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Voltage-dependent L-type calcium channel subunit alpha-1F (Voltage-gated calcium channel subunit alpha Cav1.4)

 CAC1F_HUMAN             Reviewed;        1977 AA.
O60840; A6NI29; F5CIQ9; O43901; O95226; Q9UHB1;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
14-APR-2009, sequence version 2.
05-DEC-2018, entry version 188.
RecName: Full=Voltage-dependent L-type calcium channel subunit alpha-1F {ECO:0000305};
AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.4;
Name=CACNA1F {ECO:0000312|HGNC:HGNC:1393}; Synonyms=CACNAF1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), AND VARIANTS
CSNB2A ASP-369; GLN-519; TRP-1060 AND HIS-1375.
TISSUE=Retina;
PubMed=9662399; DOI=10.1038/940;
Strom T.M., Nyakatura G., Apfelstedt-Sylla E., Hellebrand H.,
Lorenz B., Weber B.H.F., Wutz K., Gutwillinger N., Ruether K.,
Drescher B., Sauer C., Zrenner E., Meitinger T., Rosenthal A.,
Meindl A.;
"An L-type calcium-channel gene mutated in incomplete X-linked
congenital stationary night blindness.";
Nat. Genet. 19:260-263(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND INVOLVEMENT IN CSNB2A.
PubMed=9662400; DOI=10.1038/947;
Bech-Hansen N.T., Naylor M.J., Maybaum T.A., Pearce W.G., Koop B.,
Fishman G.A., Mets M., Musarella M.A., Boycott K.M.;
"Loss-of-function mutations in a calcium-channel alpha1-subunit gene
in Xp11.23 cause incomplete X-linked congenital stationary night
blindness.";
Nat. Genet. 19:264-267(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
PubMed=10873387; DOI=10.1006/geno.2000.6204;
Naylor M.J., Rancourt D.E., Bech-Hansen N.T.;
"Isolation and characterization of a calcium channel gene, cacna1f,
the murine orthologue of the gene for incomplete X-linked congenital
stationary night blindness.";
Genomics 66:324-327(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Retina;
PubMed=19029287; DOI=10.1124/mol.108.049981;
Sinnegger-Brauns M.J., Huber I.G., Koschak A., Wild C., Obermair G.J.,
Einzinger U., Hoda J.C., Sartori S.B., Striessnig J.;
"Expression and 1,4-dihydropyridine-binding properties of brain L-type
calcium channel isoforms.";
Mol. Pharmacol. 75:407-414(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1211-1977.
PubMed=9344658; DOI=10.1006/geno.1997.4941;
Fisher S.E., Ciccodicola A., Tanaka K., Curci A., Desicato S.,
D'Urso M., Craig I.W.;
"Sequence-based exon prediction around the synaptophysin locus reveals
a gene-rich area containing novel genes in human proximal Xp.";
Genomics 45:340-347(1997).
[7]
ALTERNATIVE SPLICING (ISOFORM 4; ISOFORM 5 AND ISOFORM 6), TISSUE
SPECIFICITY, INTERACTION WITH CABP4, AND FUNCTION.
PubMed=27226626; DOI=10.1074/jbc.M116.731737;
Haeseleer F., Williams B., Lee A.;
"Characterization of C-terminal Splice Variants of Cav1.4 Ca2+
Channels in Human Retina.";
J. Biol. Chem. 291:15663-15673(2016).
[8]
VARIANTS CSNB2A ASP-369; ASP-674 AND ASP-928.
PubMed=11281458; DOI=10.1007/s004390100461;
Boycott K.M., Maybaum T.A., Naylor M.J., Weleber R.G., Robitaille J.,
Miyake Y., Bergen A.A.B., Pierpont M.E., Pearce W.G.,
Bech-Hansen N.T.;
"A summary of 20 CACNA1F mutations identified in 36 families with
incomplete X-linked congenital stationary night blindness, and
characterization of splice variants.";
Hum. Genet. 108:91-97(2001).
[9]
VARIANTS CSNB2A ARG-74; PRO-229; ARG-261; ASP-369; CYS-753; PRO-860;
ARG-1018; TRP-1060; PRO-1079; ARG-1499; ARG-1500 AND PRO-1508.
