functioni

  • syntaxin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107227. 98 interactors.
IntActiO00555. 92 interactors.
STRINGi9606.ENSP00000353362.

Chemistry databases

BindingDBiO00555.

Structurei

Secondary structure

12505
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1956 – 1970Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BXKX-ray2.55B/D1955-1975[»]
ProteinModelPortaliO00555.
SMRiO00555.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00555.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati85 – 363IAdd BLAST279
Repeati473 – 717IIAdd BLAST245
Repeati1231 – 1514IIIAdd BLAST284
Repeati1551 – 1814IVAdd BLAST264

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni383 – 400Binding to the beta subunitBy similarityAdd BLAST18

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi13 – 18Poly-Gly6
Compositional biasi727 – 732Poly-Glu6
Compositional biasi1002 – 1007Poly-Arg6
Compositional biasi1204 – 1207Poly-Glu4
Compositional biasi2211 – 2220Poly-His10
Compositional biasi2221 – 2224Poly-Pro4
Compositional biasi2314 – 2324Poly-GlnAdd BLAST11

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.

Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2301. Eukaryota.
ENOG410XNP6. LUCA.
GeneTreeiENSGT00830000128247.
HOGENOMiHOG000231530.
HOVERGENiHBG050763.
InParanoidiO00555.
KOiK04344.
PhylomeDBiO00555.
TreeFamiTF312805.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR005448. CACNA1A.
IPR027359. Channel_four-helix_dom.
IPR031649. GPHH_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR002077. VDCCAlpha1.
[Graphical view]
PANTHERiPTHR10037:SF59. PTHR10037:SF59. 3 hits.
PfamiPF08763. Ca_chan_IQ. 1 hit.
PF16905. GPHH. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSiPR00167. CACHANNEL.
PR01632. PQVDCCALPHA1.
SMARTiSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: O00555-1) [UniParc]FASTAAdd to basket
Also known as: 1A-1, BI-1-GGCAG

