[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BI-1-GGCAG AND BI-1). TISSUE=Neuron; PubMed=10049321 [NCBI, ExPASy, EBI, Israel, Japan] Hans M., Urrutia A., Deal C., Brust P.F., Stauderman K., Ellis S.B., Harpold M.M., Johnson E.C., Williams M.E.; "Structural elements in domain IV that influence biophysical and pharmacological properties of human alpha1A-containing high-voltage-activated calcium channels."; Biophys. J. 76:1384-1400(1999).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM BI-1(V1)), VARIANTS FHM, AND INVOLVEMENT IN EA2. TISSUE=Cerebellum; DOI=10.1016/S0092-8674(00)81373-2; PubMed=8898206 [NCBI, ExPASy, EBI, Israel, Japan] Ophoff R.A., Terwindt G.M., Vergouwe M.N., van Eijk R., Oefner P.J., Hoffman S.M.G., Lamerdin J.E., Mohrenweiser H.W., Bulman D.E., Ferrari M., Haan J., Lindhout D., van Ommen G.-J.B., Hofker M.H., Ferrari M.D., Frants R.R.; "Familial hemiplegic migraine and episodic ataxia type-2 are caused by mutations in the Ca2+ channel gene CACNL1A4."; Cell 87:543-552(1996).
[3]	NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND INVOLVEMENT IN SCA6. TISSUE=Brain; DOI=10.1038/ng0197-62; PubMed=8988170 [NCBI, ExPASy, EBI, Israel, Japan] Zhuchenko O., Bailey J., Bonnen P.E., Ashizawa T., Stockton D.W., Amos C., Dobyns W.B., Subramony S.H., Zoghbi H.Y., Lee C.C.; "Autosomal dominant cerebellar ataxia (SCA6) associated with small polyglutamine expansions in the alpha 1A-voltage-dependent calcium channel."; Nat. Genet. 15:62-69(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/nature02399; PubMed=15057824 [NCBI, ExPASy, EBI, Israel, Japan] Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.; "The DNA sequence and biology of human chromosome 19."; Nature 428:529-535(2004).
[5]	NUCLEOTIDE SEQUENCE [MRNA] OF 1693-1807. TISSUE=Lung carcinoma; PubMed=7823133 [NCBI, ExPASy, EBI, Israel, Japan] Barry E.L.R., Viglione M.P., Kim Y.I., Froehner S.C.; "Expression and antibody inhibition of P-type calcium channels in human small-cell lung carcinoma cells."; J. Neurosci. 15:274-283(1995).
[6]	NUCLEOTIDE SEQUENCE [MRNA] OF 2038-2258. TISSUE=Frontal cortex; DOI=10.1007/BF02255782; PubMed=8525433 [NCBI, ExPASy, EBI, Israel, Japan] Margolis R.L., Breschel T.S., Li S.H., Kidwai A.S., Antonarakis S.E., McInnis M.G., Ross C.A.; "Characterization of cDNA clones containing CCA trinucleotide repeats derived from human brain."; Somat. Cell Mol. Genet. 21:279-284(1995).
[7]	VARIANT SCA6 ARG-293. DOI=10.1086/301613; PubMed=9345107 [NCBI, ExPASy, EBI, Israel, Japan] Yue Q., Jen J.C., Nelson S.F., Baloh R.W.; "Progressive ataxia due to a missense mutation in a calcium-channel gene."; Am. J. Hum. Genet. 61:1078-1087(1997).
[8]	POLYMORPHISM, AND INVOLVEMENT IN SCA6 AND EA2. DOI=10.1093/hmg/6.11.1973; PubMed=9302278 [NCBI, ExPASy, EBI, Israel, Japan] Jodice C., Mantuano E., Veneziano L., Trettel F., Sabbadini G., Calandriello L., Francia A., Spadaro M., Pierelli F., Salvi F., Ophoff R.A., Frants R.R., Frontali M.; "Episodic ataxia type 2 (EA2) and spinocerebellar ataxia type 6 (SCA6) due to CAG repeat expansion in the CACNA1A gene on chromosome 19p."; Hum. Mol. Genet. 6:1973-1978(1997).
[9]	VARIANT EA2 HIS-1661. DOI=10.1007/s004390051099; PubMed=10987655 [NCBI, ExPASy, EBI, Israel, Japan] Friend K.L., Crimmins D., Phan T.G., Sue C.M., Colley A., Fung V.S., Morris J.G., Sutherland G.R., Richards R.I.; "Detection of a novel missense mutation and second recurrent mutation in the CACNA1A gene in individuals with EA-2 and FHM."; Hum. Genet. 105:261-265(1999).
