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O60840

- CAC1F_HUMAN

UniProt

O60840 - CAC1F_HUMAN

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
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (14 Apr 2009)
      Previous versions | rss
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    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

    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

    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

    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.6 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 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    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

    ArrayExpressiO60840.
    BgeeiO60840.
    CleanExiHS_CACNA1F.
    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...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 9292CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini112 – 12918ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini150 – 16112CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini181 – 20121ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini221 – 23919CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini260 – 34788ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini373 – 529157CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini550 – 56415ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini584 – 5918CytoplasmicSequence Analysis
    Topological domaini611 – 62010ExtracellularSequence Analysis
    Topological domaini640 – 65819CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini680 – 73354ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini759 – 871113CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini891 – 90616ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini927 – 93812CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini958 – 9636ExtracellularSequence Analysis
    Topological domaini984 – 100219CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1023 – 111290ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1134 – 119057CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1210 – 122415ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1245 – 12517CytoplasmicSequence Analysis
    Topological domaini1274 – 129017ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1311 – 132919CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1350 – 141667ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1442 – 1977536CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei93 – 11119Helical; Name=S1 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei130 – 14920Helical; Name=S2 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei162 – 18019Helical; Name=S3 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei202 – 22019Helical; Name=S4 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei240 – 25920Helical; Name=S5 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei348 – 37225Helical; Name=S6 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei530 – 54920Helical; Name=S1 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei565 – 58319Helical; Name=S2 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei592 – 61019Helical; Name=S3 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei621 – 63919Helical; Name=S4 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei659 – 67921Helical; Name=S5 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei734 – 75825Helical; Name=S6 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei872 – 89019Helical; Name=S1 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei907 – 92620Helical; Name=S2 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei939 – 95719Helical; Name=S3 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei964 – 98320Helical; Name=S4 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1003 – 102220Helical; Name=S5 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1113 – 113321Helical; Name=S6 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1191 – 120919Helical; Name=S1 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1225 – 124420Helical; Name=S2 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1252 – 127322Helical; Name=S3 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1291 – 131020Helical; Name=S4 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1330 – 134920Helical; Name=S5 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1417 – 144125Helical; Name=S6 of repeat IVSequence AnalysisAdd
    BLAST

    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.
    HOGENOMiHOG000231529.
    HOVERGENiHBG050763.
    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