PubMed=12111638; DOI=10.1038/sj.ejhg.5200828;
Wutz K., Sauer C., Zrenner E., Lorenz B., Alitalo T., Broghammer M.,
Hergersberg M., de la Chapelle A., Weber B.H.F., Wissinger B.,
Meindl A., Pusch C.M.;
"Thirty distinct CACNA1F mutations in 33 families with incomplete type
of XLCSNB and Cacna1f expression profiling in mouse retina.";
Eur. J. Hum. Genet. 10:449-456(2002).
[10]
VARIANTS CSNB2A ARG-150 AND ILE-635.
PubMed=12187427; DOI=10.1076/opge.23.2.71.2214;
Weleber R.G.;
"Infantile and childhood retinal blindness: a molecular perspective
(The Franceschetti Lecture).";
Ophthalmic Genet. 23:71-97(2002).
[11]
VARIANT CSNB2A THR-756, AND CHARACTERIZATION OF VARIANT CSNB2A
THR-756.
PubMed=15897456; DOI=10.1073/pnas.0501907102;
Hemara-Wahanui A., Berjukow S., Hope C.I., Dearden P.K., Wu S.-B.,
Wilson-Wheeler J., Sharp D.M., Lundon-Treweek P., Clover G.M.,
Hoda J.-C., Striessnig J., Marksteiner R., Hering S., Maw M.A.;
"A CACNA1F mutation identified in an X-linked retinal disorder shifts
the voltage dependence of Cav1.4 channel activation.";
Proc. Natl. Acad. Sci. U.S.A. 102:7553-7558(2005).
[12]
VARIANT THR-746.
PubMed=16960802; DOI=10.1086/508067;
Zeitz C., Kloeckener-Gruissem B., Forster U., Kohl S., Magyar I.,
Wissinger B., Matyas G., Borruat F.-X., Schorderet D.F., Zrenner E.,
Munier F.L., Berger W.;
"Mutations in CABP4, the gene encoding the Ca2+-binding protein 4,
cause autosomal recessive night blindness.";
Am. J. Hum. Genet. 79:657-667(2006).
[13]
INVOLVEMENT IN CORDX3.
PubMed=16505158; DOI=10.1136/jmg.2006.040741;
Jalkanen R., Maentyjaervi M., Tobias R., Isosomppi J., Sankila E.-M.,
Alitalo T., Bech-Hansen N.T.;
"X linked cone-rod dystrophy, CORDX3, is caused by a mutation in the
CACNA1F gene.";
J. Med. Genet. 43:699-704(2006).
[14]
INVOLVEMENT IN AIED.
PubMed=17525176; DOI=10.1167/iovs.06-1103;
Jalkanen R., Bech-Hansen N.T., Tobias R., Sankila E.-M.,
Maentyjaervi M., Forsius H., de la Chapelle A., Alitalo T.;
"A novel CACNA1F gene mutation causes Aland Island eye disease.";
Invest. Ophthalmol. Vis. Sci. 48:2498-2502(2007).
[15]
VARIANT CSNB2A ARG-603, AND VARIANT AIED ARG-603.
PubMed=22194652;
Vincent A., Wright T., Day M.A., Westall C.A., Heon E.;
"A novel p.Gly603Arg mutation in CACNA1F causes Aland island eye
disease and incomplete congenital stationary night blindness
phenotypes in a family.";
Mol. Vis. 17:3262-3270(2011).
-!- FUNCTION: Isoform 1: 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-1F 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, and by benzothiazepines. Activates at
more negative voltages and does not undergo calcium-dependent
inactivation (CDI), due to incoming calcium ions, during
depolarization. {ECO:0000269|PubMed:27226626}.
-!- FUNCTION: Isoform 4: Voltage-dependent L-type calcium channel
activates at more hyperpolarized voltages and exhibits a robust
calcium-dependent inactivation (CDI), due to incoming calcium
ions, during depolarizations. {ECO:0000269|PubMed:27226626}.