[10]	VARIANT VAL-993, AND VARIANT FHM LEU-1456. PubMed=10408532 [NCBI, ExPASy, EBI, Israel, Japan] Carrera P., Piatti M., Stenirri S., Grimaldi L.M., Marchioni E., Curcio M., Righetti P.G., Ferrari M., Gelfi C.; "Genetic heterogeneity in Italian families with familial hemiplegic migraine."; Neurology 53:26-33(1999).
[11]	VARIANT FHM LEU-218. DOI=10.1002/ana.1031; PubMed=11409427 [NCBI, ExPASy, EBI, Israel, Japan] Kors E.E., Terwindt G.M., Vermeulen F.L., Fitzsimons R.B., Jardine P.E., Heywood P., Love S., van den Maagdenberg A.M., Haan J., Frants R.R., Ferrari M.D.; "Delayed cerebral edema and fatal coma after minor head trauma: role of the CACNA1A calcium channel subunit gene and relationship with familial hemiplegic migraine."; Ann. Neurol. 49:753-760(2001).
[12]	VARIANT EA2 LYS-1756. DOI=10.1001/archneur.58.2.292; PubMed=11176968 [NCBI, ExPASy, EBI, Israel, Japan] Denier C., Ducros A., Durr A., Eymard B., Chassande B., Tournier-Lasserve E.; "Missense CACNA1A mutation causing episodic ataxia type 2."; Arch. Neurol. 58:292-295(2001).
[13]	VARIANTS FHM LYS-195; GLN-583; MET-666; GLU-715; GLU-1335; CYS-1384; TRP-1667 AND ARG-1683. DOI=10.1056/NEJM200107053450103; PubMed=11439943 [NCBI, ExPASy, EBI, Israel, Japan] Ducros A., Denier C., Joutel A., Cecillon M., Lescoat C., Vahedi K., Darcel F., Vicaut E., Bousser M.G., Tournier-Lasserve E.; "The clinical spectrum of familial hemiplegic migraine associated with mutations in a neuronal calcium channel."; N. Engl. J. Med. 345:17-24(2001).
[14]	VARIANT EA2 CYS-1404, AND CHARACTERIZATION OF VARIANT EA2 CYS-1404. PubMed=11723274 [NCBI, ExPASy, EBI, Israel, Japan] Jen J., Wan J., Graves M., Yu H., Mock A.F., Coulin C.J., Kim G., Yue Q., Papazian D.M., Baloh R.W.; "Loss-of-function EA2 mutations are associated with impaired neuromuscular transmission."; Neurology 57:1843-1848(2001).
[15]	VARIANT EA2 TYR-253. DOI=10.1007/s00415-002-0860-8; PubMed=12420090 [NCBI, ExPASy, EBI, Israel, Japan] van den Maagdenberg A.M., Kors E.E., Brunt E.R., van Paesschen W., Pascual J., Ravine D., Keeling S., Vanmolkot K.R., Vermeulen F.L., Terwindt G.M., Haan J., Frants R.R., Ferrari M.D.; "Episodic ataxia type 2. Three novel truncating mutations and one novel missense mutation in the CACNA1A gene."; J. Neurol. 249:1515-1519(2002).
[16]	VARIANT EA2 LEU-1736. DOI=10.1002/ana.20169; PubMed=15293273 [NCBI, ExPASy, EBI, Israel, Japan] Spacey S.D., Hildebrand M.E., Materek L.A., Bird T.D., Snutch T.P.; "Functional implications of a novel EA2 mutation in the P/Q-type calcium channel."; Ann. Neurol. 56:213-220(2004).
[17]	VARIANT FHM GLN-1346. DOI=10.1111/j..2004.00187.x; PubMed=15032980 [NCBI, ExPASy, EBI, Israel, Japan] Alonso I., Barros J., Tuna A., Seixas A., Coutinho P., Sequeiros J., Silveira I.; "A novel R1347Q mutation in the predicted voltage sensor segment of the P/Q-type calcium-channel alpha-subunit in a family with progressive cerebellar ataxia and hemiplegic migraine."; Clin. Genet. 65:70-72(2004).
[18]	VARIANTS EA2 ARG-256; ARG-1482; SER-1490; ILE-1493 AND CYS-2135. DOI=10.1136/jmg.2003.015396; PubMed=15173248 [NCBI, ExPASy, EBI, Israel, Japan] Mantuano E., Veneziano L., Spadaro M., Giunti P., Guida S., Leggio M.G., Verriello L., Wood N., Jodice C., Frontali M.; "Clusters of non-truncating mutations of P/Q type Ca2+ channel subunit Ca(v)2.1 causing episodic ataxia 2."; J. Med. Genet. 41:E82-E82(2004).
[19]	VARIANTS EA2 TYR-287; ARG-293 AND MET-666. DOI=10.1159/000077703; PubMed=14718690 [NCBI, ExPASy, EBI, Israel, Japan] Jen J., Kim G.W., Baloh R.W.; "Clinical spectrum of episodic ataxia type 2."; Neurology 62:17-22(2004).

