ID I3KUE7_ORENI Unreviewed; 2253 AA.
AC I3KUE7;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 24-JAN-2024, entry version 58.
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:ENSONIP00000024743.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Ensembl:ENSONIP00000024743.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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; ENSONIT00000024764.2; ENSONIP00000024743.2; ENSONIG00000019655.2.
DR GeneTree; ENSGT00940000159664; -.
DR HOGENOM; CLU_000540_2_0_1; -.
DR Proteomes; UP000005207; 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: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 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 107..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 367..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 395..420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 777..795
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 807..828
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 898..917
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 974..997
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1004..1027
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1211..1229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1249..1270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1282..1300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1349..1368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1448..1471
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1547..1564
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1584..1603
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1682..1706
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1766..1787
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 115..431
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 776..1002
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1209..1481
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1547..1798
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1481..1502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2007..2034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2176..2236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1787..1821
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 505..539
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2007..2029
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2222..2236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 380
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 956
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1420
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 2253 AA; 251295 MW; 530BD355D3DE569C CRC64;
MAEDGGNLSG VPDAGASEGR SSLPRTFIRL NDLSGLGTGG GEHGEVSAVE PASPAPDGIS
AAGEEMSASG GDSLPYPTLA PVVFFYLKQT TRPRSWCLKM VCNPYPFLFL LTQPSMLVIL
LNCVTLGMFH PCEDINCDSE RCKILQDFDD FIFAFFAIEM VIKMVALGNF GKKCYLGDTW
NRLDFFIVLA GMLEYSLNLQ NVSLSAVRTV RVLRPLRAIN RVPSMRILVT LLLDTLPMLG
NVLLLCFFVF FIFGIVGVQL WSGLLRNRCF VEDNFSFPLS VERGKYYHTE NDDENPFICS
QPRENGMRDC SSIPKLYEEG GLECTLDIDS YNSTDNTTCV NWNQYYTNCS AGLINPFKGA
INFDNICYAW IAIFQVITLE GWVDIMYFVM DAHSFYNFIY FILLIIIGSF FMINLCLVVI
ATQFSETKQR ESQLMKEQRV RFMSNASTLA SLSEPGSCYD ELLKYLVHII RKGAKQVAHI
CRLLARRAGL HIAASPPATD IQRSHSQRRR RKTSRQGSVS VHHIMHHHHQ HHHHHYHLGN
GSVRGGGSTR CLDSREIEAT SDMNLAILSS PAADSSSVCS VLNTNSGIAP GFFSLAPAPK
SRAIKRNSVP FAAPGPKNYP TLQARALAES RRGSIAASTL TNINLNIPPM PQDRRPSSLV
DPLSPTAQLS CQLSARDLST TSSAMDTAAL TLDPESCPYC AKALANESEG GTEGNETPGD
SDSDGVYEFT QDLHHRDRRD SRQPKKKHRR LGKTAAKVVH FWRLVCDTFR KIVDSKYFGR
GIMIAILINT LSMGIEYHEQ PEELTNALEI SNIVFTSLFS LEMLLKVLVY GPFGYIKNPY
NIFDGIIVVI SVWEIVGQQG GGLSVLRTFR LMRVLKLVRF MPALQRQLVV LMKTMDNVAT
FCMLLMLFIF IFSILGMHLF GCKFGSERDG DTLPDRKNFD SLLWAIVTVF QILTQEDWNK
VLYNGMASTS PVAALYFIAL MTFGNYVLFN LLVAILVEGF QAEFINFTTV KCCFCPLFSF
TFLLLVVPVN GHVDLKSNLT PPLITHTAAT PMPVPKLPVG GESNPGYESR RGSSSSVDPA
CYDKSPTSVR SSSPYAPWSS GSGRTSRRSS WNSLGRAPSY KRQKRQSGER RSLLSGEGGS
SSEDGEGGGE GGGGLMEEDD ASLARTDSML LRWLEKKQPA WCKQRDTWSL YLFPSESRFR
ILCNKIITHK MFDHVVLVII FLNCITIAME RPRIDSKSAE RVFLTVSNYI FTSIFVAEMT
VKIVSMGFFF GDKAYLRSSW NVLDGMLVMI SVIDILVSLI SQSETKILGM LRVLRLLRTL
RPLRVISRAP GLKLVVETLM SSLKPIGNIV VICCAFFIIF GILGVQLFKG KFFICQGEDV
RNITNKSDCL QANYKWVRHK YNFDNLGQAL MSLFVLASKD GWVDIMYDGL DAVGVDQQPI
MNYNPWMLLY FISFLLIVAF FVLNMFVGVV VENFHKCRRH QEAEEAKRRE EKRLKRMEKK
RRSKEKDLVV TCSGSVESAA DCGAQSKPYY SDYSPTRLLI HKMCTSHYLD LFITIVIGLN
VITMSMEHYQ QPKELDEALK ICNYIFTLIF VLESVFKLVA FGFRRFFKDK WNQLDLAIVL
LSIMGITLEE IEVNASLPIN PTIIRIMRVL RIARVLKLLK MAVGMRALLD TVMQALPQVG
NLGLLFMLLF FIFAALGVEL FGDLICDELH PCEGLGRYAT FKNFGMAFLL LFRVSTGDNW
NGIMKDTLRD CAQDTGTCYN TVVSPIYFVS FVLTAQFVLV NVVIAVLMKH LEESNKEAKE
EAELEAEMME LEMEAGDMAA RSPQLNPLTL GMDRALFDSV SLVIQGSMEG EMSLMDNLSG
SICHYYALPP KPSKHSTDKK IPLAEMDALS LASENSWSLA LTDDSTPDDF NPLFLTTLEC
NVLTVPLFIL LHCYFFSFPS AVACTVSFTG YFQSHLTLPT TKLTHWGLTR GSQLDHCALC
AGSSGSVRSQ PAEFSQQLTV PTDLFRPISP HSHSDSESIP RNPPSRRTHT FSRTLRRQVS
KTHRFRFPLD SKFTFLVLSC LHCLASYSPC PSPPPPIPAR PPQQEVSEDR EVSLINQVVL
AGSDDITAED SSSGGGNKGY GSYAGCQESR SPCLRQLKRF HSADTQGRNA LLPRPRPYSW
LDDPRRHSVE VCSPIQSQIP AQTSPRMPPP LPNRDTYLRR RAPSSDSKDS FDLAVGEGSG
QDGGSPNPNT NSKLLTLPMT SAPGLLAPTA VAI
//