Reviewed, UniProtKB/Swiss-Prot O60840 (CAC1F_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1977 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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-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).
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.2
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	Defects in CACNA1F are the cause of congenital stationary night blindness type 2A (CSNB2A) [MIM:300071]. Congenital stationary night blindness is a non-progressive retinal disorder characterized by impaired night vision. Ref.1 Ref.5 Ref.6 Ref.7 Ref.8 Defects in CACNA1F are the cause of cone-rod dystrophy X-linked type 3 (CORDX3) [MIM:300476]. CORDs are inherited retinal dystrophies belonging to the group of pigmentary retinopathies. CORDs are 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. Ref.10 Defects in CACNA1F are the cause of Aaland island eye disease (AIED) [MIM:300600]; also known as Forsius-Eriksson type ocular albinism. On the Aaland island in the Baltic Sea, AIED is an X-linked recessive 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. Ref.11
Sequence similarities	Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family. [View classification]
Sequence caution	The sequence AAB92359.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Calcium transport Ion transport Sensory transduction Transport Vision
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Cone-rod dystrophy Congenital stationary night blindness Disease mutation
Domain	Repeat Transmembrane
Ligand	Calcium
Molecular function	Calcium channel Ionic channel Voltage-gated channel
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	calcium ion transport Inferred from electronic annotation. Source: UniProtKB-KW detection of light stimulus involved in visual perception Inferred from mutant phenotype. Source: UniProtKB
Cellular component	voltage-gated calcium channel complex Ref.8 Inferred from direct assay. Source: UniProtKB
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW dihydropyridine-sensitive calcium channel activity Ref.8 Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FYN	P06241	1	EBI-1757401,EBI-515315

