ID A0A2K5Z312_MANLE Unreviewed; 2342 AA.
AC A0A2K5Z312;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Voltage-dependent T-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1G {ECO:0000313|Ensembl:ENSMLEP00000022204.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000022204.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000022204.1}
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; ENSMLET00000045710.1; ENSMLEP00000022204.1; ENSMLEG00000032994.1.
DR GeneTree; ENSGT00940000159664; -.
DR Proteomes; UP000233140; Unplaced.
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: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:UP000233140};
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 106..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 325..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 352..377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 727..745
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 757..778
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 848..867
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 924..947
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1260..1278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1298..1319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1331..1350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1395..1417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1497..1520
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1584..1605
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1617..1640
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1718..1737
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1801..1823
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 71..388
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 726..953
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1258..1530
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1583..1833
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1850..1891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2082..2101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2146..2216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2244..2342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1529..1563
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 683..699
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2146..2160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2244..2258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2279..2295
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 337
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 906
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 2342 AA; 259316 MW; 7484993E6CB1255A CRC64;
RGPAAGGVEV SEGGRPTKFQ FPEKDPGSAD SEAEGLPYPA LAPVVFFYLS QDSRPRSWCL
RTVCNPYPSG MLVILLNCVT LGMFRPCEDI ACDSQRCRIL QAFDDFIFAF FAVEMVVKMV
ALGIFGKKCY LGDTWNRLDF FIVIAGMLEY SLDLQNVSFS AVRTVRVLRP LRAINRVPSM
RILVTLLLDT LPMLGNVLLL CFFVFFIFGI VGVQLWAGLL RNRCFLPENF SLPLSVDLER
YYQTENEDES PFICSQPREN GMRSCRSVPT LRGEGGGGPP CGLDYEAYNS SSNTTCVNWN
QYYTNCSAGE HNPFKGAINF DNIGYAWIAI FQVITLEGWV DIMYFVMDAH SFYNFIYFIL
LIIVGSFFMI NLCLVVIATQ FSETKQRESQ LMREQRVRFL SNASTLASFS EPGSCYEELL
KYLVYILRKA ARRLAQVSRA AGVRAGLLSS PAPLGGQETQ PSSSCSRSHR RLSVHHLVHH
HHHHHHHYHL GNGTLRVPRA SPEIQDRDAN GSRRLMLPPP STPALSGGPP GGAESVHSFY
HADCHLEPVR CQAPPPRSPS EASGRTVGSG KVYPTVHTSP PPETLKEKAL VEVAASSGPA
TLTSLNIPPG PYSSMHKLLE TQSTGACQSS CKISSPCLKA DSGASGPDSC PYCARAGAGE
VELADREMPD SDSEVVYEFT QDAQHSDIRD PHSRRQRSLG PDAEPSSVLA FWRLICDTFR
KIVDSKYFGR GIMIAILVNT LSMGIEYHEQ PEELTNALEI SNIVFTSLFA LEMLLKLLVY
GPFGYIKNPY NIFDGVIVVI SVWEIVGQQG GGLSVLRTFR LMRVLKLVRF LPALQRQLVV
LMKTMDNVAT FCMLLMLFIF IFSILGMHLF GCKFASERDG DTLPDRKNFD SLLWAIVTVF
QILTQEDWNK VLYNGMASTS SWAALYFIAL MTFGNYVLFN LLVAILVEGF QAEEISKRED
ASGQLSCIQL PVDSQGGDAN KSESEPDFFS PSLDGDGDRK KCLALVSLGE HPELRKSLLP
PLIIHTAATP MSLPKSTSTG LGEALGPTSR RTSSSGSAEP GAAHEMKSPP SARSSPHSPW
SAASSWTSRR SSRNSLGRAP SLKRRSPSGE RRSLLSGEGQ ESQDEEESSE EERASPAGSD
RRHRESLERE AKSSFDLPDT LQVPGLHRTA SGRGSASEHQ DCNGKSASGR LARALRPDDP
PLDGDDADDE GNLSKGERVR AWIRARLPAC CLERDSWSAY IFPPQSRFRL LCHRIITHKM
FDHVVLVIIF LNCITIAMER PKIDPHSAER IFLTLSNYIF TAVFLAEMTV KVVALGWCFG
EQAYLRSSWN VLDGLLVLIS VIDILVSMVS DSGTKILGML RVLRLLRTLR PLRVISRAQG
LKLVVETLMS SLKPIGNIVV ICCAFFIIFG ILGVQLFKGK FFVCQGEDTR NITNKSDCAE
ASYRWVRHKY NFDNLGQALM SLFVLASKDG WVDIMYDGLD AVGVDQQPIM NHNPWMLLYF
ISFLLIVAFF VLNMFVGVVV ENFHKCRQHQ EEEEARRREE KRLRRLEKKR RSKEKQMAEA
QCKPYYSDYS RFRLLVHHLC TSHYLDLFIT GVIGLNVVTM AMEHYQQPQI LDEALKICNY
IFTVIFVLES VFKLVAFGFR RFFQDRWNQL DLAIVLLSIM GITLEEIEVN ASLPINPTII
RIMRVLRIAR VLKLLKMAVG MRALLDTVMQ ALPQVGNLGL LFMLLFFIFA ALGVELFGDL
ECDETHPCEG LGRHATFRNF GMAFLTLFRV STGDNWNGIM KDTLRDCDQE STCYNTVISP
IYFVSFVLTA QFVLVNVVIA VLMKHLEESN KEAKEEAELE AELELEMKTL SPQPHSPLGS
PFLWPGVEGP DSPDSPKPGA LHPAAHARSA SHFSLEHPSD RQLFDTISLL IQGSLEWELK
LMDELAGPGG QPSAFPSAPS LGGSDPQIPL AEMEALSLTS EIVSEPSCSL ALTDDSLPDD
MHTLLLSAPE SNVQPHPTEL PGPDLLTVRK SGVSRTHSLP NDSYMCRHGS IAEGPLGHRG
WGLPKAQSGS VLSVHSQPAD TSYILQLPKD APHLLQPYST PTWGTIPKLP PPGRSPLAQR
PLRRQAAIRT DSLDVQGLGS REDLLAEVSG PSLPLARAYS FWGQSSTQAQ QHSRSHSNIS
KHMPPRAPCP GPQPNWDKGP PETRSSLELD TELSWISGDL LPPGGQEEPP SPRDLKKCYS
VEAQSCQRRP TSWLDEQRRH SIAVSCLDSG SQPHLGTDPS NLGGHRPKKK LSPPSISIDP
PESQGPRPPP SPGVCLRRRA PSSDSKDPLA SGPPDSMAAS PSPKKDVLSL SGLSSDPADL
DP
//