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MARFGDEMPA RYGGGGSGAA AGVVVGSGGG RGAGGSRQGG QPGAQRMYKQ
60 70 80 90 100
SMAQRARTMA LYNPIPVRQN CLTVNRSLFL FSEDNVVRKY AKKITEWPPF
110 120 130 140 150
EYMILATIIA NCIVLALEQH LPDDDKTPMS ERLDDTEPYF IGIFCFEAGI
160 170 180 190 200
KIIALGFAFH KGSYLRNGWN VMDFVVVLTG ILATVGTEFD LRTLRAVRVL
210 220 230 240 250
RPLKLVSGIP SLQVVLKSIM KAMIPLLQIG LLLFFAILIF AIIGLEFYMG
260 270 280 290 300
KFHTTCFEEG TDDIQGESPA PCGTEEPART CPNGTKCQPY WEGPNNGITQ
310 320 330 340 350
FDNILFAVLT VFQCITMEGW TDLLYNSNDA SGNTWNWLYF IPLIIIGSFF
360 370 380 390 400
MLNLVLGVLS GEFAKERERV ENRRAFLKLR RQQQIERELN GYMEWISKAE
410 420 430 440 450
EVILAEDETD GEQRHPFDGA LRRTTIKKSK TDLLNPEEAE DQLADIASVG
460 470 480 490 500
SPFARASIKS AKLENSTFFH KKERRMRFYI RRMVKTQAFY WTVLSLVALN
510 520 530 540 550
TLCVAIVHYN QPEWLSDFLY YAEFIFLGLF MSEMFIKMYG LGTRPYFHSS
560 570 580 590 600
FNCFDCGVII GSIFEVIWAV IKPGTSFGIS VLRALRLLRI FKVTKYWASL
610 620 630 640 650
RNLVVSLLNS MKSIISLLFL LFLFIVVFAL LGMQLFGGQF NFDEGTPPTN
660 670 680 690 700
FDTFPAAIMT VFQILTGEDW NEVMYDGIKS QGGVQGGMVF SIYFIVLTLF
710 720 730 740 750
GNYTLLNVFL AIAVDNLANA QELTKDEQEE EEAANQKLAL QKAKEVAEVS
760 770 780 790 800
PLSAANMSIA VKEQQKNQKP AKSVWEQRTS EMRKQNLLAS REALYNEMDP
810 820 830 840 850
DERWKAAYTR HLRPDMKTHL DRPLVVDPQE NRNNNTNKSR AAEPTVDQRL
860 870 880 890 900
GQQRAEDFLR KQARYHDRAR DPSGSAGLDA RRPWAGSQEA ELSREGPYGR
910 920 930 940 950
ESDHHAREGS LEQPGFWEGE AERGKAGDPH RRHVHRQGGS RESRSGSPRT
960 970 980 990 1000
GADGEHRRHR AHRRPGEEGP EDKAERRARH REGSRPARGG EGEGEGPDGG
1010 1020 1030 1040 1050
ERRRRHRHGA PATYEGDARR EDKERRHRRR KENQGSGVPV SGPNLSTTRP
1060 1070 1080 1090 1100
IQQDLGRQDP PLAEDIDNMK NNKLATAESA APHGSLGHAG LPQSPAKMGN
1110 1120 1130 1140 1150
STDPGPMLAI PAMATNPQNA ASRRTPNNPG NPSNPGPPKT PENSLIVTNP
1160 1170 1180 1190 1200
SGTQTNSAKT ARKPDHTTVD IPPACPPPLN HTVVQVNKNA NPDPLPKKEE
1210 1220 1230 1240 1250
EKKEEEEDDR GEDGPKPMPP YSSMFILSTT NPLRRLCHYI LNLRYFEMCI
1260 1270 1280 1290 1300
LMVIAMSSIA LAAEDPVQPN APRNNVLRYF DYVFTGVFTF EMVIKMIDLG
1310 1320 1330 1340 1350
LVLHQGAYFR DLWNILDFIV VSGALVAFAF TGNSKGKDIN TIKSLRVLRV
1360 1370 1380 1390 1400
LRPLKTIKRL PKLKAVFDCV VNSLKNVFNI LIVYMLFMFI FAVVAVQLFK
1410 1420 1430 1440 1450
GKFFHCTDES KEFEKDCRGK YLLYEKNEVK ARDREWKKYE FHYDNVLWAL
1460 1470 1480 1490 1500
LTLFTVSTGE GWPQVLKHSV DATFENQGPS PGYRMEMSIF YVVYFVVFPF
1510 1520 1530 1540 1550
FFVNIFVALI IITFQEQGDK MMEEYSLEKN ERACIDFAIS AKPLTRHMPQ
1560 1570 1580 1590 1600
NKQSFQYRMW QFVVSPPFEY TIMAMIALNT IVLMMKFYGA SVAYENALRV
1610 1620 1630 1640 1650
FNIVFTSLFS LECVLKVMAF GILNYFRDAW NIFDFVTVLG SITDILVTEF
1660 1670 1680 1690 1700
GNNFINLSFL RLFRAARLIK LLRQGYTIRI LLWTFVQSFK ALPYVCLLIA
1710 1720 1730 1740 1750
MLFFIYAIIG MQVFGNIGID VEDEDSDEDE FQITEHNNFR TFFQALMLLF
1760 1770 1780 1790 1800
RSATGEAWHN IMLSCLSGKP CDKNSGILTR ECGNEFAYFY FVSFIFLCSF
1810 1820 1830 1840 1850
LMLNLFVAVI MDNFEYLTRD SSILGPHHLD EYVRVWAEYD PAAWGRMPYL
1860 1870 1880 1890 1900
DMYQMLRHMS PPLGLGKKCP ARVAYKRLLR MDLPVADDNT VHFNSTLMAL
1910 1920 1930 1940 1950
IRTALDIKIA KGGADKQQMD AELRKEMMAI WPNLSQKTLD LLVTPHKSTD
1960 1970 1980 1990 2000
LTVGKIYAAM MIMEYYRQSK AKKLQAMREE QDRTPLMFQR MEPPSPTQEG
2010 2020 2030 2040 2050
GPGQNALPST QLDPGGALMA HESGLKESPS WVTQRAQEMF QKTGTWSPEQ
2060 2070 2080 2090 2100
GPPTDMPNSQ PNSQSVEMRE MGRDGYSDSE HYLPMEGQGR AASMPRLPAE
2110 2120 2130 2140 2150
NQRRRGRPRG NNLSTISDTS PMKRSASVLG PKARRLDDYS LERVPPEENQ
2160 2170 2180 2190 2200
RHHQRRRDRS HRASERSLGR YTDVDTGLGT DLSMTTQSGD LPSKERDQER
2210 2220 2230 2240 2250
GRPKDRKHRQ HHHHHHHHHH PPPPDKDRYA QERPDHGRAR ARDQRWSRSP
2260 2270 2280 2290 2300
SEGREHMAHR QGSSSVSGSP APSTSGTSTP RRGRRQLPQT PSTPRPHVSY
2310 2320 2330 2340 2350
SPVIRKAGGS GPPQQQQQQQ QQQQAVARPG RAATSGPRRY PGPTAEPLAG
2360 2370 2380 2390 2400
DRPPTGGHSS GRSPRMERRV PGPARSESPR ACRHGGARWP ASGPHVSEGP
2410 2420 2430 2440 2450
PGPRHHGYYR GSDYDEADGP GSGGGEEAMA GAYDAPPPVR HASSGATGRS
2460 2470 2480 2490 2500
PRTPRASGPA CASPSRHGRR LPNGYYPAHG LARPRGPGSR KGLHEPYSES