-!- FUNCTION: Isoform 6: Voltage-dependent L-type calcium channel
activates at more hyperpolarized voltages and exibits a robust
calcium-dependent inactivation (CDI), due to incoming calcium
ions, during depolarizations. {ECO:0000269|PubMed:27226626}.
-!- 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.
Interacts (via IQ domain) with CABP4; in a calcium independent
manner (By similarity). Isoform 4: interacts with CABP4; suppreses
robust calcium-dependent inactivation of channel whithout enhances
the hyperpolarized voltage-dependent activation (PubMed:27226626).
{ECO:0000250, ECO:0000269|PubMed:27226626}.
-!- INTERACTION:
P57796-1:CABP4; NbExp=2; IntAct=EBI-14063160, EBI-14063133;
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1; Synonyms=Cav1.4FL {ECO:0000303|PubMed:27226626};
IsoId=O60840-1; Sequence=Displayed;
Name=2;
IsoId=O60840-2; Sequence=VSP_036785;
Name=3;
IsoId=O60840-4; Sequence=VSP_045172;
Name=4; Synonyms=Cav1.4Deltaex p45,47
{ECO:0000303|PubMed:27226626};
IsoId=O60840-5; Sequence=VSP_058923, VSP_058924;
Name=5; Synonyms=Cav1.4Deltaex p45 {ECO:0000303|PubMed:27226626};
IsoId=O60840-6; Sequence=VSP_058923;
Name=6; Synonyms=Cav1.4Deltaex 47 {ECO:0000303|PubMed:27226626};
IsoId=O60840-7; Sequence=VSP_058924;
-!- TISSUE SPECIFICITY: Expression in skeletal muscle and retina
(PubMed:10873387). Isoform 4 is expressed in retina
(PubMed:27226626). {ECO:0000269|PubMed:10873387,
ECO:0000269|PubMed:27226626}.
-!- 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.
-!- DISEASE: Night blindness, congenital stationary, 2A (CSNB2A)
[MIM:300071]: A non-progressive retinal disorder characterized by
impaired night vision, often associated with nystagmus and myopia.
{ECO:0000269|PubMed:11281458, ECO:0000269|PubMed:12111638,
ECO:0000269|PubMed:12187427, ECO:0000269|PubMed:15897456,
ECO:0000269|PubMed:22194652, ECO:0000269|PubMed:9662399,
ECO:0000269|PubMed:9662400}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Cone-rod dystrophy, X-linked 3 (CORDX3) [MIM:300476]: An
inherited retinal dystrophy characterized by retinal pigment
deposits visible on fundus examination, predominantly in the
macular region, and initial loss of cone photoreceptors followed
by rod degeneration. This leads to decreased visual acuity and
sensitivity in the central visual field, followed by loss of
peripheral vision. Severe loss of vision occurs earlier than in
retinitis pigmentosa, due to cone photoreceptors degenerating at a
higher rate than rod photoreceptors.
{ECO:0000269|PubMed:16505158}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Aaland island eye disease (AIED) [MIM:300600]: A retinal
disease characterized by a combination of fundus hypopigmentation,
decreased visual acuity due to foveal hypoplasia, nystagmus,
astigmatism, protan color vision defect, myopia, and defective
dark adaptation. Except for progression of axial myopia, the
disease can be considered to be a stationary condition.
Electroretinography reveals abnormalities in both photopic and
scotopic functions. {ECO:0000269|PubMed:17525176,
ECO:0000269|PubMed:22194652}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
1.A.1.11) family. CACNA1F subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB92359.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Mutations of the CCNA1F gene; Note=Retina
International's Scientific Newsletter;
URL="http://www.retina-international.org/files/sci-news/cacnamut.htm";
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EMBL; AJ006216; CAA06916.1; -; Genomic_DNA.
EMBL; AF067227; AAD03587.1; -; mRNA.
EMBL; AJ224874; CAA12175.1; -; mRNA.
EMBL; AF201304; AAF15290.1; -; mRNA.
EMBL; JF701915; AED89557.1; -; mRNA.
EMBL; AF196779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF235097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U93305; AAB92359.1; ALT_SEQ; Genomic_DNA.
