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Database: UniProt
Entry: CAC1F_HUMAN
LinkDB: CAC1F_HUMAN
Original site: CAC1F_HUMAN 
ID   CAC1F_HUMAN             Reviewed;        1977 AA.
AC   O60840; A6NI29; F5CIQ9; O43901; O95226; Q9UHB1;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 2.
DT   25-OCT-2017, entry version 179.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha-1F {ECO:0000305};
DE   AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.4;
GN   Name=CACNA1F {ECO:0000312|HGNC:HGNC:1393}; Synonyms=CACNAF1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), AND VARIANTS
RP   CSNB2A ASP-369; GLN-519; TRP-1060 AND HIS-1375.
RC   TISSUE=Retina;
RX   PubMed=9662399; DOI=10.1038/940;
RA   Strom T.M., Nyakatura G., Apfelstedt-Sylla E., Hellebrand H.,
RA   Lorenz B., Weber B.H.F., Wutz K., Gutwillinger N., Ruether K.,
RA   Drescher B., Sauer C., Zrenner E., Meitinger T., Rosenthal A.,
RA   Meindl A.;
RT   "An L-type calcium-channel gene mutated in incomplete X-linked
RT   congenital stationary night blindness.";
RL   Nat. Genet. 19:260-263(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND INVOLVEMENT IN CSNB2A.
RX   PubMed=9662400; DOI=10.1038/947;
RA   Bech-Hansen N.T., Naylor M.J., Maybaum T.A., Pearce W.G., Koop B.,
RA   Fishman G.A., Mets M., Musarella M.A., Boycott K.M.;
RT   "Loss-of-function mutations in a calcium-channel alpha1-subunit gene
RT   in Xp11.23 cause incomplete X-linked congenital stationary night
RT   blindness.";
RL   Nat. Genet. 19:264-267(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX   PubMed=10873387; DOI=10.1006/geno.2000.6204;
RA   Naylor M.J., Rancourt D.E., Bech-Hansen N.T.;
RT   "Isolation and characterization of a calcium channel gene, cacna1f,
RT   the murine orthologue of the gene for incomplete X-linked congenital
RT   stationary night blindness.";
RL   Genomics 66:324-327(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Retina;
RX   PubMed=19029287; DOI=10.1124/mol.108.049981;
RA   Sinnegger-Brauns M.J., Huber I.G., Koschak A., Wild C., Obermair G.J.,
RA   Einzinger U., Hoda J.C., Sartori S.B., Striessnig J.;
RT   "Expression and 1,4-dihydropyridine-binding properties of brain L-type
RT   calcium channel isoforms.";
RL   Mol. Pharmacol. 75:407-414(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA   Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA   Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA   Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA   Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA   Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA   Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA   Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA   Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA   Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA   Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA   Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA   Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA   Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA   Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA   Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA   Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA   Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA   Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA   Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA   Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA   Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA   Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA   Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA   de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA   Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA   Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA   Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA   Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA   Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA   Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA   Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA   Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA   Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA   Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA   Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA   Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA   Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA   Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA   Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA   Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA   Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA   Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA   Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1211-1977.
RX   PubMed=9344658; DOI=10.1006/geno.1997.4941;
RA   Fisher S.E., Ciccodicola A., Tanaka K., Curci A., Desicato S.,
RA   D'Urso M., Craig I.W.;
RT   "Sequence-based exon prediction around the synaptophysin locus reveals
RT   a gene-rich area containing novel genes in human proximal Xp.";
RL   Genomics 45:340-347(1997).
RN   [7]
RP   ALTERNATIVE SPLICING (ISOFORM 4; ISOFORM 5 AND ISOFORM 6), TISSUE
RP   SPECIFICITY, INTERACTION WITH CABP4, AND FUNCTION.
RX   PubMed=27226626; DOI=10.1074/jbc.M116.731737;
RA   Haeseleer F., Williams B., Lee A.;
RT   "Characterization of C-terminal Splice Variants of Cav1.4 Ca2+
RT   Channels in Human Retina.";
RL   J. Biol. Chem. 291:15663-15673(2016).
RN   [8]
RP   VARIANTS CSNB2A ASP-369; ASP-674 AND ASP-928.
