CAC1G_HUMAN
ID CAC1G_HUMAN Reviewed; 2377 AA.
AC O43497; D6RA64; E7EPR0; O43498; O94770; Q19QY8; Q19QY9; Q19QZ0; Q19QZ1;
AC Q19QZ2; Q19QZ3; Q19QZ4; Q19QZ5; Q19QZ6; Q19QZ7; Q19QZ8; Q19QZ9; Q19R00;
AC Q19R01; Q19R02; Q19R03; Q19R04; Q19R05; Q19R06; Q19R07; Q19R08; Q19R09;
AC Q19R10; Q19R11; Q19R12; Q19R13; Q19R15; Q19R16; Q19R17; Q19R18; Q2TAC4;
AC Q9NYU4; Q9NYU5; Q9NYU6; Q9NYU7; Q9NYU8; Q9NYU9; Q9NYV0; Q9NYV1; Q9UHN9;
AC Q9UHP0; Q9ULU6; Q9UNG7; Q9Y5T2; Q9Y5T3;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Voltage-dependent T-type calcium channel subunit alpha-1G;
DE AltName: Full=Cav3.1c;
DE AltName: Full=NBR13;
DE AltName: Full=Voltage-gated calcium channel subunit alpha Cav3.1;
GN Name=CACNA1G; Synonyms=KIAA1123;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND GENE STRUCTURE.
RC TISSUE=Prostatic carcinoma;
RX PubMed=10493502;
RA Toyota M., Ho C., Ohe-Toyota M., Baylin S.B., Issa J.-P.J.;
RT "Inactivation of CACNA1G, a T-type calcium channel gene, by aberrant
RT methylation of its 5' CpG island in human tumors.";
RL Cancer Res. 59:4535-4541(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING (ISOFORMS 4 AND 5).
RC TISSUE=Brain;
RX PubMed=10548410; DOI=10.1016/s0304-3940(99)00716-8;
RA Mittman S., Guo J., Agnew W.S.;
RT "Structure and alternative splicing of the gene encoding alpha1G, a human
RT brain T calcium channel alpha1 subunit.";
RL Neurosci. Lett. 274:143-146(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=10648811; DOI=10.1016/s0014-5793(99)01756-1;
RA Cribbs L.L., Gomora J.C., Daud A.N., Lee J.-H., Perez-Reyes E.;
RT "Molecular cloning and functional expression of ca(v)3.1c, a T-type calcium
RT channel from human brain.";
RL FEBS Lett. 466:54-58(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING (ISOFORMS 1-2 AND 6-13),
RP AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=10692398; DOI=10.1074/jbc.275.9.6090;
RA Monteil A., Chemin J., Bourinet E., Mennessier G., Lory P., Nargeot J.;
RT "Molecular and functional properties of the human alpha1G subunit that
RT forms T-type calcium channels.";
RL J. Biol. Chem. 275:6090-6100(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4; 6; 7; 8; 9; 11; 12; 13; 14;
RP 15; 16; 17; 18; 19; 20; 21; 22; 23; 24; 25; 26; 27; 28; 29; 30; 31; 33; 34
RP AND 35), AND DEVELOPMENTAL STAGE.
RC TISSUE=Brain, and Fetal brain;
RX PubMed=16671074; DOI=10.1002/prot.20877;
RA Emerick M.C., Stein R., Kunze R., McNulty M.M., Regan M.R., Hanck D.A.,
RA Agnew W.S.;
RT "Profiling the array of Ca(v)3.1 variants from the human T-type calcium
RT channel gene CACNA1G: alternative structures, developmental expression, and
RT biophysical variations.";
RL Proteins 64:320-342(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 550-2377 (ISOFORM 13).
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [9]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1126-1444; 1778-1927 AND 2021-2312.
RC TISSUE=Brain;
RX PubMed=9495342; DOI=10.1038/36110;
RA Perez-Reyes E., Cribbs L.L., Daud A., Lacerda A.E., Barclay J.,
RA Williamson M.P., Fox M., Rees M., Lee J.-H.;
RT "Molecular characterization of a neuronal low-voltage-activated T-type
RT calcium channel.";
RL Nature 391:896-900(1998).
RN [11]
RP INVOLVEMENT IN SCA42, VARIANT SCA42 HIS-1715, CHARACTERIZATION OF VARIANT
RP SCA42 HIS-1715, AND FUNCTION.
