ID A0A287D9L0_ICTTR Unreviewed; 2293 AA.
AC A0A287D9L0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Voltage-dependent T-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1G {ECO:0000313|Ensembl:ENSSTOP00000030233.1};
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:ENSSTOP00000030233.1, 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:ENSSTOP00000030233.1}
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. This channel gives rise to T-type calcium
CC currents. T-type calcium channels belong to the "low-voltage activated
CC (LVA)" group and are strongly blocked by nickel and mibefradil. A
CC particularity of this type of channels is an opening at quite negative
CC potentials, and a voltage-dependent inactivation. T-type channels serve
CC pacemaking functions in both central neurons and cardiac nodal cells
CC and support calcium signaling in secretory cells and vascular smooth
CC muscle. They may also be involved in the modulation of firing patterns
CC of neurons which is important for information processing as well as in
CC cell growth processes. {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; AGTP01023087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01023088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01023089; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005321697.1; XM_005321640.1.
DR Ensembl; ENSSTOT00000037271.1; ENSSTOP00000030233.1; ENSSTOG00000019651.2.
DR GeneID; 101977530; -.
DR CTD; 8913; -.
DR GeneTree; ENSGT00940000159664; -.
DR OrthoDB; 1110761at2759; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR Gene3D; 1.10.287.70; -; 4.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 4.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR005445; VDCC_T_a1.
DR InterPro; IPR002077; VDCCAlpha1.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037:SF137; VOLTAGE-DEPENDENT T-TYPE CALCIUM CHANNEL SUBUNIT ALPHA; 1.
DR PANTHER; PTHR10037; VOLTAGE-GATED CATION CHANNEL CALCIUM AND SODIUM; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00167; CACHANNEL.
DR PRINTS; PR01629; TVDCCALPHA1.
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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Ion channel {ECO:0000256|RuleBase:RU003808};
KW Ion transport {ECO:0000256|ARBA:ARBA00022568,
KW ECO:0000256|RuleBase:RU003808};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {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};
KW Transport {ECO:0000256|ARBA:ARBA00022568, ECO:0000256|RuleBase:RU003808};
KW Voltage-gated channel {ECO:0000256|RuleBase:RU003808}.
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 342..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 369..394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 744..762
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 774..795
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 865..884
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 941..964
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1277..1295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1315..1336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1348..1367
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1412..1434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1514..1537
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1619..1640
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1652..1675
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1753..1772
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1836..1858
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 80..405
