ID A0A2Y9M2T0_DELLE Unreviewed; 2364 AA.
AC A0A2Y9M2T0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Voltage-dependent T-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1G {ECO:0000313|RefSeq:XP_022413567.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022413567.1};
RN [1] {ECO:0000313|RefSeq:XP_022413567.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022413567.1};
RG RefSeq;
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 RefSeq; XP_022413567.1; XM_022557859.1.
DR Proteomes; UP000248483; 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:UP000248483};
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 122..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 342..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 369..394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 744..762
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 774..795
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 865..884
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 941..964
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1277..1295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1315..1336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1412..1434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1514..1537
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1594..1615
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1627..1650
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1728..1747
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1811..1833
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 80..405
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 743..970
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1275..1547
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1593..1843
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 465..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1859..1897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2090..2113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2135..2195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2258..2364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1546..1573
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 470..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..509
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1004
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2152..2173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 354
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 923
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1486
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 2364 AA; 261562 MW; 7235118CA60C44C2 CRC64;
MDEEEDGAGA EESGQPRSFM QLNDLSGAVG RPGPGSAEKD PGSVDSEAEG LPYPALAPVV
FFYLSQDSRP RSWCLRTVCN PWFERISMLV ILLNCVTLGM FRPCEDIACD SQRCRILQAF
DDFIFAFFAV EMVVKMVALG IFGKKCYLGD TWNRLDFFIV IAGMLEYSLD LQNVSFSAVR
TVRVLRPLRA INRVPSMRIL VTLLLDTLPM LGNVLLLCFF VFFIFGIVGV QLWAGLLRNR
CFLPENFSLP LSVDLERYYQ TENEDENPFI CSQPRENGMR SCRSVPTLRG DGGGGPPCGL
DYEAYNSSSN TTCVNWNQYY TNCSAGEHNP FKGAINFDNI GYAWIAIFQV ITLEGWVDIM
YFVMDAHSFY NFIYFILLII VGSFFMINLC LVVIATQFSE TKQRESQLMR EQRVRFLSNA
STLASFSEPG SCYEELLKYL VYILRKAARR LAQVSRAAGV RAGLLSSPAP HGSQEPQPSG
SCPRSHRRPS VHHLVHHHHH HHHHYHLGNG TLRVPRASPQ IQDKDANGSR RLMLPPPSTL
ALSGGPPGGA ESVHSFYHAD CHLEPVRCQA PPPRSPSEAS GRTVGSGKVY PTMHTSPPPE
MLKEKALMEV APTSGPSTLT SLNIPPRPYS SMHKLLETQS TGACQSSCKI SSPCLKADSG
ACGPDSCPYC VRTGAGEVEL AGHEMPDSDS EAVYEFTQDA QHGDRQNPHS WRRRSLGLDV
EPNSVLAFWR LVCDTFRKIV DSKYFGRGIM IAILVNTLSM GIEYHEQPEE LTNALEISNI
VFTSLFALEM LLKLLVYGPF GYIKNPYNIF DGVIVVISVW EIVGQQGGGL SVLRTFRLMR
VLKLVRFLPA LQRQLVVLMK TMDNVATFCM LLMLFIFIFS ILGMHLFGCK FASERDGDTL
PDRKNFDSLL WAIVTVFQIL TQEDWNKVLY NGMASTSSWA ALYFIALMTF GNYVLFNLLV
AILVEGFQAE EISKREDASG QLSCIQLPVD SQGGDATKSE SEPDFFSPSL DGDGDRKKRL
AMVSLGEHPE LRRSLLPPLI IHTAATPMSL PKSSSTGLAE VLGPASRRAS SSGSAEPGAP
HEMKSPPSAR SSPHSPWSAA SRWTSRRSSR NSLGRAPSLK RRSPSGERRS LLSGDGQESQ
DEQESSEEER ASPAGSDRRR RGSLEREAKS SFDLPDTLQV PGLHRTASGR SSASEHQDCN
GKSAPGRLTR ALRPDDPPLD GDDGDDEGNL SKGERMRAWV RARLPACCLE RDSWSAYIFP
PQSRFRLLCH RIITHKMFDH VVLVIIFLNC ITIAMERPKI DPHSAERIFL TLSNYIFTAV
FLAEMTVKVV ALGWCFGEQA YLRSSWNVLD GLLVLISVID ILVSTVSDSG TKILGMLRVL
RLLRTLRPLR VISRAQGLKL VVETLMSSLK PIGNIVVICC AFFIIFGILG VQLFKGKFFV
CQGEDTRNIT NKSDCAEASY RWVRHKYNFD NLGQALMSLF VLASKDGWVD IMYDGLDAVG
VDQQPIMNHN PWMLLYFISF LLIVAFFVLN MFVGVVVENF HKCRQHQEEE EARRREEKRL
RRLEKKRRKA 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 AELELEMKPL
SPQAPSPPGS PFLWPGAEGP DSPGSPKPGA PHAAAHAEAV SHFSLEHPMD RQLFDTVSLL
IQGSLEGELK LMDELAGPGG PPSAFPPTRS LGGSNPQIPL AEMEALSLTS EIVSELSCSV
ALTDDSLPDD THTLLLSALE SNMESHTEEV PVMLRPDLLT VRKSGVSRTH SLPNDSYMCR
DGSTAEGSLG HRGWGLPKAQ SGSVLSVHSQ PADTSYTLQL PKDAPHLLQP HDAPTWGTIP
KLPPPGRSPL AQRPLRRQAA IRTDSLDVQG LDSGEDLLSE VSGPSPPLAE ASSFWGRSSA
QVQQHSHGQS KISKHMPPSA PCPGPEPTWS KGPSEIRSSL ELDTELSWIS GDLLPVGSQE
EALSPRDLKK CYSVEARSCP RRPASWLDEQ RRHSIAVSCL DSGSQPRLGP GPSSLRGQPL
GGPGSRPKKK LSPPSISIEP PESQSQGPRP PPSPGVCLRR RAPSSDSKDP SASGPPDSMA
ASPPPKKDVL SLSGLSSDPA DLDP
//
