CAC1F_MOUSE
ID CAC1F_MOUSE Reviewed; 1985 AA.
AC Q9JIS7;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha-1F {ECO:0000250|UniProtKB:O60840};
DE AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.4;
GN Name=Cacna1f {ECO:0000312|MGI:MGI:1859639};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=CD-1;
RX PubMed=10873387; DOI=10.1006/geno.2000.6204;
RA Naylor M.J., Rancourt D.E., Bech-Hansen N.T.;
RT "Isolation and characterization of a calcium channel gene, cacna1f, the
RT murine orthologue of the gene for incomplete X-linked congenital stationary
RT night blindness.";
RL Genomics 66:324-327(2000).
RN [2]
RP INTERACTION WITH CABP4.
RX PubMed=15452577; DOI=10.1038/nn1320;
RA Haeseleer F., Imanishi Y., Maeda T., Possin D.E., Maeda A., Lee A.,
RA Rieke F., Palczewski K.;
RT "Essential role of Ca2+-binding protein 4, a Cav1.4 channel regulator, in
RT photoreceptor synaptic function.";
RL Nat. Neurosci. 7:1079-1087(2004).
CC -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry
CC of calcium ions into excitable cells and are also involved in a variety
CC of calcium-dependent processes, including muscle contraction, hormone
CC or neurotransmitter release, gene expression, cell motility, cell
CC division and cell death. The isoform alpha-1F gives rise to L-type
CC calcium currents. Long-lasting (L-type) calcium channels belong to the
CC 'high-voltage activated' (HVA) group. They are blocked by
CC dihydropyridines (DHP), phenylalkylamines, and by benzothiazepines (By
CC similarity). Activates at more negative voltages and does not undergo
CC calcium-dependent inactivation (CDI), due to incoming calcium ions,
CC during depolarization. {ECO:0000250|UniProtKB:O60840}.
CC -!- SUBUNIT: Voltage-dependent calcium channels are multisubunit complexes,
CC consisting of alpha-1, alpha-2, beta and delta subunits in a 1:1:1:1
CC ratio. The channel activity is directed by the pore-forming and
CC voltage-sensitive alpha-1 subunit. In many cases, this subunit is
CC sufficient to generate voltage-sensitive calcium channel activity. The
CC auxiliary subunits beta and alpha-2/delta linked by a disulfide bridge
CC regulate the channel activity (By similarity). Interacts (via IQ
CC domain) with CABP4; in a calcium independent manner. {ECO:0000250,
CC ECO:0000269|PubMed:15452577}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in the inner and outer nuclear layers and
CC the genglion cell layer of the retina. {ECO:0000269|PubMed:10873387}.
CC -!- DOMAIN: Each of the four internal repeats contains five hydrophobic
CC transmembrane segments (S1, S2, S3, S5, S6) and one positively charged
CC transmembrane segment (S4). S4 segments probably represent the voltage-
CC sensor and are characterized by a series of positively charged amino
CC acids at every third position.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. CACNA1F subfamily. {ECO:0000305}.
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DR EMBL; AF192497; AAF86764.1; -; mRNA.
DR AlphaFoldDB; Q9JIS7; -.
DR SMR; Q9JIS7; -.
DR DIP; DIP-61285N; -.
DR IntAct; Q9JIS7; 2.
DR STRING; 10090.ENSMUSP00000111391; -.
DR BindingDB; Q9JIS7; -.
DR ChEMBL; CHEMBL2176791; -.
DR DrugCentral; Q9JIS7; -.
DR GuidetoPHARMACOLOGY; 531; -.
DR GlyGen; Q9JIS7; 1 site.
DR iPTMnet; Q9JIS7; -.
DR PhosphoSitePlus; Q9JIS7; -.
DR MaxQB; Q9JIS7; -.
DR PaxDb; Q9JIS7; -.
DR PRIDE; Q9JIS7; -.
DR ProteomicsDB; 273885; -.
DR MGI; MGI:1859639; Cacna1f.
DR eggNOG; KOG2301; Eukaryota.
DR InParanoid; Q9JIS7; -.
DR PRO; PR:Q9JIS7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9JIS7; protein.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; ISO:MGI.
DR GO; GO:0008331; F:high voltage-gated calcium channel activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IMP:MGI.
DR GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; ISO:MGI.
DR GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; ISO:MGI.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR031688; CAC1F_C.
DR InterPro; IPR031649; GPHH_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR014873; VDCC_a1su_IQ.
DR InterPro; IPR005446; VDCC_L_a1su.
DR InterPro; IPR002077; VDCCAlpha1.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR Pfam; PF08763; Ca_chan_IQ; 1.
DR Pfam; PF16885; CAC1F_C; 1.
DR Pfam; PF16905; GPHH; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00167; CACHANNEL.
DR PRINTS; PR01630; LVDCCALPHA1.
DR SMART; SM01062; Ca_chan_IQ; 1.
PE 1: Evidence at protein level;
KW Calcium; Calcium channel; Calcium transport; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Metal-binding; Reference proteome;
KW Repeat; Sensory transduction; Transmembrane; Transmembrane helix;
KW Transport; Vision; Voltage-gated channel.
FT CHAIN 1..1985
FT /note="Voltage-dependent L-type calcium channel subunit
FT alpha-1F"
FT /id="PRO_0000053951"
FT TOPO_DOM 1..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..111
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..129
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..149
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..180
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..201
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..220
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..259
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..347
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..372
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..529
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..549
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 550..564
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 565..583
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 584..591
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 592..610
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 611..620
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 621..639
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 640..658
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 659..679
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 680..733
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 734..758
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 759..876
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 877..895
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 896..911
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 912..931
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 932..943
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 944..962
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 963..968
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 969..988
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 989..1007
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1008..1027
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1028..1117
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1118..1138
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1139..1195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1196..1214
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1215..1229
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1230..1249
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1250..1256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1257..1278
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1279..1295
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1296..1315
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1316..1334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1335..1354
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1355..1421
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1422..1446
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1447..1982
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 79..375
FT /note="I"
FT REPEAT 515..761
FT /note="II"
FT REPEAT 858..1140
FT /note="III"
FT REPEAT 1182..1449
FT /note="IV"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..412
FT /note="Binding to the beta subunit"
FT /evidence="ECO:0000250"
FT REGION 455..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1155
FT /note="Dihydropyridine binding"
FT /evidence="ECO:0000250"
FT REGION 1402..1468
FT /note="Dihydropyridine binding"
FT /evidence="ECO:0000250"
FT REGION 1414..1457
FT /note="Phenylalkylamine binding"
FT /evidence="ECO:0000250"
FT REGION 1643..1729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1746..1778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..782
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..831
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1644..1666
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1670..1687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1706..1729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1746..1761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 330
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT BINDING 711
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT BINDING 1091
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ 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
