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Database: UniProt
Entry: V8PDM4_OPHHA
LinkDB: V8PDM4_OPHHA
Original site: V8PDM4_OPHHA 
ID   V8PDM4_OPHHA            Unreviewed;      2386 AA.
AC   V8PDM4;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Voltage-dependent T-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
DE   Flags: Fragment;
GN   Name=Cacna1h {ECO:0000313|EMBL:ETE72455.1};
GN   ORFNames=L345_01712 {ECO:0000313|EMBL:ETE72455.1};
OS   Ophiophagus hannah (King cobra) (Naja hannah).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX   NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE72455.1, ECO:0000313|Proteomes:UP000018936};
RN   [1] {ECO:0000313|EMBL:ETE72455.1, ECO:0000313|Proteomes:UP000018936}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Blood {ECO:0000313|EMBL:ETE72455.1};
RX   PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA   Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA   McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA   Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA   de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA   Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA   Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA   Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT   "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT   snake venom system.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
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: Cytoplasm, cytoskeleton, cilium basal body
CC       {ECO:0000256|ARBA:ARBA00004120}. Membrane
CC       {ECO:0000256|RuleBase:RU003808}; Multi-pass membrane protein
CC       {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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETE72455.1}.
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DR   EMBL; AZIM01000222; ETE72455.1; -; Genomic_DNA.
DR   Proteomes; UP000018936; Unassembled WGS sequence.
DR   GO; GO:0005929; C:cilium; IEA:UniProt.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
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   GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.287.70; -; 3.
DR   Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 3.
DR   InterPro; IPR010796; C2_B9-type_dom.
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:SF192; VOLTAGE-DEPENDENT T-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1H; 1.
DR   PANTHER; PTHR10037; VOLTAGE-GATED CATION CHANNEL CALCIUM AND SODIUM; 1.
DR   Pfam; PF07162; B9-C2; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01629; TVDCCALPHA1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 3.
DR   PROSITE; PS51381; C2_B9; 1.
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};
KW   Cilium biogenesis/degradation {ECO:0000256|ARBA:ARBA00022794};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
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:UP000018936};
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        863..883
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        946..968
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1023..1046
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1327..1347
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1359..1380
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1450..1472
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1567..1593
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1649..1668
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1715..1734
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1806..1827
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1900..1921
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          824..1052
FT                   /note="Ion transport"
FT                   /evidence="ECO:0000259|Pfam:PF00520"
FT   DOMAIN          1287..1404
FT                   /note="Ion transport"
FT                   /evidence="ECO:0000259|Pfam:PF00520"
FT   DOMAIN          1426..1603
FT                   /note="Ion transport"
FT                   /evidence="ECO:0000259|Pfam:PF00520"
FT   DOMAIN          1649..1931
FT                   /note="Ion transport"
FT                   /evidence="ECO:0000259|Pfam:PF00520"
FT   REGION          248..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          272..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          548..576
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          651..686
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2120..2182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2206..2259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1602..1629
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        252..267
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2236..2258
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1005
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ETE72455.1"
SQ   SEQUENCE   2386 AA;  267231 MW;  FE04A382FD798436 CRC64;
     TWEAGCVSQK QHLRFSLTLV SHLVRARQHA GYPLELRHPW DVPAMSGYQV PNRKVHNLGG
     KRDVSLCPCG LGPLVAYGGA NAVLFLTSRV SLLLSLSPSM MEYSLDGHNV SLSAIRTVRV
     LRPLRAINRV PSKTHNLTFL HKYYRPEESE ENPFICSSLR DNGMQKCSSI PNRKEYKMDC
     TLTVDAYNPQ LDSLDLSSRN GCINWNQYYN VCRTGDLNPH NGAINFDNIG YAWIAIFQPS
     ALPHPLDSCG TANLGQPESQ SWHSTDQTLH LWQEKPDLRN PRRKQRKPPP SPISWGPSAR
     SSSERLERSS HLFLQLFQQS DEKPILGRRG MVTEGKPWRG TKACRRCLGF PYKMPPSSGF
     PAQLGGGGGG GGGEAFRAAQ LLPNELNRVL RSKLNPAEVL KIFQVDWGLQ CPGPKASPGK
     ATWHSLPPSC HLDYRVVVDI LCNQTVHQHK DCVKEWLPHL RLGICKVGSF FMINLCLVVI
     ATQFSETKQR ENQLMQEQRA RYLSNDSTIA SFSEPGSCYE ELLKYICHIF RKVKRRALRL
     YNNWQSKRRK KVNPNSGADD VQGHQSGKRR IMSIQGPRAN PGICDLELDV MKPGSQLMLP
     PSSPSHPSGG AADTESIHSI YHADCHVEGT SVKCKSSSIA AGSKAANRSS MNYPTILPSP
     ANKASVPPLS KGKKNEGSEA TSPMPVVSSP AHLNADCYGK LHHLVGERGL CRTSSILSGL
     NVPCPLPGPQ ANTLSCELQN CPFCASILED PEFEFSEADS YESGEDNNGV YEFTQDVKHG
     DLRDQIQQQR NKKKKKRKPA KERNKITKLW KAFGNKLKRI VESKYFNRGI MIAILINTLS
     MGIEYHEQPD ELTNALEISN IVFTSMFALE MLLKLLAFGI WGYIKNPYNI FDGIIVVISV
     WEIIGQADGG LSVLRTFRLL RVLKLVRFMP ALRRQLVVLM KTMDNVATFC MLLMLFIFIF
     SILGMHLFGC KFGLRTETGD TMPDRKNFDS LLWAIVTVFQ ILTQEDWNVV LYNGMASTSS
     WAALYFVALM TFGNYVLFNL LVAILVEGFQ AEGDANRSDT DEDKTSTNFE EEFEKLKELH
     ASEMKMYSLA VTPNGHLEGK GSMPPPIIMH TAATPMPTPK GSPHMDSAYP FGDSRRGSNV
     SVDPLGFDQK SLVFSQEGAR LAGLGRGGKG ERSLSGAESL DCRGALDLPE LLQVPGVHPP
     VAMLPLEYQD CNGKMLQVPS ELYLHLDGRK EDPFDYDDNM EDSFCYRIRK SLEPYKPKWC
     KNHEDWSLYL FSPQNRLRAN CQKVIAHKMF DHIVLVFIFL NCITIALERP DIDPNSTERI
     FLSVSNYIFT AIFVAEMMVK VVALGFFSGE HTYLQSSWNV LDGILVFVSI IDIIVSMASA
     GGAKILGVLR VLRLLRTLRP LRFLWEDCMF LGEPGNGMKP GGVPLLSRVI SRAPGLKLVV
     ETLISSLRPI GNIVLICCAF FIIFGILGVQ LFKGKFYHCE GVDIRNISTK TDCRKAHYKW
     VRRKYNFDNL GQASLLPQAL MSLFVLSSKD GWVNIMYDGL DAVGIDQQVD TKYPKKFSWG
     PSRNHNLWML LYFISFLLIV SFFVLNMFVG VVVENFHKCR QHQEAEEARR REEKRLRRLE
     KKRRKAQRRP YYADYSPARK YIHSLCTSHY LDLFITFIIG VNVITMSMEH FDQPKGRSCT
     SIPFARSSMD PNKQPPPNSC VSLQSLEEAL KYCNYLFTFV FVVEAILKLV AFGFRRFFKD
     RWNQLDLAIV LLSIMGITLE EIEMNAALPI NPTIIRIMRV LRIARVLKLL KMATGMRALL
     DTVVQALPQV GNLGLLFMLL FFIYAALGVE LFGKLDCSEE NPCEGLSRHA TFNNFGMAFL
     TLFRVSTGDN WNGIMKDTLR ECHRDDKHCL SYLPVISPVY FVTFVLIAQF VLVNVVVAVL
     MKHLEESNKE AKEDAEMDAE IELEMSRGVS TPERTMDGQQ TPSKGGSPLL VKHHVMGASA
     AGLRDPQNLL TLRKISVARM HSLPNDSYMF RPVMPAKPPF PLHEGELEAF SCKSPRGSVT
     SIHSQPVVTS SLRIPQLAFR PTTPPPSHNM GAPWKLLPPR PALRTPSFSR LLCRQVSFPV
     SRCSLVGEER QKVALERAEE TKELVPNRKS EPETQQLEVL PAAAAPHPSG RPGGLKIWGP
     SLLRRCGRRP RPEPPTGASG RRQFPEFDEL YCKYCFVYGP DWAPTTVGPP SGKGIPPTGA
     TTREAWKKAS HRSRPKAGTS NKTWSGTSPS TSPSKAPTPL AVGPQIVVSV YGPDLFGNDV
     VRGYGAVHVP FTPGRHQRIL PMFVPESTSR LQKLTSWLTG RYPEFTDPKV VAQGEGREVT
     RVRSQGFVTV SFNVVTKDMK KLGYDVSSPT LASSSLTSVT DAMYKF
//
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