RX   PubMed=11281458; DOI=10.1007/s004390100461;
RA   Boycott K.M., Maybaum T.A., Naylor M.J., Weleber R.G., Robitaille J.,
RA   Miyake Y., Bergen A.A.B., Pierpont M.E., Pearce W.G.,
RA   Bech-Hansen N.T.;
RT   "A summary of 20 CACNA1F mutations identified in 36 families with
RT   incomplete X-linked congenital stationary night blindness, and
RT   characterization of splice variants.";
RL   Hum. Genet. 108:91-97(2001).
RN   [9]
RP   VARIANTS CSNB2A ARG-74; PRO-229; ARG-261; ASP-369; CYS-753; PRO-860;
RP   ARG-1018; TRP-1060; PRO-1079; ARG-1499; ARG-1500 AND PRO-1508.
RX   PubMed=12111638; DOI=10.1038/sj.ejhg.5200828;
RA   Wutz K., Sauer C., Zrenner E., Lorenz B., Alitalo T., Broghammer M.,
RA   Hergersberg M., de la Chapelle A., Weber B.H.F., Wissinger B.,
RA   Meindl A., Pusch C.M.;
RT   "Thirty distinct CACNA1F mutations in 33 families with incomplete type
RT   of XLCSNB and Cacna1f expression profiling in mouse retina.";
RL   Eur. J. Hum. Genet. 10:449-456(2002).
RN   [10]
RP   VARIANTS CSNB2A ARG-150 AND ILE-635.
RX   PubMed=12187427; DOI=10.1076/opge.23.2.71.2214;
RA   Weleber R.G.;
RT   "Infantile and childhood retinal blindness: a molecular perspective
RT   (The Franceschetti Lecture).";
RL   Ophthalmic Genet. 23:71-97(2002).
RN   [11]
RP   VARIANT CSNB2A THR-756, AND CHARACTERIZATION OF VARIANT CSNB2A
RP   THR-756.
RX   PubMed=15897456; DOI=10.1073/pnas.0501907102;
RA   Hemara-Wahanui A., Berjukow S., Hope C.I., Dearden P.K., Wu S.-B.,
RA   Wilson-Wheeler J., Sharp D.M., Lundon-Treweek P., Clover G.M.,
RA   Hoda J.-C., Striessnig J., Marksteiner R., Hering S., Maw M.A.;
RT   "A CACNA1F mutation identified in an X-linked retinal disorder shifts
RT   the voltage dependence of Cav1.4 channel activation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:7553-7558(2005).
RN   [12]
RP   VARIANT THR-746.
RX   PubMed=16960802; DOI=10.1086/508067;
RA   Zeitz C., Kloeckener-Gruissem B., Forster U., Kohl S., Magyar I.,
RA   Wissinger B., Matyas G., Borruat F.-X., Schorderet D.F., Zrenner E.,
RA   Munier F.L., Berger W.;
RT   "Mutations in CABP4, the gene encoding the Ca2+-binding protein 4,
RT   cause autosomal recessive night blindness.";
RL   Am. J. Hum. Genet. 79:657-667(2006).
RN   [13]
RP   INVOLVEMENT IN CORDX3.
RX   PubMed=16505158; DOI=10.1136/jmg.2006.040741;
RA   Jalkanen R., Maentyjaervi M., Tobias R., Isosomppi J., Sankila E.-M.,
RA   Alitalo T., Bech-Hansen N.T.;
RT   "X linked cone-rod dystrophy, CORDX3, is caused by a mutation in the
RT   CACNA1F gene.";
RL   J. Med. Genet. 43:699-704(2006).
RN   [14]
RP   INVOLVEMENT IN AIED.
RX   PubMed=17525176; DOI=10.1167/iovs.06-1103;
RA   Jalkanen R., Bech-Hansen N.T., Tobias R., Sankila E.-M.,
RA   Maentyjaervi M., Forsius H., de la Chapelle A., Alitalo T.;
RT   "A novel CACNA1F gene mutation causes Aland Island eye disease.";
RL   Invest. Ophthalmol. Vis. Sci. 48:2498-2502(2007).
RN   [15]
RP   VARIANT CSNB2A ARG-603, AND VARIANT AIED ARG-603.
