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O60840

- CAC1F_HUMAN

UniProt

O60840 - CAC1F_HUMAN

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Protein

Voltage-dependent L-type calcium channel subunit alpha-1F

Gene

CACNA1F

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-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, 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).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei330 – 3301Calcium ion selectivity and permeabilityBy similarity
Sitei711 – 7111Calcium ion selectivity and permeabilityBy similarity
Sitei1086 – 10861Calcium ion selectivity and permeabilityBy similarity
Sitei1383 – 13831Calcium ion selectivity and permeabilityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi1470 – 148112By similarityAdd
BLAST

GO - Molecular functioni

  1. high voltage-gated calcium channel activity Source: RefGenome
  2. metal ion binding Source: UniProtKB-KW
  3. voltage-gated calcium channel activity Source: UniProtKB

GO - Biological processi

  1. axonogenesis Source: Ensembl
  2. calcium ion import Source: RefGenome
  3. cellular calcium ion homeostasis Source: Ensembl
  4. dendrite morphogenesis Source: Ensembl
  5. detection of light stimulus involved in visual perception Source: UniProtKB
  6. membrane depolarization during action potential Source: RefGenome
  7. retina development in camera-type eye Source: Ensembl
  8. visual perception Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel, Voltage-gated channel

Keywords - Biological processi

Calcium transport, Ion transport, Sensory transduction, Transport, Vision

Keywords - Ligandi

Calcium, Metal-binding

Protein family/group databases

TCDBi1.A.1.11.11. the voltage-gated ion channel (vic) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Voltage-dependent L-type calcium channel subunit alpha-1F
Alternative name(s):
Voltage-gated calcium channel subunit alpha Cav1.4
Gene namesi
Name:CACNA1F
Synonyms:CACNAF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:1393. CACNA1F.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 9292CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei93 – 11119Helical; Name=S1 of repeat ISequence AnalysisAdd
BLAST
Topological domaini112 – 12918ExtracellularSequence AnalysisAdd
BLAST
Transmembranei130 – 14920Helical; Name=S2 of repeat ISequence AnalysisAdd
BLAST
Topological domaini150 – 16112CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei162 – 18019Helical; Name=S3 of repeat ISequence AnalysisAdd
BLAST
Topological domaini181 – 20121ExtracellularSequence AnalysisAdd
BLAST
Transmembranei202 – 22019Helical; Name=S4 of repeat ISequence AnalysisAdd
BLAST
Topological domaini221 – 23919CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei240 – 25920Helical; Name=S5 of repeat ISequence AnalysisAdd
BLAST
Topological domaini260 – 34788ExtracellularSequence AnalysisAdd
BLAST
Transmembranei348 – 37225Helical; Name=S6 of repeat ISequence AnalysisAdd
BLAST
Topological domaini373 – 529157CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei530 – 54920Helical; Name=S1 of repeat IISequence AnalysisAdd
BLAST
Topological domaini550 – 56415ExtracellularSequence AnalysisAdd
BLAST
Transmembranei565 – 58319Helical; Name=S2 of repeat IISequence AnalysisAdd
BLAST
Topological domaini584 – 5918CytoplasmicSequence Analysis
Transmembranei592 – 61019Helical; Name=S3 of repeat IISequence AnalysisAdd
BLAST
Topological domaini611 – 62010ExtracellularSequence Analysis
Transmembranei621 – 63919Helical; Name=S4 of repeat IISequence AnalysisAdd
BLAST
Topological domaini640 – 65819CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei659 – 67921Helical; Name=S5 of repeat IISequence AnalysisAdd
BLAST
Topological domaini680 – 73354ExtracellularSequence AnalysisAdd
BLAST
Transmembranei734 – 75825Helical; Name=S6 of repeat IISequence AnalysisAdd
BLAST
Topological domaini759 – 871113CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei872 – 89019Helical; Name=S1 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini891 – 90616ExtracellularSequence AnalysisAdd
BLAST
Transmembranei907 – 92620Helical; Name=S2 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini927 – 93812CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei939 – 95719Helical; Name=S3 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini958 – 9636ExtracellularSequence Analysis