    MSESEGGKDT TPEPSPANGA GPGPEWGLCP GPPAVEGESS GASGLGTPKR     50
    RNQHSKHKTV AVASAQRSPR ALFCLTLANP LRRSCISIVE WKPFDILILL 100
    TIFANCVALG VYIPFPEDDS NTANHNLEQV EYVFLVIFTV ETVLKIVAYG 150
    LVLHPSAYIR NGWNLLDFII VVVGLFSVLL EQGPGRPGDA PHTGGKPGGF 200
    DVKALRAFRV LRPLRLVSGV PSLHIVLNSI MKALVPLLHI ALLVLFVIII 250
    YAIIGLELFL GRMHKTCYFL GSDMEAEEDP SPCASSGSGR ACTLNQTECR 300
    GRWPGPNGGI TNFDNFFFAM LTVFQCVTME GWTDVLYWMQ DAMGYELPWV 350
    YFVSLVIFGS FFVLNLVLGV LSGEFSKERE KAKARGDFQK QREKQQMEED 400
    LRGYLDWITQ AEELDMEDPS ADDNLGSMAE EGRAGHRPQL AELTNRRRGR 450
    LRWFSHSTRS THSTSSHASL PASDTGSMTE TQGDEDEEEG ALASCTRCLN 500
    KIMKTRVCRR LRRANRVLRA RCRRAVKSNA CYWAVLLLVF LNTLTIASEH 550
    HGQPVWLTQI QEYANKVLLC LFTVEMLLKL YGLGPSAYVS SFFNRFDCFV 600
    VCGGILETTL VEVGAMQPLG ISVLRCVRLL RIFKVTRHWA SLSNLVASLL 650
    NSMKSIASLL LLLFLFIIIF SLLGMQLFGG KFNFDQTHTK RSTFDTFPQA 700
    LLTVFQILTG EDWNVVMYDG IMAYGGPFFP GMLVCIYFII LFICGNYILL 750
    NVFLAIAVDN LASGDAGTAK DKGGEKSNEK DLPQENEGLV PGVEKEEEEG 800
    ARREGADMEE EEEEEEEEEE EEEEEGAGGV ELLQEVVPKE KVVPIPEGSA 850
    FFCLSQTNPL RKGCHTLIHH HVFTNLILVF IILSSVSLAA EDPIRAHSFR 900
    NHILGYFDYA FTSIFTVEIL LKMTVFGAFL HRGSFCRSWF NMLDLLVVSV 950
    SLISFGIHSS AISVVKILRV LRVLRPLRAI NRAKGLKHVV QCVFVAIRTI 1000
    GNIMIVTTLL QFMFACIGVQ LFKGKFYTCT DEAKHTPQEC KGSFLVYPDG 1050
    DVSRPLVRER LWVNSDFNFD NVLSAMMALF TVSTFEGWPA LLYKAIDAYA 1100
    EDHGPIYNYR VEISVFFIVY IIIIAFFMMN IFVGFVIITF RAQGEQEYQN 1150
    CELDKNQRQC VEYALKAQPL RRYIPKNPHQ YRVWATVNSA AFEYLMFLLI 1200
    LLNTVALAMQ HYEQTAPFNY AMDILNMVFT GLFTIEMVLK IIAFKPKHYF 1250
    TDAWNTFDAL IVVGSIVDIA VTEVNNGGHL GESSEDSSRI SITFFRLFRV 1300
    MRLVKLLSKG EGIRTLLWTF IKSFQALPYV ALLIAMIFFI YAVIGMQMFG 1350
    KVALQDGTQI NRNNNFQTFP QAVLLLFRCA TGEAWQEIML ASLPGNRCDP 1400
    ESDFGPGEEF TCGSNFAIAY FISFFMLCAF LIINLFVAVI MDNFDYLTRD 1450
    WSILGPHHLD EFKRIWSEYD PGAKGRIKHL DVVALLRRIQ PPLGFGKLCP 1500
    HRVACKRLVA MNMPLNSDGT VTFNATLFAL VRTSLKIKTE GNLEQANQEL 1550
    RIVIKKIWKR MKQKLLDEVI PPPDEEEVTV GKFYATFLIQ DYFRKFRRRK 1600
    EKGLLGNDAA PSTSSALQAG LRSLQDLGPE MRQALTCDTE EEEEEGQEGV 1650
    EEEDEKDLET NKATMVSQPS ARRGSGISVS LPVGDRLPDS LSFGPSDDDR 1700
    GTPTSSQPSV PQAGSNTHRR GSGALIFTIP EEGNSQPKGT KGQNKQDEDE 1750
    EVPDRLSYLD EQAGTPPCSV LLPPHRAQRY MDGHLVPRRR LLPPTPAGRK 1800
    PSFTIQCLQR QGSCEDLPIP GTYHRGRNSG PNRAQGSWAT PPQRGRLLYA 1850
    PLLLVEEGAA GEGYLGRSSG PLRTFTCLHV PGTHSDPSHG KRGSADSLVE 1900
    AVLISEGLGL FARDPRFVAL AKQEIADACR LTLDEMDNAA SDLLAQGTSS 1950
    LYSDEESILS RFDEEDLGDE MACVHAL 1977
    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.

    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 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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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

    BindingDBi O60840.
    ChEMBLi CHEMBL2363032.
    DrugBanki 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.
    HOGENOMi HOG000231529.
    HOVERGENi HBG050763.
    KOi K04853.
    OMAi AVKSTAC.
    PhylomeDBi O60840.
    TreeFami TF312805.

    Miscellaneous databases

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

    Gene expression databases

    ArrayExpressi O60840.
    Bgeei O60840.
    CleanExi HS_CACNA1F.
    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

    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.

    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: October 1, 2014
    This is version 148 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