CCDS; CCDS35253.1; -. [O60840-1]
CCDS; CCDS59166.1; -. [O60840-4]
CCDS; CCDS59167.1; -. [O60840-2]
RefSeq; NP_001243718.1; NM_001256789.2. [O60840-2]
RefSeq; NP_001243719.1; NM_001256790.2. [O60840-4]
RefSeq; NP_005174.2; NM_005183.3. [O60840-1]
UniGene; Hs.632799; -.
ProteinModelPortal; O60840; -.
SMR; O60840; -.
BioGrid; 107232; 1.
IntAct; O60840; 3.
STRING; 9606.ENSP00000365441; -.
BindingDB; O60840; -.
ChEMBL; CHEMBL2363032; -.
DrugBank; DB00568; Cinnarizine.
DrugBank; DB04920; Clevidipine.
DrugBank; DB04855; Dronedarone.
DrugBank; DB01388; Mibefradil.
DrugBank; DB00393; Nimodipine.
DrugBank; DB00421; Spironolactone.
DrugBank; DB00661; Verapamil.
GuidetoPHARMACOLOGY; 531; -.
TCDB; 1.A.1.11.11; the voltage-gated ion channel (vic) superfamily.
iPTMnet; O60840; -.
PhosphoSitePlus; O60840; -.
BioMuta; CACNA1F; -.
PaxDb; O60840; -.
PeptideAtlas; O60840; -.
PRIDE; O60840; -.
ProteomicsDB; 49626; -.
ProteomicsDB; 49627; -. [O60840-2]
Ensembl; ENST00000323022; ENSP00000321618; ENSG00000102001. [O60840-2]
Ensembl; ENST00000376251; ENSP00000365427; ENSG00000102001. [O60840-4]
Ensembl; ENST00000376265; ENSP00000365441; ENSG00000102001. [O60840-1]
GeneID; 778; -.
KEGG; hsa:778; -.
UCSC; uc004dnb.3; human. [O60840-1]
CTD; 778; -.
DisGeNET; 778; -.
EuPathDB; HostDB:ENSG00000102001.12; -.
GeneCards; CACNA1F; -.
GeneReviews; CACNA1F; -.
HGNC; HGNC:1393; CACNA1F.
HPA; HPA068379; -.
MalaCards; CACNA1F; -.
MIM; 300071; phenotype.
MIM; 300110; gene.
MIM; 300476; phenotype.
MIM; 300600; phenotype.
neXtProt; NX_O60840; -.
OpenTargets; ENSG00000102001; -.
Orphanet; 178333; Aaland Islands eye disease.
Orphanet; 1872; Cone rod dystrophy.
Orphanet; 215; Congenital stationary night blindness.
PharmGKB; PA26010; -.
eggNOG; KOG2301; Eukaryota.
eggNOG; ENOG410XNP6; LUCA.
GeneTree; ENSGT00940000159855; -.
HOGENOM; HOG000231529; -.
HOVERGEN; HBG050763; -.
InParanoid; O60840; -.
KO; K04853; -.
OMA; CRGRWAG; -.
OrthoDB; EOG091G0TKO; -.
PhylomeDB; O60840; -.
TreeFam; TF312805; -.
Reactome; R-HSA-5576892; Phase 0 - rapid depolarisation.
Reactome; R-HSA-5576893; Phase 2 - plateau phase.
ChiTaRS; CACNA1F; human.
GeneWiki; Cav1.4; -.
GenomeRNAi; 778; -.
PRO; PR:O60840; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000102001; Expressed in 70 organ(s), highest expression level in right lung.
CleanEx; HS_CACNA1F; -.
ExpressionAtlas; O60840; baseline and differential.
Genevisible; O60840; HS.
GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IEA:Ensembl.
GO; GO:0001750; C:photoreceptor outer segment; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:UniProtKB.
GO; GO:0008331; F:high voltage-gated calcium channel activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:UniProtKB.
GO; GO:0070509; P:calcium ion import; IBA:GO_Central.
GO; GO:0006816; P:calcium ion transport; IBA:GO_Central.
GO; GO:0050908; P:detection of light stimulus involved in visual perception; IMP:UniProtKB.
GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; IDA:UniProtKB.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
GO; GO:0050856; P:regulation of T cell receptor signaling pathway; IEA:InterPro.
GO; GO:0043029; P:T cell homeostasis; IEA:InterPro.
GO; GO:0007601; P:visual perception; IMP:UniProtKB.
Gene3D; 1.20.120.350; -; 4.
InterPro; IPR031688; CAC1F_C.
InterPro; IPR031649; GPHH_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR014873; VDCC_a1su_IQ.
InterPro; IPR030157; VDCC_L_a1F.
InterPro; IPR005446; VDCC_L_a1su.
InterPro; IPR002077; VDCCAlpha1.
InterPro; IPR027359; Volt_channel_dom_sf.
PANTHER; PTHR10037:SF184; PTHR10037:SF184; 1.
Pfam; PF08763; Ca_chan_IQ; 1.
Pfam; PF16885; CAC1F_C; 1.
Pfam; PF16905; GPHH; 1.
Pfam; PF00520; Ion_trans; 4.
PRINTS; PR00167; CACHANNEL.
PRINTS; PR01630; LVDCCALPHA1.
SMART; SM01062; Ca_chan_IQ; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Calcium channel; Calcium transport;
Complete proteome; Cone-rod dystrophy;
Congenital stationary night blindness; Disease mutation;
Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
Metal-binding; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; Sensory transduction; Transmembrane; Transmembrane helix;
Transport; Vision; Voltage-gated channel.
CHAIN 1 1977 Voltage-dependent L-type calcium channel
subunit alpha-1F.
/FTId=PRO_0000053950.
TOPO_DOM 1 92 Cytoplasmic. {ECO:0000255}.
TRANSMEM 93 111 Helical; Name=S1 of repeat I.
{ECO:0000255}.
TOPO_DOM 112 129 Extracellular. {ECO:0000255}.
TRANSMEM 130 149 Helical; Name=S2 of repeat I.
{ECO:0000255}.
TOPO_DOM 150 161 Cytoplasmic. {ECO:0000255}.
TRANSMEM 162 180 Helical; Name=S3 of repeat I.
{ECO:0000255}.
TOPO_DOM 181 201 Extracellular. {ECO:0000255}.
TRANSMEM 202 220 Helical; Name=S4 of repeat I.
{ECO:0000255}.
TOPO_DOM 221 239 Cytoplasmic. {ECO:0000255}.
TRANSMEM 240 259 Helical; Name=S5 of repeat I.
{ECO:0000255}.
TOPO_DOM 260 347 Extracellular. {ECO:0000255}.
TRANSMEM 348 372 Helical; Name=S6 of repeat I.
{ECO:0000255}.
TOPO_DOM 373 529 Cytoplasmic. {ECO:0000255}.
TRANSMEM 530 549 Helical; Name=S1 of repeat II.
{ECO:0000255}.
TOPO_DOM 550 564 Extracellular. {ECO:0000255}.
TRANSMEM 565 583 Helical; Name=S2 of repeat II.
{ECO:0000255}.
TOPO_DOM 584 591 Cytoplasmic. {ECO:0000255}.
TRANSMEM 592 610 Helical; Name=S3 of repeat II.
{ECO:0000255}.
TOPO_DOM 611 620 Extracellular. {ECO:0000255}.
TRANSMEM 621 639 Helical; Name=S4 of repeat II.
{ECO:0000255}.
TOPO_DOM 640 658 Cytoplasmic. {ECO:0000255}.
TRANSMEM 659 679 Helical; Name=S5 of repeat II.
{ECO:0000255}.
TOPO_DOM 680 733 Extracellular. {ECO:0000255}.
TRANSMEM 734 758 Helical; Name=S6 of repeat II.
{ECO:0000255}.
TOPO_DOM 759 871 Cytoplasmic. {ECO:0000255}.
TRANSMEM 872 890 Helical; Name=S1 of repeat III.
{ECO:0000255}.
TOPO_DOM 891 906 Extracellular. {ECO:0000255}.
TRANSMEM 907 926 Helical; Name=S2 of repeat III.
{ECO:0000255}.