RX PubMed=26456284; DOI=10.1016/j.ajhg.2015.09.007;
RA Coutelier M., Blesneac I., Monteil A., Monin M.L., Ando K., Mundwiller E.,
RA Brusco A., Le Ber I., Anheim M., Castrioto A., Duyckaerts C., Brice A.,
RA Durr A., Lory P., Stevanin G.;
RT "A recurrent mutation in CACNA1G alters Cav3.1 T-type calcium-channel
RT conduction and causes autosomal-dominant cerebellar ataxia.";
RL Am. J. Hum. Genet. 97:726-737(2015).
RN [12]
RP INVOLVEMENT IN SCA42, VARIANT SCA42 HIS-1715, CHARACTERIZATION OF VARIANT
RP SCA42 HIS-1715, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26715324; DOI=10.1186/s13041-015-0180-4;
RA Morino H., Matsuda Y., Muguruma K., Miyamoto R., Ohsawa R., Ohtake T.,
RA Otobe R., Watanabe M., Maruyama H., Hashimoto K., Kawakami H.;
RT "A mutation in the low voltage-gated calcium channel CACNA1G alters the
RT physiological properties of the channel, causing spinocerebellar ataxia.";
RL Mol. Brain 8:89-89(2015).
RN [13]
RP INVOLVEMENT IN SCA42ND, FUNCTION, VARIANTS SCA42ND THR-961 AND VAL-1531,
RP AND CHARACTERIZATION OF VARIANTS SCA42ND THR-961 AND VAL-1531.
RX PubMed=29878067; DOI=10.1093/brain/awy145;
RA Chemin J., Siquier-Pernet K., Nicouleau M., Barcia G., Ahmad A.,
RA Medina-Cano D., Hanein S., Altin N., Hubert L., Bole-Feysot C., Fourage C.,
RA Nitschke P., Thevenon J., Rio M., Blanc P., Vidal C., Bahi-Buisson N.,
RA Desguerre I., Munnich A., Lyonnet S., Boddaert N., Fassi E., Shinawi M.,
RA Zimmerman H., Amiel J., Faivre L., Colleaux L., Lory P., Cantagrel V.;
RT "De novo mutation screening in childhood-onset cerebellar atrophy
RT identifies gain-of-function mutations in the CACNA1G calcium channel
RT gene.";
RL Brain 141:1998-2013(2018).
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. The isoform alpha-1G gives rise to T-type
CC calcium currents. T-type calcium channels belong to the 'low-voltage
CC activated (LVA)' group and are strongly blocked by mibefradil. A
CC particularity of this type of channel 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:0000269|PubMed:10648811,
CC ECO:0000269|PubMed:10692398, ECO:0000269|PubMed:26456284,
CC ECO:0000269|PubMed:26715324, ECO:0000269|PubMed:29878067}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26715324};
CC Multi-pass membrane protein {ECO:0000255}. Cytoplasm
CC {ECO:0000269|PubMed:26715324}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=35;
CC Name=5;
CC IsoId=O43497-1; Sequence=Displayed;
CC Name=1; Synonyms=Variant 89;
CC IsoId=O43497-2; Sequence=VSP_000940, VSP_000943, VSP_000946;
CC Name=2; Synonyms=Variant 25;
CC IsoId=O43497-3; Sequence=VSP_000940, VSP_000944, VSP_000946;
CC Name=3;
CC IsoId=O43497-4; Sequence=VSP_000940;
CC Name=4; Synonyms=Variant 88;
CC IsoId=O43497-5; Sequence=VSP_000940, VSP_000943, VSP_000946,
CC VSP_000948;
CC Name=6; Synonyms=Variant 217;
CC IsoId=O43497-6; Sequence=VSP_000943, VSP_000946;
CC Name=7; Synonyms=Variant 221;
CC IsoId=O43497-7; Sequence=VSP_000943, VSP_000947;
CC Name=8; Synonyms=Variant 93;
CC IsoId=O43497-8; Sequence=VSP_000940, VSP_000943, VSP_000947;
CC Name=9; Synonyms=Variant 57;
CC IsoId=O43497-9; Sequence=VSP_000940, VSP_000946;
CC Name=10;
CC IsoId=O43497-10; Sequence=VSP_000940, VSP_000945;
CC Name=11; Synonyms=Variant 185;
CC IsoId=O43497-11; Sequence=VSP_000946;
CC Name=12; Synonyms=Variant 189;
CC IsoId=O43497-12; Sequence=VSP_000947;
CC Name=13; Synonyms=Variant 153;
