ID I3MW93_ICTTR Unreviewed; 1981 AA.
AC I3MW93;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1F {ECO:0000313|Ensembl:ENSSTOP00000016388.2};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000016388.2, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000016388.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|RuleBase:RU003808}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003808}; Multi-
CC pass membrane protein {ECO:0000256|RuleBase:RU003808}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. {ECO:0000256|RuleBase:RU003808}.
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DR EMBL; AGTP01099242; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 43179.ENSSTOP00000016388; -.
DR Ensembl; ENSSTOT00000028916.2; ENSSTOP00000016388.2; ENSSTOG00000023000.2.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00940000159855; -.
DR HOGENOM; CLU_000540_0_1_1; -.
DR InParanoid; I3MW93; -.
DR TreeFam; TF312805; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:Ensembl.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IEA:Ensembl.
DR Gene3D; 1.10.287.70; -; 4.
DR Gene3D; 6.10.250.2180; -; 1.
DR Gene3D; 6.10.250.2500; -; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 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 PANTHER; PTHR45628; VOLTAGE-DEPENDENT CALCIUM CHANNEL TYPE A SUBUNIT ALPHA-1; 1.
DR PANTHER; PTHR45628:SF2; VOLTAGE-DEPENDENT L-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1F; 1.
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.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR602077-1};
KW Calcium channel {ECO:0000256|ARBA:ARBA00022673,
KW ECO:0000256|RuleBase:RU003808};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW ECO:0000256|RuleBase:RU003808};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|PIRSR:PIRSR602077-3};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602077-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW ECO:0000256|RuleBase:RU003808}.
FT TRANSMEM 96..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 347..369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 528..546
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 561..579
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 657..676
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 726..748
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 874..892
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 912..932
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 990..1019
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1074..1095
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1115..1142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1183..1210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1222..1241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1328..1346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1419..1443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1577..1611
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1638..1756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1787..1806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..830
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1641..1658
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1671..1728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1739..1756
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 328
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 709
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1088
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ SEQUENCE 1981 AA; 221385 MW; 025C8A014ACD2EF8 CRC64;
MSESEVGKDT TPDPSPANGT GPGPDWGICP GPPVVEGDTG GASGLGTPRR KAQHNKHKTV
AVASAQRSPR ALFCLTLANP LRRSCISIVE WKPFDILILL TIFANCVALG VYIPFPEDDS
NTANHNLEQV EYVFLVIFTV ETVLKIVAYG LVLHPSAYIR NGWNLLDFII VVVGLFSVLL
EQGSGRPGEA PHTKPGGFDV KALRAFRVLR PLRLVSGVPS LHIVLNSIMK ALVPLLHIAL
LVLFVIIIYA IIGLELFLGR MHKTCYFLGS DVEAEEDPSP CASSGSGRAC TLNQTECRGR
WPGPNGGITN FDNFFFAMLT VFQCITMEGW TDVLYWMQDA MGHELPWLYF VSLVIFGSFF
VLNLVLGVLS GEFSKEREKA KARGDFQKLR EKQQMEEDLR GYLDWITQAE ELDLEDPSAD
GNFGSMAEEG RAGNRPHLAE LTNRRRGRLR WFRHSTRSTH STSSHASLPA SDTGSMAETP
ADEEEEEGAL ASCARCLNKI MKTSVCRRFR RANRGLRAHC RKAVKSNACY WAVLLLVFLN
TLTIASEHHG QPVWLTRIQE YANKVLLCLF TVEMLLKLYG LGPSVYVASF FNRFDCFVVC
GGILETTLVE VGAMQPLGIS VLRCVRLLRI FKVTRHWASL SNLVASLLNS MKSIASLLLL
LFLFIIIFSL LGMQLFGGKF NFDQTQTKRS TFDTFPQALL TVFQILTGED WNVVMYDGIM
AYGGPFFPGM LVCVYFIILF ICGNYILLNV FLAIAVDNLA SGDAGTATDK SREKSSEESV
PKENGILVPG GENEEQEGTK TEEAVPGVEE EEEEDEEEEE EEEEEEAGAG HEELLQEVVP
KEKVMPIPEG SAFFCLSQTN PLRKACHTLI HHHIFTNLIL VFIILSSVSL AAEDPIRAHS
FRNHILGYFD YAFTSIFTVE ILLKMTVFGA FLHRGSFCRS WFNLLDLLVV SVSLISFGIH
SSAISVVKIL RVLRVLRPLR AINRAKGLKH VVQCVFVAIR TIGNIMIVTT LLQFMFACIG
VQLFKGKFYS CTDEAKHTPK ECKGTFLVYP DGDVSRPLVR ERLWVNSDFN FDNVLSAMMA
LFTVSTFEGW PALLYKAIDA HAENRGPIYN YRVEISVFFI VYIIIIAFFM MNIFVGFVII
TFRAQGEQEY QNCELDKNQR QCVEYALKAQ PLRRYIPKNP HQYRVWAAVN SAAFEYLMFL
LILLNTVALA MQHYEQTAPF NYAMDILNMV FTGLFTIEMV LKIIAFKPKH YFTDAWNTFD
ALIVVGSVVD IAVTEVNNGG HLGESSEDSS RISITFFRLF RVMRLVKLLS KGEGIRTLLW
TFIKSFQALP YVALLIAMIF FIYAVIGMQM FGKVALQDGT QINRNNNFQT FPQAVLLLFR
CATGEAWQEI MLASLPGSRC DPESDYGPGE EFTCGSNFAI AYFISFFMLC AFLIINLFVA
VIMDNFDYLT RDWSILGPHH LDEFKRIWSE YDPGAKGRIK HLDVVALLRR IQPPLGFGKL
CPHRVACKRL VAMNVPLNSD GTVTFNATLF ALVRTSLKIK TEGNLEQANQ ELRMVIKKIW
KRIKQKLLDE IIPPPDEEEV TVGKFYATFL IQDYFRKFRR RKEKGLLGTE APSSTSSVLQ
AGLRSLQDLG PEIRQALTCD TDEEGEEEEE GQEGEEEAEK DPETYKAPME SQPPSRRNSR
ISVSLPVGSK NPDSLSLGPS DDDGRASNSR QPSVNPAGSH NQRRSSGVFM FTIPEEGSSQ
PKETKEQNKQ VEEEEIPDRL SYLDEQREAP PHPALLPPHQ PQRYVNGHNA PRRRLLPPTP
AGRKPSFTIQ CLQRQGSCED LPIPGTYHRG RNTGPSRAQG SWATPPQRGR LLYAPLLLVE
EGAAGEGYLG KSSGPLRTFT CLHVPGSRSD PSHGKRGSAD SLVEAVLISE GLGLFARDPR
FVALAKKEIA DACRLTLDEM DSAASDLLAQ GTSSLYSDEE SILSRFDEED LGDEMACVHA
L
//