TOPO_DOM 927 938 Cytoplasmic. {ECO:0000255}.
TRANSMEM 939 957 Helical; Name=S3 of repeat III.
{ECO:0000255}.
TOPO_DOM 958 963 Extracellular. {ECO:0000255}.
TRANSMEM 964 983 Helical; Name=S4 of repeat III.
{ECO:0000255}.
TOPO_DOM 984 1002 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1003 1022 Helical; Name=S5 of repeat III.
{ECO:0000255}.
TOPO_DOM 1023 1112 Extracellular. {ECO:0000255}.
TRANSMEM 1113 1133 Helical; Name=S6 of repeat III.
{ECO:0000255}.
TOPO_DOM 1134 1190 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1191 1209 Helical; Name=S1 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1210 1224 Extracellular. {ECO:0000255}.
TRANSMEM 1225 1244 Helical; Name=S2 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1245 1251 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1252 1273 Helical; Name=S3 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1274 1290 Extracellular. {ECO:0000255}.
TRANSMEM 1291 1310 Helical; Name=S4 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1311 1329 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1330 1349 Helical; Name=S5 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1350 1416 Extracellular. {ECO:0000255}.
TRANSMEM 1417 1441 Helical; Name=S6 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1442 1977 Cytoplasmic. {ECO:0000255}.
REPEAT 79 375 I.
REPEAT 515 761 II.
REPEAT 858 1140 III.
REPEAT 1177 1444 IV.
CA_BIND 1470 1481 {ECO:0000250}.
REGION 395 412 Binding to the beta subunit.
{ECO:0000250}.
REGION 1060 1150 Dihydropyridine binding. {ECO:0000250}.
REGION 1397 1463 Dihydropyridine binding. {ECO:0000250}.
REGION 1409 1452 Phenylalkylamine binding. {ECO:0000250}.
COMPBIAS 659 665 Poly-Leu.
COMPBIAS 794 799 Poly-Glu.
COMPBIAS 809 825 Poly-Glu.
COMPBIAS 1121 1124 Poly-Ile.
COMPBIAS 1640 1645 Poly-Glu.
SITE 330 330 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 711 711 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1086 1086 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1383 1383 Calcium ion selectivity and permeability.
{ECO:0000250}.
MOD_RES 1452 1452 Phosphoserine; by PKA. {ECO:0000255}.
CARBOHYD 295 295 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 9 86 DTTPEPSPANGAGPGPEWGLCPGPPAVEGESSGASGLGTPK
RRNQHSKHKTVAVASAQRSPRALFCLTLANPLRRSCI ->
GERILPSLQTLGA (in isoform 3).
{ECO:0000303|PubMed:9662400}.
/FTId=VSP_045172.
VAR_SEQ 427 437 Missing (in isoform 2).
{ECO:0000303|PubMed:19029287,
ECO:0000303|PubMed:9662399}.
/FTId=VSP_036785.
VAR_SEQ 1756 1775 Missing (in isoform 4 and isoform 5).
{ECO:0000303|PubMed:27226626}.
/FTId=VSP_058923.
VAR_SEQ 1836 1901 Missing (in isoform 4 and isoform 6).
{ECO:0000303|PubMed:27226626}.
/FTId=VSP_058924.
VARIANT 14 14 P -> L (in dbSNP:rs6520408).
/FTId=VAR_030807.
VARIANT 74 74 C -> R (in CSNB2A).
{ECO:0000269|PubMed:12111638}.
/FTId=VAR_030808.
VARIANT 150 150 G -> R (in CSNB2A).
{ECO:0000269|PubMed:12187427}.
/FTId=VAR_030809.
VARIANT 229 229 S -> P (in CSNB2A).
{ECO:0000269|PubMed:12111638}.
/FTId=VAR_030810.
VARIANT 261 261 G -> R (in CSNB2A).
{ECO:0000269|PubMed:12111638}.
/FTId=VAR_030811.
VARIANT 369 369 G -> D (in CSNB2A; dbSNP:rs122456133).
{ECO:0000269|PubMed:11281458,
ECO:0000269|PubMed:12111638,
ECO:0000269|PubMed:9662399}.