CC IsoId=O43497-13; Sequence=VSP_000944, VSP_000946;
CC Name=14; Synonyms=Variant 137;
CC IsoId=O43497-15; Sequence=VSP_000944, VSP_047550, VSP_000946;
CC Name=15; Synonyms=Variant 157;
CC IsoId=O43497-16; Sequence=VSP_000944, VSP_000947;
CC Name=16; Synonyms=Variant 169;
CC IsoId=O43497-17; Sequence=VSP_047550, VSP_000946;
CC Name=17; Synonyms=Variant 184;
CC IsoId=O43497-18; Sequence=VSP_000946, VSP_000948;
CC Name=18; Synonyms=Variant 216;
CC IsoId=O43497-19; Sequence=VSP_000943, VSP_000946, VSP_000948;
CC Name=19; Synonyms=Variant 223;
CC IsoId=O43497-20; Sequence=VSP_000943;
CC Name=20; Synonyms=Variant 249;
CC IsoId=O43497-21; Sequence=VSP_047548, VSP_000946;
CC Name=21; Synonyms=Variant 313;
CC IsoId=O43497-22; Sequence=VSP_000940, VSP_047545, VSP_000946;
CC Name=22; Synonyms=Variant 409;
CC IsoId=O43497-23; Sequence=VSP_047545, VSP_000944, VSP_000946;
CC Name=23; Synonyms=Variant 441;
CC IsoId=O43497-24; Sequence=VSP_047545, VSP_000946;
CC Name=24; Synonyms=Variant 477;
CC IsoId=O43497-25; Sequence=VSP_047545, VSP_000943, VSP_000947;
CC Name=25; Synonyms=Variant 473;
CC IsoId=O43497-26; Sequence=VSP_047545, VSP_000943, VSP_000946;
CC Name=26; Synonyms=Variant 17;
CC IsoId=O43497-27; Sequence=VSP_000940, VSP_000944, VSP_047551,
CC VSP_047553;
CC Name=27; Synonyms=Variant 33;
CC IsoId=O43497-28; Sequence=VSP_000940, VSP_047549, VSP_047552;
CC Name=28; Synonyms=Variant 49;
CC IsoId=O43497-29; Sequence=VSP_000940, VSP_047551, VSP_047553;
CC Name=29; Synonyms=Variant 145;
CC IsoId=O43497-30; Sequence=VSP_000944, VSP_047551, VSP_047553;
CC Name=30; Synonyms=Variant 177;
CC IsoId=O43497-31; Sequence=VSP_047551, VSP_047553;
CC Name=31; Synonyms=Variant 209;
CC IsoId=O43497-32; Sequence=VSP_000943, VSP_047551, VSP_047553;
CC Name=32;
CC IsoId=O43497-33; Sequence=VSP_000940, VSP_000943;
CC Name=33; Synonyms=Variant 441-d81;
CC IsoId=O43497-34; Sequence=VSP_047546, VSP_000946;
CC Name=34; Synonyms=Variant 473-d75;
CC IsoId=O43497-35; Sequence=VSP_047547, VSP_000943, VSP_000946;
CC Name=35; Synonyms=Variant 473-d81;
CC IsoId=O43497-36; Sequence=VSP_047546, VSP_000943, VSP_000946;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, in particular in the
CC amygdala, subthalamic nuclei, cerebellum and thalamus. Moderate
CC expression in heart; low expression in placenta, kidney and lung. Also
CC expressed in colon and bone marrow and in tumoral cells to a lesser
CC extent. Highly expressed in fetal brain, but also in peripheral fetal
CC tissues as heart, kidney and lung, suggesting a developmentally
CC regulated expression.
CC -!- DEVELOPMENTAL STAGE: Isoform 4, isoform 7, isoform 18, isoform 19,
CC isoform 24, isoform 25 and isoform 31 are adult-specific. Isoform 8,
CC isoform 14, isoform 15, isoform 16, isoform 17, isoform 20, isoform 21,
CC isoform 22, isoform 23, isoform 26, isoform 27, isoform 28, isoform 29
CC and isoform 30 are fetal-specific. Isoform 1, isoform 2, isoform 6,
CC isoform 9, isoform 11, isoform 12 and isoform 13 are expressed in both
CC fetus and adult. {ECO:0000269|PubMed:16671074}.
CC -!- DOMAIN: Each of the four internal repeats contains five hydrophobic
CC transmembrane segments (S1, S2, S3, S5, S6) and one positively charged
CC transmembrane segment (S4). S4 segments probably represent the voltage-
CC sensor and are characterized by a series of positively charged amino
CC acids at every third position.
