ID H0WQ35_OTOGA Unreviewed; 2342 AA.
AC H0WQ35;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Voltage-dependent T-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1G {ECO:0000313|Ensembl:ENSOGAP00000004043.2};
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000004043.2, ECO:0000313|Proteomes:UP000005225};
RN [1] {ECO:0000313|Proteomes:UP000005225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOGAP00000004043.2}
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. 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; AAQR03043567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03043568; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03043569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 30611.ENSOGAP00000004043; -.
DR Ensembl; ENSOGAT00000004530.2; ENSOGAP00000004043.2; ENSOGAG00000004520.2.
DR eggNOG; KOG2302; Eukaryota.
DR GeneTree; ENSGT00940000159664; -.
DR HOGENOM; CLU_000540_2_0_1; -.
DR InParanoid; H0WQ35; -.
DR OMA; GQAWSCG; -.
DR TreeFam; TF313555; -.
DR Proteomes; UP000005225; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR GO; GO:0008332; F:low voltage-gated calcium channel activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
DR GO; GO:0070509; P:calcium ion import; IEA:Ensembl.
DR GO; GO:0042391; P:regulation of membrane potential; IEA:Ensembl.
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:UP000005225};
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 125..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 217..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 372..397
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 749..767
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 779..800
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 870..889
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 946..969
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1284..1302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1322..1343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1419..1441
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1521..1544
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 84..408
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 748..975
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1282..1554
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 469..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 996..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1052..1233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1886..1924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2143..2175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2190..2209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2239..2342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1553..1580
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 489..513
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 357
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 928
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1493
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 2342 AA; 259488 MW; D03E83C7665F25C4 CRC64;
MDEEEDGAGA EESGQPRSFT RLNDLSGAGG RPGPGSTEKD PGSADSEAEG LPYPALAPVV
FFYLSQDSRP RSWCLRTVCN PPNTWFERIS MLVILLNCVT LGMFRPCEDI ACDSQRCRIL
QAFDDFIFAF FAVEMVVKMV ALGIFGKKCY LGDTWNRLDF FIVIAGMLEY SLDLQNVSFS
AVRTVRVLRP LRAINRVPSM RILVTLLLDT LPMLGNVLLL CFFVFFIFGI VGVQLWAGLL
RNRCFLPENF SLPLSVDLER YYQTENEDES PFICSQPREN GMRSCRSVPT LRGEGGGGPP
CGLDYESYNS SSNTTCVNWN QYYTNCSAGE HNPFKGAINF DNIGYAWIAI FQVITLEGWV
DIMYFVMDAH SFYNFIYFIL LIIVGSFFMI NLCLVVIATQ FSETKQRESQ LMREQRVRFL
SNASTLASFS EPGSCYEELL KYLVYILRKA ARRLAQISRA AGVRAGLLSS PAPVGGQEPQ
PSSTCSRSHR RLSVHHLVHH HHHHHHHHYH LGNGTLRAPR ASPEIQDRDA NGSRRLMLPP
PPSTPALSGG PPAGAESVHS FYHADCHLEP VRRQAPPPKS PSEASGRTVG SGKVYPTVHT
SPPPEMLKEK ALVEVAPSSG PPTLTSLNIP PGPYSSMHKL LETQSTGACQ SSCKISSPCS
KADSGACGPD SCPYCARVGS GEVELTDHEM PDSDSEAVYE FTQDAQHSDL RDPHSRRQRS
LSQDAEPSSV LAFWRLICDT FRKIVDSKYF GRGIMIAILV NTLSMGIEYH EQPEELTNAL
EISNIVFTSL FALEMLLKLL VYGPFGYIKN PYNIFDGVIV VISVWEIVGQ QGGGLSVLRT
FRLMRVLKLV RFLPALQRQL VVLMKTMDNV ATFCMLLMLF IFIFSILGMH LFGCKFASER
DGDTLPDRKN FDSLLWAIVT VFQILTQEDW NKVLYNGMAS TSSWAALYFI ALMTFGNYVL
FNLLVAILVE GFQAEEISKR EDASGQLSCI QLPVDSQGGD ATKSESEPDF FSPSLDGDGD
RKKRLALVSL GEHPELRKSL LPPLIIHTAA TPMSLPKSSS TGLGEALGPP SRRTSSSGSA
EPGVAHEIKS PPSARSSPHS PWSAASSWAS RRSSRNSLGR APSLKRRSPS GERRSLLSGE
GQESQDEEES SEEERASPAG SDRRHRGSLE REAKSSFDLP DTLQVPGLHR TASGRSSASE
HQDCNGKSAS GRLARALRPD EPPLEGDDAD DEGNLSKAER VRAWIQARLP ACCRERDSWS
AYIFPPQSRS RFRLLCHRII THKMFDHVVL VIIFLNCITI AMERPKIDPH SAERIFLTLS
NYVFTAVFLA EMTVKVVALG WCFGEQAYLR SSWNVLDGLL ALISVIDILV SMVSDSGTKI
LGMLRVLRLL RTLRPLRVIS RAQGLKLVVE TLMSSLKPIG NIVVICCAFF IIFGILGVQL
FKGKFFVCLG EDTRNITNKS DCAEASYRWV RHKYNFDNLG QALMSLFVLA SKDGWVDIMY
DGLDAVGVDQ QPIMNHNPWM LLYFISFLLI VAFFVLNMFV GVVVENFHKC RQHQEEEEAR
RREEKRLRRL EKKRRNLMLD 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 GVTGPDSPDS PDPGALRTQA
HARAASRLSL EHPLDRQLFD TMSLLIQGSL EGELKLMDEL AGPEGQPSAF PSAPCWGGSD
PQMEPHPEKT PVTLGPDLLT VWKSGVSRTH SLPNDSYMCR DGSTAERPLG RRGWRLPKAQ
SGSVLSVHSQ PADTSYTPQL PKDAPHLLQP HCALVWGTIP KLPPPGRSPL AQRPLRRQAA
IRTDSLDVQG LGSREDLLSE VSGPSPPLAR AYSFWGQSSI QVQQHSRSQN KISKHMPPPA
PCPRPEPSWG KDPLETRSSL ELDTELSWIS GDLLPTGGQE EAPSPRDLKK CYSVEAQSGQ
RRPVSWLDEQ RRHSIAVSCL DSGSQPRLGP GPSNLGGQLL GGPGSRPKKK LSPPSISIDP
PESQGSRPPP SPGICLRRRA PSSESKDPLA SGPPDSMAAS PSPKKDVLSL SGLSSDPGAL
EP
//