DDDWC
Length:2,505
Mass (Da):282,365
Last modified:July 15, 1999 - v2
Checksum:i2F2F378ACE02FD56
GO
Isoform 2 (identifier: O00555-2) [UniParc]FASTAAdd to basket
Also known as: 1A-2,BI-1

The sequence of this isoform differs from the canonical sequence as follows:
     2262-2505: Missing.

Show »
Length:2,261
Mass (Da):256,932
Checksum:i08A864BB400F218B
GO
Isoform 3 (identifier: O00555-3) [UniParc]FASTAAdd to basket
Also known as: BI-1(V1)

The sequence of this isoform differs from the canonical sequence as follows:
     1844-1875: WGRMPYLDMYQMLRHMSPPLGLGKKCPARVAY → CGRIHYKDMYSLLRVISPPLGLGKKCPHRVAC
     2262-2505: Missing.

Show »
Length:2,261
Mass (Da):256,777
Checksum:i41408D8C7EB70094
GO
Isoform 4 (identifier: O00555-4) [UniParc]FASTAAdd to basket
Also known as: BI-1(V1)-GGCAG

The sequence of this isoform differs from the canonical sequence as follows:
     1844-1875: WGRMPYLDMYQMLRHMSPPLGLGKKCPARVAY → CGRIHYKDMYSLLRVISPPLGLGKKCPHRVAC

Show »
Length:2,505
Mass (Da):282,209
Checksum:iED4AA00D118EF46B
GO
Isoform 5 (identifier: O00555-5) [UniParc]FASTAAdd to basket
Also known as: BI-1(V2)

The sequence of this isoform differs from the canonical sequence as follows:
     2103-2114: Missing.
     2262-2505: Missing.

Show »
Length:2,249
Mass (Da):255,511
Checksum:i729D79965A9714A4
GO
Isoform 6 (identifier: O00555-6) [UniParc]FASTAAdd to basket
Also known as: BI-1(V2)-GGCAG

The sequence of this isoform differs from the canonical sequence as follows:
     2103-2114: Missing.

Show »
Length:2,493
Mass (Da):280,944
Checksum:i212024798B9867E3
GO
Isoform 8 (identifier: O00555-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     419-419: Missing.
     2314-2314: Q → QQQ