CC -!- DOMAIN: The linker region between repeat III and IV probably plays a
CC role in the inactivation of the channel. The C-terminal part may be
CC implicated in the anchoring of the protein to the membrane by
CC interfering with or restricting its lateral diffusion.
CC -!- PTM: In response to raising of intracellular calcium, the T-type
CC channels are activated by CaM-kinase II.
CC -!- DISEASE: Spinocerebellar ataxia 42 (SCA42) [MIM:616795]: A form of
CC spinocerebellar ataxia, a clinically and genetically heterogeneous
CC group of cerebellar disorders. Patients show progressive incoordination
CC of gait and often poor coordination of hands, speech and eye movements,
CC due to degeneration of the cerebellum with variable involvement of the
CC brainstem and spinal cord. SCA42 is a slowly progressive, autosomal
CC dominant form with variable severity. {ECO:0000269|PubMed:26456284,
CC ECO:0000269|PubMed:26715324}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Spinocerebellar ataxia 42, early-onset, severe, with
CC neurodevelopmental deficits (SCA42ND) [MIM:618087]: A form of
CC spinocerebellar ataxia, a clinically and genetically heterogeneous
CC group of cerebellar disorders. Patients show progressive incoordination
CC of gait and often poor coordination of hands, speech and eye movements,
CC due to degeneration of the cerebellum with variable involvement of the
CC brainstem and spinal cord. SCA42ND is an early-onset, severe form
CC associated with motor and cognitive impairment, cerebellar atrophy as
CC well as variable features such as facial dysmorphisms, digital
CC anomalies, microcephaly and epilepsy. SCA42ND inheritance is autosomal
CC dominant. {ECO:0000269|PubMed:29878067}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. CACNA1G subfamily. {ECO:0000305}.
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DR EMBL; AF124351; AAD34352.1; -; mRNA.
DR EMBL; AF134985; AAF19346.1; -; mRNA.
DR EMBL; AF134986; AAF19347.1; -; mRNA.
DR EMBL; AF190860; AAF35287.1; -; mRNA.
DR EMBL; AF126965; AAD29400.1; -; mRNA.
DR EMBL; AF126966; AAD29401.1; -; mRNA.
DR EMBL; AF227744; AAF37689.1; -; mRNA.
DR EMBL; AF227745; AAF37690.1; -; mRNA.
DR EMBL; AF227746; AAF37691.1; -; mRNA.
DR EMBL; AF227747; AAF37692.1; -; mRNA.
DR EMBL; AF227748; AAF37693.1; -; mRNA.
DR EMBL; AF227749; AAF37694.1; -; mRNA.
DR EMBL; AF227750; AAF37695.1; -; mRNA.
DR EMBL; AF227751; AAF37696.1; -; mRNA.
DR EMBL; DQ494449; ABF69900.1; -; mRNA.
DR EMBL; DQ494450; ABF69901.1; -; mRNA.
DR EMBL; DQ494451; ABF69902.1; -; mRNA.
DR EMBL; DQ494452; ABF69903.1; -; mRNA.
DR EMBL; DQ494453; ABF69904.1; -; mRNA.
DR EMBL; DQ494454; ABF69905.1; -; mRNA.
DR EMBL; DQ494455; ABF69906.1; -; mRNA.
DR EMBL; DQ494456; ABF69907.1; -; mRNA.
DR EMBL; DQ494457; ABF69908.1; -; mRNA.
DR EMBL; DQ494458; ABF69909.1; -; mRNA.
DR EMBL; DQ494459; ABF69910.1; -; mRNA.
DR EMBL; DQ494460; ABF69911.1; -; mRNA.
DR EMBL; DQ494461; ABF69912.1; -; mRNA.
DR EMBL; DQ494462; ABF69913.1; -; mRNA.
DR EMBL; DQ494463; ABF69914.1; -; mRNA.
DR EMBL; DQ494464; ABF69915.1; -; mRNA.
DR EMBL; DQ494465; ABF69916.1; -; mRNA.
DR EMBL; DQ494466; ABF69917.1; -; mRNA.
DR EMBL; DQ494467; ABF69918.1; -; mRNA.
DR EMBL; DQ494468; ABF69919.1; -; mRNA.
DR EMBL; DQ494469; ABF69920.1; -; mRNA.
DR EMBL; DQ494470; ABF69921.1; -; mRNA.
