ID A0A2K5NZN8_CERAT Unreviewed; 2193 AA.
AC A0A2K5NZN8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Voltage-dependent T-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1I {ECO:0000313|Ensembl:ENSCATP00000042958.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000042958.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000042958.1}
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; ENSCATT00000067394.1; ENSCATP00000042958.1; ENSCATG00000044010.1.
DR GeneTree; ENSGT00940000158594; -.
DR OMA; CNFDESD; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000044010; Expressed in frontal cortex.
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: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}; 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:UP000233060};
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 117..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 204..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 341..362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 368..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 723..745
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 801..823
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1141..1159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1179..1201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1216..1244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1279..1298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1378..1401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1457..1474
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1494..1513
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1592..1611
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1678..1700
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 82..404
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 601..829
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1139..1411
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1457..1710
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 463..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1727..1753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1841..1864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1907..1930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1983..2032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2050..2193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1410..1437
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 528..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1026
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1983..2008
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2052..2070
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 782
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1350
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 2193 AA; 241942 MW; 289123FEF40AF20A CRC64;
MAESASPPSS AAAPAAEPGV TTEQPGPQSP PSSPPGLEEP LDGADPHVPH PDLAPVAFFC
LRQTTSPRNW CIKMVCNPYP PMLVILLNCV TLGMYQPCDD MDCLSDRCKI LQVFDDFIFI
FFAMEMVLKM VALGIFGKKC YLGDTWNRLD FFIVMAGMVE YSLDLQNINL SAIRTVRVLR
PLKAINRVPS MRILVNLLLD TLPMLGNVLL LCFFVFFIFG IIGVQLWAGL LRNRCFLEEN
FTIQGDVALP PYYQPEEDDE MPFICSLSGD NGIMGCHEIP PLKEQGRECC LSKDDVYDFG
AGRQDLNASG LCVNWNRYYN VCRTGSANPH KGAINFDNIG YAWIVIFQVI TLEGWVEIMY
YVMDAHSFYN FIYFILLIIV GSFFMINLCL VVIATQFSET KQREHRLMLE QRQRYLSSST
VASYAEPGDC YEEIFQYVCH ILRKAKRRAL GLYQALQSRR QALGPEAPVP AKPGPHAKEP
RHYKLCPRHS PLDATPHTLV QPIPATLASD PASCPCCQHE AGRRPSGLGS TDSGQEGSGS
GSSAGGEDEA DGDGTRSSED GASSELGKEE EEEEQADGAV WLCGDVWRET RAKLRGIVDS
KYFNRGIMMA ILVNTVSMGI EHHEQPEELT NILEICNVVF TSMFALEMIL KLAAFGLFDY
LRNPYNIFDS IIVIISIWEI VGQADGGLSV LRTFRLLRVL KLVRFMPALR RQLVVLMKTM
DNVATFCMLL MLFIFIFSIL GMHIFGCKFS LRTDTGDTVP DRKNFDSLLW AIVTVFQILT
QEDWNVVLYN GMASTSPWAS LYFVALMTFG NYVLFNLLVA ILVEGFQAEG DANRSYSDDD
QSSSNMEEFD KLQEGLDSSG DPKLFPIPMT PNGHLDPSLP LGGHLGPAGA AGPAPRLSLQ
PDPMLVALGS RKSSVMSLGR MSYDQRSLSS SRSSYYGPWG RSGAWASRRS SWNSLKHKPP
SAEHESLLSA ERGGGARVCE VAGDEGLPRP APLHAPHAPH APHAPHAHHA HHGPHLAHRH
RHHRRTLSLD TRDSVDLAEL VPTVGAHPRA AWRAAGPAPG HEDCNGRMPS IAKDVFTKMG
DRRDRGEDEE EIDYTLCFRV RKMIDVYKPD WCEVREDWSV YLFSPENRFR VLCQTIIAHK
LFDYVVLAFI FLNCITIALE RPQIEAGSTE RIFLTVSNYI FTAIFVGEMT LKVVSLGLYF
GEQAYLRSSW NVLDGFLVFV SIIDIVVSLA SAGGAKILGV LRVLRLLRTL RPLRVISRAP
GLKLVVETLI SSLKPIGNIV LICCAFFIIF GILGVQLFKG KFYHCLGVDT RNITNRSDCM
AANYRWVHHK YNFDNLGQAL MSLFVLASKD GWVNIMYNGL DAVAVDQQPV TNHNPWMLLY
FISFLLIVSF FVLNMFVGVV VENFHKCRQH QEAEEARRRE EKRLRRLEKK RRKAQRLPYY
ATYCHTRLLI HSMCTSHYLD IFITFIICLN VVTMSLEHYN QPTSLETALK YCNYMFTTVF
VLEAVLKLVA FGLRRFFKDR WNQLDLAIVL LSVMGITLEE IEINAALPIN PTIIRIMRVL
RIARVLKLLK MATGMRALLD TVVQALPQVG NLGLLFMLLF FIYAALGVEL FGKLVCNDEN
PCEGMSRHAT FENFGMAFLT LFQVSTGDNW NGIMKDTLRD CTHDERSCLS SLQFVSPLYF
VSFVLTAQFV LINVVVAVLM KHLDDSNKEA QEDAEMDAEL ELEMAHSLGP GPRLPAGSPG
APGRGPGGAG GGGDADGGLC RRCYSPAQEN LWLDSVSLII KDSLEGELTI IDNLSGSIFH
HYSSPAGCKK CHHDKQEVQL AETEAFSLNS DRSSSILLGD DLSLEDPTAC PPGPKDSKGE
LDPPEPMCVR DLDECFFPLS STAVSPGPEN FLCEMEEIPF NPVQSWLKHD SSQAPPSPFS
PDASSPLLPM PAEFFHPAVS ASQKGPEKGT GTGTLPKIAL QGSWASLRSP RVNCTLLRQA
TGSDTSLDAS PSSSAGSLQT TLEDSLTLSD SPRRALGPPA PAPGPRAGLS PAAHRRLSLR
GRGLFSLRGL RAHQRSHSSG GSTSPGCTYH DSMDPSDEEG RGGAGGGGAG SEHSETLSSL
SLTSLFCPPP PPPLPGLTPA RKFSSTSSLA APGRPHAAAP AHGLARSPSW AADRSKDPLG
RAPLPMGLGP LASPPQPLPG ELEPGDAASK RKR
//
