ID A0A383ZN21_BALAS Unreviewed; 2341 AA.
AC A0A383ZN21;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-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_007176522.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007176522.1};
RN [1] {ECO:0000313|RefSeq:XP_007176522.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007176522.1};
RG RefSeq;
RL Submitted (JAN-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_007176522.1; XM_007176460.1.
DR CTD; 8913; -.
DR OrthoDB; 1110761at2759; -.
DR Proteomes; UP000261681; 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:UP000261681};
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 1348..1367
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 1619..1640
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1652..1675
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1753..1772
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1836..1858
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 1618..1868
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 1..48
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 567..591
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 1896..1923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2069..2089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2132..2172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2234..2341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1546..1580
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 470..485
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 1085..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..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 2132..2152
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 2341 AA; 259073 MW; 175107AD3302BE88 CRC64;
MDEEEDGAGA EESGQPRSFM RLNDLSGAGG RPGPGSAEKD PGSADSEAEG 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 RGSQEPQPSG
SCSRSHRRPS VHHLVHHHHH HHHHYHLGNG TLRVPRASPQ IQDKDANGSR RLMLPPPSTL
ALSGGPPGGA ESVHSFYHAD CHLEPVRCQA PPPRSPSEAS GRTVGSGKVY PTMHTSPPPE
MLKEKALMEV APTSGPPTLT SLNIPPRPYS SMHKLLETQS TGTCQSSCKI SSPCLKADSG
ACGPDSCPYC VRTGAGEVEL AGHEMPDSDS EAVYEFTQDA QHGDRRNPHS WRRRSLGLDV
EPNSVLAFWR LICDTFRKIV 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 DGDGDRRKRL
ALVSLGDHPE LRSSLLPPLI IHTAATPMSL PKSSSTGLAE ALGPASRRAS SSGSAEPGAP
HETKSPPSAR SSPHSPWSAA SSWASRRSSR NSLGRAPSLK RRSPSGERRS LLSGEGQESQ
DEEESSEEEH TSPAGSDRRH RGSLEREAKS SFDLPDTLQV PGLHRTASGR SSASEHQDCN
GKSAPGRLTR ALRPDDPPLD GDDGDDEGNL SKGERMRAWV RARLPACCLE RDSWSAYIFP
PQSRFRLLCH RIITHKMFDH VVLVIIFLNC ITIAMERPKI DPHSAERIFL TLSNYIFTAV
FLAEMTVKVV ALGWCFGEQA YLRSSWNVLD GLLVLISIID ILVSMVSDSG TKILGMLRVL
RLLRTLRPLR VISRAQGLKL VVETLMSSLK PIGNIVVICC AFFIIFGILG VQLFKGKFFV
CQGEDTRNIT NKSDCAEASY RWVRHKYNFD NLGQALMSLF VLASKDGWVD IMYDGLDAVG
VDQQPIMNHN PWMLLYFISF LLIVAFFVLN MFVGVVVENF HKCRQHQEEE EARRREEKRL
RRLEKKRRSK EKQMADLMLD DVIASGSSAS AAPEAQCKPY YSDYSRFRLL VHHLCTSHYL
DLFITGVIGL NVVTMAMEHY QQPQILDEAL KICNYVFTVI FVLESVFKLV AFGFRRFFQD
RWNQLDLAIV LLSIMGITLE EIEVNASLPI NPTIIRIMRV LRIARVLKLL KMAVGMRALL
DTVMQALPQV GNLGLLFMLL FFIFAALGVE LFGDLECDET HPCEGLGRHA TFRNFGMAFL
TLFRVSTGDN WNGIMKDTLR DCDQESTCYN TVISPIYFVS FVLTAQFVLV NVVIAVLMKH
LEESNKEAKE EAELEAELEL EMKTLSPQAP SPLGSPFLWP GVEGPDSPGS PKSRAPHAAA
HAETVSHFSL EHPMIPLAEM EALSLTSEIV SELSCSVALT DDSLPDDTHT LLLSALESNM
ESRTEEVPVM LRPDLLTVRK SGVSRTHSLP NDSYMCRDGS TAEGSLGHRG WGLPKAQSGS
VLSVHSQPAD TSYILQLPKD APQLLQPHGA PTLGTIPKLP PPGRSPLAQR PLRRQAAIRT
DSLDIQGLGS REDLLSEVSG PSPPLAVASS FWGRSSTQAQ QHSHSQSKIS KHMPPSAPCP
GPEPTWSKGP SEIRSSLELD TELSWISGDL LPVGSQAEAP SPRDLKKCYS VEARSCPRRP
ASWLDEQRRH SIAVSCLDRG SQPRLGPGPS SLRGQPLGGP GSRPKKKLSP PSISIDPPES
QSQGPRPPPS PGVCLRRRAP SSDSKDPSAS GPPDSMAASL PPKKDVLSLS GLSSDPADLE
P
//