Alternative products

This entry describes 2 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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1977	1977	Voltage-dependent L-type calcium channel subunit alpha-1F		PRO_0000053950
Regions
	Topological domain	1 – 92	92	Cytoplasmic Potential
	Transmembrane	93 – 111	19	S1 of repeat I Potential
	Topological domain	112 – 129	18	Extracellular Potential
	Transmembrane	130 – 149	20	S2 of repeat I Potential
	Topological domain	150 – 161	12	Cytoplasmic Potential
	Transmembrane	162 – 180	19	S3 of repeat I Potential
	Topological domain	181 – 201	21	Extracellular Potential
	Transmembrane	202 – 220	19	S4 of repeat I Potential
	Topological domain	221 – 239	19	Cytoplasmic Potential
	Transmembrane	240 – 259	20	S5 of repeat I Potential
	Topological domain	260 – 347	88	Extracellular Potential
	Transmembrane	348 – 372	25	S6 of repeat I Potential
	Topological domain	373 – 529	157	Cytoplasmic Potential
	Transmembrane	530 – 549	20	S1 of repeat II Potential
	Topological domain	550 – 564	15	Extracellular Potential
	Transmembrane	565 – 583	19	S2 of repeat II Potential
	Topological domain	584 – 591	8	Cytoplasmic Potential
	Transmembrane	592 – 610	19	S3 of repeat II Potential
	Topological domain	611 – 620	10	Extracellular Potential
	Transmembrane	621 – 639	19	S4 of repeat II Potential
	Topological domain	640 – 658	19	Cytoplasmic Potential
	Transmembrane	659 – 679	21	S5 of repeat II Potential
	Topological domain	680 – 733	54	Extracellular Potential
	Transmembrane	734 – 758	25	S6 of repeat II Potential
	Topological domain	759 – 871	113	Cytoplasmic Potential
	Transmembrane	872 – 890	19	S1 of repeat III Potential
	Topological domain	891 – 906	16	Extracellular Potential
	Transmembrane	907 – 926	20	S2 of repeat III Potential
	Topological domain	927 – 938	12	Cytoplasmic Potential
	Transmembrane	939 – 957	19	S3 of repeat III Potential
	Topological domain	958 – 963	6	Extracellular Potential
	Transmembrane	964 – 983	20	S4 of repeat III Potential
	Topological domain	984 – 1002	19	Cytoplasmic Potential
	Transmembrane	1003 – 1022	20	S5 of repeat III Potential
	Topological domain	1023 – 1112	90	Extracellular Potential
	Transmembrane	1113 – 1133	21	S6 of repeat III Potential
	Topological domain	1134 – 1190	57	Cytoplasmic Potential
	Transmembrane	1191 – 1209	19	S1 of repeat IV Potential
	Topological domain	1210 – 1224	15	Extracellular Potential
	Transmembrane	1225 – 1244	20	S2 of repeat IV Potential
	Topological domain	1245 – 1251	7	Cytoplasmic Potential
	Transmembrane	1252 – 1273	22	S3 of repeat IV Potential
	Topological domain	1274 – 1290	17	Extracellular Potential
	Transmembrane	1291 – 1310	20	S4 of repeat IV Potential
	Topological domain	1311 – 1329	19	Cytoplasmic Potential
	Transmembrane	1330 – 1349	20	S5 of repeat IV Potential
	Topological domain	1350 – 1416	67	Extracellular Potential
	Transmembrane	1417 – 1441	25	S6 of repeat IV Potential
	Topological domain	1442 – 1977	536	Cytoplasmic Potential
	Repeat	79 – 375	297	I
	Repeat	515 – 761	247	II
	Repeat	858 – 1140	283	III
	Repeat	1177 – 1444	268	IV
	Calcium binding	1470 – 1481	12	By similarity
	Region	395 – 412	18	Binding to the beta subunit By similarity
	Region	1060 – 1150	91	Dihydropyridine binding By similarity
	Region	1397 – 1463	67	Dihydropyridine binding By similarity
	Region	1409 – 1452	44	Phenylalkylamine binding By similarity
	Compositional bias	659 – 665	7	Poly-Leu
	Compositional bias	794 – 799	6	Poly-Glu
	Compositional bias	809 – 825	17	Poly-Glu
	Compositional bias	1121 – 1124	4	Poly-Ile
	Compositional bias	1640 – 1645	6	Poly-Glu
Sites
	Site	330	1	Calcium ion selectivity and permeability By similarity
	Site	711	1	Calcium ion selectivity and permeability By similarity
	Site	1086	1	Calcium ion selectivity and permeability By similarity
	Site	1383	1	Calcium ion selectivity and permeability By similarity
Amino acid modifications
	Modified residue	1452	1	Phosphoserine; by PKA Potential
	Glycosylation	295	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	427 – 437	11	Missing in isoform 2.		VSP_036785
	Natural variant	14	1	P → L: dbSNP rs6520408.		VAR_030807
	Natural variant	74	1	C → R in CSNB2A. Ref.6		VAR_030808
	Natural variant	150	1	G → R in CSNB2A. Ref.7		VAR_030809
	Natural variant	229	1	S → P in CSNB2A. Ref.6		VAR_030810
	Natural variant	261	1	G → R in CSNB2A. Ref.6		VAR_030811
	Natural variant	369	1	G → D in CSNB2A. Ref.1 Ref.5 Ref.6		VAR_001504
	Natural variant	519	1	R → Q in CSNB2A. dbSNP rs34162630. Ref.1		VAR_001505
	Natural variant	635	1	V → I in CSNB2A. Ref.7		VAR_030812
	Natural variant	674	1	G → D in CSNB2A. Ref.5		VAR_030813
	Natural variant	746	1	N → T		VAR_029376
	Natural variant	753	1	F → C in CSNB2A. Ref.6		VAR_030814
	Natural variant	756	1	I → T in CSNB2A; increases the number of mutant channels open at physiologic membrane potential and allows for persistent Ca(2+) entry due to reduced channel inactivation resulting in a gain-of-function defect. Ref.8		VAR_030815
	Natural variant	860	1	L → P in CSNB2A. Ref.6		VAR_030816
	Natural variant	928	1	A → D in CSNB2A. Ref.5		VAR_030817
	Natural variant	1018	1	G → R in CSNB2A. Ref.6		VAR_030818
	Natural variant	1060	1	R → W in CSNB2A. Ref.1 Ref.6		VAR_001506
	Natural variant	1079	1	L → P in CSNB2A. Ref.6		VAR_030819
	Natural variant	1259	1	A → T: dbSNP rs34308720.		VAR_055662
	Natural variant	1270	1	A → T: dbSNP rs34308720.		VAR_031822
	Natural variant	1375	1	L → H in CSNB2A. Ref.1		VAR_001507
	Natural variant	1499	1	C → R in CSNB2A. Ref.6		VAR_030820
	Natural variant	1500	1	P → R in CSNB2A. Ref.6		VAR_030821
	Natural variant	1508	1	L → P in CSNB2A. Ref.6		VAR_030822
	Natural variant	1930	1	R → H: dbSNP rs33910054.		VAR_054818
Experimental info
	Sequence conflict	1236	1	E → V in AAB92359. Ref.4
	Sequence conflict	1860	1	A → G in AAB92359. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 14, 2009. Version 2. Checksum: 354336550C6D8E73	FASTA	1,977	220,678
	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
	Isoform 2. Checksum: FEB47E19FA57E31D	FASTA	1,966	219,496
	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 ADDNLGPQLA ELTNRRRGRL RWFSHSTRST HSTSSHASLP ASDTGSMTET QGDEDEEEGA 490 500 510 520 530 540 LASCTRCLNK IMKTRVCRRL RRANRVLRAR CRRAVKSNAC YWAVLLLVFL NTLTIASEHH 550 560 570 580 590 600 GQPVWLTQIQ EYANKVLLCL FTVEMLLKLY GLGPSAYVSS FFNRFDCFVV CGGILETTLV 610 620 630 640 650 660 EVGAMQPLGI SVLRCVRLLR IFKVTRHWAS LSNLVASLLN SMKSIASLLL LLFLFIIIFS 670 680 690 700 710 720 LLGMQLFGGK FNFDQTHTKR STFDTFPQAL LTVFQILTGE DWNVVMYDGI MAYGGPFFPG 730 740 750 760 770 780 MLVCIYFIIL FICGNYILLN VFLAIAVDNL ASGDAGTAKD KGGEKSNEKD LPQENEGLVP 790 800 810 820 830 840 GVEKEEEEGA RREGADMEEE EEEEEEEEEE EEEEGAGGVE LLQEVVPKEK VVPIPEGSAF 850 860 870 880 890 900 FCLSQTNPLR KGCHTLIHHH VFTNLILVFI ILSSVSLAAE DPIRAHSFRN HILGYFDYAF 910 920 930 940 950 960 TSIFTVEILL KMTVFGAFLH RGSFCRSWFN MLDLLVVSVS LISFGIHSSA ISVVKILRVL 970 980 990 1000 1010 1020 RVLRPLRAIN RAKGLKHVVQ CVFVAIRTIG NIMIVTTLLQ FMFACIGVQL FKGKFYTCTD 1030 1040 1050 1060 1070 1080 EAKHTPQECK GSFLVYPDGD VSRPLVRERL WVNSDFNFDN VLSAMMALFT VSTFEGWPAL 1090 1100 1110 1120 1130 1140 LYKAIDAYAE DHGPIYNYRV EISVFFIVYI IIIAFFMMNI FVGFVIITFR AQGEQEYQNC 1150 1160 1170 1180 1190 1200 ELDKNQRQCV EYALKAQPLR RYIPKNPHQY RVWATVNSAA FEYLMFLLIL LNTVALAMQH 1210 1220 1230 1240 1250 1260 YEQTAPFNYA MDILNMVFTG LFTIEMVLKI IAFKPKHYFT DAWNTFDALI VVGSIVDIAV 1270 1280 1290 1300 1310 1320 TEVNNGGHLG ESSEDSSRIS ITFFRLFRVM RLVKLLSKGE GIRTLLWTFI KSFQALPYVA 1330 1340 1350 1360 1370 1380 LLIAMIFFIY AVIGMQMFGK VALQDGTQIN RNNNFQTFPQ AVLLLFRCAT GEAWQEIMLA 1390 1400 1410 1420 1430 1440 SLPGNRCDPE SDFGPGEEFT CGSNFAIAYF ISFFMLCAFL IINLFVAVIM DNFDYLTRDW 1450 1460 1470 1480 1490 1500 SILGPHHLDE FKRIWSEYDP GAKGRIKHLD VVALLRRIQP PLGFGKLCPH RVACKRLVAM 1510 1520 1530 1540 1550 1560 NMPLNSDGTV TFNATLFALV RTSLKIKTEG NLEQANQELR IVIKKIWKRM KQKLLDEVIP 1570 1580 1590 1600 1610 1620 PPDEEEVTVG KFYATFLIQD YFRKFRRRKE KGLLGNDAAP STSSALQAGL RSLQDLGPEM 1630 1640 1650 1660 1670 1680 RQALTCDTEE EEEEGQEGVE EEDEKDLETN KATMVSQPSA RRGSGISVSL PVGDRLPDSL 1690 1700 1710 1720 1730 1740 SFGPSDDDRG TPTSSQPSVP QAGSNTHRRG SGALIFTIPE EGNSQPKGTK GQNKQDEDEE 1750 1760 1770 1780 1790 1800 VPDRLSYLDE QAGTPPCSVL LPPHRAQRYM DGHLVPRRRL LPPTPAGRKP SFTIQCLQRQ 1810 1820 1830 1840 1850 1860 GSCEDLPIPG TYHRGRNSGP NRAQGSWATP PQRGRLLYAP LLLVEEGAAG EGYLGRSSGP 1870 1880 1890 1900 1910 1920 LRTFTCLHVP GTHSDPSHGK RGSADSLVEA VLISEGLGLF ARDPRFVALA KQEIADACRL 1930 1940 1950 1960 TLDEMDNAAS DLLAQGTSSL YSDEESILSR FDEEDLGDEM ACVHAL

References

	« Hide 'large scale' referencesShow '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: 9662399] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), VARIANTS CSNB2A ASP-369; GLN-519; TRP-1060 AND HIS-1375. Tissue: Retina.
[2]	"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: 10873387] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[3]	"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: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: 9344658] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1211-1977.
[5]	"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: 11281458] [Abstract] Cited for: VARIANTS CSNB2A ASP-369; ASP-674 AND ASP-928.
[6]	"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: 12111638] [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.
[7]	"Infantile and childhood retinal blindness: a molecular perspective (The Franceschetti Lecture)." Weleber R.G. Ophthalmic Genet. 23:71-97(2002) [PubMed: 12187427] [Abstract] Cited for: VARIANTS CSNB2A ARG-150 AND ILE-635.
[8]	"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: 15897456] [Abstract] Cited for: VARIANT CSNB2A THR-756, CHARACTERIZATION OF VARIANT CSNB2A THR-756.
[9]	"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: 16960802] [Abstract] Cited for: VARIANT THR-746.
[10]	"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: 16505158] [Abstract] Cited for: INVOLVEMENT IN CORDX3.
[11]	"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: 17525176] [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
EMBLGenBankDDBJ	AJ006216 Genomic DNA. Translation: CAA06916.1. AJ224874 mRNA. Translation: CAA12175.1. AF201304 mRNA. Translation: AAF15290.1. AF196779 Genomic DNA. No translation available. AF235097 Genomic DNA. No translation available. U93305 Genomic DNA. Translation: AAB92359.1. Sequence problems.
IPI	IPI00465135. IPI00925706.
RefSeq	NP_005174.2.
UniGene	Hs.632799
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	O60840. 1 interaction.
STRING	O60840.
Protein family/group databases
TCDB	1.A.1.11.11. voltage-gated ion channel (VIC) superfamily. 1.A.1.11.15. voltage-gated ion channel (VIC) superfamily.
Proteomic databases
PRIDE	O60840.
Genome annotation databases
Ensembl	ENST00000323022; ENSP00000321618; ENSG00000102001; Homo sapiens. [Genome view] ENST00000376251; ENSP00000365427; ENSG00000102001; Homo sapiens. [Genome view] ENST00000376265; ENSP00000365441; ENSG00000102001; Homo sapiens. [Genome view]
GeneID	778.
KEGG	hsa:778.
UCSC	uc004dnb.1. human. uc010nip.1. human.
Organism-specific databases
CTD	778.
GeneCards	GC0XM048948.
HGNC	HGNC:1393. CACNA1F.
MIM	300071. phenotype. 300110. gene. 300476. phenotype. 300600. phenotype.
Orphanet	178333. Aland Island eye disease. 1872. Cone rod dystrophy. 215. Night blindness, stationary, congenital.
PharmGKB	PA26010.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	O60840.
OMA	ETTLVEV.
Gene expression databases
ArrayExpress	O60840.
Bgee	O60840.
CleanEx	HS_CACNA1F.
Genevestigator	O60840.
GermOnline	ENSG00000102001. Homo sapiens.
Family and domain databases
InterPro	IPR005821. Ion_trans. IPR014873. VDCC_a1su_IQ. IPR005446. VDCC_L_a1su. IPR002077. VDCCAlpha1. [Graphical view]
Pfam	PF08763. Ca_chan_IQ. 1 hit. PF00520. Ion_trans. 4 hits. [Graphical view]
PRINTS	PR00167. CACHANNEL. PR01630. LVDCCALPHA1.
ProtoNet	Search...
Other Resources
DrugBank	DB00661. Verapamil.
SOURCE	Search...

Entry information

Entry name

CAC1F_HUMAN

Accession

Primary (citable) accession number: O60840
Secondary accession number(s): A6NI29, O43901, Q9UHB1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	April 14, 2009
Last modified:	November 3, 2009
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.