Show »
Length:2,506
Mass (Da):282,564
Checksum:iAEDF4D2A5E49263F
GO

Sequence cautioni

The sequence AAB49678 differs from that shown. Aberrant splicing.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti725K → KVEA in AAB61613 (PubMed:10049321).Curated1
Sequence conflicti725K → KVEA in AAB61612 (PubMed:10049321).Curated1
Sequence conflicti896G → D in CAA68172 (PubMed:8898206).Curated1
Sequence conflicti896G → D in BAA94766 (PubMed:10753886).Curated1
Sequence conflicti953D → N in BAA94766 (PubMed:10753886).Curated1
Sequence conflicti964R → S in BAA94766 (PubMed:10753886).Curated1
Sequence conflicti1207E → EE in CAA68172 (PubMed:8898206).Curated1
Sequence conflicti1313 – 1315WNI → ILP in AAB49674 (PubMed:8988170).Curated3
Sequence conflicti1313 – 1315WNI → ILP in AAB49675 (PubMed:8988170).Curated3
Sequence conflicti1313 – 1315WNI → ILP in AAB49676 (PubMed:8988170).Curated3
Sequence conflicti1313 – 1315WNI → ILP in AAB49677 (PubMed:8988170).Curated3
Sequence conflicti1313 – 1315WNI → ILP in AAB49678 (PubMed:8988170).Curated3
Sequence conflicti1459G → A in CAA68172 (PubMed:8898206).Curated1
Sequence conflicti1604V → A in CAA68172 (PubMed:8898206).Curated1
Sequence conflicti1617V → A in CAA68172 (PubMed:8898206).Curated1
Sequence conflicti1651G → GNP in AAB61613 (PubMed:10049321).Curated1
Sequence conflicti1651G → GNP in AAB61612 (PubMed:10049321).Curated1
Sequence conflicti1693P → A in AAB33068 (PubMed:7823133).Curated1
Sequence conflicti2038E → G in U06702 (PubMed:8525433).Curated1
Sequence conflicti2314Q → QQ in AAB49676 (PubMed:8988170).Curated1