Comments

FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-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).
SUBUNIT: 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.
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.

ALTERNATIVE PRODUCTS: 7 named isoforms [FASTA] produced by alternative splicing. Additional isoforms seem to exist.

Name	BI-1-GGCAG
Synonyms	1A-1
Isoform ID	O00555-1
This is the isoform sequence displayed in this entry.

Name	BI-1
Synonyms	1A-2
Isoform ID	O00555-2
Features which should be applied to build the isoform sequence: VSP_000875.

Name	BI-1(V1)
Isoform ID	O00555-3
Features which should be applied to build the isoform sequence: VSP_000871, VSP_000875.

Name	BI-1(V1)-GGCAG
Isoform ID	O00555-4
Features which should be applied to build the isoform sequence: VSP_000871.

Name	BI-1(V2)
Isoform ID	O00555-5
Features which should be applied to build the isoform sequence: VSP_000872, VSP_000875.

Name	BI-1(V2)-GGCAG
Isoform ID	O00555-6
Features which should be applied to build the isoform sequence: VSP_000872.

Name	BI-1(V2,V3)
Isoform ID	O00555-7
Features which should be applied to build the isoform sequence: VSP_000873, VSP_000874.

TISSUE SPECIFICITY: Brain specific; mainly found in cerebellum, cerebral cortex, thalamus and hypothalamus. 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.
DOMAIN: Each of the four internal repeats contains five hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one positively charged transmembrane segment (S4). S4 segments probably represent the voltage-sensor and are characterized by a series of positively charged amino acids at every third position.
POLYMORPHISM: 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.
DISEASE: Defects in CACNA1A are the cause of spinocerebellar ataxia type 6 (SCA6) [MIM:183086]. Spinocerebellar 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 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.
DISEASE: Defects in CACNA1A are the cause of familial hemiplegic migraine (FHM) [MIM:141500]; also known as migraine familial hemiplegic 1 (MHP1). FHM, a rare autosomal dominant subtype of migraine with aura, is associated with ictal hemiparesis and, in some families, progressive cerebellar atrophy.
DISEASE: Defects in CACNA1A are the cause of episodic ataxia type 2 (EA2) [MIM:108500]; also known as acetazolamide-responsive hereditary paroxysmal cerebellar ataxia (APCA). EA2 is an autosomal dominant disorder characterized by acetozolamide-responsive attacks of ataxia, migraine-like symptoms, interictal nystagmus, and cerebellar atrophy.
SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family [view classification].
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=CACNA1A";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF004884; AAB61613.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF004883; AAB61612.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X99897; CAA68172.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z80114; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
Z80115; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
U79666; AAB64179.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U79663; AAB49674.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U79664; AAB49675.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U79665; AAB49676.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U79667; AAB49677.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U79668; AAB49678.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AC005305; AAC26839.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AC011446; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
AC026805; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
AC124224; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
AC022436; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
AC098781; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
AC008540; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
S76537; AAB33068.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U06702; -; NOT_ANNOTATED_CDS; mRNA.	[EMBL / GenBank / DDBJ]

IPI

IPI00012136; -.
IPI00217497; -.
IPI00217498; -.
IPI00217499; -.
IPI00291347; -.
IPI00397553; -.
IPI00397554; -.

RefSeq

NP_001120693.1; -.
NP_001120694.1; -.

UniGene

Hs.501632

3D structure databases

PDB

3BXK; X-ray; 2.55 A; B/D=1955-1975.	[ExPASy / RCSB / EBI]
3BXL; X-ray; 2.30 A; B=1955-1973.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

3BXK; -.
3BXL; -.

PTM databases

O00555; -.

Enzyme and pathway databases

Reactome

REACT_13685; Synaptic Transmission.

Organism-specific databases

GC19M013178; -.

HIX0039929; -.

HGNC:1388; CACNA1A.

108500; phenotype. [NCBI / EBI]
141500; phenotype. [NCBI / EBI]
183086; phenotype. [NCBI / EBI]
601011; gene. [NCBI / EBI]

Orphanet

97; Ataxia, familial paroxysmal.
98758; Ataxia, spinocerebellar, type 6.
99; Autosomal dominant cerebellar ataxia.
71518; Benign paroxysmal torticollis of infancy.
569; Hemiplegic migraine, familial or sporadic.