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 743..970
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1275..1547
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1618..1868
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 991..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1048..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1886..1923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2097..2132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2188..2293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1546..1580
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 495..509
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1076
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2188..2203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2230..2246
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 354
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 923
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1486
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 2293 AA; 253743 MW; C79FE82894AAD862 CRC64;
MDEEEDGAGT EESGQPRSFM RFNDLSGAGG QPGPGSAEKD PGSADSEAEG LPYPALAPVV
FFYLSQDSRP RSWCLRTVCN PWFERISMLV ILLNCVTLGM FRPCEDIACD SQRCRILQAF
DDFIFAFFAV EMVVKMVALG IFGKKCYLGD TWNRLDFFIV IAGMLEYSLD LQNVSFSAVR
TVRVLRPLRA INRVPSMRIL VTLLLDTLPM LGNVLLLCFF VFFIFGIVGV QLWAGLLRNR
CFLPENFSLP LSVDLEPYYQ TENEDESPFI CSQPRENGMR SCRSVPTLRG EGGGGPPCGL
DYEAYNSSSN TTCVNWNQYY TNCSAGEHNP FKGAINFDNI GYAWIAIFQV ITLEGWVDIM
YFVMDAHSFY NFIYFILLII VGSFFMINLC LVVIATQFSE TKQRESQLMR EQRVRFLSNA
STLASFSEPG SCYEELLKYL VYIIRKAARR LAQLSRAVGV RAGLLSSPAA LRSQEPQPSG
SCSRSHRRLS VHHLVHHHHH HHHHYHLGNG TLRAPRASPE IQDRDANGSR RLMLPPPSTP
TLSGGPPGGA ESVHSFYHAD CHLEPVRCPA PPPRSPSEAS GRTVGSGKVY PTVHTSPPPE
MLKEKALVEV APSSGPPTLT SLNIPPGPYS SMHKLLETQS TGACQSSCKI SSPCLKADSG
ACGPDSCPYC ARPGAGELEP ADHEVPDSDS EAVYEFTQDA QHSDLRDPHS RRRRSLGPVT
EPGSVLAFWK LICDTFRKIV DSKYFGRGIM IAILVNTLSM GIEYHEQPEE LTNALEISNI
VFTSLFALEM LLKLLVYGPF GYIKNPYNIF DGVIVVISVW EIVGQQGGGL SVLRTFRLMR
VLKLVRFLPA LQRQLVVLMK TMDNVATFCM LLMLFIFIFS ILGMHLFGCK FASERDGDTL
PDRKNFDSLL WAIVTVFQIL TQEDWNKVLY NGMASTSSWA ALYFIALMTF GNYVLFNLLV
AILVEGFQAE EISKREDASG QLSCIQLPVD SQGGDATKSE SEPDFFSPSV DGDGDRKKRL
ALVSLGEHPE LQKSLLPPLI IHTAATPMSL PKSSSTGLGE ALGPSSRRTS SSGSAEPGAV
HEMKSPPSAR SSPHSPWSAA SSWTSRRSSR NSLGRAPSLK RRSPSGERRS LLSGEGRESQ
DEEDSSEEER ASPVGSDHHH RGSLEREAKS SFDLPDTLQV PGLHRTASGR SSASEHQDCN
GKSASGRLAR ALRPNDPPLD GDDADDEGNL SKGERIRAWI RARLPACCRE RDSWSAYIFP
PQSRFRLLCH RIITHKMFDH VVLIIIFLNC ITIAMERPKI DPHSAERIFL TLSNYIFTAV
FLAEMTVKVV ALGWCFGEQA YLRSSWNVLD GLLVLISVID ILVSMVSDSG TKILGMLRVL
RLLRTLRPLR VISRAQGLKL VVETLMSSLK PIGNIVVICC AFFIIFGILG VQLFKGKFFV
CQGEDTRNIT NKSDCAEASY RWVRHKYNFD NLGQALMSLF VLASKDGWVD IMYDGLDAVG
VDQQPIMNHN PWMLLYFISF LLIVAFFVLN MFVGVVVENF HKCRQHQEEE EARRREEKRL
RRLEKKRRSK EKQMADLMLD DVIASGSSAS AASEAQCKPY YSDYSRFRLL VHHLCTSHYL
DLFITGVIGL NVVTMAMEHY QQPQILDEAL KICNYIFTVI FVLESVFKLV AFGFRRFFQD
RWNQLDLAIV LLSIMGITLE EIEVNASLPI NPTIIRIMRV LRIARVLKLL KMAVGMRALL
DTVMQALPQV GNLGLLFMLL FFIFAALGVE LFGDLECDET HPCEGLGRHA TFRNFGMAFL
TLFRVSTGDN WNGIMKDTLR DCDQESTCYN TVISPIYFVS FVLTAQFVLV NVVIAVLMKH
LEESNKEAKE EAELEAELEL EMKTLSPQPH SPLSSPFLWP GVEGADSPDS PKPGVPHTAA
HAGAASHFSL EHPTMEPQPE EVPVTLGSNL LTVRKSGVSR THSLPNDSYM CRDGSAAEGS
PGHRGWGLPK AQSGSILSVH SQPADTTYIL QLPKDAPHLL QPHSAPTWGT IPKLPPPARS
PLAQRPLRRQ AAIRTDSLDV QGLGSQEDLL SEVSGPSPPL ARSSSFWGQS SIQVQQHFRS
QSKVSKHMPP PALCPGPEPN WSKGPPETRS SLELDTELSW ISGDLLPLGS QEPLSTRDLK
KCYSVESQSG RRRPASWLDE QRRHSIAVSC LDSGSQPHLG PSPSTLGGQP LGGPGSRPKK
KLSPPSISID PPEIQGPRPP PSPGVCLRRR APSSDSKDPS ASGPPDSMAA SPSPKKDVLS
LSGLSSDPAD LDP
//