Polymorphismi

The poly-Gln region of CACNA1A is polymorphic: 6 to 17 repeats in the normal population, expanded to about 21 to 30 repeats in SCA6. Repeat expansion has been reported also in a EA2 family.1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01445621A → V.Corresponds to variant rs15999dbSNPEnsembl.1
Natural variantiVAR_001491192R → Q in FHM1. 1 PublicationCorresponds to variant rs121908211dbSNPEnsembl.1
Natural variantiVAR_043820195R → K in FHM1. 1 PublicationCorresponds to variant rs121908222dbSNPEnsembl.1
Natural variantiVAR_043821218S → L in FHM1. 1 PublicationCorresponds to variant rs121908225dbSNPEnsembl.1
Natural variantiVAR_063683248Y → C in EA2. 1 PublicationCorresponds to variant rs121908238dbSNPEnsembl.1
Natural variantiVAR_043822253H → Y in EA2. 1 PublicationCorresponds to variant rs121908228dbSNPEnsembl.1
Natural variantiVAR_043823256C → R in EA2. 1 PublicationCorresponds to variant rs121908231dbSNPEnsembl.1
Natural variantiVAR_043824287C → Y in EA2. 1 PublicationCorresponds to variant rs121908236dbSNPEnsembl.1
Natural variantiVAR_043825293G → R in EA2 and SCA6. 2 PublicationsCorresponds to variant rs121908215dbSNPEnsembl.1
Natural variantiVAR_067342388E → K in EA2. 1 Publication1
Natural variantiVAR_063684389L → F in EA2. 1 PublicationCorresponds to variant rs121908239dbSNPEnsembl.1
Natural variantiVAR_063685405A → T in SCA6. 1 PublicationCorresponds to variant rs121908245dbSNPEnsembl.1
Natural variantiVAR_063686454A → T.1 PublicationCorresponds to variant rs41276886dbSNPEnsembl.1
Natural variantiVAR_063687501T → M in EA2. 1 PublicationCorresponds to variant rs121908240dbSNPEnsembl.1
Natural variantiVAR_043826583R → Q in FHM1. 1 PublicationCorresponds to variant rs121908217dbSNPEnsembl.1
Natural variantiVAR_063688638G → D in EA2; reduces P/Q current densities. 1 PublicationCorresponds to variant rs121908246dbSNPEnsembl.1
Natural variantiVAR_001492666T → M in FHM1 and EA2. 3 PublicationsCorresponds to variant rs121908212dbSNPEnsembl.1
Natural variantiVAR_001493714V → A in FHM1. 1 PublicationCorresponds to variant rs121908213dbSNPEnsembl.1
Natural variantiVAR_043827715D → E in FHM1. 1 PublicationCorresponds to variant rs121908218dbSNPEnsembl.1
Natural variantiVAR_059221732E → A.Corresponds to variant rs16019dbSNPEnsembl.1
Natural variantiVAR_063689798M → T in EA2. 1 PublicationCorresponds to variant rs121908241dbSNPEnsembl.1
Natural variantiVAR_063690897P → R in EA2. 1 PublicationCorresponds to variant rs121908242dbSNPEnsembl.1
Natural variantiVAR_014458914P → S.Corresponds to variant rs16020dbSNPEnsembl.1
Natural variantiVAR_014459918E → D.2 PublicationsCorresponds to variant rs16022dbSNPEnsembl.1
Natural variantiVAR_043828993E → V.3 PublicationsCorresponds to variant rs16023dbSNPEnsembl.1
Natural variantiVAR_0144611015E → K.Corresponds to variant rs16024dbSNPEnsembl.1
Natural variantiVAR_0144621105G → S.2 PublicationsCorresponds to variant rs16027dbSNPEnsembl.1
Natural variantiVAR_0592221173P → L.Corresponds to variant rs16028dbSNPEnsembl.1
Natural variantiVAR_0438291335K → E in FHM1. 1 PublicationCorresponds to variant rs121908223dbSNPEnsembl.1
Natural variantiVAR_0438301346R → Q in FHM1; with progressive cerebellar ataxia. 2 PublicationsCorresponds to variant rs121908230dbSNPEnsembl.1
Natural variantiVAR_0438311384Y → C in FHM1. 1 PublicationCorresponds to variant rs121908219dbSNPEnsembl.1
Natural variantiVAR_0438321403F → C in EA2; loss of function. 1 PublicationCorresponds to variant rs121908227dbSNPEnsembl.1
Natural variantiVAR_0438331456V → L in FHM1. 1 PublicationCorresponds to variant rs121908237dbSNPEnsembl.1
Natural variantiVAR_0438341482G → R in EA2. 1 PublicationCorresponds to variant rs121908232dbSNPEnsembl.1
Natural variantiVAR_0438351490F → S in EA2. 1 PublicationCorresponds to variant rs121908233dbSNPEnsembl.1
Natural variantiVAR_0438361493V → I in EA2. 1 PublicationCorresponds to variant rs121908234dbSNPEnsembl.1
Natural variantiVAR_0438371661R → H in EA2. 1 PublicationCorresponds to variant rs121908216dbSNPEnsembl.1
Natural variantiVAR_0636911664R → Q in SCA6. 1 PublicationCorresponds to variant rs121908247dbSNPEnsembl.1
Natural variantiVAR_0438381667R → W in FHM1. 1 PublicationCorresponds to variant rs121908220dbSNPEnsembl.1
Natural variantiVAR_0636921679R → C in EA2. 1 PublicationCorresponds to variant rs121908243dbSNPEnsembl.1
Natural variantiVAR_0438391683W → R in FHM1. 1 PublicationCorresponds to variant rs121908221dbSNPEnsembl.1
Natural variantiVAR_0637061695V → I in FHM1. 1 PublicationCorresponds to variant rs121908224dbSNPEnsembl.1
Natural variantiVAR_0438401736H → L in EA2. 1 PublicationCorresponds to variant rs121908229dbSNPEnsembl.1
Natural variantiVAR_0438411756E → K in EA2. 1 PublicationCorresponds to variant rs121908226dbSNPEnsembl.1
Natural variantiVAR_0014941810I → L in FHM1. 1 PublicationCorresponds to variant rs121908214dbSNPEnsembl.1
Natural variantiVAR_0636931869C → R in EA2. 1 PublicationCorresponds to variant rs121908244dbSNPEnsembl.1
Natural variantiVAR_0438422135R → C in EA2. 1 PublicationCorresponds to variant rs121908235dbSNPEnsembl.1
Natural variantiVAR_0144632394P → S.Corresponds to variant rs16056dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_046165419Missing in isoform 8. 1 Publication1
Alternative sequenceiVSP_0008711844 – 1875WGRMP…ARVAY → CGRIHYKDMYSLLRVISPPL GLGKKCPHRVAC in isoform 3 and isoform 4. 2 PublicationsAdd BLAST32
Alternative sequenceiVSP_0008722103 – 2114Missing in isoform 5 and isoform 6. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_0008752262 – 2505Missing in isoform 2, isoform 3 and isoform 5. 3 PublicationsAdd BLAST244
Alternative sequenceiVSP_0461662314Q → QQQ in isoform 8. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF004883 mRNA. Translation: AAB61612.1.
AF004884 mRNA. Translation: AAB61613.1.
X99897 mRNA. Translation: CAA68172.1.
Z80114 Genomic DNA. No translation available.
Z80115 Genomic DNA. No translation available.
U79663 mRNA. Translation: AAB49674.1.
U79664 mRNA. Translation: AAB49675.1.
U79665 mRNA. Translation: AAB49676.1.
U79666 mRNA. Translation: AAB64179.1.
U79667 mRNA. Translation: AAB49677.1.
U79668 mRNA. Translation: AAB49678.1. Sequence problems.
AB035727 mRNA. Translation: BAA94766.2.
AC005305 Genomic DNA. Translation: AAC26839.1.
AC005513 Genomic DNA. No translation available.
AC008540 Genomic DNA. No translation available.
AC011446 Genomic DNA. No translation available.
AC022436 Genomic DNA. No translation available.
AC026805 Genomic DNA. No translation available.
AC093062 Genomic DNA. No translation available.
AC098781 Genomic DNA. No translation available.
AC124224 Genomic DNA. No translation available.
S76537 mRNA. Translation: AAB33068.1.
U06702 mRNA. No translation available.
CCDSiCCDS45998.1. [O00555-8]
CCDS45999.1. [O00555-3]
RefSeqiNP_000059.3. NM_000068.3.
NP_001120693.1. NM_001127221.1. [O00555-3]
NP_001120694.1. NM_001127222.1. [O00555-8]
NP_001167551.1. NM_001174080.1.
NP_075461.2. NM_023035.2.
UniGeneiHs.501632.