Transmembranei964 – 98320Helical; Name=S4 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini984 – 100219CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1003 – 102220Helical; Name=S5 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini1023 – 111290ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1113 – 113321Helical; Name=S6 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini1134 – 119057CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1191 – 120919Helical; Name=S1 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1210 – 122415ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1225 – 124420Helical; Name=S2 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1245 – 12517CytoplasmicSequence Analysis
Transmembranei1252 – 127322Helical; Name=S3 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1274 – 129017ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1291 – 131020Helical; Name=S4 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1311 – 132919CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1330 – 134920Helical; Name=S5 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1350 – 141667ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1417 – 144125Helical; Name=S6 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1442 – 1977536CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB
  2. perikaryon Source: Ensembl
  3. photoreceptor outer segment Source: Ensembl
  4. voltage-gated calcium channel complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Night blindness, congenital stationary, 2A (CSNB2A) [MIM:300071]: A non-progressive retinal disorder characterized by impaired night vision, often associated with nystagmus and myopia.7 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti74 – 741C → R in CSNB2A. 1 Publication
VAR_030808
Natural varianti150 – 1501G → R in CSNB2A. 1 Publication
VAR_030809
Natural varianti229 – 2291S → P in CSNB2A. 1 Publication
VAR_030810
Natural varianti261 – 2611G → R in CSNB2A. 1 Publication
VAR_030811
Natural varianti369 – 3691G → D in CSNB2A. 3 Publications
VAR_001504
Natural varianti519 – 5191R → Q in CSNB2A. 1 Publication
Corresponds to variant rs34162630 [ dbSNP | Ensembl ].
VAR_001505
Natural varianti603 – 6031G → R in AIED and CSNB2A. 1 Publication
VAR_071433
Natural varianti635 – 6351V → I in CSNB2A. 1 Publication
Corresponds to variant rs141010716 [ dbSNP | Ensembl ].
VAR_030812
Natural varianti674 – 6741G → D in CSNB2A. 1 Publication
VAR_030813
Natural varianti753 – 7531F → C in CSNB2A. 1 Publication
VAR_030814
Natural varianti756 – 7561I → 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. 1 Publication
VAR_030815
Natural varianti860 – 8601L → P in CSNB2A. 1 Publication
VAR_030816
Natural varianti928 – 9281A → D in CSNB2A. 1 Publication
VAR_030817
Natural varianti1018 – 10181G → R in CSNB2A. 1 Publication
VAR_030818
Natural varianti1060 – 10601R → W in CSNB2A. 2 Publications
VAR_001506
Natural varianti1079 – 10791L → P in CSNB2A. 1 Publication
VAR_030819
Natural varianti1375 – 13751L → H in CSNB2A. 1 Publication
VAR_001507
Natural varianti1499 – 14991C → R in CSNB2A. 1 Publication
VAR_030820
Natural varianti1500 – 15001P → R in CSNB2A. 1 Publication
VAR_030821
Natural varianti1508 – 15081L → P in CSNB2A. 1 Publication
VAR_030822
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti603 – 6031G → R in AIED and CSNB2A. 1 Publication
VAR_071433

Keywords - Diseasei

Cone-rod dystrophy, Congenital stationary night blindness, Disease mutation

Organism-specific databases

MIMi300071. phenotype.
300476. phenotype.
300600. phenotype.
Orphaneti178333. Aland Islands eye disease.
1872. Cone rod dystrophy.
215. Congenital stationary night blindness.
PharmGKBiPA26010.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19771977Voltage-dependent L-type calcium channel subunit alpha-1FPRO_0000053950Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi295 – 2951N-linked (GlcNAc...)Sequence Analysis
Modified residuei1452 – 14521Phosphoserine; by PKASequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiO60840.
PRIDEiO60840.

PTM databases

PhosphoSiteiO60840.

Expressioni

Tissue specificityi

Expression in skeletal muscle and retina.1 Publication

Gene expression databases

BgeeiO60840.
CleanExiHS_CACNA1F.
ExpressionAtlasiO60840. baseline.
GenevestigatoriO60840.

