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Voltage-dependent L-type calcium channel subunit alpha-1F (Voltage-gated calcium channel subunit alpha Cav1.4)

 CAC1F_MOUSE             Reviewed;        1985 AA.
Q9JIS7;
14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
05-JUL-2017, entry version 129.
RecName: Full=Voltage-dependent L-type calcium channel subunit alpha-1F {ECO:0000250|UniProtKB:O60840};
AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.4;
Name=Cacna1f {ECO:0000312|MGI:MGI:1859639};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=CD-1;
PubMed=10873387; DOI=10.1006/geno.2000.6204;
Naylor M.J., Rancourt D.E., Bech-Hansen N.T.;
"Isolation and characterization of a calcium channel gene, cacna1f,
the murine orthologue of the gene for incomplete X-linked congenital
stationary night blindness.";
Genomics 66:324-327(2000).
[2]
INTERACTION WITH CABP4.
PubMed=15452577; DOI=10.1038/nn1320;
Haeseleer F., Imanishi Y., Maeda T., Possin D.E., Maeda A., Lee A.,
Rieke F., Palczewski K.;
"Essential role of Ca2+-binding protein 4, a Cav1.4 channel regulator,
in photoreceptor synaptic function.";
Nat. Neurosci. 7:1079-1087(2004).
-!- 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) (By
similarity). Activates at more negative voltages and does not
undergo calcium-dependent inactivation (CDI), due to incoming
calcium ions, during depolarization.
{ECO:0000250|UniProtKB:O60840}.
-!- SUBUNIT: 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 (By
similarity). Interacts (via IQ domain) with CABP4; in a calcium
independent manner. {ECO:0000250, ECO:0000269|PubMed:15452577}.
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- TISSUE SPECIFICITY: Expressed in the inner and outer nuclear
layers and the genglion cell layer of the retina.
{ECO:0000269|PubMed:10873387}.
-!- 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.
-!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
1.A.1.11) family. CACNA1F subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF192497; AAF86764.1; -; mRNA.
UniGene; Mm.289647; -.
ProteinModelPortal; Q9JIS7; -.
SMR; Q9JIS7; -.
DIP; DIP-61285N; -.
MINT; MINT-4998297; -.
STRING; 10090.ENSMUSP00000111391; -.
ChEMBL; CHEMBL2176791; -.
GuidetoPHARMACOLOGY; 531; -.
iPTMnet; Q9JIS7; -.
PhosphoSitePlus; Q9JIS7; -.
MaxQB; Q9JIS7; -.
PaxDb; Q9JIS7; -.
PRIDE; Q9JIS7; -.
MGI; MGI:1859639; Cacna1f.
eggNOG; KOG2301; Eukaryota.
eggNOG; ENOG410XNP6; LUCA.
HOGENOM; HOG000231529; -.
HOVERGEN; HBG050763; -.
InParanoid; Q9JIS7; -.
Reactome; R-MMU-419037; NCAM1 interactions.
PRO; PR:Q9JIS7; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0016021; C:integral component of membrane; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0005891; C:voltage-gated calcium channel complex; ISO:MGI.
GO; GO:0008331; F:high voltage-gated calcium channel activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005245; F:voltage-gated calcium channel activity; IMP:MGI.
GO; GO:0007409; P:axonogenesis; IMP:MGI.
GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
GO; GO:0050908; P:detection of light stimulus involved in visual perception; ISO:MGI.
GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
GO; GO:0050856; P:regulation of T cell receptor signaling pathway; IEA:InterPro.
GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
GO; GO:0043029; P:T cell homeostasis; IEA:InterPro.
GO; GO:0007601; P:visual perception; IMP:MGI.
InterPro; IPR031688; CAC1F_C.
InterPro; IPR031649; GPHH_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR014873; VDCC_a1su_IQ.
InterPro; IPR030157; VDCC_L_a1F.
InterPro; IPR005446; VDCC_L_a1su.
InterPro; IPR002077; VDCCAlpha1.
PANTHER; PTHR10037:SF234; PTHR10037:SF234; 1.
Pfam; PF08763; Ca_chan_IQ; 1.
Pfam; PF16885; CAC1F_C; 1.
Pfam; PF16905; GPHH; 1.
Pfam; PF00520; Ion_trans; 4.
PRINTS; PR00167; CACHANNEL.
PRINTS; PR01630; LVDCCALPHA1.
SMART; SM01062; Ca_chan_IQ; 1.
1: Evidence at protein level;
Calcium; Calcium channel; Calcium transport; Complete proteome;
Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
Metal-binding; Reference proteome; Repeat; Sensory transduction;
Transmembrane; Transmembrane helix; Transport; Vision;
Voltage-gated channel.
CHAIN 1 1985 Voltage-dependent L-type calcium channel
subunit alpha-1F.
/FTId=PRO_0000053951.
TOPO_DOM 1 92 Cytoplasmic. {ECO:0000255}.
TRANSMEM 93 111 Helical; Name=S1 of repeat I.
{ECO:0000255}.
TOPO_DOM 112 129 Extracellular. {ECO:0000255}.
TRANSMEM 130 149 Helical; Name=S2 of repeat I.
{ECO:0000255}.
TOPO_DOM 150 161 Cytoplasmic. {ECO:0000255}.
TRANSMEM 162 180 Helical; Name=S3 of repeat I.
{ECO:0000255}.
TOPO_DOM 181 201 Extracellular. {ECO:0000255}.
TRANSMEM 202 220 Helical; Name=S4 of repeat I.
{ECO:0000255}.
TOPO_DOM 221 239 Cytoplasmic. {ECO:0000255}.
TRANSMEM 240 259 Helical; Name=S5 of repeat I.
{ECO:0000255}.
TOPO_DOM 260 347 Extracellular. {ECO:0000255}.
TRANSMEM 348 372 Helical; Name=S6 of repeat I.
{ECO:0000255}.
TOPO_DOM 373 529 Cytoplasmic. {ECO:0000255}.
TRANSMEM 530 549 Helical; Name=S1 of repeat II.
{ECO:0000255}.
TOPO_DOM 550 564 Extracellular. {ECO:0000255}.
TRANSMEM 565 583 Helical; Name=S2 of repeat II.
{ECO:0000255}.
TOPO_DOM 584 591 Cytoplasmic. {ECO:0000255}.
TRANSMEM 592 610 Helical; Name=S3 of repeat II.
{ECO:0000255}.
TOPO_DOM 611 620 Extracellular. {ECO:0000255}.
TRANSMEM 621 639 Helical; Name=S4 of repeat II.
{ECO:0000255}.
TOPO_DOM 640 658 Cytoplasmic. {ECO:0000255}.
TRANSMEM 659 679 Helical; Name=S5 of repeat II.
{ECO:0000255}.
TOPO_DOM 680 733 Extracellular. {ECO:0000255}.
TRANSMEM 734 758 Helical; Name=S6 of repeat II.
{ECO:0000255}.
TOPO_DOM 759 876 Cytoplasmic. {ECO:0000255}.
TRANSMEM 877 895 Helical; Name=S1 of repeat III.
{ECO:0000255}.
TOPO_DOM 896 911 Extracellular. {ECO:0000255}.
TRANSMEM 912 931 Helical; Name=S2 of repeat III.
{ECO:0000255}.
TOPO_DOM 932 943 Cytoplasmic. {ECO:0000255}.
TRANSMEM 944 962 Helical; Name=S3 of repeat III.
{ECO:0000255}.
TOPO_DOM 963 968 Extracellular. {ECO:0000255}.
TRANSMEM 969 988 Helical; Name=S4 of repeat III.
{ECO:0000255}.
TOPO_DOM 989 1007 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1008 1027 Helical; Name=S5 of repeat III.
{ECO:0000255}.
TOPO_DOM 1028 1117 Extracellular. {ECO:0000255}.
TRANSMEM 1118 1138 Helical; Name=S6 of repeat III.
{ECO:0000255}.
TOPO_DOM 1139 1195 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1196 1214 Helical; Name=S1 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1215 1229 Extracellular. {ECO:0000255}.
TRANSMEM 1230 1249 Helical; Name=S2 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1250 1256 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1257 1278 Helical; Name=S3 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1279 1295 Extracellular. {ECO:0000255}.
TRANSMEM 1296 1315 Helical; Name=S4 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1316 1334 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1335 1354 Helical; Name=S5 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1355 1421 Extracellular. {ECO:0000255}.
TRANSMEM 1422 1446 Helical; Name=S6 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1447 1982 Cytoplasmic. {ECO:0000255}.
REPEAT 79 375 I.
REPEAT 515 761 II.
REPEAT 858 1140 III.
REPEAT 1182 1449 IV.
CA_BIND 1475 1486 {ECO:0000250}.
REGION 395 412 Binding to the beta subunit.
{ECO:0000250}.
REGION 1065 1155 Dihydropyridine binding. {ECO:0000250}.
REGION 1402 1468 Dihydropyridine binding. {ECO:0000250}.
REGION 1414 1457 Phenylalkylamine binding. {ECO:0000250}.
COMPBIAS 659 665 Poly-Leu.
COMPBIAS 811 829 Poly-Glu.
COMPBIAS 1126 1129 Poly-Ile.
COMPBIAS 1645 1652 Poly-Glu.
COMPBIAS 1657 1664 Poly-Glu.
SITE 330 330 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 711 711 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1091 1091 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1388 1388 Calcium ion selectivity and permeability.
{ECO:0000250}.