PharmGKB

PA26007; -.

Gene expression databases

ArrayExpress

O00555; -.

Bgee

O00555; -.

GermOnline

ENSG00000141837; Homo sapiens.

Ontologies

GO:0042995;	Cellular component: cell projection (inferred from direct assay from UniProtKB).
GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from UniProtKB).
GO:0005634;	Cellular component: nucleus (inferred from direct assay from UniProtKB).
GO:0005891;	Cellular component: voltage-gated calcium channel complex (inferred from electronic annotation from InterPro).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0019905;	Molecular function: syntaxin binding (inferred from direct assay from UniProtKB).
GO:0005245;	Molecular function: voltage-gated calcium channel activity (inferred from direct assay from UniProtKB).
GO:0006816;	Biological process: calcium ion transport (inferred from electronic annotation from UniProtKB-KW).
GO:0008219;	Biological process: cell death (inferred from direct assay from UniProtKB).
GO:0007204;	Biological process: elevation of cytosolic calcium ion concentration (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR005821; Ion_trans.
IPR014873; VDCC_a1su_IQ.
IPR005448; VDCC_P/Q_a1su.
IPR002077; VDCCAlpha1.
Graphical view of domain structure.

PANTHER

PTHR10037:SF59; PQVDCCAlpha1; 1.

Pfam

PF08763; Ca_chan_IQ; 1.
PF00520; Ion_trans; 4.
Pfam graphical view of domain structure.

PRINTS

PR00167; CACHANNEL.
PR01632; PQVDCCALPHA1.

Proteomic databases

PRIDE

O00555; -.

Genome annotation databases

Ensembl

ENSG00000141837; Homo sapiens. [Contig view]

GeneID

773; -.

KEGG

hsa:773; -.

Phylogenomic databases

HOVERGEN

O00555; -.

Other

DrugBank

DB01244; Bepridil.
DB00568; Cinnarizine.
DB00836; Loperamide.
DB00401; Nisoldipine.
DB00230; Pregabalin.

NextBio

3122; -.

SOURCE

CACNA1A; Homo sapiens.