Interactioni

Subunit structurei

Voltage-dependent calcium channels are multisubunit complexes, consisting of alpha-1, alpha-2, beta and delta subunits in a 1:1:1:1 ratio. The channel activity is directed by the pore-forming and voltage-sensitive alpha-1 subunit. In many cases, this subunit is sufficient to generate voltage-sensitive calcium channel activity. The auxiliary subunits beta and alpha-2/delta linked by a disulfide bridge regulate the channel activity. Interacts (via IQ domain) with CABP4; in a calcium independent manner (By similarity).By similarity

Protein-protein interaction databases

BioGridi107232. 1 interaction.
IntActiO60840. 2 interactions.
STRINGi9606.ENSP00000365441.

Structurei

3D structure databases

ProteinModelPortaliO60840.
SMRiO60840. Positions 94-371, 386-414, 534-770, 866-1137, 1179-1442, 1525-1605.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati79 – 375297IAdd
BLAST
Repeati515 – 761247IIAdd
BLAST
Repeati858 – 1140283IIIAdd
BLAST
Repeati1177 – 1444268IVAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni395 – 41218Binding to the beta subunitBy similarityAdd
BLAST
Regioni1060 – 115091Dihydropyridine bindingBy similarityAdd
BLAST
Regioni1397 – 146367Dihydropyridine bindingBy similarityAdd
BLAST
Regioni1409 – 145244Phenylalkylamine bindingBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi659 – 6657Poly-Leu
Compositional biasi794 – 7996Poly-Glu
Compositional biasi809 – 82517Poly-GluAdd
BLAST
Compositional biasi1121 – 11244Poly-Ile
Compositional biasi1640 – 16456Poly-Glu

Domaini

Each of the four internal repeats contains five hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one positively charged transmembrane segment (S4). S4 segments probably represent the voltage-sensor and are characterized by a series of positively charged amino acids at every third position.

Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1226.
GeneTreeiENSGT00760000118827.
HOGENOMiHOG000231529.
HOVERGENiHBG050763.
InParanoidiO60840.
KOiK04853.
OMAiAVKSTAC.
PhylomeDBiO60840.
TreeFamiTF312805.

Family and domain databases

Gene3Di1.20.120.350. 5 hits.
InterProiIPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005446. VDCC_L_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PfamiPF08763. Ca_chan_IQ. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSiPR00167. CACHANNEL.
PR01630. LVDCCALPHA1.
SMARTiSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O60840-1) [UniParc]FASTAAdd to Basket