CARBOHYD 295 295 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 1985 AA; 221926 MW; C365A105614ACAD5 CRC64;
MSESEVGKDT TPEPSPANGT GPGPEWGLCP GPPTVGTDTS GASGLGTPRR RTQHNKHKTV
AVASAQRSPR ALFCLTLTNP IRRSCISIVE WKPFDILILL TIFANCVALG VYIPFPEDDS
NTANHNLEQV EYVFLVIFTV ETVLKIVAYG LVLHPSAYIR NGWNLLDFII VVVGLFSVLL
EQGPGRPGDA PHTGGKPGGF DVKALRAFRV LRPLRLVSGV PSLHIVVNSI MKALVPLLHI
ALLVLFVIII YAIIGLELFL GRMHKTCYFL GSDMEAEEDP SPCASSGSGR SCTLNHTECR
GRWPGPNGGI TNFDNFFFAM LTVFQCITME GWTDVLYWMQ DAMGYELPWV YFVSLVIFGS
FFVLNLVLGV LSGEFSKERE KAKARGDFQK LREKQQMEED LRGYLDWITQ AEELDLHDPS
VDGNLASLAE EGRAGHRPQL SELTNRRRGR LRWFSHSTRS THSTSSHASL PASDTGSMTD
TPGDEDEEEG TMASCTRCLN KIMKTRICRH FRRANRGLRA RCRRAVKSNA CYWAVLLLVF
LNTLTIASEH HGQPLWLTQT QEYANKVLLC LFTVEMLLKL YGLGPSVYVA SFFNRFDCFV
VCGGILETTL VEVGAMQPLG ISVLRCVRLL RIFKVTRHWA SLSNLVASLL NSMKSIASLL
LLLFLFIIIF SLLGMQLFGG KFNFDQTHTK RSTFDTFPQA LLTVFQILTG EDWNVVMYDG
IMAYGGPFFP GMLVCVYFII LFICGNYILL NVFLAIAVDN LASGDAGTAK DKGREKSSEG
NPPKENKVLV PGGENEDAKG ARSEGAAPGM EEEEEEEEEE EEEEEEEEEN GAGHVELLQE
VVPKEKVVPI PEGSAFFCLS QTNPLRKACH TLIHHHIFTS LILVFIILSS VSLAAEDPIR
AHSFRNHILG YFDYAFTSIF TVEILLKMTV FGAFLHRGSF CRSWFNLLDL LVVSVSLISF
GIHSSAISVV KILRVLRVLR PLRAINRAKG LKHVVQCVFV AIRTIGNIMI VTTLLQFMFA
CIGVQLFKGK FYSCTDEAKH TLKESKGSFL IYPDGDVSRP LVRERLWVNS DFNFDNVLSA
MMALFTVSTF EGWPALLYKA IDANAEDEGP IYNYHVEISV FFIVYIIIIA FFMMNIFVGF
VIITFRAQGE QEYQNCELDK NQRQCVEYAL KAQPLRRYIP KNPHQYRVWA TVNSRAFEYL
MFLLILLNTV ALAMQHYEQT APFNYAMDIL NMVFTGLFTI EMVLKIIAFK PKHYFADAWN
TFDALIVVGS VVDIAVTEVN NGGHLGESSE DTSRISITFF RLFRVMRLVK LLSKGEGIRT
LLWTFIKSFQ ALPYVALLIA MIFFIYAVIG MQMFGLVALQ DGTQINRNNN FQTFPQAVLL
LFRCATGEAW QEIMLASLPG NRCDPESDFG PGEEFTCGSS FAIVYFISFF MLCAFLIINL
FVAVIMDNFD YLTRDWSILG PHHLDEFKRI WSEYDPGAKG RIKHLDVVAL LRRIQPPLGF
GKLCPHRVAC KRLVAMNVPL NSDGTVTFNA TLFALVRTSL KIKTEGNLDQ ANQELRMVIK
KIWKRIKQKL LDEVIPPPDE EEVTVGKFYA TFLIQDYFRK FRRRKEKGLL GREAPTSTSS
ALQAGLRSLQ DLGPEIRQAL TYVTEEEEEE EEAVGQEAEE EEAENNPEPY KDSIDSQPQS
RWNSRISVSL PVKEKLPDSL STGPSDDDGL APNSRQPSVI QAGSQPHRRS SGVFMFTIPE
EGSIQLKGTQ GQDNQNEEQE LPDWTPDLDR AGRDSFEPSP FTTSLVQQHV NGHMSTPTFA
APHACRSEPS FTIQCLQRLG SCEDLPIPGT YHRGRTSGPS RAQGSWAAPP QKGRLLYAPL
LLVEESTVGE GYLGKLGGPL RTFTCLQVPG AHPNPSHRKR GSADSLVEAV LISEGLGLFA
QDPRFVALAK QEIADACHLT LDEMDSAASD LLAQRTISLY SDEESILSRF DEEDLGDEMA
CVHAL


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