ID A0A267G578_9PLAT Unreviewed; 1899 AA.
AC A0A267G578;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Voltage-dependent T-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN ORFNames=BOX15_Mlig033357g1 {ECO:0000313|EMBL:PAA81183.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA81183.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA81183.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA81183.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA81183.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:PAA81183.1}.
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DR EMBL; NIVC01000544; PAA81183.1; -; Genomic_DNA.
DR STRING; 282301.A0A267G578; -.
DR Proteomes; UP000215902; Unassembled WGS sequence.
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:SF230; CA[2+]-CHANNEL PROTEIN ALPHA[[1]] SUBUNIT T, ISOFORM F; 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:UP000215902};
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 189..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 341..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 760..782
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 836..860
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1179..1197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1218..1238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1250..1270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1317..1336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1416..1440
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1497..1520
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1532..1552
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1630..1650
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1719..1741
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 70..350
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 637..869
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1178..1450
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1495..1746
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 473..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1017..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1765..1789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 976..1003
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1449..1476
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 516..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..913
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1056
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 819
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1389
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 1899 AA; 214357 MW; 1EDD4E7A036F2412 CRC64;
MHQSSGDVIE EAWSPAASGC GVAMETDDAS PEIEVRAEEE IPYPGFYPIV LRYLHQRHPV
RAWCLRVITW PWFERVSMLV ILVNCVTLGM YQPCTDEQCV TTRCQVLHGF DHAVFAFFAC
ELAAKVCAMG LWGQLAYLGD SWNRLDFFIV IAGLLEYLPQ TKDLSLTAIR AIRVLRPLRA
INRIPSMRIL VMLLLDTLPM LGNVLLLCFF VFFIFGIIGV QLWKGVLRNR CFLGINDTIA
HPGLNLTEYY QLNSSVDSLV APKDFICTLN DANGIQTCDQ INPTVMWLST ESYMVCNRTA
DPFGDNLPTN DSCVNWNQYY SVCNASVSNP YMGSINFDNI GFAWVAIFQI GSFFMINLCL
VVIATQFSET KKREVEKMLQ ERKRFKSTSS LPSSADPGSC YGQIVKLLIR QVRRLRRGLR
RRYQEFQRQR GANATVVSAT AVLEAGETMT AGGRPPLYRF GCRECQQRNE AVTFRQQLSP
PRASPEVSSD FVDEESTSAS AASAAVATAR RVSLQPPPHL QTHQALSVND AQGSRRSSWN
NSDCRCRRNE SARSSLNCRS LLAGYRESDL FPGWRLAHWS SISSSIAARE MTAAAPQTEK
LLGRLSRAPL GRLRSSGNLL TSFWKTIRRQ VKQLIDHRFF QRGILIAILI NTMSMGIEFH
NQPQTLTDII EYSNVFFCGV FALEMLLKLL GDGLIDYVSS GFNVFDASIV ILSGFELLQG
HGSGLSVLRT FRLLRILKLV RFLPALRQQL FVMLKTMDNV ATFFALLVLF IFIFSILGMS
LFGCQFCGTT PRGNYRCARQ NFDTLLWATV TVFQILTQED WNTVLYNGMA RTSPWAALYF
IALMTFGNYV LFNLLVAILV EGFSSEKAAS SVQLNSVHGA DSGLGPGSDA EDAEDGEPPD
TVELSKRRLP SRLFDEPSAA AGRPDQQQQQ PQPPSSALIP PIITHTAATP QPTPPQGSPA
IEATFAAAET AVAKYRATET AELLQQQQQL QQQQQQKQQL DLSSAFRFSS TSIASIDRSL
SQNDKSVSEG SPVRKVRSTS QGESFYSGSC NGNPASPLPP TCGPNGRIFR PVTPQSLSGR
QPPGQSQHRR GSFSGSYRTV TPQDSISSCW NKAEQADALP TGSVRCQDKR DDAFWPPWLA
RWLPAPHGCF KERENYALYL LGPDNRLRIL CQRIVTLKSF DYTVLFFIAL NCITLAMERP
SIPLDSIERQ FLRISNNIFT WIFTVEMSLK VAAKGLVLGQ HAYLKSGWNI MDGALVAVSL
IDALITLIAG SSNRIFGILR VFRLLRTLRP LRVISRAPGL KLVVQTLLSS LRPIGNIVLI
CCTFFIIFGI LGVQLFKGKF YYCDGPDVSN VMNITDCLAD KRNKWIKHKY NFDNLGQALM
ALFVLSSKDG WVQIMYTGLD AVGENMQPKE NHNEWLLLYF ISFLLLVGFF VLNMFVGVVV
ENFHKCRASQ EKEEKARRAA KRARRMEKRR KRIRERPYWS SYPPWRLRIH KLVDSKYFDL
VIATIIGLNV ITMAMEFYLM PKELELGLKA TNYFFTTVFI IEAAFKIIAL GFKRYFMDRW
NQLDVIIVIL SVSGIVLEEM EAKIIPINPT IIRVMRVLRI ARVLKLLKMA KGIRALLDTV
IQALPQVGNL GLLFFLLFFI FAALGVELFG RLECSLDNPC VGLSRHAHFE NFGMAFLTLF
RIATGDNWNG IMKDTLREKC DWSDDCIKNC CVSPIIAPIY FVVFVLMAQF VLVNVVVAVL
MKHLEESHKM MSDDEELEKE IRRELEEENR ENQRQMERQE RERKESQESL SAYAFDEQQQ
QKQQPQLQTF LVEHESNQVT SPIIQSCRIS CSDRLIERRL SSIYDRQNSL SADSSSADKK
RRRYSEIRLG AFEVAPDTND DELSLSHLKA LDTRPVTDL
//