ProtoNet

O00555.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Calcium; Calcium channel; Calcium transport; Disease mutation; Disulfide bond; Glycoprotein; Ion transport; Ionic channel; Membrane; Neurodegeneration; Phosphoprotein; Polymorphism; Repeat; Spinocerebellar ataxia; Transmembrane; Transport; Triplet repeat expansion; Voltage-gated channel.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 2505`	`2505`	`Voltage-dependent P/Q-type calcium channel subunit alpha-1A.`	`PRO_0000053916`
`TOPO_DOM`	`1 98`	`98`	`Cytoplasmic (Potential).`
`TRANSMEM`	`99 117`	`19`	`S1 of repeat I (Potential).`
`TOPO_DOM`	`118 135`	`18`	`Extracellular (Potential).`
`TRANSMEM`	`136 155`	`20`	`S2 of repeat I (Potential).`
`TOPO_DOM`	`156 167`	`12`	`Cytoplasmic (Potential).`
`TRANSMEM`	`168 185`	`18`	`S3 of repeat I (Potential).`
`TOPO_DOM`	`186 190`	`5`	`Extracellular (Potential).`
`TRANSMEM`	`191 209`	`19`	`S4 of repeat I (Potential).`
`TOPO_DOM`	`210 228`	`19`	`Cytoplasmic (Potential).`
`TRANSMEM`	`229 248`	`20`	`S5 of repeat I (Potential).`
`TOPO_DOM`	`249 335`	`87`	`Extracellular (Potential).`
`TRANSMEM`	`336 360`	`25`	`S6 of repeat I (Potential).`
`TOPO_DOM`	`361 487`	`127`	`Cytoplasmic (Potential).`
`TRANSMEM`	`488 506`	`19`	`S1 of repeat II (Potential).`
`TOPO_DOM`	`507 521`	`15`	`Extracellular (Potential).`
`TRANSMEM`	`522 541`	`20`	`S2 of repeat II (Potential).`
`TOPO_DOM`	`542 549`	`8`	`Cytoplasmic (Potential).`
`TRANSMEM`	`550 568`	`19`	`S3 of repeat II (Potential).`
`TOPO_DOM`	`569 578`	`10`	`Extracellular (Potential).`
`TRANSMEM`	`579 597`	`19`	`S4 of repeat II (Potential).`
`TOPO_DOM`	`598 616`	`19`	`Cytoplasmic (Potential).`
`TRANSMEM`	`617 636`	`20`	`S5 of repeat II (Potential).`
`TOPO_DOM`	`637 689`	`53`	`Extracellular (Potential).`
`TRANSMEM`	`690 714`	`25`	`S6 of repeat II (Potential).`
`TOPO_DOM`	`715 1242`	`528`	`Cytoplasmic (Potential).`
`TRANSMEM`	`1243 1261`	`19`	`S1 of repeat III (Potential).`
`TOPO_DOM`	`1262 1277`	`16`	`Extracellular (Potential).`
`TRANSMEM`	`1278 1297`	`20`	`S2 of repeat III (Potential).`
`TOPO_DOM`	`1298 1309`	`12`	`Cytoplasmic (Potential).`
`TRANSMEM`	`1310 1328`	`19`	`S3 of repeat III (Potential).`
`TOPO_DOM`	`1329 1339`	`11`	`Extracellular (Potential).`
`TRANSMEM`	`1340 1358`	`19`	`S4 of repeat III (Potential).`
`TOPO_DOM`	`1359 1377`	`19`	`Cytoplasmic (Potential).`
`TRANSMEM`	`1378 1397`	`20`	`S5 of repeat III (Potential).`
`TOPO_DOM`	`1398 1484`	`87`	`Extracellular (Potential).`
`TRANSMEM`	`1485 1509`	`25`	`S6 of repeat III (Potential).`
`TOPO_DOM`	`1510 1564`	`55`	`Cytoplasmic (Potential).`
`TRANSMEM`	`1565 1593`	`29`	`S1 of repeat IV (Potential).`
`TOPO_DOM`	`1594 1598`	`5`	`Extracellular (Potential).`
`TRANSMEM`	`1599 1618`	`20`	`S2 of repeat IV (Potential).`
`TOPO_DOM`	`1619 1626`	`8`	`Cytoplasmic (Potential).`
`TRANSMEM`	`1627 1645`	`19`	`S3 of repeat IV (Potential).`
`TOPO_DOM`	`1646 1652`	`7`	`Extracellular (Potential).`
`TRANSMEM`	`1653 1671`	`19`	`S4 of repeat IV (Potential).`
`TOPO_DOM`	`1672 1690`	`19`	`Cytoplasmic (Potential).`
`TRANSMEM`	`1691 1710`	`20`	`S5 of repeat IV (Potential).`
`TOPO_DOM`	`1711 1782`	`72`	`Extracellular (Potential).`
`TRANSMEM`	`1783 1807`	`25`	`S6 of repeat IV (Potential).`
`TOPO_DOM`	`1808 2505`	`698`	`Cytoplasmic (Potential).`
`REPEAT`	`85 363`	`279`	`I.`
`REPEAT`	`473 717`	`245`	`II.`
`REPEAT`	`1231 1514`	`284`	`III.`
`REPEAT`	`1551 1814`	`264`	`IV.`
`CA_BIND`	`1840 1851`	`12`	`By similarity.`
`REGION`	`383 400`	`18`	`Binding to the beta subunit (By similarity).`
`COMPBIAS`	`13 18`	`6`	`Poly-Gly.`
`COMPBIAS`	`727 732`	`6`	`Poly-Glu.`
`COMPBIAS`	`1002 1007`	`6`	`Poly-Arg.`
`COMPBIAS`	`1204 1207`	`4`	`Poly-Glu.`
`COMPBIAS`	`2211 2220`	`10`	`Poly-His.`
`COMPBIAS`	`2221 2224`	`4`	`Poly-Pro.`
`COMPBIAS`	`2314 2324`	`11`	`Poly-Gln.`
`SITE`	`318 318`	`1`	`Calcium ion selectivity and permeability (By similarity).`
`SITE`	`668 668`	`1`	`Calcium ion selectivity and permeability (By similarity).`
`SITE`	`1460 1460`	`1`	`Calcium ion selectivity and permeability (By similarity).`
`SITE`	`1756 1756`	`1`	`Calcium ion selectivity and permeability (By similarity).`
`MOD_RES`	`750 750`		`Phosphoserine (By similarity).`
`MOD_RES`	`1822 1822`		`Phosphoserine; by PKA (Potential).`
`MOD_RES`	`2030 2030`		`Phosphoserine (By similarity).`
`MOD_RES`	`2076 2076`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`2269 2269`		`Phosphoserine (By similarity).`
`MOD_RES`	`2378 2378`		`Phosphoserine (By similarity).`
`CARBOHYD`	`283 283`		`N-linked (GlcNAc...) (Potential).`
`VAR_SEQ`	`1844 1875`		`WGRMPYLDMYQMLRHMSPPLGLGKKCPARVAY -> CGRIHYKDMYSLLRVISPPLGLGKKCPHRVAC (in isoform BI-1(V1) and isoform BI-1(V1)-GGCAG).`	`VSP_000871`
`VAR_SEQ`	`2103 2114`		`Missing (in isoform BI-1(V2) and isoform BI-1(V2)-GGCAG).`	`VSP_000872`
`VAR_SEQ`	`2220 2240`		`HPPPPDKDRYAQERPDHGRAR -> RFLCFFFPFFLPCLKTVGLGL (in isoform BI-1(V2,V3)).`	`VSP_000873`
`VAR_SEQ`	`2241 2505`		`Missing (in isoform BI-1(V2,V3)).`	`VSP_000874`
`VAR_SEQ`	`2262 2505`		`Missing (in isoform BI-1, isoform BI-1(V1) and isoform BI-1(V2)).`	`VSP_000875`
`VARIANT`	`21 21`	`1`	`A -> V (in dbSNP:rs15999 [NCBI]).`	`VAR_014456`
`VARIANT`	`192 192`	`1`	`R -> Q (in FHM).`	`VAR_001491`
`VARIANT`	`195 195`	`1`	`R -> K (in FHM).`	`VAR_043820`
`VARIANT`	`218 218`	`1`	`S -> L (in FHM).`	`VAR_043821`
`VARIANT`	`253 253`	`1`	`H -> Y (in EA2).`	`VAR_043822`
`VARIANT`	`256 256`	`1`	`C -> R (in EA2).`	`VAR_043823`
`VARIANT`	`287 287`	`1`	`C -> Y (in EA2).`	`VAR_043824`
`VARIANT`	`293 293`	`1`	`G -> R (in EA2 and SCA6).`	`VAR_043825`
`VARIANT`	`583 583`	`1`	`R -> Q (in FHM).`	`VAR_043826`
`VARIANT`	`666 666`	`1`	`T -> M (in FHM and EA2).`	`VAR_001492`
`VARIANT`	`714 714`	`1`	`V -> A (in FHM).`	`VAR_001493`
`VARIANT`	`715 715`	`1`	`D -> E (in FHM).`	`VAR_043827`
`VARIANT`	`914 914`	`1`	`P -> S (in dbSNP:rs16020 [NCBI]).`	`VAR_014458`
`VARIANT`	`918 918`	`1`	`E -> D (in dbSNP:rs16022 [NCBI]).`	`VAR_014459`
`VARIANT`	`993 993`	`1`	`E -> V.`	`VAR_043828`
`VARIANT`	`1015 1015`	`1`	`E -> K (in dbSNP:rs16024 [NCBI]).`	`VAR_014461`
`VARIANT`	`1105 1105`	`1`	`G -> S (in dbSNP:rs16027 [NCBI]).`	`VAR_014462`
`VARIANT`	`1335 1335`	`1`	`K -> E (in FHM).`	`VAR_043829`
`VARIANT`	`1346 1346`	`1`	`R -> Q (in FHM; with progressive cerebellar ataxia).`	`VAR_043830`
`VARIANT`	`1384 1384`	`1`	`Y -> C (in FHM).`	`VAR_043831`
`VARIANT`	`1404 1404`	`1`	`F -> C (in EA2; loss of function).`	`VAR_043832`
`VARIANT`	`1456 1456`	`1`	`V -> L (in FHM).`	`VAR_043833`
`VARIANT`	`1482 1482`	`1`	`G -> R (in EA2).`	`VAR_043834`
`VARIANT`	`1490 1490`	`1`	`F -> S (in EA2).`	`VAR_043835`
`VARIANT`	`1493 1493`	`1`	`V -> I (in EA2).`	`VAR_043836`
`VARIANT`	`1661 1661`	`1`	`R -> H (in EA2).`	`VAR_043837`
`VARIANT`	`1667 1667`	`1`	`R -> W (in FHM).`	`VAR_043838`
`VARIANT`	`1683 1683`	`1`	`W -> R (in FHM).`	`VAR_043839`
`VARIANT`	`1736 1736`	`1`	`H -> L (in EA2).`	`VAR_043840`
`VARIANT`	`1756 1756`	`1`	`E -> K (in EA2).`	`VAR_043841`
`VARIANT`	`1810 1810`	`1`	`I -> L (in FHM).`	`VAR_001494`
`VARIANT`	`2135 2135`	`1`	`R -> C (in EA2).`	`VAR_043842`
`VARIANT`	`2394 2394`	`1`	`P -> S (in dbSNP:rs16056 [NCBI]).`	`VAR_014463`
`CONFLICT`	`725 725`		`K -> KVEA (in Ref. 1; AAB61613/AAB61612).`
`CONFLICT`	`896 896`		`G -> D (in Ref. 2; CAA68172).`
`CONFLICT`	`1207 1207`		`E -> EE (in Ref. 2; CAA68172).`
`CONFLICT`	`1459 1459`		`G -> A (in Ref. 2; CAA68172).`
`CONFLICT`	`1604 1604`		`V -> A (in Ref. 2; CAA68172).`
`CONFLICT`	`1617 1617`		`V -> A (in Ref. 2; CAA68172).`
`CONFLICT`	`1651 1651`		`G -> GNP (in Ref. 1; AAB61613/AAB61612).`
`CONFLICT`	`1693 1693`		`P -> A (in Ref. 5).`
`CONFLICT`	`2038 2038`		`E -> G (in Ref. 6).`

