ID E0CXK2_MOUSE Unreviewed; 1835 AA.
AC E0CXK2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Voltage-dependent T-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=Cacna1i {ECO:0000313|Ensembl:ENSMUSP00000125229.2,
GN ECO:0000313|MGI:MGI:2178051};
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 {ECO:0000313|Ensembl:ENSMUSP00000125229.2, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000125229.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000125229.2,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000125229.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000125229.2};
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 SMR; E0CXK2; -.
DR SwissPalm; E0CXK2; -.
DR ProteomicsDB; 324882; -.
DR Antibodypedia; 26656; 114 antibodies from 25 providers.
DR Ensembl; ENSMUST00000162155.8; ENSMUSP00000125229.2; ENSMUSG00000022416.16.
DR AGR; MGI:2178051; -.
DR MGI; MGI:2178051; Cacna1i.
DR VEuPathDB; HostDB:ENSMUSG00000022416; -.
DR GeneTree; ENSGT00940000158594; -.
DR HOGENOM; CLU_000540_2_0_1; -.
DR PhylomeDB; E0CXK2; -.
DR ChiTaRS; Cacna1i; mouse.
DR Proteomes; UP000000589; Chromosome 15.
DR Bgee; ENSMUSG00000022416; Expressed in striatum and 40 other cell types or tissues.
DR ExpressionAtlas; E0CXK2; baseline and differential.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IBA:GO_Central.
DR GO; GO:0008332; F:low voltage-gated calcium channel activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070509; P:calcium ion import; ISO:MGI.
DR GO; GO:0006816; P:calcium ion transport; ISO:MGI.
DR GO; GO:0060402; P:calcium ion transport into cytosol; ISO:MGI.
DR GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR GO; GO:0019228; P:neuronal action potential; IMP:MGI.
DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:MGI.
DR GO; GO:0030431; P:sleep; IMP:MGI.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
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:SF209; 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 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|ProteomicsDB:E0CXK2};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
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 119..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 206..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 343..364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 370..395
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 720..742
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 762..778
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 798..820
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1130..1148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1168..1189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1201..1227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1265..1287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1366..1390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1446..1463
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1483..1502
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1566..1593
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1668..1689
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 76..406
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 598..826
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1128..1400
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1446..1699
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1399..1426
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 11..38
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..954
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 355
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 779
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1339
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 1835 AA; 205417 MW; 02A75351A1373D4B CRC64;
MADSNLPPSS SAAPDPEPGI TEQPGPRSPP PSPPGLEEPL DGTNPDVPHP DLAPVAFFCL
RQTTSPRNWC IKMVCNPWFE CVSMLVILLN CVTLGMYQPC DDMECLSDRC KILQVFDDFI
FIFFAMEMVL KMVALGIFGK KCYLGDTWNR LDFFIVMAGM VEYSLDLQNI NLSAIRTVRV
LRPLKAINRV PSMRILVNLL LDTLPMLGNV LLLCFFVFFI FGIIGVQLWA GLLRNRCFLE
ENFTIQGDVA LPPYYQPEED DEMPFICSLS GDNGIMGCHE IPPLKEQGRE CCLSKDDMYD
FGAGRQDLNA SGLCVNWNRY YNVCRTGNAN PHKGAINFDN IGYAWIVIFQ VITLEGWVEI
MYYVMDAHSF YNFIYFILLI IVGSFFMINL CLVVIATQFS ETKQREHRLM LEQRQRYLSS
STVASYAEPG DCYEEIFQYV CHILRKAKRR ALGLYQALQN RRQATGPGTP APAKPGPHAK
EPSHCKLCPR HSPLDTTPHT LVQPISAILA SDPSSCPRCQ HEAGRRPSGL GSTDSGQEGS
GSGGSAEAEA NGDGPQSSED GVSSGLGKEE EQEDGAARLC GDVWRETRAK LRGIVDSKYF
NRGIMMAILV NTVSMGIEHH EQPEELTNIL EICNVVFTSM FALEMILKLA AFGLFDYLRN
PYNIFDSIIV IISIWEIVGQ ADGGLSVLRT FRLLRVLKLV RFMPALRRQL VVLMKTMDNV
ATFCMLLMLF IFIFSILGMH IFGCKFSLRT DTGDTVPDRK NFDSLLWAIV TVFQILTQED
WNVVLYNGMA STTPWASLYF VALMTFGNYV LFNLLVAILV EGFQAEGDAN RSYSDEDQSS
SNLEELDKLP EGLDSSRDLK LCPIPMTPNG HLDPSLPLGG HLGPAGAMGA APRLSLQPDP
VLVALESRKS SVMSLGRMSY DQRSLSSSRS SYYGPWGRSG TWASRRSSWN SLKHKPPSAE
HESLLSGERG GSCVRACEGA REDAPPRAAP LHAPHTHHAH HGPHLAHRHR HHRRTLSLDT
RDSVDLAELV PVVGAHSRAA WRAAGQAPGH EDCNGRMPNI AKDVFTKMDD RRDRGEDEEE
IDYTLCFRVR KMIDVYKPDW CEVREDWSVY LFSPENKFRI LCQTIIAHKL FDYVVLAFIF
LNCITIALER PQIEAGSTER IFLTVSNYIF TAIFVGEMTL KVVSLGLYFG EQAYLRSSWN
VLDGFLVFVS IIDIVVSVAS AGGAKILGVL RVLRLLRTLR PLRVISRAPG LKLVVETLIS
SLKPIGNIVL ICCAFFIIFG ILGVQLFKGK FYHCLGVDTR NITNRSDCVA ANYRWVHHKY
NFDNLGQALM SLFVLASKDG WVNIMYNGLD AVAVDQQPVT NHNPWMLLYF ISFLLIVSFF
VLNMFVGVVV ENFHKCRQHQ EAEEARRREE KRLRRLEKKR RKAQRLPYYA TYCPTRLLIH
SMCTSHYLDI FITFIICLNV VTMSLEHYNQ PTSLETALKY CNYMFTTVFV LEAVLKLVAF
GLRRFFKDRW NQLDLAIVLL SVMGITLEEI EINAALPINP TIIRIMRVLR IARVLKLLKM
ATGMRALLDT VVQALPQVGN LGLLFMLLFF IYAALGVELF GKLVCNDENP CEGMSRHATF
ENFGMAFLTL FQVSTGDNWN GIMKDTLRDC THDERSCLSS LQFVSPLYFV SFVLTAQFVL
INVVVAVLMK HLDDSNKEAQ EDAEMDAEIE LEMAHGLGPG PGPCPCPCPC PCPCPCPGPR
MPTSSPGAPG RGSGGAGVGG DTESHLCRHC YSPAQETLWL DSVSLIIKDS LEGELTIIDN
LSGSIFHHYS SPAGCDKCHH DKQETGPRPS CWGMT
//
