ID A0A1S3K4F9_LINUN Unreviewed; 2516 AA.
AC A0A1S3K4F9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Voltage-dependent T-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=LOC106178756 {ECO:0000313|RefSeq:XP_013417523.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013417523.1};
RN [1] {ECO:0000313|RefSeq:XP_013417523.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013417523.1};
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_013417523.1; XM_013562069.1.
DR EnsemblMetazoa; XM_013562069.1; XP_013417523.1; LOC106178756.
DR GeneID; 106178756; -.
DR OrthoDB; 1110761at2759; -.
DR Proteomes; UP000085678; 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: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:UP000085678};
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 138..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 233..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 358..376
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 396..418
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 715..733
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 745..766
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 778..798
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 836..858
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 925..948
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1401..1419
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1439..1455
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1476..1498
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1536..1558
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1640..1663
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1743..1765
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1777..1799
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1811..1831
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1876..1895
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1965..1987
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 95..429
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 715..958
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1400..1672
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1741..1994
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1142..1350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2014..2037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2147..2180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2208..2516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1666..1693
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..687
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2247..2265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2266..2287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2312..2341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2391..2451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2452..2481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2482..2508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 378
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 907
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1612
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 2516 AA; 283148 MW; 4219BDAF88E0D84C CRC64;
MSTTNTPSTS NGDTKYTVAP TKEEPGSWST SSQNNLDEQS SEKEKNIVKC VIEDAEDSSE
EEEEELPYPG FIPTTLYCLK QTTWPRTWCL KLLTWSWFER TSMMVILLNC VTLGMYQPCV
DGNCDTTRCK VLEGFDHFIF AFFAVEMVIK IIAMGFFGKM TYLADTWNRL DCFIVLAGIT
ELVFFNAIEY SIDTEEISIT AIRTVRVLRP LRAINRIPSM RILVMLLLDT LPMLGNVLLL
CFFVFFIFGI VGVQLWAGLL RNRCFLSLNY SYLPENFTAP VPKYYKPAGG GDYVCAKPDS
NGLMSCDKLP PFELEGEICN SSLLSYGNMT TANDSSCINW NQYYTDCKSR GENPFQGAIS
FDNIGLAWVA IFQVISLEGW VDIMYYIQNS HSFWDWIYFV ALIVIGSFFM INLCLVVIAT
QFSETKKRET ERMNKERKRY QSSSTLASSS EPGGCYDEIL KYIGHLFRKG KRRFIRKCCS
VYANRQKKVI PEKSISLKKK RKKKTLHLHH HHHYHHHYHI NSSPTTAVVA PRASPETSVI
DPISSPRRPN HLQLPSNNNS LNPSTESLQN PTLIAPYDPL MTSKNCQSSP NHVVVSISPA
PSMNSSCSVP CSDVLATKSK LTPEYDVNRL SPYHAFEKGD KMSPRLTATS ADFDCRHSNC
SYSEYEWTDS DDSGKEWDED EESEEEEENK KQTSMIKSCW IKFRQKIKVF VESDYFTWGI
MGLIFVNTCS MGVEYHNQPD SLTIALEYCN IVFTALFALE MLLKIIAEGV LGYVKNGFNV
FDAVIVIMSI VEIAYGGASG LSVLRTFRLL RVLKLVRFMP ALRRQLVVML RTMDNVATFI
LLLLLFMFIF SILGMTLFGG KFCSREDGTQ CTCSDIVNPE IICNCERMNF DTTIWAMVTV
FQILTQEDWN QVLYNGMEKT SPWAALYFIA LMTFGNYVLF NLLVAILVEG FSADSEEKKK
EQVKKAKEEE KEEAKRKDKL SDVNGNTECE VDIKNNKEKA KLLCTSTSAW CNIKEGNLSK
GTPCLSCGSS PSLALPIITH TVPTPLPSRP NSPTHQDFVS SLTAKMLALP PPAVSVTKED
PCCQHPEAPK YPPPIITHTA ATPAATPAAT PHGSPHEISC KDNNKLSVKD AFNLSSSSIE
TIDRTSNGSL SSRSSPRLCT STTPKLVRRT SSKSSQRSWK FRNEPKEDEA NLVGQSDSSD
QSDAEDIFSK NSLKPAGPVA PPSPSPSQSD CNGHAPLNNQ RPLTPRNSVK SNHSISPQNS
IKGNRRLEPK NSFTENHSRQ NSLNSNKSNA TRCNSFHHRQ ENSAHSHKTL SPQVSIGSVT
PIEDYKQNNL NRTQDSQAEP KEEEDCLDEA DPDAMDETDW SCSWCPEPKG CFKERWEWSL
FLLSPHNKFR ILLHHLVAKN WFDYTVLFFI ALNCITLAME RPSIPPDSVE RQFLTCSNYV
FTAVFAFEMT VKVLAKGFMF GTHCYLKSGW NVMDGFLVFI SLLDIIIANT ATSSPRIFGI
LRVFRLLRTL RPLRVISRAP GLKLVVETLL SSLRPIGNIV LICCTFFIIF GILGVQLFKG
TFYHCRGPDV SDVKNRTMCE AKGREYKWMN HRYNFDNLGQ ALMALFVLSS KDGWVSIMYT
GLDAVGVDQQ PIENYSEWRI VYFISFLLLV AFFVLNMFVG VVVENFHKCR ADLEEEERAR
REAKRARKLE KKRKTEATND AAVIMPNAFL QPLLQKLEVA EVSYWLDYSK PRLLVHTVVN
SKYFDLAIAA VIGLNVVTMA MEFYLMPAEL AFALKIFNYF FTSVFVIEAS LKIAATGFVR
YIRDSWNQLD MFIVILSIVG IALEEMESGL IPINPTIIRV MRVLRIARVL KLLKMAKGIR
ALLDTVIQAL PQVGNLALLF FLLFFIFAAL GVELFGRLEC SREHPCEGLS EHASFKDFGI
AFLTLFRVAT GDNWNGIMKD TLREDCDDSA DCEINCCVSQ VIAPIYFVIF VLMAQFVLVN
VVVAVLMKHL EESNKLAVED AEIEKEIENE LKDEHIKKKE GDEKECPSDV KDENPDKEEC
VRQRNKVRKQ YSLPSNFTYH QSGSPRETKV VYVQSGKYYE CVTTPVGKDE DRNRDSVSLK
ILDKPTIAAL TSNRRKFPKS DIPSVLYLPS SSKNQEPEIL LSRSCSEKLK PTSSPKHLPT
PLTPHVPIRD SRRWKPEHAQ RKISPMTLCS SVPNVMLAKT IEIAYPEPVD PLYGSQPVLR
RCPGSGEKPP TSGAAQSKPN SKEKSVPPIG DIKENSERQQ IKDAKTSSIC DHSQPPQDQQ
PQQSVEIWTD DEGCDEEVRQ ITGLSTSQED EDAQPTFDRA RDSMTEIETI ENPKHSNTDG
KDSGNTDSLR PLNPPLQKPI PNRPSSRRLL HSKANVDLPS PPAFLNEHIK DPSITINSDK
NVNDSLNTKS DCANTESEPL NTKSDSVDIK SDPVNSKSDS ANAVSHSVNT SSDSDDKTKD
PVEANYDAST ERSDGQTDME TKNKETNATS VKIQIPQSNQ QNNGPIHIVP INESEV
//
