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Protein

Voltage-dependent T-type calcium channel subunit alpha-1G

Gene

Cacna1g

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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-1G gives rise to T-type calcium currents. T-type calcium channels belong to the "low-voltage activated (LVA)" group and are strongly blocked by nickel and mibefradil. A particularity of this type of channels is an opening at quite negative potentials and a voltage-dependent inactivation. T-type channels serve pacemaking functions in both central neurons and cardiac nodal cells and support calcium signaling in secretory cells and vascular smooth muscle. They may also be involved in the modulation of firing patterns of neurons which is important for information processing as well as in cell growth processes.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei354 – 3541Calcium ion selectivity and permeabilityBy similarity
Sitei924 – 9241Calcium ion selectivity and permeabilityBy similarity
Sitei1465 – 14651Calcium ion selectivity and permeabilityBy similarity
Sitei1770 – 17701Calcium ion selectivity and permeabilityBy similarity

GO - Molecular functioni

GO - Biological processi

  • artery smooth muscle contraction Source: RGD
  • AV node cell action potential Source: BHF-UCL
  • AV node cell to bundle of His cell signaling Source: BHF-UCL
  • calcium ion import Source: RGD
  • calcium ion transport into cytosol Source: RGD
  • cellular response to dexamethasone stimulus Source: RGD
  • membrane depolarization during action potential Source: GO_Central
  • membrane depolarization during AV node cell action potential Source: BHF-UCL
  • membrane depolarization during SA node cell action potential Source: BHF-UCL
  • positive regulation of calcium ion-dependent exocytosis Source: RGD
  • positive regulation of cytosolic calcium ion concentration Source: RGD
  • regulation of calcium ion transport Source: RGD
  • regulation of heart rate by cardiac conduction Source: BHF-UCL
  • SA node cell action potential Source: BHF-UCL
  • SA node cell to atrial cardiac muscle cell signalling Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel, Voltage-gated channel

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Voltage-dependent T-type calcium channel subunit alpha-1G
Alternative name(s):
Voltage-gated calcium channel subunit alpha Cav3.1
Gene namesi
Name:Cacna1g
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi68942. Cacna1g.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 8080CytoplasmicSequence analysisAdd
BLAST
Transmembranei81 – 10121Helical; Name=S1 of repeat IAdd
BLAST
Topological domaini102 – 11918ExtracellularSequence analysisAdd
BLAST
Transmembranei120 – 14122Helical; Name=S2 of repeat ISequence analysisAdd
BLAST
Topological domaini142 – 1509CytoplasmicSequence analysis
Transmembranei151 – 17020Helical; Name=S3 of repeat IAdd
BLAST
Topological domaini171 – 1755ExtracellularSequence analysis
Transmembranei176 – 19318Helical; Name=S4 of repeat IAdd
BLAST
Topological domaini194 – 21320CytoplasmicSequence analysisAdd
BLAST
Transmembranei214 – 23421Helical; Name=S5 of repeat ISequence analysisAdd
BLAST
Topological domaini235 – 370136ExtracellularSequence analysisAdd
BLAST
Transmembranei371 – 39525Helical; Name=S6 of repeat IAdd
BLAST
Topological domaini396 – 744349CytoplasmicSequence analysisAdd
BLAST
Transmembranei745 – 76521Helical; Name=S1 of repeat IISequence analysisAdd
BLAST
Topological domaini766 – 77813ExtracellularSequence analysisAdd
BLAST
Transmembranei779 – 80022Helical; Name=S2 of repeat IISequence analysisAdd
BLAST
Topological domaini801 – 8066CytoplasmicSequence analysis
Transmembranei807 – 82519Helical; Name=S3 of repeat IISequence analysisAdd
BLAST
Topological domaini826 – 8338ExtracellularSequence analysis
Transmembranei834 – 85724Helical; Name=S4 of repeat IISequence analysisAdd
BLAST
Topological domaini858 – 86811CytoplasmicSequence analysisAdd
BLAST
Transmembranei869 – 88921Helical; Name=S5 of repeat IISequence analysisAdd
BLAST
Topological domaini890 – 94051ExtracellularSequence analysisAdd
BLAST
Transmembranei941 – 96525Helical; Name=S6 of repeat IISequence analysisAdd
BLAST
Topological domaini966 – 1251286CytoplasmicSequence analysisAdd
BLAST
Transmembranei1252 – 127423Helical; Name=S1 of repeat IIISequence analysisAdd
BLAST
Topological domaini1275 – 129218ExtracellularSequence analysisAdd
BLAST
Transmembranei1293 – 131321Helical; Name=S2 of repeat IIISequence analysisAdd
BLAST
Topological domaini1314 – 132310CytoplasmicSequence analysis
Transmembranei1324 – 134320Helical; Name=S3 of repeat IIISequence analysisAdd
BLAST
Topological domaini1344 – 135714ExtracellularSequence analysisAdd
BLAST
Transmembranei1358 – 137922Helical; Name=S4 of repeat IIISequence analysisAdd
BLAST
Topological domaini1380 – 138910CytoplasmicSequence analysis
Transmembranei1390 – 141324Helical; Name=S5 of repeat IIISequence analysisAdd
BLAST
Topological domaini1414 – 149077ExtracellularSequence analysisAdd
BLAST
Transmembranei1491 – 151626Helical; Name=S6 of repeat IIISequence analysisAdd
BLAST
Topological domaini1517 – 157862CytoplasmicSequence analysisAdd
BLAST
Transmembranei1579 – 159921Helical; Name=S1 of repeat IVSequence analysisAdd
BLAST
Topological domaini1600 – 161314ExtracellularSequence analysisAdd
BLAST
Transmembranei1614 – 163522Helical; Name=S2 of repeat IVSequence analysisAdd
BLAST
Topological domaini1636 – 16427CytoplasmicSequence analysis
Transmembranei1643 – 166119Helical; Name=S3 of repeat IVSequence analysisAdd
BLAST
Topological domaini1662 – 167514ExtracellularSequence analysisAdd
BLAST
Transmembranei1676 – 169924Helical; Name=S4 of repeat IVSequence analysisAdd
BLAST
Topological domaini1700 – 171314CytoplasmicSequence analysisAdd
BLAST
Transmembranei1714 – 173421Helical; Name=S5 of repeat IVSequence analysisAdd
BLAST
Topological domaini1735 – 179460ExtracellularSequence analysisAdd
BLAST
Transmembranei1795 – 182228Helical; Name=S6 of repeat IVSequence analysisAdd
BLAST
Topological domaini1823 – 2254432CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell body Source: RGD
  • dendrite Source: RGD
  • membrane Source: RGD
  • neuronal cell body Source: RGD
  • perinuclear region of cytoplasm Source: RGD
  • plasma membrane Source: RGD
  • voltage-gated calcium channel complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Chemistry

GuidetoPHARMACOLOGYi535.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 22542254Voltage-dependent T-type calcium channel subunit alpha-1GPRO_0000053953Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi173 – 1731N-linked (GlcNAc...)Sequence analysis
Glycosylationi246 – 2461N-linked (GlcNAc...)Sequence analysis
Glycosylationi306 – 3061N-linked (GlcNAc...)Sequence analysis
Glycosylationi310 – 3101N-linked (GlcNAc...)Sequence analysis
Glycosylationi322 – 3221N-linked (GlcNAc...)Sequence analysis
Modified residuei467 – 4671PhosphoserineCombined sources
Modified residuei716 – 7161PhosphoserineCombined sources
Modified residuei1118 – 11181PhosphoserineCombined sources
Modified residuei1124 – 11241PhosphoserineCombined sources
Modified residuei1125 – 11251PhosphoserineCombined sources
Glycosylationi1427 – 14271N-linked (GlcNAc...)Sequence analysis
Glycosylationi1430 – 14301N-linked (GlcNAc...)Sequence analysis
Glycosylationi1666 – 16661N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

In response to raising of intracellular calcium, the T-type channels are activated by CaM-kinase II.

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiO54898.
PRIDEiO54898.

PTM databases

iPTMnetiO54898.

Expressioni

Tissue specificityi

Highly expressed in brain. Moderate expression in heart; low expression in placenta, kidney and lung.

Interactioni

Protein-protein interaction databases

BioGridi248334. 1 interaction.
STRINGi10116.ENSRNOP00000061436.

Structurei

3D structure databases

ProteinModelPortaliO54898.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati68 – 398331IAdd
BLAST
Repeati730 – 968239IIAdd
BLAST
Repeati1242 – 1519278IIIAdd
BLAST
Repeati1564 – 1822259IVAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi290 – 2956Poly-Gly
Compositional biasi496 – 50611Poly-HisAdd
BLAST
Compositional biasi1527 – 15304Poly-Glu

Domaini

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.

Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2302. Eukaryota.
ENOG410XNP6. LUCA.
HOGENOMiHOG000007742.
HOVERGENiHBG050764.
InParanoidiO54898.
PhylomeDBiO54898.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR005445. VDCC_T_a1.
IPR030154. VDCC_T_a1G.
[Graphical view]
PANTHERiPTHR10037:SF137. PTHR10037:SF137. 6 hits.
PfamiPF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSiPR01629. TVDCCALPHA1.

Sequencei

Sequence statusi: Complete.

O54898-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDEEEDGAGA EESGQPRSFT QLNDLSGAGG RQGPGSTEKD PGSADSEAEG
60 70 80 90 100
LPYPALAPVV FFYLSQDSRP RSWCLRTVCN PWFERVSMLV ILLNCVTLGM
110 120 130 140 150
FRPCEDIACD SQRCRILQAF DDFIFAFFAV EMVVKMVALG IFGKKCYLGD
160 170 180 190 200
TWNRLDFFIV IAGMLEYSLD LQNVSFSAVR TVRVLRPLRA INRVPSMRIL
210 220 230 240 250
VTLLLDTLPM LGNVLLLCFF VFFIFGIVGV QLWAGLLRNR CFLPENFSLP
260 270 280 290 300
LSVDLEPYYQ TENEDESPFI CSQPRENGMR SCRSVPTLRG EGGGGPPCSL
310 320 330 340 350
DYETYNSSSN TTCVNWNQYY TNCSAGEHNP FKGAINFDNI GYAWIAIFQV
360 370 380 390 400
ITLEGWVDIM YFVMDAHSFY NFIYFILLII VGSFFMINLC LVVIATQFSE
410 420 430 440 450
TKQRESQLMR EQRVRFLSNA STLASFSEPG SCYEELLKYL VYILRKAARR
460 470 480 490 500
LAQVSRAIGV RAGLLSSPVA RSGQEPQPSG SCTRSHRRLS VHHLVHHHHH
510 520 530 540 550
HHHHYHLGNG TLRVPRASPE IQDRDANGSR RLMLPPPSTP TPSGGPPRGA
560 570 580 590 600
ESVHSFYHAD CHLEPVRCQA PPPRCPSEAS GRTVGSGKVY PTVHTSPPPE
610 620 630 640 650
ILKDKALVEV APSPGPPTLT SFNIPPGPFS SMHKLLETQS TGACHSSCKI
660 670 680 690 700
SSPCSKADSG ACGPDSCPYC ARTGAGEPES ADHVMPDSDS EAVYEFTQDA
710 720 730 740 750
QHSDLRDPHS RRRQRSLGPD AEPSSVLAFW RLICDTFRKI VDSKYFGRGI
760 770 780 790 800
MIAILVNTLS MGIEYHEQPE ELTNALEISN IVFTSLFALE MLLKLLVYGP
810 820 830 840 850
FGYIKNPYNI FDGVIVVISV WEIVGQQGGG LSVLRTFRLM RVLKLVRFLP
860 870 880 890 900
ALQRQLVVLM KTMDNVATFC MLLMLFIFIF SILGMHLFGC KFASERDGDT
910 920 930 940 950
LPDRKNFDSL LWAIVTVFQI LTQEDWNKVL YNGMASTSSW AALYFIALMT
960 970 980 990 1000
FGNYVLFNLL VAILVEGFQA EGDATKSESE PDFFSPSVDG DGDRKKRLAL
1010 1020 1030 1040 1050
VALGEHAELR KSLLPPLIIH TAATPMSHPK SSSTGVGEAL GSGSRRTSSS
1060 1070 1080 1090 1100
GSAEPGAAHH EMKCPPSARS SPHSPWSAAS SWTSRRSSRN SLGRAPSLKR
1110 1120 1130 1140 1150
RSPSGERRSL LSGEGQESQD EEESSEEDRA SPAGSDHRHR GSLEREAKSS
1160 1170 1180 1190 1200
FDLPDTLQVP GLHRTASGRS SASEHQDCNG KSASGRLART LRTDDPQLDG
1210 1220 1230 1240 1250
DDDNDEGNLS KGERIQAWVR SRLPACCRER DSWSAYIFPP QSRFRLLCHR
1260 1270 1280 1290 1300
IITHKMFDHV VLVIIFLNCI TIAMERPKID PHSAERIFLT LSNYIFTAVF
1310 1320 1330 1340 1350
LAEMTVKVVA LGWCFGEQAY LRSSWNVLDG LLVLISVIDI LVSMVSDSGT
1360 1370 1380 1390 1400
KILGMLRVLR LLRTLRPLRV ISRAQGLKLV VETLMSSLKP IGNIVVICCA
1410 1420 1430 1440 1450
FFIIFGILGV QLFKGKFFVC QGEDTRNITN KSDCAEASYR WVRHKYNFDN
1460 1470 1480 1490 1500
LGQALMSLFV LASKDGWVDI MYDGLDAVGV DQQPIMNHNP WMLLYFISFL
1510 1520 1530 1540 1550
LIVAFFVLNM FVGVVVENFH KCRQHQEEEE ARRREEKRLR RLEKKRRSKE
1560 1570 1580 1590 1600
KQMAEAQCKP YYSDYSRFRL LVHHLCTSHY LDLFITGVIG LNVVTMAMEH
1610 1620 1630 1640 1650
YQQPQILDEA LKICNYIFTV IFVFESVFKL VAFGFRRFFQ DRWNQLDLAI
1660 1670 1680 1690 1700
VLLSIMGITL EEIEVNLSLP INPTIIRIMR VLRIARVLKL LKMAVGMRAL
1710 1720 1730 1740 1750
LHTVMQALPQ VGNLGLLFML LFFIFAALGV ELFGDLECDE THPCEGLGRH
1760 1770 1780 1790 1800
ATFRNFGMAF LTLFRVSTGD NWNGIMKDTL RDCDQESTCY NTVISPIYFV
1810 1820 1830 1840 1850
SFVLTAQFVL VNVVIAVLMK HLEESNKEAK EEAELEAELE LEMKTLSPQP
1860 1870 1880 1890 1900
HSPLGSPFLW PGVEGVNSTD SPKPGAPHTT AHIGAASGFS LEHPTMVPHP
1910 1920 1930 1940 1950
EEVPVPLGPD LLTVRKSGVS RTHSLPNDSY MCRNGSTAER SLGHRGWGLP
1960 1970 1980 1990 2000
KAQSGSILSV HSQPADTSCI LQLPKDVHYL LQPHGAPTWG AIPKLPPPGR
2010 2020 2030 2040 2050
SPLAQRPLRR QAAIRTDSLD VQGLGSREDL LSEVSGPSCP LTRSSSFWGG
2060 2070 2080 2090 2100
SSIQVQQRSG IQSKVSKHIR LPAPCPGLEP SWAKDPPETR SSLELDTELS
2110 2120 2130 2140 2150
WISGDLLPSS QEEPLFPRDL KKCYSVETQS CRRRPGFWLD EQRRHSIAVS
2160 2170 2180 2190 2200
CLDSGSQPRL CPSPSSLGGQ PLGGPGSRPK KKLSPPSISI DPPESQGSRP
2210 2220 2230 2240 2250
PCSPGVCLRR RAPASDSKDP SVSSPLDSTA ASPSPKKDTL SLSGLSSDPT

DMDP
Length:2,254
Mass (Da):250,407
Last modified:January 1, 1999 - v2
Checksum:i697BBE06360CF0F6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF027984 mRNA. Translation: AAC67372.1.
AF290212 mRNA. Translation: AAG35186.2.
PIRiT09053.
UniGeneiRn.86960.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF027984 mRNA. Translation: AAC67372.1.
AF290212 mRNA. Translation: AAG35186.2.
PIRiT09053.
UniGeneiRn.86960.

3D structure databases

ProteinModelPortaliO54898.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248334. 1 interaction.
STRINGi10116.ENSRNOP00000061436.

Chemistry

GuidetoPHARMACOLOGYi535.

PTM databases

iPTMnetiO54898.

Proteomic databases

PaxDbiO54898.
PRIDEiO54898.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi68942. Cacna1g.

Phylogenomic databases

eggNOGiKOG2302. Eukaryota.
ENOG410XNP6. LUCA.
HOGENOMiHOG000007742.
HOVERGENiHBG050764.
InParanoidiO54898.
PhylomeDBiO54898.

Miscellaneous databases

PROiO54898.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR005445. VDCC_T_a1.
IPR030154. VDCC_T_a1G.
[Graphical view]
PANTHERiPTHR10037:SF137. PTHR10037:SF137. 6 hits.
PfamiPF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSiPR01629. TVDCCALPHA1.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of a neuronal low-voltage-activated T-type calcium channel."
    Perez-Reyes E., Cribbs L.L., Daud A., Lacerda A.E., Barclay J., Williamson M.P., Fox M., Rees M., Lee J.-H.
    Nature 391:896-900(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. "Molecular and functional characterization of a family of rat brain T-type calcium channels."
    McRory J.E., Santi C.M., Hamming K.S.C., Mezeyova J., Sutton K.G., Baillie D.L., Stea A., Snutch T.P.
    J. Biol. Chem. 276:3999-4011(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467; SER-716; SER-1118; SER-1124 AND SER-1125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCAC1G_RAT
AccessioniPrimary (citable) accession number: O54898
Secondary accession number(s): Q548R1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1999
Last modified: July 6, 2016
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.