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

« Hide

        10         20         30         40         50
MSESEGGKDT TPEPSPANGA GPGPEWGLCP GPPAVEGESS GASGLGTPKR
60 70 80 90 100
RNQHSKHKTV AVASAQRSPR ALFCLTLANP LRRSCISIVE WKPFDILILL
110 120 130 140 150
TIFANCVALG VYIPFPEDDS NTANHNLEQV EYVFLVIFTV ETVLKIVAYG
160 170 180 190 200
LVLHPSAYIR NGWNLLDFII VVVGLFSVLL EQGPGRPGDA PHTGGKPGGF
210 220 230 240 250
DVKALRAFRV LRPLRLVSGV PSLHIVLNSI MKALVPLLHI ALLVLFVIII
260 270 280 290 300
YAIIGLELFL GRMHKTCYFL GSDMEAEEDP SPCASSGSGR ACTLNQTECR
310 320 330 340 350
GRWPGPNGGI TNFDNFFFAM LTVFQCVTME GWTDVLYWMQ DAMGYELPWV
360 370 380 390 400
YFVSLVIFGS FFVLNLVLGV LSGEFSKERE KAKARGDFQK QREKQQMEED
410 420 430 440 450
LRGYLDWITQ AEELDMEDPS ADDNLGSMAE EGRAGHRPQL AELTNRRRGR
460 470 480 490 500
LRWFSHSTRS THSTSSHASL PASDTGSMTE TQGDEDEEEG ALASCTRCLN
510 520 530 540 550
KIMKTRVCRR LRRANRVLRA RCRRAVKSNA CYWAVLLLVF LNTLTIASEH
560 570 580 590 600
HGQPVWLTQI QEYANKVLLC LFTVEMLLKL YGLGPSAYVS SFFNRFDCFV
610 620 630 640 650
VCGGILETTL VEVGAMQPLG ISVLRCVRLL RIFKVTRHWA SLSNLVASLL
660 670 680 690 700
NSMKSIASLL LLLFLFIIIF SLLGMQLFGG KFNFDQTHTK RSTFDTFPQA
710 720 730 740 750
LLTVFQILTG EDWNVVMYDG IMAYGGPFFP GMLVCIYFII LFICGNYILL
760 770 780 790 800
NVFLAIAVDN LASGDAGTAK DKGGEKSNEK DLPQENEGLV PGVEKEEEEG
810 820 830 840 850
ARREGADMEE EEEEEEEEEE EEEEEGAGGV ELLQEVVPKE KVVPIPEGSA
860 870 880 890 900
FFCLSQTNPL RKGCHTLIHH HVFTNLILVF IILSSVSLAA EDPIRAHSFR
910 920 930 940 950
NHILGYFDYA FTSIFTVEIL LKMTVFGAFL HRGSFCRSWF NMLDLLVVSV
960 970 980 990 1000
SLISFGIHSS AISVVKILRV LRVLRPLRAI NRAKGLKHVV QCVFVAIRTI
1010 1020 1030 1040 1050
GNIMIVTTLL QFMFACIGVQ LFKGKFYTCT DEAKHTPQEC KGSFLVYPDG
1060 1070 1080 1090 1100
DVSRPLVRER LWVNSDFNFD NVLSAMMALF TVSTFEGWPA LLYKAIDAYA
1110 1120 1130 1140 1150
EDHGPIYNYR VEISVFFIVY IIIIAFFMMN IFVGFVIITF RAQGEQEYQN
1160 1170 1180 1190 1200
CELDKNQRQC VEYALKAQPL RRYIPKNPHQ YRVWATVNSA AFEYLMFLLI
1210 1220 1230 1240 1250
LLNTVALAMQ HYEQTAPFNY AMDILNMVFT GLFTIEMVLK IIAFKPKHYF
1260 1270 1280 1290 1300
TDAWNTFDAL IVVGSIVDIA VTEVNNGGHL GESSEDSSRI SITFFRLFRV
1310 1320 1330 1340 1350
MRLVKLLSKG EGIRTLLWTF IKSFQALPYV ALLIAMIFFI YAVIGMQMFG
1360 1370 1380 1390 1400
KVALQDGTQI NRNNNFQTFP QAVLLLFRCA TGEAWQEIML ASLPGNRCDP
1410 1420 1430 1440 1450
ESDFGPGEEF TCGSNFAIAY FISFFMLCAF LIINLFVAVI MDNFDYLTRD
1460 1470 1480 1490 1500
WSILGPHHLD EFKRIWSEYD PGAKGRIKHL DVVALLRRIQ PPLGFGKLCP
1510 1520 1530 1540 1550
HRVACKRLVA MNMPLNSDGT VTFNATLFAL VRTSLKIKTE GNLEQANQEL
1560 1570 1580 1590 1600
RIVIKKIWKR MKQKLLDEVI PPPDEEEVTV GKFYATFLIQ DYFRKFRRRK
1610 1620 1630 1640 1650
EKGLLGNDAA PSTSSALQAG LRSLQDLGPE MRQALTCDTE EEEEEGQEGV
1660 1670 1680 1690 1700
EEEDEKDLET NKATMVSQPS ARRGSGISVS LPVGDRLPDS LSFGPSDDDR
1710 1720 1730 1740 1750
GTPTSSQPSV PQAGSNTHRR GSGALIFTIP EEGNSQPKGT KGQNKQDEDE
1760 1770 1780 1790 1800
EVPDRLSYLD EQAGTPPCSV LLPPHRAQRY MDGHLVPRRR LLPPTPAGRK
1810 1820 1830 1840 1850
PSFTIQCLQR QGSCEDLPIP GTYHRGRNSG PNRAQGSWAT PPQRGRLLYA
1860 1870 1880 1890 1900
PLLLVEEGAA GEGYLGRSSG PLRTFTCLHV PGTHSDPSHG KRGSADSLVE
1910 1920 1930 1940 1950
AVLISEGLGL FARDPRFVAL AKQEIADACR LTLDEMDNAA SDLLAQGTSS
1960 1970
LYSDEESILS RFDEEDLGDE MACVHAL
Length:1,977
Mass (Da):220,678
Last modified:April 14, 2009 - v2
Checksum:i354336550C6D8E73
GO
Isoform 2 (identifier: O60840-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     427-437: Missing.

Show »
Length:1,966
Mass (Da):219,496
Checksum:iFEB47E19FA57E31D
GO
Isoform 3 (identifier: O60840-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,912
Mass (Da):214,033
Checksum:i0E2C45C8E4156E0D
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1236 – 12361E → V in AAB92359. (PubMed:9344658)Curated
Sequence conflicti1860 – 18601A → G in AAB92359. (PubMed:9344658)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141P → L.
Corresponds to variant rs6520408 [ dbSNP | Ensembl ].
VAR_030807
Natural varianti74 – 741C → R in CSNB2A. 1 Publication
VAR_030808
Natural varianti150 – 1501G → R in CSNB2A. 1 Publication
VAR_030809
Natural varianti229 – 2291S → P in CSNB2A. 1 Publication
VAR_030810
Natural varianti261 – 2611G → R in CSNB2A. 1 Publication
VAR_030811
Natural varianti369 – 3691G → D in CSNB2A. 3 Publications
VAR_001504
Natural varianti519 – 5191R → Q in CSNB2A. 1 Publication
Corresponds to variant rs34162630 [ dbSNP | Ensembl ].
VAR_001505
Natural varianti603 – 6031G → R in AIED and CSNB2A. 1 Publication
VAR_071433
Natural varianti635 – 6351V → I in CSNB2A. 1 Publication
Corresponds to variant rs141010716 [ dbSNP | Ensembl ].
VAR_030812
Natural varianti674 – 6741G → D in CSNB2A. 1 Publication
VAR_030813
Natural varianti746 – 7461N → T.1 Publication
Corresponds to variant rs141159097 [ dbSNP | Ensembl ].
VAR_029376
Natural varianti753 – 7531F → C in CSNB2A. 1 Publication
VAR_030814
Natural varianti756 – 7561I → 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. 1 Publication
VAR_030815
Natural varianti860 – 8601L → P in CSNB2A. 1 Publication
VAR_030816
Natural varianti928 – 9281A → D in CSNB2A. 1 Publication
VAR_030817
Natural varianti1018 – 10181G → R in CSNB2A. 1 Publication
VAR_030818
Natural varianti1060 – 10601R → W in CSNB2A. 2 Publications
VAR_001506
Natural varianti1079 – 10791L → P in CSNB2A. 1 Publication
VAR_030819
Natural varianti1259 – 12591A → T.
Corresponds to variant rs34308720 [ dbSNP | Ensembl ].
VAR_055662
Natural varianti1270 – 12701A → T.
Corresponds to variant rs34308720 [ dbSNP | Ensembl ].
VAR_031822
Natural varianti1375 – 13751L → H in CSNB2A. 1 Publication
VAR_001507
Natural varianti1499 – 14991C → R in CSNB2A. 1 Publication
VAR_030820
Natural varianti1500 – 15001P → R in CSNB2A. 1 Publication
VAR_030821
Natural varianti1508 – 15081L → P in CSNB2A. 1 Publication
VAR_030822
Natural varianti1930 – 19301R → H.
Corresponds to variant rs33910054 [ dbSNP | Ensembl ].
VAR_054818

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei9 – 8678DTTPE…RRSCI → GERILPSLQTLGA in isoform 3. 1 PublicationVSP_045172Add
BLAST
Alternative sequencei427 – 43711Missing in isoform 2. 2 PublicationsVSP_036785Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS35253.1. [O60840-1]
CCDS59166.1. [O60840-4]
CCDS59167.1. [O60840-2]
RefSeqiNP_001243718.1. NM_001256789.2. [O60840-2]
NP_001243719.1. NM_001256790.2. [O60840-4]
NP_005174.2. NM_005183.3. [O60840-1]
UniGeneiHs.632799.

Genome annotation databases

EnsembliENST00000323022; ENSP00000321618; ENSG00000102001. [O60840-2]
ENST00000376251; ENSP00000365427; ENSG00000102001. [O60840-4]
ENST00000376265; ENSP00000365441; ENSG00000102001. [O60840-1]
GeneIDi778.
KEGGihsa:778.
UCSCiuc004dnb.3. human. [O60840-1]
uc031tjm.1. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Mutations of the CCNA1F gene

Retina International's Scientific Newsletter

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSi CCDS35253.1. [O60840-1 ]
CCDS59166.1. [O60840-4 ]
CCDS59167.1. [O60840-2 ]
RefSeqi NP_001243718.1. NM_001256789.2. [O60840-2 ]
NP_001243719.1. NM_001256790.2. [O60840-4 ]
NP_005174.2. NM_005183.3. [O60840-1 ]
UniGenei Hs.632799.

3D structure databases

ProteinModelPortali O60840.
SMRi O60840. Positions 94-371, 386-414, 534-770, 866-1137, 1179-1442, 1525-1605.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107232. 1 interaction.
IntActi O60840. 2 interactions.
STRINGi 9606.ENSP00000365441.

Chemistry

ChEMBLi CHEMBL2095229.
DrugBanki DB00568. Cinnarizine.
DB04920. Clevidipine.
DB04855. Dronedarone.
DB00393. Nimodipine.
DB00421. Spironolactone.
DB00661. Verapamil.
GuidetoPHARMACOLOGYi 531.

Protein family/group databases

TCDBi 1.A.1.11.11. the voltage-gated ion channel (vic) superfamily.

PTM databases

PhosphoSitei O60840.

Proteomic databases

PaxDbi O60840.
PRIDEi O60840.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000323022 ; ENSP00000321618 ; ENSG00000102001 . [O60840-2 ]
ENST00000376251 ; ENSP00000365427 ; ENSG00000102001 . [O60840-4 ]
ENST00000376265 ; ENSP00000365441 ; ENSG00000102001 . [O60840-1 ]
GeneIDi 778.
KEGGi hsa:778.
UCSCi uc004dnb.3. human. [O60840-1 ]
uc031tjm.1. human.

Organism-specific databases

CTDi 778.
GeneCardsi GC0XM049061.
GeneReviewsi CACNA1F.
HGNCi HGNC:1393. CACNA1F.
MIMi 300071. phenotype.
300110. gene.
300476. phenotype.
300600. phenotype.
neXtProti NX_O60840.
Orphaneti 178333. Aland Islands eye disease.
1872. Cone rod dystrophy.
215. Congenital stationary night blindness.
PharmGKBi PA26010.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1226.
GeneTreei ENSGT00760000118827.
HOGENOMi HOG000231529.
HOVERGENi HBG050763.
InParanoidi O60840.
KOi K04853.
OMAi AVKSTAC.
PhylomeDBi O60840.
TreeFami TF312805.

Miscellaneous databases

ChiTaRSi CACNA1F. human.
GeneWikii Cav1.4.
GenomeRNAii 778.
NextBioi 3144.
PROi O60840.
SOURCEi Search...

Gene expression databases

Bgeei O60840.
CleanExi HS_CACNA1F.
ExpressionAtlasi O60840. baseline.
Genevestigatori O60840.

Family and domain databases

Gene3Di 1.20.120.350. 5 hits.
InterProi IPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005446. VDCC_L_a1su.
IPR002077. VDCCAlpha1.
[Graphical view ]
Pfami PF08763. Ca_chan_IQ. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view ]
PRINTSi PR00167. CACHANNEL.
PR01630. LVDCCALPHA1.
SMARTi SM01062. Ca_chan_IQ. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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. 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. Cited for: INVOLVEMENT IN AIED.
  14. "A novel p.Gly603Arg mutation in CACNA1F causes Aland island eye disease and incomplete congenital stationary night blindness phenotypes in a family."
    Vincent A., Wright T., Day M.A., Westall C.A., Heon E.
    Mol. Vis. 17:3262-3270(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CSNB2A ARG-603, VARIANT AIED ARG-603.

Entry informationi

Entry nameiCAC1F_HUMAN
AccessioniPrimary (citable) accession number: O60840
Secondary accession number(s): A6NI29
, F5CIQ9, O43901, O95226, Q9UHB1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: April 14, 2009
Last modified: November 26, 2014
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3