Genome annotation databases

EnsembliENST00000360228; ENSP00000353362; ENSG00000141837. [O00555-8]
ENST00000635895; ENSP00000490323; ENSG00000141837. [O00555-2]
ENST00000637276; ENSP00000489777; ENSG00000141837. [O00555-5]
ENST00000638009; ENSP00000489913; ENSG00000141837. [O00555-3]
GeneIDi773.
KEGGihsa:773.
UCSCiuc002mwy.5. human. [O00555-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism, Triplet repeat expansion

Cross-referencesi

Web resourcesi

Calcium channel, voltage-dependent, P/Q type, alpha 1A subunit (CACNA1A)

Leiden Open Variation Database (LOVD)

Familial hemiplegic migraine (FHM) variation database, calcium channel, voltage-dependent, P/Q type, alpha 1A subunit (CACNA1A)

Leiden Open Variation Database (LOVD)

Undiagnosed Disease Network

CACNA1A

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF004883 mRNA. Translation: AAB61612.1.
AF004884 mRNA. Translation: AAB61613.1.
X99897 mRNA. Translation: CAA68172.1.
Z80114 Genomic DNA. No translation available.
Z80115 Genomic DNA. No translation available.
U79663 mRNA. Translation: AAB49674.1.
U79664 mRNA. Translation: AAB49675.1.
U79665 mRNA. Translation: AAB49676.1.
U79666 mRNA. Translation: AAB64179.1.
U79667 mRNA. Translation: AAB49677.1.
U79668 mRNA. Translation: AAB49678.1. Sequence problems.
AB035727 mRNA. Translation: BAA94766.2.
AC005305 Genomic DNA. Translation: AAC26839.1.
AC005513 Genomic DNA. No translation available.
AC008540 Genomic DNA. No translation available.
AC011446 Genomic DNA. No translation available.
AC022436 Genomic DNA. No translation available.
AC026805 Genomic DNA. No translation available.
AC093062 Genomic DNA. No translation available.
AC098781 Genomic DNA. No translation available.
AC124224 Genomic DNA. No translation available.
S76537 mRNA. Translation: AAB33068.1.
U06702 mRNA. No translation available.
CCDSiCCDS45998.1. [O00555-8]
CCDS45999.1. [O00555-3]
RefSeqiNP_000059.3. NM_000068.3.
NP_001120693.1. NM_001127221.1. [O00555-3]
NP_001120694.1. NM_001127222.1. [O00555-8]
NP_001167551.1. NM_001174080.1.
NP_075461.2. NM_023035.2.
UniGeneiHs.501632.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BXKX-ray2.55B/D1955-1975[»]
ProteinModelPortaliO00555.
SMRiO00555.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107227. 98 interactors.
IntActiO00555. 92 interactors.
STRINGi9606.ENSP00000353362.

Chemistry databases

BindingDBiO00555.
ChEMBLiCHEMBL4266.
DrugBankiDB01244. Bepridil.
DB00836. Loperamide.
DB00230. Pregabalin.
DB00421. Spironolactone.
DB00661. Verapamil.

Protein family/group databases

TCDBi1.A.1.11.27. the voltage-gated ion channel (vic) superfamily.

PTM databases

iPTMnetiO00555.
PhosphoSitePlusiO00555.

Polymorphism and mutation databases

BioMutaiCACNA1A.

Proteomic databases

MaxQBiO00555.
PaxDbiO00555.
PeptideAtlasiO00555.
PRIDEiO00555.

Protocols and materials databases

DNASUi773.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360228; ENSP00000353362; ENSG00000141837. [O00555-8]
ENST00000635895; ENSP00000490323; ENSG00000141837. [O00555-2]
ENST00000637276; ENSP00000489777; ENSG00000141837. [O00555-5]
ENST00000638009; ENSP00000489913; ENSG00000141837. [O00555-3]
GeneIDi773.
KEGGihsa:773.
UCSCiuc002mwy.5. human. [O00555-1]

Organism-specific databases

CTDi773.
DisGeNETi773.
GeneCardsiCACNA1A.
GeneReviewsiCACNA1A.
HGNCiHGNC:1388. CACNA1A.
HPAiHPA064258.
MalaCardsiCACNA1A.
MIMi108500. phenotype.
141500. phenotype.
183086. phenotype.
601011. gene.
neXtProtiNX_O00555.
OpenTargetsiENSG00000141837.
Orphaneti2131. Alternating hemiplegia of childhood.
71518. Benign paroxysmal torticollis of infancy.
569. Familial or sporadic hemiplegic migraine.
97. Familial paroxysmal ataxia.
98758. Spinocerebellar ataxia type 6.
PharmGKBiPA26007.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2301. Eukaryota.
ENOG410XNP6. LUCA.
GeneTreeiENSGT00830000128247.
HOGENOMiHOG000231530.
HOVERGENiHBG050763.
InParanoidiO00555.
KOiK04344.
PhylomeDBiO00555.
TreeFamiTF312805.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000141837-MONOMER.
ReactomeiR-HSA-112308. Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels.
R-HSA-422356. Regulation of insulin secretion.

Miscellaneous databases

ChiTaRSiCACNA1A. human.
EvolutionaryTraceiO00555.
GeneWikiiCav2.1.
GenomeRNAii773.
PROiO00555.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000141837.
ExpressionAtlasiO00555. baseline and differential.
GenevisibleiO00555. HS.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR005448. CACNA1A.
IPR027359. Channel_four-helix_dom.
IPR031649. GPHH_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR002077. VDCCAlpha1.
[Graphical view]
PANTHERiPTHR10037:SF59. PTHR10037:SF59. 3 hits.
PfamiPF08763. Ca_chan_IQ. 1 hit.
PF16905. GPHH. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSiPR00167. CACHANNEL.
PR01632. PQVDCCALPHA1.
SMARTiSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCAC1A_HUMAN
AccessioniPrimary (citable) accession number: O00555
Secondary accession number(s): J3KP41
, P78510, P78511, Q16290, Q92690, Q99790, Q99791, Q99792, Q99793, Q9NS88, Q9UDC4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 15, 1999
Last modified: November 30, 2016
This is version 176 of the entry and version 2 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 19
    Human chromosome 19: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.