RX   PubMed=22194652;
RA   Vincent A., Wright T., Day M.A., Westall C.A., Heon E.;
RT   "A novel p.Gly603Arg mutation in CACNA1F causes Aland island eye
RT   disease and incomplete congenital stationary night blindness
RT   phenotypes in a family.";
RL   Mol. Vis. 17:3262-3270(2011).
CC   -!- FUNCTION: Isoform 1: Voltage-sensitive calcium channels (VSCC)
CC       mediate the entry of calcium ions into excitable cells and are
CC       also involved in a variety of calcium-dependent processes,
CC       including muscle contraction, hormone or neurotransmitter release,
CC       gene expression, cell motility, cell division and cell death. The
CC       isoform alpha-1F gives rise to L-type calcium currents. Long-
CC       lasting (L-type) calcium channels belong to the 'high-voltage
CC       activated' (HVA) group. They are blocked by dihydropyridines
CC       (DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-
CC       IIIA (omega-Aga-IIIA). They are however insensitive to omega-
CC       conotoxin-GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-
CC       IVA). Activates at more negative voltages and does not undergo
CC       calcium-dependent inactivation (CDI), due to incoming calcium
CC       ions, during depolarization. {ECO:0000269|PubMed:27226626}.
CC   -!- FUNCTION: Isoform 4: Voltage-dependent L-type calcium channel
CC       activates at more hyperpolarized voltages and exibits a robust
CC       calcium-dependent inactivation (CDI), due to incoming calcium
CC       ions, during depolarizations. {ECO:0000269|PubMed:27226626}.
CC   -!- FUNCTION: Isoform 6: Voltage-dependent L-type calcium channel
CC       activates at more hyperpolarized voltages and exibits a robust
CC       calcium-dependent inactivation (CDI), due to incoming calcium
CC       ions, during depolarizations. {ECO:0000269|PubMed:27226626}.
CC   -!- SUBUNIT: Voltage-dependent calcium channels are multisubunit
CC       complexes, consisting of alpha-1, alpha-2, beta and delta subunits
CC       in a 1:1:1:1 ratio. The channel activity is directed by the pore-
CC       forming and voltage-sensitive alpha-1 subunit. In many cases, this
CC       subunit is sufficient to generate voltage-sensitive calcium
CC       channel activity. The auxiliary subunits beta and alpha-2/delta
CC       linked by a disulfide bridge regulate the channel activity.
CC       Interacts (via IQ domain) with CABP4; in a calcium independent
CC       manner (By similarity). Isoform 4: interacts with CABP4; suppreses
CC       robust calcium-dependent inactivation of channel whithout enhances
CC       the hyperpolarized voltage-dependent activation (PubMed:27226626).
CC       {ECO:0000250, ECO:0000269|PubMed:27226626}.
CC   -!- INTERACTION:
CC       P57796-1:CABP4; NbExp=2; IntAct=EBI-14063160, EBI-14063133;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1; Synonyms=Cav1.4FL {ECO:0000303|PubMed:27226626};
CC         IsoId=O60840-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O60840-2; Sequence=VSP_036785;
CC       Name=3;
CC         IsoId=O60840-4; Sequence=VSP_045172;
CC       Name=4; Synonyms=Cav1.4Deltaex p45,47
CC       {ECO:0000303|PubMed:27226626};
CC         IsoId=O60840-5; Sequence=VSP_058923, VSP_058924;
CC       Name=5; Synonyms=Cav1.4Deltaex p45 {ECO:0000303|PubMed:27226626};
CC         IsoId=O60840-6; Sequence=VSP_058923;
CC       Name=6; Synonyms=Cav1.4Deltaex 47 {ECO:0000303|PubMed:27226626};
CC         IsoId=O60840-7; Sequence=VSP_058924;
CC   -!- TISSUE SPECIFICITY: Expression in skeletal muscle and retina
CC       (PubMed:10873387). Isoform 4 is expressed in retina
CC       (PubMed:27226626). {ECO:0000269|PubMed:10873387,
CC       ECO:0000269|PubMed:27226626}.
CC   -!- DOMAIN: Each of the four internal repeats contains five
CC       hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one
CC       positively charged transmembrane segment (S4). S4 segments
CC       probably represent the voltage-sensor and are characterized by a
CC       series of positively charged amino acids at every third position.
CC   -!- DISEASE: Night blindness, congenital stationary, 2A (CSNB2A)
CC       [MIM:300071]: A non-progressive retinal disorder characterized by
CC       impaired night vision, often associated with nystagmus and myopia.
CC       {ECO:0000269|PubMed:11281458, ECO:0000269|PubMed:12111638,
CC       ECO:0000269|PubMed:12187427, ECO:0000269|PubMed:15897456,
CC       ECO:0000269|PubMed:22194652, ECO:0000269|PubMed:9662399,
CC       ECO:0000269|PubMed:9662400}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Cone-rod dystrophy, X-linked 3 (CORDX3) [MIM:300476]: An
CC       inherited retinal dystrophy characterized by retinal pigment
CC       deposits visible on fundus examination, predominantly in the
CC       macular region, and initial loss of cone photoreceptors followed
CC       by rod degeneration. This leads to decreased visual acuity and
CC       sensitivity in the central visual field, followed by loss of
CC       peripheral vision. Severe loss of vision occurs earlier than in
CC       retinitis pigmentosa, due to cone photoreceptors degenerating at a
CC       higher rate than rod photoreceptors.
CC       {ECO:0000269|PubMed:16505158}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Aaland island eye disease (AIED) [MIM:300600]: A retinal
CC       disease characterized by a combination of fundus hypopigmentation,
CC       decreased visual acuity due to foveal hypoplasia, nystagmus,
CC       astigmatism, protan color vision defect, myopia, and defective
CC       dark adaptation. Except for progression of axial myopia, the
CC       disease can be considered to be a stationary condition.
CC       Electroretinography reveals abnormalities in both photopic and
CC       scotopic functions. {ECO:0000269|PubMed:17525176,
CC       ECO:0000269|PubMed:22194652}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC       1.A.1.11) family. CACNA1F subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB92359.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Mutations of the CCNA1F gene; Note=Retina
CC       International's Scientific Newsletter;
CC       URL="http://www.retina-international.org/files/sci-news/cacnamut.htm";
DR   EMBL; AJ006216; CAA06916.1; -; Genomic_DNA.
DR   EMBL; AF067227; AAD03587.1; -; mRNA.
DR   EMBL; AJ224874; CAA12175.1; -; mRNA.
DR   EMBL; AF201304; AAF15290.1; -; mRNA.
DR   EMBL; JF701915; AED89557.1; -; mRNA.
DR   EMBL; AF196779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF235097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; U93305; AAB92359.1; ALT_SEQ; Genomic_DNA.
DR   CCDS; CCDS35253.1; -. [O60840-1]
DR   CCDS; CCDS59166.1; -. [O60840-4]
DR   CCDS; CCDS59167.1; -. [O60840-2]
DR   RefSeq; NP_001243718.1; NM_001256789.2. [O60840-2]
DR   RefSeq; NP_001243719.1; NM_001256790.2. [O60840-4]
DR   RefSeq; NP_005174.2; NM_005183.3. [O60840-1]
DR   UniGene; Hs.632799; -.
DR   ProteinModelPortal; O60840; -.
DR   SMR; O60840; -.
DR   BioGrid; 107232; 1.
DR   IntAct; O60840; 3.
DR   STRING; 9606.ENSP00000365441; -.
DR   BindingDB; O60840; -.
DR   ChEMBL; CHEMBL2363032; -.
DR   DrugBank; DB00568; Cinnarizine.
DR   DrugBank; DB04920; Clevidipine.
DR   DrugBank; DB04855; Dronedarone.
DR   DrugBank; DB01388; Mibefradil.
DR   DrugBank; DB00393; Nimodipine.
DR   DrugBank; DB00421; Spironolactone.
DR   DrugBank; DB00661; Verapamil.
DR   GuidetoPHARMACOLOGY; 531; -.
DR   TCDB; 1.A.1.11.11; the voltage-gated ion channel (vic) superfamily.
DR   iPTMnet; O60840; -.
DR   PhosphoSitePlus; O60840; -.
DR   BioMuta; CACNA1F; -.
DR   PaxDb; O60840; -.
DR   PeptideAtlas; O60840; -.
DR   PRIDE; O60840; -.
DR   Ensembl; ENST00000323022; ENSP00000321618; ENSG00000102001. [O60840-2]
DR   Ensembl; ENST00000376251; ENSP00000365427; ENSG00000102001. [O60840-4]
DR   Ensembl; ENST00000376265; ENSP00000365441; ENSG00000102001. [O60840-1]
DR   GeneID; 778; -.
DR   KEGG; hsa:778; -.
DR   UCSC; uc004dnb.3; human. [O60840-1]
DR   CTD; 778; -.
DR   DisGeNET; 778; -.
DR   EuPathDB; HostDB:ENSG00000102001.12; -.
DR   GeneCards; CACNA1F; -.
DR   GeneReviews; CACNA1F; -.
DR   HGNC; HGNC:1393; CACNA1F.
DR   MalaCards; CACNA1F; -.
DR   MIM; 300071; phenotype.
DR   MIM; 300110; gene.
DR   MIM; 300476; phenotype.
DR   MIM; 300600; phenotype.
DR   neXtProt; NX_O60840; -.
DR   OpenTargets; ENSG00000102001; -.
DR   Orphanet; 178333; Aland Islands eye disease.
DR   Orphanet; 1872; Cone rod dystrophy.
DR   Orphanet; 215; Congenital stationary night blindness.
DR   PharmGKB; PA26010; -.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   HOGENOM; HOG000231529; -.
DR   HOVERGEN; HBG050763; -.
DR   InParanoid; O60840; -.
DR   KO; K04853; -.
DR   OMA; LNQTECR; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   PhylomeDB; O60840; -.
DR   TreeFam; TF312805; -.
DR   Reactome; R-HSA-5576892; Phase 0 - rapid depolarisation.
DR   Reactome; R-HSA-5576893; Phase 2 - plateau phase.
DR   ChiTaRS; CACNA1F; human.
DR   GeneWiki; Cav1.4; -.
DR   GenomeRNAi; 778; -.
DR   PRO; PR:O60840; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   Bgee; ENSG00000102001; -.
DR   CleanEx; HS_CACNA1F; -.
DR   ExpressionAtlas; O60840; baseline and differential.
DR   Genevisible; O60840; HS.
DR   GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR   GO; GO:0043204; C:perikaryon; IEA:Ensembl.
DR   GO; GO:0001750; C:photoreceptor outer segment; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:UniProtKB.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:UniProtKB.
DR   GO; GO:0061337; P:cardiac conduction; TAS:Reactome.
DR   GO; GO:0050908; P:detection of light stimulus involved in visual perception; IMP:UniProtKB.
DR   GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR   GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; IDA:UniProtKB.
DR   GO; GO:0050856; P:regulation of T cell receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0043029; P:T cell homeostasis; IEA:InterPro.
DR   GO; GO:0007601; P:visual perception; IMP:UniProtKB.
DR   InterPro; IPR031688; CAC1F_C.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR030157; VDCC_L_a1F.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF184; PTHR10037:SF184; 1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16885; CAC1F_C; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01630; LVDCCALPHA1.
DR   SMART; SM01062; Ca_chan_IQ; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW   Complete proteome; Cone-rod dystrophy;
KW   Congenital stationary night blindness; Disease mutation;
KW   Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
KW   Metal-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW   Repeat; Sensory transduction; Transmembrane; Transmembrane helix;
KW   Transport; Vision; Voltage-gated channel.
FT   CHAIN         1   1977       Voltage-dependent L-type calcium channel
FT                                subunit alpha-1F.
FT                                /FTId=PRO_0000053950.
FT   TOPO_DOM      1     92       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     93    111       Helical; Name=S1 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    112    129       Extracellular. {ECO:0000255}.
FT   TRANSMEM    130    149       Helical; Name=S2 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    150    161       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    162    180       Helical; Name=S3 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    181    201       Extracellular. {ECO:0000255}.
FT   TRANSMEM    202    220       Helical; Name=S4 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    221    239       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    240    259       Helical; Name=S5 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    260    347       Extracellular. {ECO:0000255}.
FT   TRANSMEM    348    372       Helical; Name=S6 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    373    529       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    530    549       Helical; Name=S1 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    550    564       Extracellular. {ECO:0000255}.
FT   TRANSMEM    565    583       Helical; Name=S2 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    584    591       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    592    610       Helical; Name=S3 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    611    620       Extracellular. {ECO:0000255}.
FT   TRANSMEM    621    639       Helical; Name=S4 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    640    658       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    659    679       Helical; Name=S5 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    680    733       Extracellular. {ECO:0000255}.
FT   TRANSMEM    734    758       Helical; Name=S6 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    759    871       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    872    890       Helical; Name=S1 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM    891    906       Extracellular. {ECO:0000255}.
FT   TRANSMEM    907    926       Helical; Name=S2 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM    927    938       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    939    957       Helical; Name=S3 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM    958    963       Extracellular. {ECO:0000255}.
FT   TRANSMEM    964    983       Helical; Name=S4 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM    984   1002       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1003   1022       Helical; Name=S5 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1023   1112       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1113   1133       Helical; Name=S6 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1134   1190       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1191   1209       Helical; Name=S1 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1210   1224       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1225   1244       Helical; Name=S2 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1245   1251       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1252   1273       Helical; Name=S3 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1274   1290       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1291   1310       Helical; Name=S4 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1311   1329       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1330   1349       Helical; Name=S5 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1350   1416       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1417   1441       Helical; Name=S6 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1442   1977       Cytoplasmic. {ECO:0000255}.
FT   REPEAT       79    375       I.
FT   REPEAT      515    761       II.
FT   REPEAT      858   1140       III.
FT   REPEAT     1177   1444       IV.
FT   CA_BIND    1470   1481       {ECO:0000250}.
FT   REGION      395    412       Binding to the beta subunit.
FT                                {ECO:0000250}.
FT   REGION     1060   1150       Dihydropyridine binding. {ECO:0000250}.
FT   REGION     1397   1463       Dihydropyridine binding. {ECO:0000250}.
FT   REGION     1409   1452       Phenylalkylamine binding. {ECO:0000250}.
FT   COMPBIAS    659    665       Poly-Leu.
FT   COMPBIAS    794    799       Poly-Glu.
FT   COMPBIAS    809    825       Poly-Glu.
FT   COMPBIAS   1121   1124       Poly-Ile.
FT   COMPBIAS   1640   1645       Poly-Glu.
FT   SITE        330    330       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   SITE        711    711       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   SITE       1086   1086       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   SITE       1383   1383       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   MOD_RES    1452   1452       Phosphoserine; by PKA. {ECO:0000255}.
FT   CARBOHYD    295    295       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   VAR_SEQ       9     86       DTTPEPSPANGAGPGPEWGLCPGPPAVEGESSGASGLGTPK
FT                                RRNQHSKHKTVAVASAQRSPRALFCLTLANPLRRSCI ->
FT                                GERILPSLQTLGA (in isoform 3).
FT                                {ECO:0000303|PubMed:9662400}.
FT                                /FTId=VSP_045172.
FT   VAR_SEQ     427    437       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:19029287,
FT                                ECO:0000303|PubMed:9662399}.
FT                                /FTId=VSP_036785.
FT   VAR_SEQ    1756   1775       Missing (in isoform 4 and isoform 5).
FT                                {ECO:0000303|PubMed:27226626}.
FT                                /FTId=VSP_058923.
FT   VAR_SEQ    1836   1901       Missing (in isoform 4 and isoform 6).
FT                                {ECO:0000303|PubMed:27226626}.
FT                                /FTId=VSP_058924.
FT   VARIANT      14     14       P -> L (in dbSNP:rs6520408).
FT                                /FTId=VAR_030807.
FT   VARIANT      74     74       C -> R (in CSNB2A).
FT                                {ECO:0000269|PubMed:12111638}.
FT                                /FTId=VAR_030808.
FT   VARIANT     150    150       G -> R (in CSNB2A).
FT                                {ECO:0000269|PubMed:12187427}.
FT                                /FTId=VAR_030809.
FT   VARIANT     229    229       S -> P (in CSNB2A).
FT                                {ECO:0000269|PubMed:12111638}.
FT                                /FTId=VAR_030810.
FT   VARIANT     261    261       G -> R (in CSNB2A).
FT                                {ECO:0000269|PubMed:12111638}.
FT                                /FTId=VAR_030811.
FT   VARIANT     369    369       G -> D (in CSNB2A; dbSNP:rs122456133).
FT                                {ECO:0000269|PubMed:11281458,
FT                                ECO:0000269|PubMed:12111638,
FT                                ECO:0000269|PubMed:9662399}.
FT                                /FTId=VAR_001504.
FT   VARIANT     519    519       R -> Q (in CSNB2A; dbSNP:rs34162630).
FT                                {ECO:0000269|PubMed:9662399}.
FT                                /FTId=VAR_001505.
FT   VARIANT     603    603       G -> R (in AIED and CSNB2A;
FT                                dbSNP:rs201654095).
FT                                {ECO:0000269|PubMed:22194652}.
FT                                /FTId=VAR_071433.
FT   VARIANT     635    635       V -> I (in CSNB2A; dbSNP:rs141010716).
FT                                {ECO:0000269|PubMed:12187427}.
FT                                /FTId=VAR_030812.
FT   VARIANT     674    674       G -> D (in CSNB2A).
FT                                {ECO:0000269|PubMed:11281458}.
FT                                /FTId=VAR_030813.
FT   VARIANT     746    746       N -> T (in dbSNP:rs141159097).
FT                                {ECO:0000269|PubMed:16960802}.
FT                                /FTId=VAR_029376.
FT   VARIANT     753    753       F -> C (in CSNB2A).
FT                                {ECO:0000269|PubMed:12111638}.
FT                                /FTId=VAR_030814.
FT   VARIANT     756    756       I -> T (in CSNB2A; increases the number
FT                                of mutant channels open at physiologic
FT                                membrane potential and allows for
FT                                persistent Ca(2+) entry due to reduced
FT                                channel inactivation resulting in a gain-
FT                                of-function defect; dbSNP:rs122456136).
FT                                {ECO:0000269|PubMed:15897456}.
FT                                /FTId=VAR_030815.
FT   VARIANT     860    860       L -> P (in CSNB2A).
FT                                {ECO:0000269|PubMed:12111638}.
FT                                /FTId=VAR_030816.
FT   VARIANT     928    928       A -> D (in CSNB2A).
FT                                {ECO:0000269|PubMed:11281458}.
FT                                /FTId=VAR_030817.
FT   VARIANT    1018   1018       G -> R (in CSNB2A).
FT                                {ECO:0000269|PubMed:12111638}.
FT                                /FTId=VAR_030818.
FT   VARIANT    1060   1060       R -> W (in CSNB2A).
FT                                {ECO:0000269|PubMed:12111638,
FT                                ECO:0000269|PubMed:9662399}.
FT                                /FTId=VAR_001506.
FT   VARIANT    1079   1079       L -> P (in CSNB2A).
FT                                {ECO:0000269|PubMed:12111638}.
FT                                /FTId=VAR_030819.
FT   VARIANT    1259   1259       A -> T (in dbSNP:rs34308720).
FT                                /FTId=VAR_055662.
FT   VARIANT    1270   1270       A -> T (in dbSNP:rs34308720).
FT                                /FTId=VAR_031822.
FT   VARIANT    1375   1375       L -> H (in CSNB2A).
FT                                {ECO:0000269|PubMed:9662399}.
FT                                /FTId=VAR_001507.
FT   VARIANT    1499   1499       C -> R (in CSNB2A).
FT                                {ECO:0000269|PubMed:12111638}.
FT                                /FTId=VAR_030820.
FT   VARIANT    1500   1500       P -> R (in CSNB2A).
FT                                {ECO:0000269|PubMed:12111638}.
FT                                /FTId=VAR_030821.
FT   VARIANT    1508   1508       L -> P (in CSNB2A).
FT                                {ECO:0000269|PubMed:12111638}.
FT                                /FTId=VAR_030822.
FT   VARIANT    1930   1930       R -> H (in dbSNP:rs33910054).
FT                                /FTId=VAR_054818.
FT   CONFLICT   1236   1236       E -> V (in Ref. 6; AAB92359).
FT                                {ECO:0000305}.
FT   CONFLICT   1860   1860       A -> G (in Ref. 6; AAB92359).
FT                                {ECO:0000305}.
SQ   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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