ID A0A2Y9T691_PHYMC Unreviewed; 2294 AA.
AC A0A2Y9T691;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Voltage-dependent T-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1G {ECO:0000313|RefSeq:XP_023985853.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023985853.1};
RN [1] {ECO:0000313|RefSeq:XP_023985853.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_023985853.1};
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_007103594.1; XM_007103532.1.
DR RefSeq; XP_023985853.1; XM_024130085.2.
DR Proteomes; UP000248484; Chromosome 14.
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:UP000248484};
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 463..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 991..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1064..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1885..1922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2023..2044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2067..2164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2187..2294
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 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 2075..2106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2187..2201
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 2294 AA; 253676 MW; D2B9EB4E61F4EEB2 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 TENEDESPFI CSQPRENGMR SCRSVPALRG DGGGGPPCGL
DYEAYNSSSN TTCVNWNQYY TNCSAGEHNP FKGAINFDNI GYAWIAIFQV ITLEGWVDIM
YFVMDAHSFY NFIYFILLII VGSFFMINLC LVVIATQFSE TKQRESQLMR EQRVRFLSNA
STLASFSEPG SCYEELLKYL VYILRKAARR LAQVSRAAGV RAGLLSSPPP RGNQEAQPSG
SCSRSHRRPS VHHLVHHHHH HHHHYHLGNG TLRVPRASPQ IQDKDARGSR RLMLPPPSTL
ALSGGPPGGA ESVHSFYHAD CHLEPVRCQA PPPRSPSEAS GRTGGSGKVY PTMHTSPPPA
MLKEKALMEV APTSGPPTLT SLNIPPRPYS SMHKLLETQS TGACQSSCRI SSPCLKADSG
ACGPDSCPYC VRTGAGEVEL AGHEMPDSDS EAVYEFTQDA QHGDRQNPHS 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 DGGGGRKKRL
ALVSLGEHPE VRKSLLPPLI IHTAATPMSL PKSSSTGLAE VLGPVSRRAS SSGSAEPGAP
HETKSPPSAR SSPHSPWSAA SSWASRRSSR NSLGRAPSLK RRSPSGERRS LLSGEGQESQ
DEEESSEEER TSPAGSDRRH RGSLEREAKS SFDLPDTLQV PGLHRTASGR SSASEYQDCN
GKSAPGRLTR ALRPDDPPLD GDDGDDEGNL SKGERMRAWV RARLPACCLE RDSWSAFIFP
PQSRFRLLCH RIITHKMFDH VVLVIIFLNC ITIAMERPKI DPHSAERIFL TLSNYIFTAV
FLAEMTVKVV ALGWCFGEQA YLRSSWNVLD GLLVLISVID ILVSMISDSG 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 KICNYIFTVI FVLESVFKLV AFGFRRFFQD
RWNQLDLAIV LLSIMGITLE EIEVNASLPI NPTIIRIMRV LRIARVLKLL KMAVGMRALL
DTVMQALPQV GNLGLLFMLL FFIFAALGVE LFGDLECDET HPCEGLGRHA TFRNFGMAFL
TLFRVSTGDN WNGIMKDTLR DCDQESTCYN TVISPIYFVS FVLTAQFVLV NVVIAVLMKH
LEESNKEAKE EAELEAELEL EMKTLSPQAP SPPGSPFLWP GVEGPDGPGS PKPGAPHAAA
HAEAVSHFSL EHPMVSKHPL RLKGVPDLLT VRKSGVSRTH SLPNDSYMCR DGSTAEGSLG
HRGWGLPKAQ SGSVLSVHSQ PADTSYILQL PKDAPHLLQP HGAPTWGTIP KLPPPGRSPL
AQRPLRRQAA IRTDSLDIQG LGSREDLLSE VSGSSPPLAG ASSFWGRSST QAQQHSHSQS
KTSKHMPPSA PCPGPEPTWS KGPSDIRSSL ELDTELSWIS GDLLPVGSQD DAPSPRDLKK
CYSVEARSCP RRPASWLDEQ RRHSIAVSCL DSGSQPRLGP GPSSLRGQPL GGPGSRPKKK
LSPPSISIDP PESQSQGPRP PPSPGVCLRR RAPSSDSKDP LASGPPDSMA ASPPPKKDVL
SLSGLSSDPA DLDP
//
