ID A0A3P9MVL7_POERE Unreviewed; 2365 AA.
AC A0A3P9MVL7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Voltage-dependent T-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1G {ECO:0000313|Ensembl:ENSPREP00000001351.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000001351.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000001351.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000001351.1};
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 Ensembl; ENSPRET00000001391.1; ENSPREP00000001351.1; ENSPREG00000000913.1.
DR GeneTree; ENSGT00940000159664; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000000913; Expressed in caudal fin and 1 other cell type or tissue.
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:UP000242638};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..2365
FT /note="Voltage-dependent T-type calcium channel subunit
FT alpha"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018239908"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 252..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 280..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 694..712
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 724..745
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 815..834
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 891..914
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1253..1271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1291..1312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1324..1343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1388..1410
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1448..1469
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1489..1513
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1586..1603
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1623..1642
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1721..1745
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1757..1775
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1805..1826
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..316
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 693..921
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1251..1523
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1586..1837
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 379..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1153..1203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1868..1904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1963..2062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2123..2156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2230..2365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1826..1854
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 390..406
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1068
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1888..1904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1963..2054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2236..2259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2338..2365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 265
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 873
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1462
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 2365 AA; 263286 MW; 66E5428ABDBA6469 CRC64;
MLVILLNCVT LGMFHPCEDI NCDSERCKIL QDFDDFIFAF FAIEMVIKMV ALGIFGKKCY
LGDTWNRLDF FIVLAGMLEY SLNLQNVSFS AVRTVRVLRP LRAINRVPSM RILVTLLLDT
LPMLGNVLLL CFFVFFIFGI VGVQLWAGLL RNRCFVKDNF SFPLSVELGK YYHTENDDEN
PFICSMPRDN GMRDCGSIPK LYDEAGQQCS LDIDSYNSTD NTTCVNWNQY YTNCSAGLIN
PFKGAINFDN ICYAWIAIFQ VITLEGWVDI MYFVMDAHSF YNFIYFILLI IIGSFFMINL
CLVVIATQFS ETKQRESQLM KEQRVRFMSN ASTLASLSEP GSCYDELLKY LVHIIRKGAK
QVAHVCRFLA RRAGLNIASS PPATEPTHSQ RQKRRRKSSR QGSMSVHHMV HHHHYLHHHY
HLGNGSIREG GSTRCLEGRD VEAGPPKAST SVVPLGLAPP SSLIAATSDS NLAVLGNLTS
GAGDSSSGCG VLRGEPSHCT LFPANRGMNP VAFLAPTPTS RAMKRNSVPF AAPGPKNYPT
LQARALAESR RGSITASTLT NLSYNLNIPP MHLDRRPSSL VDTRTPTAQL SCQLSARELI
TMDAAGLTMD PETCPDCAKA LAHELEGFTE GNETPGDSDS DGVYELSQDH HHRDRRDSRQ
PRKKSRRLGK TAANVVHFWR LVCDTFRKIV DSKYFGRGIM IAILINTLSM GIEYHEQPEE
LTNALEISNI VFTSLFSLEM LLKVLVYGPF GYIKNPYNIF DGIIVVISVW EIVGQQGGGL
SVLRTFRLMR VLKLVRFMPA LQRQLVVLMK TMDNVATFCM LLMLFIFIFS ILGMHLFGCK
FGSERDGDTL PDRKNFDSLL WAIVTVFQIL TQEDWNKVLY NGMASTSPVA ALYFIALMTF
GNYVLFNLLV AILVEGFQTE EISKREDLHA QLSLIQLPVD SGGDASKTGS EIDSVARSME
DVNGSKKDLS PSTVVPVNGH VEMKTSLTPP LITHTAATPM PVPKLPVAGD PILGYESRQG
SNISMDPACF DKSPTSARSS PHGQWTTGSG WGSRRSSWNS LSRAPSYKRQ KRQSGERRSL
LSGEGNSSSD EGDGGGEGGG GLVDEDDTSL PRTDSMSQPH GGPRHRRMES VETRSSMDLP
PEALLQVPYL HRSASMHSSR PPSLAHLRPP EHSDCNGKGT PSALGPTNVS LEENTEDENA
EEEVNQSRFA RILRWMEKKQ PAWCRQRDTW SLYLFPPESR FRILCNKIIT HKMFDHVVLV
IIFLNCITIA MERPRIHPTS AERIFLTFSN YIFTAIFVAE MTVKIAAMGF FFGDKAYLRS
SWNILDGMLV MISVIDILVS LISNTGTKIL GMLRVLRLLR TLRPLRVISR APGLKLVVET
LMSSLKPIGN IVVICCAFFI IFGILGVQLF KGKFYVCQGE DVRNITNRTD CEGAHYKWVR
HKYNFDNLGQ ALMSLFVLAS KDGWVDIMYD GLDAVGVDQQ PIMNYNPWML LYFISFLLIV
AFFVLNMFVG VVVENFHKCR RHQEAEEAKR REEKRLKRME KKRRNLLVPG VSWALSDGTL
KEAQSKPYYS DYSPTRLLIH KMCTSHYLDL FITIVIGLNV ITMSMEHYEQ PQELDNALKI
CNYIFTLIFV LESVFKLVAF GFRRFFKDKW NQLDLAIVLL SIMGITLEEI EVNASLPINP
TIIRIMRVLR IARVLKLLKM AVGMRALLDT VMQALPQVGN LGLLFMLLFF IFAALGVELF
GDLICDELHP CEGLGRYATF RNFGMAFLLL FRVSTGDNWN GIMKDTLRDC AHETGTCYNT
VVSPIYFVSF VLTAQFVLVN VVIAVLMKHL EESNKEAKEE AELEAELKLE LQMEGADMAP
RSPQLNPLAL GMDRSSSGGS PWRSAGGGDM EQEREGPMDS PTADITRDSV DIRAEPPAYP
EPQLELEAPK ANLLSVRKPA VGRTHSLPND SYMFFPLHPF GSSSPSPAQL VAQSQGPQHL
VGTHRAQSGS RGSVRSQPEE CSQQLTVPTD IFRPISPHSH SDSESIPRQP PSRRTHALSR
TLRRQVAVST DSQEALCSDE RESREGLLNV AALGLPPSTS PSHQHHHPHL HPALCLVPAT
PGAFPKPSSV HTQQHDQHCL ASYSSSALPS TSSHPLPPPL PARPQQQQQE EVEAVSEDRE
VSLIICGGLV GSDSVTVEDT VCQDSRSPCT RQLKRFHSVD TQGRSTLLPR PRPYSWLDDP
RRHSVEVYPA EDPCPQRSAA STSSGFVSRS DSLQIPTQAP LPSPRRKKKM SPPCISVDPP
DELEPQSGLY PSLSGMGLAG LGVPPPLPSR DTCLRRRAPS SDSKDSFDLG VGEGSGQDGG
SPNPNPSSKL LTLPSFSFEK TSSEH
//