Sequence information

Length: 2505 AA [This is the length of the unprocessed precursor]

Molecular weight: 282365 Da [This is the MW of the unprocessed precursor]

CRC64: 2F2F378ACE02FD56 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MARFGDEMPA RYGGGGSGAA AGVVVGSGGG RGAGGSRQGG QPGAQRMYKQ SMAQRARTMA 

        70         80         90        100        110        120 
LYNPIPVRQN CLTVNRSLFL FSEDNVVRKY AKKITEWPPF EYMILATIIA NCIVLALEQH 

       130        140        150        160        170        180 
LPDDDKTPMS ERLDDTEPYF IGIFCFEAGI KIIALGFAFH KGSYLRNGWN VMDFVVVLTG 

       190        200        210        220        230        240 
ILATVGTEFD LRTLRAVRVL RPLKLVSGIP SLQVVLKSIM KAMIPLLQIG LLLFFAILIF 

       250        260        270        280        290        300 
AIIGLEFYMG KFHTTCFEEG TDDIQGESPA PCGTEEPART CPNGTKCQPY WEGPNNGITQ 

       310        320        330        340        350        360 
FDNILFAVLT VFQCITMEGW TDLLYNSNDA SGNTWNWLYF IPLIIIGSFF MLNLVLGVLS 

       370        380        390        400        410        420 
GEFAKERERV ENRRAFLKLR RQQQIERELN GYMEWISKAE EVILAEDETD GEQRHPFDGA 

       430        440        450        460        470        480 
LRRTTIKKSK TDLLNPEEAE DQLADIASVG SPFARASIKS AKLENSTFFH KKERRMRFYI 

       490        500        510        520        530        540 
RRMVKTQAFY WTVLSLVALN TLCVAIVHYN QPEWLSDFLY YAEFIFLGLF MSEMFIKMYG 

       550        560        570        580        590        600 
LGTRPYFHSS FNCFDCGVII GSIFEVIWAV IKPGTSFGIS VLRALRLLRI FKVTKYWASL 

       610        620        630        640        650        660 
RNLVVSLLNS MKSIISLLFL LFLFIVVFAL LGMQLFGGQF NFDEGTPPTN FDTFPAAIMT 

       670        680        690        700        710        720 
VFQILTGEDW NEVMYDGIKS QGGVQGGMVF SIYFIVLTLF GNYTLLNVFL AIAVDNLANA 

       730        740        750        760        770        780 
QELTKDEQEE EEAANQKLAL QKAKEVAEVS PLSAANMSIA VKEQQKNQKP AKSVWEQRTS 

       790        800        810        820        830        840 
EMRKQNLLAS REALYNEMDP DERWKAAYTR HLRPDMKTHL DRPLVVDPQE NRNNNTNKSR 

       850        860        870        880        890        900 
AAEPTVDQRL GQQRAEDFLR KQARYHDRAR DPSGSAGLDA RRPWAGSQEA ELSREGPYGR 

       910        920        930        940        950        960 
ESDHHAREGS LEQPGFWEGE AERGKAGDPH RRHVHRQGGS RESRSGSPRT GADGEHRRHR 

       970        980        990       1000       1010       1020 
AHRRPGEEGP EDKAERRARH REGSRPARGG EGEGEGPDGG ERRRRHRHGA PATYEGDARR 

      1030       1040       1050       1060       1070       1080 
EDKERRHRRR KENQGSGVPV SGPNLSTTRP IQQDLGRQDP PLAEDIDNMK NNKLATAESA 

      1090       1100       1110       1120       1130       1140 
APHGSLGHAG LPQSPAKMGN STDPGPMLAI PAMATNPQNA ASRRTPNNPG NPSNPGPPKT 

