ID I3J182_ORENI Unreviewed; 1580 AA.
AC I3J182;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Voltage-dependent T-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000002622.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000002622.2}
RP IDENTIFICATION.
RG Ensembl;
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 Ensembl; ENSONIT00000002623.2; ENSONIP00000002622.2; ENSONIG00000002104.2.
DR GeneTree; ENSGT00940000158594; -.
DR HOGENOM; CLU_000540_2_0_1; -.
DR Proteomes; UP000005207; Linkage group LG4.
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:SF209; 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};
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:UP000005207};
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 120..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 355..377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 383..408
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 627..645
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 657..683
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 748..770
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 825..848
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 981..1002
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1014..1038
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1076..1098
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1177..1201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1262..1279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1299..1318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1382..1409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1489..1510
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 79..419
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 626..854
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 941..1211
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1262..1520
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1212..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 368
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 807
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 1580 AA; 179483 MW; B462E5C786C52F60 CRC64;
MTSEECPVPL GSISSAGPGQ NEEYSSAQAD DIIEEMGPGD DVSIGSDLST LVVPFPELAP
VVFFCLKQTT CPRNCLVNTW FERISIMVIL LNCVTLGMYQ PCENIDCTSD RCQILQAFDA
FIYIFFALEM VVKMVALGIF GRRCYLGDTW NRLDFFIVMA GMVEYSLDLQ NINLSAIRTV
RVLRPLKAIN RVPSMRILVN LLLDTLPMLG NVLLLCFFVF FIFGIIGVQL WAGLLRNRCY
PEENFTVPSG MTLPAPYYRP EEDDERPFIC SLASDNGIMS CTDVPARREG GRICCLDKED
ALHRQALGLS PEPLANSSGA GEAIGLCINW NQYYTRCHTG NTNPHKGAIN FDNIVYAWIV
IFQVITLEGW VEIMYYVMDA HSFYNFIYFI LLIIIGSFFM INLCLVVIAT QFSETKQREH
QLMQEQRAQC LSSSTLASMA EPGDCYEEIF QLVCHVLRKA KRRSAALYYT LRGKPPPAGG
GRGNRRGGGN VNGERHHLRH PRYCIHIFYF PCHSVSAVSV AFHCPHQNKQ DHDSQPLANS
ISLSVPQNPE DCPICALSLK EGVRAVGDSA NGEENEEDAV KETSKEENHL EERGDGERKR
KRTCFGHCKD LWNGMRRKLW GIVESKYFSR GIMIAILINT ISMGIEHHNQ PEELTNVLEI
CNIVFTSMFT LEMILKLTAF GFFEYLRNPY NIFDGIIVII SVCEIIGQAD GGLSVLRTFR
LLRVIKLVRF MPALRRQLVV LMKTMDNVAT FCMLLMLFIF IFSILGMHIF GCKFSLKTEA
GDTVPDRKNF DSLLWAIVTV FQILTQEDWN MVLYNGMAST SPCAALYFVA LMTFGNYVLF
NLLVAILVEG FQAEGDANRS YSDDDRSSCN FDDSDKQKDS LHLSGECYLP QLHCIFFLCF
RIQKMLEAYR PDWCETREDW SVFLFSPQNK FRQICQSIIA HKLFDYVVLA FIFSNCITVA
LERPKILQGS LERVFLTISN YIFTAIFVGE MTLKVVSMGL YMGEQAYLRS SWNILDGFLV
FVSLIDIVVS MAGGAKILGV LRVLRLLRTL RPLRVISRAP GLKLVVETLI TSLKPIGNIV
LICCAFFIIF GILGVQLFKG KFFYCLGPDV KNITNKSDCL QANYKWVHHK YNFDNLGQAL
MSLFVLASKD GWVNIMYHGL DAVGVDQQPI TNNNPWMLLY FISFLLIVSF FVLNMFVGVV
VENFHKCRQH QEVEEAKRRE EKRQRRMEKK RRTVPNPRAQ KLPYYASYGN MRLMIHTLCT
NHYLDLIITF IICINVITMS LEHYNQPHSL DLALKYCNYF FTSMFVLEAV LKLIAFGVRR
FFKDRWNQLD LAIVLLSVMG ITLEEIEISA ALPINPTIIR IMRVLRIARV LKLLKMATGM
RALLDTVVQA LPQVGNLGLL FMLLFFIYAA LGVELFGELV CNEDYPCEGM SRHATFENFG
MAFLTLFQVS TGDNWNGIMK DTLRECPPDH GTDVDYACNP SLQFISPMYF VSFVLTAQFV
LINVVVAVLM KHLDDSNKEA QEEAEMDAEI ELELAQGTLC CMGAQRGQET EDVCDMQSLL
RTRDHITPVT PARLCTHQHK
//