/FTId=VAR_001504.
VARIANT 519 519 R -> Q (in CSNB2A; dbSNP:rs34162630).
{ECO:0000269|PubMed:9662399}.
/FTId=VAR_001505.
VARIANT 603 603 G -> R (in AIED and CSNB2A;
dbSNP:rs201654095).
{ECO:0000269|PubMed:22194652}.
/FTId=VAR_071433.
VARIANT 635 635 V -> I (in CSNB2A; dbSNP:rs141010716).
{ECO:0000269|PubMed:12187427}.
/FTId=VAR_030812.
VARIANT 674 674 G -> D (in CSNB2A).
{ECO:0000269|PubMed:11281458}.
/FTId=VAR_030813.
VARIANT 746 746 N -> T (in dbSNP:rs141159097).
{ECO:0000269|PubMed:16960802}.
/FTId=VAR_029376.
VARIANT 753 753 F -> C (in CSNB2A).
{ECO:0000269|PubMed:12111638}.
/FTId=VAR_030814.
VARIANT 756 756 I -> T (in CSNB2A; increases the number
of mutant channels open at physiologic
membrane potential and allows for
persistent Ca(2+) entry due to reduced
channel inactivation resulting in a gain-
of-function defect; dbSNP:rs122456136).
{ECO:0000269|PubMed:15897456}.
/FTId=VAR_030815.
VARIANT 860 860 L -> P (in CSNB2A).
{ECO:0000269|PubMed:12111638}.
/FTId=VAR_030816.
VARIANT 928 928 A -> D (in CSNB2A).
{ECO:0000269|PubMed:11281458}.
/FTId=VAR_030817.
VARIANT 1018 1018 G -> R (in CSNB2A; dbSNP:rs1249437161).
{ECO:0000269|PubMed:12111638}.
/FTId=VAR_030818.
VARIANT 1060 1060 R -> W (in CSNB2A).
{ECO:0000269|PubMed:12111638,
ECO:0000269|PubMed:9662399}.
/FTId=VAR_001506.
VARIANT 1079 1079 L -> P (in CSNB2A).
{ECO:0000269|PubMed:12111638}.
/FTId=VAR_030819.
VARIANT 1259 1259 A -> T (in dbSNP:rs34308720).
/FTId=VAR_055662.
VARIANT 1270 1270 A -> T (in dbSNP:rs34308720).
/FTId=VAR_031822.
VARIANT 1375 1375 L -> H (in CSNB2A).
{ECO:0000269|PubMed:9662399}.
/FTId=VAR_001507.
VARIANT 1499 1499 C -> R (in CSNB2A).
{ECO:0000269|PubMed:12111638}.
/FTId=VAR_030820.
VARIANT 1500 1500 P -> R (in CSNB2A).
{ECO:0000269|PubMed:12111638}.
/FTId=VAR_030821.
VARIANT 1508 1508 L -> P (in CSNB2A).
{ECO:0000269|PubMed:12111638}.
/FTId=VAR_030822.
VARIANT 1930 1930 R -> H (in dbSNP:rs33910054).
/FTId=VAR_054818.
CONFLICT 1236 1236 E -> V (in Ref. 6; AAB92359).
{ECO:0000305}.
CONFLICT 1860 1860 A -> G (in Ref. 6; AAB92359).
{ECO:0000305}.
SEQUENCE 1977 AA; 220678 MW; 354336550C6D8E73 CRC64;
MSESEGGKDT TPEPSPANGA GPGPEWGLCP GPPAVEGESS GASGLGTPKR RNQHSKHKTV
AVASAQRSPR ALFCLTLANP LRRSCISIVE WKPFDILILL TIFANCVALG VYIPFPEDDS
NTANHNLEQV EYVFLVIFTV ETVLKIVAYG LVLHPSAYIR NGWNLLDFII VVVGLFSVLL
EQGPGRPGDA PHTGGKPGGF DVKALRAFRV LRPLRLVSGV PSLHIVLNSI MKALVPLLHI
ALLVLFVIII YAIIGLELFL GRMHKTCYFL GSDMEAEEDP SPCASSGSGR ACTLNQTECR
GRWPGPNGGI TNFDNFFFAM LTVFQCVTME GWTDVLYWMQ DAMGYELPWV YFVSLVIFGS
FFVLNLVLGV LSGEFSKERE KAKARGDFQK QREKQQMEED LRGYLDWITQ AEELDMEDPS
ADDNLGSMAE EGRAGHRPQL AELTNRRRGR LRWFSHSTRS THSTSSHASL PASDTGSMTE
TQGDEDEEEG ALASCTRCLN KIMKTRVCRR LRRANRVLRA RCRRAVKSNA CYWAVLLLVF
LNTLTIASEH HGQPVWLTQI QEYANKVLLC LFTVEMLLKL YGLGPSAYVS SFFNRFDCFV
VCGGILETTL VEVGAMQPLG ISVLRCVRLL RIFKVTRHWA SLSNLVASLL NSMKSIASLL
LLLFLFIIIF SLLGMQLFGG KFNFDQTHTK RSTFDTFPQA LLTVFQILTG EDWNVVMYDG
IMAYGGPFFP GMLVCIYFII LFICGNYILL NVFLAIAVDN LASGDAGTAK DKGGEKSNEK
DLPQENEGLV PGVEKEEEEG ARREGADMEE EEEEEEEEEE EEEEEGAGGV ELLQEVVPKE
KVVPIPEGSA FFCLSQTNPL RKGCHTLIHH HVFTNLILVF IILSSVSLAA EDPIRAHSFR
NHILGYFDYA FTSIFTVEIL LKMTVFGAFL HRGSFCRSWF NMLDLLVVSV SLISFGIHSS
AISVVKILRV LRVLRPLRAI NRAKGLKHVV QCVFVAIRTI GNIMIVTTLL QFMFACIGVQ
LFKGKFYTCT DEAKHTPQEC KGSFLVYPDG DVSRPLVRER LWVNSDFNFD NVLSAMMALF
TVSTFEGWPA LLYKAIDAYA EDHGPIYNYR VEISVFFIVY IIIIAFFMMN IFVGFVIITF
RAQGEQEYQN CELDKNQRQC VEYALKAQPL RRYIPKNPHQ YRVWATVNSA AFEYLMFLLI
LLNTVALAMQ HYEQTAPFNY AMDILNMVFT GLFTIEMVLK IIAFKPKHYF TDAWNTFDAL
IVVGSIVDIA VTEVNNGGHL GESSEDSSRI SITFFRLFRV MRLVKLLSKG EGIRTLLWTF
IKSFQALPYV ALLIAMIFFI YAVIGMQMFG KVALQDGTQI NRNNNFQTFP QAVLLLFRCA
TGEAWQEIML ASLPGNRCDP ESDFGPGEEF TCGSNFAIAY FISFFMLCAF LIINLFVAVI
MDNFDYLTRD WSILGPHHLD EFKRIWSEYD PGAKGRIKHL DVVALLRRIQ PPLGFGKLCP
HRVACKRLVA MNMPLNSDGT VTFNATLFAL VRTSLKIKTE GNLEQANQEL RIVIKKIWKR
MKQKLLDEVI PPPDEEEVTV GKFYATFLIQ DYFRKFRRRK EKGLLGNDAA PSTSSALQAG
LRSLQDLGPE MRQALTCDTE EEEEEGQEGV EEEDEKDLET NKATMVSQPS ARRGSGISVS
LPVGDRLPDS LSFGPSDDDR GTPTSSQPSV PQAGSNTHRR GSGALIFTIP EEGNSQPKGT
KGQNKQDEDE EVPDRLSYLD EQAGTPPCSV LLPPHRAQRY MDGHLVPRRR LLPPTPAGRK
PSFTIQCLQR QGSCEDLPIP GTYHRGRNSG PNRAQGSWAT PPQRGRLLYA PLLLVEEGAA
GEGYLGRSSG PLRTFTCLHV PGTHSDPSHG KRGSADSLVE AVLISEGLGL FARDPRFVAL
AKQEIADACR LTLDEMDNAA SDLLAQGTSS LYSDEESILS RFDEEDLGDE MACVHAL


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