      1150       1160       1170       1180       1190       1200 
PENSLIVTNP SGTQTNSAKT ARKPDHTTVD IPPACPPPLN HTVVQVNKNA NPDPLPKKEE 

      1210       1220       1230       1240       1250       1260 
EKKEEEEDDR GEDGPKPMPP YSSMFILSTT NPLRRLCHYI LNLRYFEMCI LMVIAMSSIA 

      1270       1280       1290       1300       1310       1320 
LAAEDPVQPN APRNNVLRYF DYVFTGVFTF EMVIKMIDLG LVLHQGAYFR DLWNILDFIV 

      1330       1340       1350       1360       1370       1380 
VSGALVAFAF TGNSKGKDIN TIKSLRVLRV LRPLKTIKRL PKLKAVFDCV VNSLKNVFNI 

      1390       1400       1410       1420       1430       1440 
LIVYMLFMFI FAVVAVQLFK GKFFHCTDES KEFEKDCRGK YLLYEKNEVK ARDREWKKYE 

      1450       1460       1470       1480       1490       1500 
FHYDNVLWAL LTLFTVSTGE GWPQVLKHSV DATFENQGPS PGYRMEMSIF YVVYFVVFPF 

      1510       1520       1530       1540       1550       1560 
FFVNIFVALI IITFQEQGDK MMEEYSLEKN ERACIDFAIS AKPLTRHMPQ NKQSFQYRMW 

      1570       1580       1590       1600       1610       1620 
QFVVSPPFEY TIMAMIALNT IVLMMKFYGA SVAYENALRV FNIVFTSLFS LECVLKVMAF 

      1630       1640       1650       1660       1670       1680 
GILNYFRDAW NIFDFVTVLG SITDILVTEF GNNFINLSFL RLFRAARLIK LLRQGYTIRI 

      1690       1700       1710       1720       1730       1740 
LLWTFVQSFK ALPYVCLLIA MLFFIYAIIG MQVFGNIGID VEDEDSDEDE FQITEHNNFR 

      1750       1760       1770       1780       1790       1800 
TFFQALMLLF RSATGEAWHN IMLSCLSGKP CDKNSGILTR ECGNEFAYFY FVSFIFLCSF 

      1810       1820       1830       1840       1850       1860 
LMLNLFVAVI MDNFEYLTRD SSILGPHHLD EYVRVWAEYD PAAWGRMPYL DMYQMLRHMS 

      1870       1880       1890       1900       1910       1920 
PPLGLGKKCP ARVAYKRLLR MDLPVADDNT VHFNSTLMAL IRTALDIKIA KGGADKQQMD 

      1930       1940       1950       1960       1970       1980 
AELRKEMMAI WPNLSQKTLD LLVTPHKSTD LTVGKIYAAM MIMEYYRQSK AKKLQAMREE 

      1990       2000       2010       2020       2030       2040 
QDRTPLMFQR MEPPSPTQEG GPGQNALPST QLDPGGALMA HESGLKESPS WVTQRAQEMF 

      2050       2060       2070       2080       2090       2100 
QKTGTWSPEQ GPPTDMPNSQ PNSQSVEMRE MGRDGYSDSE HYLPMEGQGR AASMPRLPAE 

      2110       2120       2130       2140       2150       2160 
NQRRRGRPRG NNLSTISDTS PMKRSASVLG PKARRLDDYS LERVPPEENQ RHHQRRRDRS 

      2170       2180       2190       2200       2210       2220 
HRASERSLGR YTDVDTGLGT DLSMTTQSGD LPSKERDQER GRPKDRKHRQ HHHHHHHHHH 

      2230       2240       2250       2260       2270       2280 
PPPPDKDRYA QERPDHGRAR ARDQRWSRSP SEGREHMAHR QGSSSVSGSP APSTSGTSTP 

      2290       2300       2310       2320       2330       2340 
RRGRRQLPQT PSTPRPHVSY SPVIRKAGGS GPPQQQQQQQ QQQQAVARPG RAATSGPRRY 

      2350       2360       2370       2380       2390       2400 
PGPTAEPLAG DRPPTGGHSS GRSPRMERRV PGPARSESPR ACRHGGARWP ASGPHVSEGP 

      2410       2420       2430       2440       2450       2460 
PGPRHHGYYR GSDYDEADGP GSGGGEEAMA GAYDAPPPVR HASSGATGRS PRTPRASGPA 

      2470       2480       2490       2500 
CASPSRHGRR LPNGYYPAHG LARPRGPGSR KGLHEPYSES DDDWC

O00555 in FASTA format

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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools