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O60840 (CAC1F_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Voltage-dependent L-type calcium channel subunit alpha-1F
Alternative name(s):
Voltage-gated calcium channel subunit alpha Cav1.4
Gene names
Name:CACNA1F
Synonyms:CACNAF1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1977 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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-1Fgives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to omega-conotoxin-GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA).

Subunit structure

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.

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Expression in skeletal muscle and retina. Ref.3

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.

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.2 Ref.7 Ref.8 Ref.9 Ref.10

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13

Sequence similarities

Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family. CACNA1F subfamily. [View classification]

Sequence caution

The sequence AAB92359.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Sensory transduction
Transport
Vision
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCone-rod dystrophy
Congenital stationary night blindness
Disease mutation
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   Molecular functionCalcium channel
Ion channel
Voltage-gated channel
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxonogenesis

Inferred from electronic annotation. Source: Ensembl

calcium ion import

Inferred from Biological aspect of Ancestor. Source: RefGenome

cellular calcium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

dendrite morphogenesis

Inferred from electronic annotation. Source: Ensembl

detection of light stimulus involved in visual perception

Inferred from mutant phenotype PubMed 7571473. Source: UniProtKB

membrane depolarization during action potential

Inferred from Biological aspect of Ancestor. Source: RefGenome

retina development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

visual perception

Inferred from mutant phenotype Ref.12Ref.1Ref.2. Source: UniProtKB

   Cellular_componentintegral component of membrane

Inferred from direct assay Ref.10. Source: UniProtKB

perikaryon

Inferred from electronic annotation. Source: Ensembl

photoreceptor outer segment

Inferred from electronic annotation. Source: Ensembl

voltage-gated calcium channel complex

Inferred from direct assay Ref.10. Source: UniProtKB

   Molecular_functionhigh voltage-gated calcium channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

voltage-gated calcium channel activity

Inferred from direct assay Ref.10. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O60840-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O60840-2)

The sequence of this isoform differs from the canonical sequence as follows:
     427-437: Missing.
Isoform 3 (identifier: O60840-4)

The sequence of this isoform differs from the canonical sequence as follows:
     9-86: DTTPEPSPAN...LANPLRRSCI → GERILPSLQTLGA

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 19771977Voltage-dependent L-type calcium channel subunit alpha-1F
PRO_0000053950

Regions

Topological domain1 – 9292Cytoplasmic Potential
Transmembrane93 – 11119Helical; Name=S1 of repeat I; Potential
Topological domain112 – 12918Extracellular Potential
Transmembrane130 – 14920Helical; Name=S2 of repeat I; Potential
Topological domain150 – 16112Cytoplasmic Potential
Transmembrane162 – 18019Helical; Name=S3 of repeat I; Potential
Topological domain181 – 20121Extracellular Potential
Transmembrane202 – 22019Helical; Name=S4 of repeat I; Potential
Topological domain221 – 23919Cytoplasmic Potential
Transmembrane240 – 25920Helical; Name=S5 of repeat I; Potential
Topological domain260 – 34788Extracellular Potential
Transmembrane348 – 37225Helical; Name=S6 of repeat I; Potential
Topological domain373 – 529157Cytoplasmic Potential
Transmembrane530 – 54920Helical; Name=S1 of repeat II; Potential
Topological domain550 – 56415Extracellular Potential
Transmembrane565 – 58319Helical; Name=S2 of repeat II; Potential
Topological domain584 – 5918Cytoplasmic Potential
Transmembrane592 – 61019Helical; Name=S3 of repeat II; Potential
Topological domain611 – 62010Extracellular Potential
Transmembrane621 – 63919Helical; Name=S4 of repeat II; Potential
Topological domain640 – 65819Cytoplasmic Potential
Transmembrane659 – 67921Helical; Name=S5 of repeat II; Potential
Topological domain680 – 73354Extracellular Potential
Transmembrane734 – 75825Helical; Name=S6 of repeat II; Potential
Topological domain759 – 871113Cytoplasmic Potential
Transmembrane872 – 89019Helical; Name=S1 of repeat III; Potential
Topological domain891 – 90616Extracellular Potential
Transmembrane907 – 92620Helical; Name=S2 of repeat III; Potential
Topological domain927 – 93812Cytoplasmic Potential
Transmembrane939 – 95719Helical; Name=S3 of repeat III; Potential
Topological domain958 – 9636Extracellular Potential
Transmembrane964 – 98320Helical; Name=S4 of repeat III; Potential
Topological domain984 – 100219Cytoplasmic Potential
Transmembrane1003 – 102220Helical; Name=S5 of repeat III; Potential
Topological domain1023 – 111290Extracellular Potential
Transmembrane1113 – 113321Helical; Name=S6 of repeat III; Potential
Topological domain1134 – 119057Cytoplasmic Potential
Transmembrane1191 – 120919Helical; Name=S1 of repeat IV; Potential
Topological domain1210 – 122415Extracellular Potential
Transmembrane1225 – 124420Helical; Name=S2 of repeat IV; Potential
Topological domain1245 – 12517Cytoplasmic Potential
Transmembrane1252 – 127322Helical; Name=S3 of repeat IV; Potential
Topological domain1274 – 129017Extracellular Potential
Transmembrane1291 – 131020Helical; Name=S4 of repeat IV; Potential
Topological domain1311 – 132919Cytoplasmic Potential
Transmembrane1330 – 134920Helical; Name=S5 of repeat IV; Potential
Topological domain1350 – 141667Extracellular Potential
Transmembrane1417 – 144125Helical; Name=S6 of repeat IV; Potential
Topological domain1442 – 1977536Cytoplasmic Potential
Repeat79 – 375297I
Repeat515 – 761247II
Repeat858 – 1140283III
Repeat1177 – 1444268IV
Calcium binding1470 – 148112 By similarity
Region395 – 41218Binding to the beta subunit By similarity
Region1060 – 115091Dihydropyridine binding By similarity
Region1397 – 146367Dihydropyridine binding By similarity
Region1409 – 145244Phenylalkylamine binding By similarity
Compositional bias659 – 6657Poly-Leu
Compositional bias794 – 7996Poly-Glu
Compositional bias809 – 82517Poly-Glu
Compositional bias1121 – 11244Poly-Ile
Compositional bias1640 – 16456Poly-Glu

Sites

Site3301Calcium ion selectivity and permeability By similarity
Site7111Calcium ion selectivity and permeability By similarity
Site10861Calcium ion selectivity and permeability By similarity
Site13831Calcium ion selectivity and permeability By similarity

Amino acid modifications

Modified residue14521Phosphoserine; by PKA Potential
Glycosylation2951N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence9 – 8678DTTPE…RRSCI → GERILPSLQTLGA in isoform 3.
VSP_045172
Alternative sequence427 – 43711Missing in isoform 2.
VSP_036785
Natural variant141P → L.
Corresponds to variant rs6520408 [ dbSNP | Ensembl ].
VAR_030807
Natural variant741C → R in CSNB2A. Ref.8
VAR_030808
Natural variant1501G → R in CSNB2A. Ref.9
VAR_030809
Natural variant2291S → P in CSNB2A. Ref.8
VAR_030810
Natural variant2611G → R in CSNB2A. Ref.8
VAR_030811
Natural variant3691G → D in CSNB2A. Ref.1 Ref.7 Ref.8
VAR_001504
Natural variant5191R → Q in CSNB2A. Ref.1
Corresponds to variant rs34162630 [ dbSNP | Ensembl ].
VAR_001505
Natural variant6351V → I in CSNB2A. Ref.9
Corresponds to variant rs141010716 [ dbSNP | Ensembl ].
VAR_030812
Natural variant6741G → D in CSNB2A. Ref.7
VAR_030813
Natural variant7461N → T. Ref.11
Corresponds to variant rs141159097 [ dbSNP | Ensembl ].
VAR_029376
Natural variant7531F → C in CSNB2A. Ref.8
VAR_030814
Natural variant7561I → 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. Ref.10
VAR_030815
Natural variant8601L → P in CSNB2A. Ref.8
VAR_030816
Natural variant9281A → D in CSNB2A. Ref.7
VAR_030817
Natural variant10181G → R in CSNB2A. Ref.8
VAR_030818
Natural variant10601R → W in CSNB2A. Ref.1 Ref.8
VAR_001506
Natural variant10791L → P in CSNB2A. Ref.8
VAR_030819
Natural variant12591A → T.
Corresponds to variant rs34308720 [ dbSNP | Ensembl ].
VAR_055662
Natural variant12701A → T.
Corresponds to variant rs34308720 [ dbSNP | Ensembl ].
VAR_031822
Natural variant13751L → H in CSNB2A. Ref.1
VAR_001507
Natural variant14991C → R in CSNB2A. Ref.8
VAR_030820
Natural variant15001P → R in CSNB2A. Ref.8
VAR_030821
Natural variant15081L → P in CSNB2A. Ref.8
VAR_030822
Natural variant19301R → H.
Corresponds to variant rs33910054 [ dbSNP | Ensembl ].
VAR_054818

Experimental info

Sequence conflict12361E → V in AAB92359. Ref.6
Sequence conflict18601A → G in AAB92359. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 14, 2009. Version 2.
Checksum: 354336550C6D8E73

FASTA1,977220,678
        10         20         30         40         50         60 
MSESEGGKDT TPEPSPANGA GPGPEWGLCP GPPAVEGESS GASGLGTPKR RNQHSKHKTV 

        70         80         90        100        110        120 
AVASAQRSPR ALFCLTLANP LRRSCISIVE WKPFDILILL TIFANCVALG VYIPFPEDDS 

       130        140        150        160        170        180 
NTANHNLEQV EYVFLVIFTV ETVLKIVAYG LVLHPSAYIR NGWNLLDFII VVVGLFSVLL 

       190        200        210        220        230        240 
EQGPGRPGDA PHTGGKPGGF DVKALRAFRV LRPLRLVSGV PSLHIVLNSI MKALVPLLHI 

       250        260        270        280        290        300 
ALLVLFVIII YAIIGLELFL GRMHKTCYFL GSDMEAEEDP SPCASSGSGR ACTLNQTECR 

       310        320        330        340        350        360 
GRWPGPNGGI TNFDNFFFAM LTVFQCVTME GWTDVLYWMQ DAMGYELPWV YFVSLVIFGS 

       370        380        390        400        410        420 
FFVLNLVLGV LSGEFSKERE KAKARGDFQK QREKQQMEED LRGYLDWITQ AEELDMEDPS 

       430        440        450        460        470        480 
ADDNLGSMAE EGRAGHRPQL AELTNRRRGR LRWFSHSTRS THSTSSHASL PASDTGSMTE 

       490        500        510        520        530        540 
TQGDEDEEEG ALASCTRCLN KIMKTRVCRR LRRANRVLRA RCRRAVKSNA CYWAVLLLVF 

       550        560        570        580        590        600 
LNTLTIASEH HGQPVWLTQI QEYANKVLLC LFTVEMLLKL YGLGPSAYVS SFFNRFDCFV 

       610        620        630        640        650        660 
VCGGILETTL VEVGAMQPLG ISVLRCVRLL RIFKVTRHWA SLSNLVASLL NSMKSIASLL 

       670        680        690        700        710        720 
LLLFLFIIIF SLLGMQLFGG KFNFDQTHTK RSTFDTFPQA LLTVFQILTG EDWNVVMYDG 

       730        740        750        760        770        780 
IMAYGGPFFP GMLVCIYFII LFICGNYILL NVFLAIAVDN LASGDAGTAK DKGGEKSNEK 

       790        800        810        820        830        840 
DLPQENEGLV PGVEKEEEEG ARREGADMEE EEEEEEEEEE EEEEEGAGGV ELLQEVVPKE 

       850        860        870        880        890        900 
KVVPIPEGSA FFCLSQTNPL RKGCHTLIHH HVFTNLILVF IILSSVSLAA EDPIRAHSFR 

       910        920        930        940        950        960 
NHILGYFDYA FTSIFTVEIL LKMTVFGAFL HRGSFCRSWF NMLDLLVVSV SLISFGIHSS 

       970        980        990       1000       1010       1020 
AISVVKILRV LRVLRPLRAI NRAKGLKHVV QCVFVAIRTI GNIMIVTTLL QFMFACIGVQ 

      1030       1040       1050       1060       1070       1080 
LFKGKFYTCT DEAKHTPQEC KGSFLVYPDG DVSRPLVRER LWVNSDFNFD NVLSAMMALF 

      1090       1100       1110       1120       1130       1140 
TVSTFEGWPA LLYKAIDAYA EDHGPIYNYR VEISVFFIVY IIIIAFFMMN IFVGFVIITF 

      1150       1160       1170       1180       1190       1200 
RAQGEQEYQN CELDKNQRQC VEYALKAQPL RRYIPKNPHQ YRVWATVNSA AFEYLMFLLI 

      1210       1220       1230       1240       1250       1260 
LLNTVALAMQ HYEQTAPFNY AMDILNMVFT GLFTIEMVLK IIAFKPKHYF TDAWNTFDAL 

      1270       1280       1290       1300       1310       1320 
IVVGSIVDIA VTEVNNGGHL GESSEDSSRI SITFFRLFRV MRLVKLLSKG EGIRTLLWTF 

      1330       1340       1350       1360       1370       1380 
IKSFQALPYV ALLIAMIFFI YAVIGMQMFG KVALQDGTQI NRNNNFQTFP QAVLLLFRCA 

      1390       1400       1410       1420       1430       1440 
TGEAWQEIML ASLPGNRCDP ESDFGPGEEF TCGSNFAIAY FISFFMLCAF LIINLFVAVI 

      1450       1460       1470       1480       1490       1500 
MDNFDYLTRD WSILGPHHLD EFKRIWSEYD PGAKGRIKHL DVVALLRRIQ PPLGFGKLCP 

      1510       1520       1530       1540       1550       1560 
HRVACKRLVA MNMPLNSDGT VTFNATLFAL VRTSLKIKTE GNLEQANQEL RIVIKKIWKR 

      1570       1580       1590       1600       1610       1620 
MKQKLLDEVI PPPDEEEVTV GKFYATFLIQ DYFRKFRRRK EKGLLGNDAA PSTSSALQAG 

      1630       1640       1650       1660       1670       1680 
LRSLQDLGPE MRQALTCDTE EEEEEGQEGV EEEDEKDLET NKATMVSQPS ARRGSGISVS 

      1690       1700       1710       1720       1730       1740 
LPVGDRLPDS LSFGPSDDDR GTPTSSQPSV PQAGSNTHRR GSGALIFTIP EEGNSQPKGT 

      1750       1760       1770       1780       1790       1800 
KGQNKQDEDE EVPDRLSYLD EQAGTPPCSV LLPPHRAQRY MDGHLVPRRR LLPPTPAGRK 

      1810       1820       1830       1840       1850       1860 
PSFTIQCLQR QGSCEDLPIP GTYHRGRNSG PNRAQGSWAT PPQRGRLLYA PLLLVEEGAA 

      1870       1880       1890       1900       1910       1920 
GEGYLGRSSG PLRTFTCLHV PGTHSDPSHG KRGSADSLVE AVLISEGLGL FARDPRFVAL 

      1930       1940       1950       1960       1970 
AKQEIADACR LTLDEMDNAA SDLLAQGTSS LYSDEESILS RFDEEDLGDE MACVHAL 

« Hide

Isoform 2 [UniParc].

Checksum: FEB47E19FA57E31D
Show »

FASTA1,966219,496
Isoform 3 [UniParc].

Checksum: 0E2C45C8E4156E0D
Show »

FASTA1,912214,033

References

« Hide 'large scale' references
[1]"An L-type calcium-channel gene mutated in incomplete X-linked congenital stationary night blindness."
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.
Nat. Genet. 19:260-263(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), VARIANTS CSNB2A ASP-369; GLN-519; TRP-1060 AND HIS-1375.
Tissue: Retina.
[2]"Loss-of-function mutations in a calcium-channel alpha1-subunit gene in Xp11.23 cause incomplete X-linked congenital stationary night blindness."
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.
Nat. Genet. 19:264-267(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INVOLVEMENT IN CSNB2A.
[3]"Isolation and characterization of a calcium channel gene, cacna1f, the murine orthologue of the gene for incomplete X-linked congenital stationary night blindness."
Naylor M.J., Rancourt D.E., Bech-Hansen N.T.
Genomics 66:324-327(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[4]"Expression and 1,4-dihydropyridine-binding properties of brain L-type calcium channel isoforms."
Sinnegger-Brauns M.J., Huber I.G., Koschak A., Wild C., Obermair G.J., Einzinger U., Hoda J.C., Sartori S.B., Striessnig J.
Mol. Pharmacol. 75:407-414(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Retina.
[5]"The DNA sequence of the human X chromosome."
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. expand/collapse author list , 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.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"Sequence-based exon prediction around the synaptophysin locus reveals a gene-rich area containing novel genes in human proximal Xp."
Fisher S.E., Ciccodicola A., Tanaka K., Curci A., Desicato S., D'Urso M., Craig I.W.
Genomics 45:340-347(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1211-1977.
[7]"A summary of 20 CACNA1F mutations identified in 36 families with incomplete X-linked congenital stationary night blindness, and characterization of splice variants."
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.
Hum. Genet. 108:91-97(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CSNB2A ASP-369; ASP-674 AND ASP-928.
[8]"Thirty distinct CACNA1F mutations in 33 families with incomplete type of XLCSNB and Cacna1f expression profiling in mouse retina."
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.
Eur. J. Hum. Genet. 10:449-456(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: 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.
[9]"Infantile and childhood retinal blindness: a molecular perspective (The Franceschetti Lecture)."
Weleber R.G.
Ophthalmic Genet. 23:71-97(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CSNB2A ARG-150 AND ILE-635.
[10]"A CACNA1F mutation identified in an X-linked retinal disorder shifts the voltage dependence of Cav1.4 channel activation."
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.
Proc. Natl. Acad. Sci. U.S.A. 102:7553-7558(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CSNB2A THR-756, CHARACTERIZATION OF VARIANT CSNB2A THR-756.
[11]"Mutations in CABP4, the gene encoding the Ca2+-binding protein 4, cause autosomal recessive night blindness."
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.
Am. J. Hum. Genet. 79:657-667(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THR-746.
[12]"X linked cone-rod dystrophy, CORDX3, is caused by a mutation in the CACNA1F gene."
Jalkanen R., Maentyjaervi M., Tobias R., Isosomppi J., Sankila E.-M., Alitalo T., Bech-Hansen N.T.
J. Med. Genet. 43:699-704(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CORDX3.
[13]"A novel CACNA1F gene mutation causes Aland Island eye disease."
Jalkanen R., Bech-Hansen N.T., Tobias R., Sankila E.-M., Maentyjaervi M., Forsius H., de la Chapelle A., Alitalo T.
Invest. Ophthalmol. Vis. Sci. 48:2498-2502(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN AIED.
+Additional computationally mapped references.

Web resources

Mutations of the CCNA1F gene

Retina International's Scientific Newsletter

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ006216 Genomic DNA. Translation: CAA06916.1.
AF067227 mRNA. Translation: AAD03587.1.
AJ224874 mRNA. Translation: CAA12175.1.
AF201304 mRNA. Translation: AAF15290.1.
JF701915 mRNA. Translation: AED89557.1.
AF196779 Genomic DNA. No translation available.
AF235097 Genomic DNA. No translation available.
U93305 Genomic DNA. Translation: AAB92359.1. Sequence problems.
CCDSCCDS35253.1. [O60840-1]
CCDS59166.1. [O60840-4]
CCDS59167.1. [O60840-2]
RefSeqNP_001243718.1. NM_001256789.2. [O60840-2]
NP_001243719.1. NM_001256790.2. [O60840-4]
NP_005174.2. NM_005183.3. [O60840-1]
UniGeneHs.632799.

3D structure databases

ProteinModelPortalO60840.
SMRO60840. Positions 94-371, 386-414, 534-770, 866-1137, 1179-1442, 1525-1605.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107232. 1 interaction.
IntActO60840. 2 interactions.
STRING9606.ENSP00000365441.

Chemistry

BindingDBO60840.
ChEMBLCHEMBL2363032.
DrugBankDB00661. Verapamil.
GuidetoPHARMACOLOGY531.

Protein family/group databases

TCDB1.A.1.11.11. the voltage-gated ion channel (vic) superfamily.

PTM databases

PhosphoSiteO60840.

Proteomic databases

PaxDbO60840.
PRIDEO60840.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000323022; ENSP00000321618; ENSG00000102001. [O60840-2]
ENST00000376251; ENSP00000365427; ENSG00000102001. [O60840-4]
ENST00000376265; ENSP00000365441; ENSG00000102001. [O60840-1]
ENST00000598102; ENSP00000473223; ENSG00000269057. [O60840-2]
ENST00000599684; ENSP00000469166; ENSG00000269057. [O60840-1]
ENST00000601604; ENSP00000469529; ENSG00000269057. [O60840-4]
GeneID778.
KEGGhsa:778.
UCSCuc004dnb.3. human. [O60840-1]
uc031tjm.1. human.

Organism-specific databases

CTD778.
GeneCardsGC0XM049061.
GeneReviewsCACNA1F.
HGNCHGNC:1393. CACNA1F.
MIM300071. phenotype.
300110. gene.
300476. phenotype.
300600. phenotype.
neXtProtNX_O60840.
Orphanet178333. Aland Islands eye disease.
1872. Cone rod dystrophy.
215. Congenital stationary night blindness.
PharmGKBPA26010.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1226.
HOGENOMHOG000231529.
HOVERGENHBG050763.
KOK04853.
OMAAVKSTAC.
PhylomeDBO60840.
TreeFamTF312805.

Gene expression databases

ArrayExpressO60840.
BgeeO60840.
CleanExHS_CACNA1F.
GenevestigatorO60840.

Family and domain databases

Gene3D1.20.120.350. 5 hits.
InterProIPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005446. VDCC_L_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PfamPF08763. Ca_chan_IQ. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSPR00167. CACHANNEL.
PR01630. LVDCCALPHA1.
SMARTSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCav1.4.
GenomeRNAi778.
NextBio3144.
PROO60840.
SOURCESearch...

Entry information

Entry nameCAC1F_HUMAN
AccessionPrimary (citable) accession number: O60840
Secondary accession number(s): A6NI29 expand/collapse secondary AC list , F5CIQ9, O43901, O95226, Q9UHB1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: April 14, 2009
Last modified: July 9, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM