ID U3JF91_FICAL Unreviewed; 2322 AA.
AC U3JF91;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 24-JAN-2024, entry version 62.
DE RecName: Full=Voltage-dependent T-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1G {ECO:0000313|Ensembl:ENSFALP00000001445.2};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000001445.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000001445.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000001445.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 STRING; 59894.ENSFALP00000001445; -.
DR Ensembl; ENSFALT00000001453.2; ENSFALP00000001445.2; ENSFALG00000001356.2.
DR eggNOG; KOG2302; Eukaryota.
DR GeneTree; ENSGT00940000159664; -.
DR HOGENOM; CLU_000540_2_0_1; -.
DR Proteomes; UP000016665; Chromosome 18.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR GO; GO:0008332; F:low voltage-gated calcium channel activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
DR GO; GO:0001508; P:action potential; IEA:Ensembl.
DR GO; GO:0070509; P:calcium ion import; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0060371; P:regulation of atrial cardiac muscle cell membrane depolarization; IEA:Ensembl.
DR GO; GO:0002027; P:regulation of heart rate; IEA:Ensembl.
DR GO; GO:0010045; P:response to nickel cation; IEA:Ensembl.
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 Glycoprotein {ECO:0000256|PIRSR:PIRSR602077-3};
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:UP000016665};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..2322
FT /note="Voltage-dependent T-type calcium channel subunit
FT alpha"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5032512610"
FT TRANSMEM 42..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 665..683
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 695..716
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 786..805
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 862..885
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1204..1222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1242..1263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1339..1361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1440..1464
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1537..1556
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1568..1589
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1671..1691
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1755..1776
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..321
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 664..892
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1202..1474
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1537..1787
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 383..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1983..2009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2060..2079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2115..2164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2240..2322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1470..1500
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 391..423
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1990..2009
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2128..2164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2295..2322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 270
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 844
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1413
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ SEQUENCE 2322 AA; 260431 MW; 8BD3427866A5389F CRC64;
WFERVSMLVI LLNCVTLGMF HPCEDIACDS PRCRILQSFD DFIFAFFAVE MIVKMIALGI
FGKKCYLGDT WNRLDFFIVI AGMLEYSLDL QNVSFSAVRT VRVLRPLRAI NRVPSMRILV
TLLLDTLPML GNVLLLCFFV FFIFGIVGVQ LWAGLLRNRC FLPENFSIPY TVDLERYYQT
ENEDENPFIC SQPRENGMRY CRSIPTRREE GLECTLDYYS YNDTTNTSCV NWNQYYTNCS
AGEHNPFKGA INFDNIGYAW IAIFQVITLE GWVDIMYFVM DAHSFYNFIY FILLIIVGSF
FMINLCLVVI ATQFSETKQR ESQLMKEQRV RYLSNASTLA SFSEPGSCYD ELLKYLVYIA
RKGSKQLVKA YRAAGVRMGI LSSPSSKAGA ERHARKRRGR KRSSVHHLIH HHHHHHHHYH
LGNGNLRAPH ASPEISDVET SSLHNSTNRL MLPPSAPHSL GAPSASPSNT ESVHSIYHAD
CHFEPVRCRA SLTQPGLGLP SPEGIPKSMV GSKVYPTVHS STSHEVLKEK NLGEAAVGAG
SSTLTSLNIP PGPYSTMHKL LETQSTGPCQ SSCKISSPCT KLEGGSCTPE SCPYCLAALA
GEAELSDNET ADSDSEGVYE FTQDAHYSDQ RDPQRGRARA RRAHLVLAFW HVVCETFRKI
VDSKYFGRGI MVAILINTLS MGIEYHEQPE ELTNALEISN IVFTSLFALE MLLKVLVYGP
FGYIKNPYNI FDGIIVVISV WEIVGQQGGG LSVLRTFRLM RVLKLVRFMP ALQRQLVVLM
KTMDNVATFC MLLMLFIFIF SILGMHLFGC KFASERDGDT LPDRKNFDSL LWAIVTVFQI
LTQEDWNKVL YNGMASTSSW AALYFIALMT FGNYVLFNLL VAILVEGFQT EEISKREEAS
GQLSCIQLPV DSSGGDASKS DSEGEVFPRS LEEEGELKKN LSNPALMALS DQAELKKSLT
PPLIIHTAAT PMPMPKSAVF GDAAQGYESR RASGVSVEPV ATHELKSPPS TRSSPHSPWR
GRSSWNSRRS SWNSLGRAPS LKRRAQSGER RSLLSGEGND SSGDGDSSDE ERSSRAGSFN
GSLPQRMESL ETKGSFDLQD TLQVPSLYRS GSMHSTRTSV SEHQDCNGRT SPGLLLHQVH
LDEPPPDGDD GDDEGSMSKR DRLRAWVWAQ LPSCCKDRDS WSIYIFAPHS RFRLMCNKII
THKMFDHVVL VIIFLNCITI AMERPKIEPH SAERIFLTLS NYIFTVIFLT EMTVKVVALG
LCFGEKAYLK SSWNVLDGVL VLISVIDILV SMVSDSGTKI LGMLRVLRLL RTLRPLRVIS
RAQGLKLVVE TLMSSLKPIG NIVVICCAFF IIFGILGVQL FKGKFFVCQG EDTRNITNKS
DCTEASYKWV RHKYNFDNLG QALMSLFVLA SKDGWVDIMY DGLDAVGVDQ QPVMNYNPWM
LLYFISFLLI VAFFVLNMFV GVVVENFHKC RQHQEEEEAK RREEKRLRRL EKKRRNLMLD
DVLMESSASA VQEAQCKPYY SDYSRFRLLI HQMCTSHYLD LFITGVIGLN VITMAMEHYQ
QPKVLDEALK ICNYIFTIIF VLESVFKLIA FGFRRFFQDR WNQLDLAIVL LSIMGITLEE
IEVNASLPIN PTIIRIMRVL RIARVLKLLK MAVGMRALLD TVMQALPQVG NLGLLFMLLF
FIFAALGVEL FGDLECDDTH PCEGLGRHAT FRNFGMAFLT LFRVSTGDNW NGIMKDTLRD
CDQESTCYNT VISPIYFVSF VLTAQFVLVN VVIAVLMKHL EESNKEAKEE AELEAELEME
MKTISPGQHS PSDIFTWTGT SGGERPESPR GFTNPMQIKV DSQLSLAYHM ERHLFDTISL
MIQESLEGEL KLMDNLSGSV CHHYALPAPE YYNSENQIPL AEMEALSLTS DILSEKSWSL
ALTDDSFPDD INTLLLNALE SNVHTLVTVY KDLLSVRKPS VGRTHSLPND SYMFQPYSSP
FPASLGDRKP AHHTSQSGSK VSVQSQPADT SSLLQIPKDH FHPVRAHVVG ESKPRVSQQV
HSPSAERLLR RQMAMRNDSL DSKENLHTEE ESPVALAPSE ENELAAWSRA SVHTQQHSHN
QYNISKQAPA SCACADSYQE TPEDSMDQEV SEINSSSEPF TSETCTASSA CSEGQPLTPQ
RNMGNTGNVV LKDLKKCHSV DTQGLLKKLP SWLDDQRRHS IEICSIENSP QHYSTSSSSG
FISQVVSEME CLQGTRQKKK LSPPCISIDP PDGQSLVPRG PHSISPASGD VCLRRRAPSC
ESKDSMDIGD SLLPDSMSAS PTPKKDLLTF PSFSFDQTET DS
//
