ID A0A2K5WTA8_MACFA Unreviewed; 1846 AA.
AC A0A2K5WTA8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Voltage-dependent T-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1I {ECO:0000313|Ensembl:ENSMFAP00000040371.2};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000040371.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000040371.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000040371.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 Ensembl; ENSMFAT00000014639.2; ENSMFAP00000040371.2; ENSMFAG00000046252.2.
DR VEuPathDB; HostDB:ENSMFAG00000046252; -.
DR GeneTree; ENSGT00940000158594; -.
DR Proteomes; UP000233100; Chromosome 10.
DR Bgee; ENSMFAG00000046252; Expressed in cerebellum and 3 other cell types or tissues.
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 GO; GO:0019228; P:neuronal action potential; IEA:Ensembl.
DR GO; GO:0030431; P:sleep; 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: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 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 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:UP000233100};
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 180..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 306..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 333..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 697..719
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 775..797
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1072..1094
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1109..1137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1172..1191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1271..1294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1354..1371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1391..1410
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1474..1501
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1576..1597
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 102..346
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 575..802
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1032..1304
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1354..1607
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1630..1651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1732..1820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..923
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..956
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1734..1789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 318
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 756
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1243
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 1846 AA; 203536 MW; B50AC384E04D359E CRC64;
MAESASPPSS AAAPAAEPGV TTEQPGPQSP PSSPPGLEEP LDGADPHVPH PDLAPVAFFC
LRQTTSPRNW CIKMVCNPYP PQPWLIGALQ GLKGRGLGLS PMVLKMVALG IFGKKCYLGD
TWNRLDFFIV MAGMVEYSLD LQNINLSAIR TVRVLRPLKA INRVPSMRIL VNLLLDTLPM
LGNVLLLCFF VFFIFGIIGV QLWAGLLRNR DVALPPYYQP EEDDEMPFIC SLSGDNGIMG
CHEIPPLKEQ GRECCLSKDD VYDFGAGRQD LNASGLCVNW NRYYNVCRTG SANPHKGAIN
FDNIGYAWIV IFQVITLEGW VEIMYYVMDA HSFYNFIYFI LLIIVSVREP GLLGASLSTK
QREHRLMLEQ RQRYLSSSTV ASYAEPGDCY EEIFQYVCHI LRKAKRRALG LYQALQSRRQ
ALGPEAPGAS NLGPMPRSPG TTVSGPASDT ALSEDRGPQH SASAAGVSYP RPCSGKPSPS
SLHGLGIDSW EASRRMHAQS CHPPILGCQP SRRGLGGGPR WPVGRPGMRI QEPGPGKAGT
GVAGGREGEA DGAVWLCGDV WRETRAKLRG IVDSKYFNRG IMMAILVNTV SMGIEHHEQP
EELTNILEIC NVVFTSMFAL EMILKLAAFG LFDYLRNPYN IFDSIIVIIS IWEIVGQADG
GLSVLRTFRL LRVLKLVRFM PALRRQLVVL MKTMDNVATF CMLLMLFIFI FSILGMHIFG
CKFSLRTDTG DTVPDRKNFD SLLWAIVTVF QILTQEDWNV VLYNGMASTS PWASLYFVAL
MTFGNYVLFN LLVAILVEGF QAEVTVVLAE EAPPQGLQKT GRGRGRGVLG SIPSPTGQAS
DPLRATVGVQ AAFGHLVPHP WVCLWGADPS GNSSQSSSRS SYYGPWGRSG AWASRRSSWN
SLKHKPPSAE HESLLSAERR RRPGLRGCRG RGAATARTPA RPSRPARPPR SSRAPSGTPP
PWRDGRMGGD RQPCASLTPG APSSFCQTLC FRVRKMIDVY KPDWCEVRED WSVYLFSPEN
RFRVLCQTII AHKLFDYVVL AFIFLNCITI ALERPQIEAG STERIFLTVS NYIFTAIFVG
EMTLKVVSLG LYFGEQAYLR SSWNVLDGFL VFVSIIDIVV SLASAGGAKI LGVLRVLRLL
RTLRPLRVIS RAPGLKLVVE TLISSLKPIG NIVLICCAFF IIFGILGVQL FKGKFYHCLG
VDTRNITNRS DCMAANYRWV HHKYNFDNLG QALMSLFVLA SKDGWVNIMY NGLDAVAVDQ
QPVTNHNPWM LLYFISFLLI VSFFVLNMFV GVVVENFHKC RQHQEAEEAR RREEKRLRRL
EKKRRSEWVP AQRLPYYATY CHTRLLIHSM CTSHYLDIFI TFIICLNVVT MSLEHYNQPT
SLETALKYCN YMFTTVFVLE AVLKLVAFGL RRFFKDRWNQ LDLAIVLLSV MGITLEEIEI
NAALPINPTI IRIMRVLRIA RVLKLLKMAT GMRALLDTVV QALPQVGNLG LLFMLLFFIY
AALGVELFGK LVCNDENPCE GMSRHATFEN FGMAFLTLFQ VSTGDNWNGI MKDTLRDCTH
DERSCLSSLQ FVSPLYFVSF VLTAQFVLIN VVVAVLMKHL DDSNKEAQED AEMDAELELE
MAHGLGPGPR LPAGSPGAPW PRAGRGGRRG RRRGRLVPAL LLLPWPGQIG SLSQGQVWAC
GVVAAATDPS TVPHTVGAWV GQLPHLVYCR CQAGSLCVTC RTACPFCDMK GSSARSSPRA
SSWHSTSSRC PALVSSSGLR PTQLRGSHGS TSSAGAGSPL PSPQQCGPLS SPWGAPAPRV
APASGGCRAG PQEPSAGAGS LGCPTPLPCG GCRFSSVSGP RSVPCL
//