DR EMBL; DQ494471; ABF69922.1; -; mRNA.
DR EMBL; DQ494472; ABF69923.1; -; mRNA.
DR EMBL; DQ494473; ABF69924.1; -; mRNA.
DR EMBL; DQ494474; ABF69925.1; -; mRNA.
DR EMBL; DQ494475; ABF69926.1; -; mRNA.
DR EMBL; DQ494476; ABF69927.1; -; mRNA.
DR EMBL; DQ494477; ABF69928.1; -; mRNA.
DR EMBL; DQ494478; ABF69929.1; -; mRNA.
DR EMBL; DQ494479; ABF69930.1; -; mRNA.
DR EMBL; AC004590; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC021491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC110995; AAI10996.1; -; mRNA.
DR EMBL; AB032949; BAA86437.2; -; mRNA.
DR EMBL; AF029228; AAD12731.1; -; mRNA.
DR EMBL; AF029229; AAD12732.1; -; mRNA.
DR CCDS; CCDS45730.1; -. [O43497-1]
DR CCDS; CCDS45731.1; -. [O43497-12]
DR CCDS; CCDS45732.1; -. [O43497-11]
DR CCDS; CCDS45733.1; -. [O43497-13]
DR CCDS; CCDS45734.1; -. [O43497-33]
DR CCDS; CCDS45735.1; -. [O43497-2]
DR CCDS; CCDS45736.1; -. [O43497-5]
DR CCDS; CCDS45737.1; -. [O43497-10]
DR CCDS; CCDS54142.1; -. [O43497-7]
DR CCDS; CCDS54143.1; -. [O43497-6]
DR CCDS; CCDS54144.1; -. [O43497-9]
DR CCDS; CCDS54145.1; -. [O43497-3]
DR CCDS; CCDS54146.1; -. [O43497-8]
DR CCDS; CCDS58565.1; -. [O43497-17]
DR CCDS; CCDS58566.1; -. [O43497-18]
DR CCDS; CCDS58567.1; -. [O43497-15]
DR CCDS; CCDS58568.1; -. [O43497-16]
DR CCDS; CCDS58569.1; -. [O43497-21]
DR CCDS; CCDS58570.1; -. [O43497-20]
DR CCDS; CCDS58571.1; -. [O43497-19]
DR CCDS; CCDS58572.1; -. [O43497-24]
DR CCDS; CCDS58573.1; -. [O43497-23]
DR CCDS; CCDS58574.1; -. [O43497-25]
DR CCDS; CCDS58575.1; -. [O43497-26]
DR CCDS; CCDS58576.1; -. [O43497-22]
DR RefSeq; NP_001243253.1; NM_001256324.1. [O43497-16]
DR RefSeq; NP_001243254.1; NM_001256325.1. [O43497-21]
DR RefSeq; NP_001243255.1; NM_001256326.1. [O43497-25]
DR RefSeq; NP_001243256.1; NM_001256327.1. [O43497-17]
DR RefSeq; NP_001243257.1; NM_001256328.1. [O43497-15]
DR RefSeq; NP_001243258.1; NM_001256329.1. [O43497-24]
DR RefSeq; NP_001243259.1; NM_001256330.1. [O43497-26]
DR RefSeq; NP_001243260.1; NM_001256331.1. [O43497-23]
DR RefSeq; NP_001243261.1; NM_001256332.1. [O43497-22]
DR RefSeq; NP_001243262.1; NM_001256333.1. [O43497-18]
DR RefSeq; NP_001243263.1; NM_001256334.1. [O43497-19]
DR RefSeq; NP_001243288.1; NM_001256359.1. [O43497-34]
DR RefSeq; NP_001243289.1; NM_001256360.1. [O43497-35]
DR RefSeq; NP_001243290.1; NM_001256361.1. [O43497-36]
DR RefSeq; NP_061496.2; NM_018896.4. [O43497-1]
DR RefSeq; NP_938190.1; NM_198376.2. [O43497-5]
DR RefSeq; NP_938191.2; NM_198377.2. [O43497-20]
DR RefSeq; NP_938192.1; NM_198378.2. [O43497-6]
DR RefSeq; NP_938193.1; NM_198379.2. [O43497-8]
DR RefSeq; NP_938194.1; NM_198380.2. [O43497-7]
DR RefSeq; NP_938196.1; NM_198382.2. [O43497-9]
DR RefSeq; NP_938197.1; NM_198383.2. [O43497-10]
DR RefSeq; NP_938198.1; NM_198384.2. [O43497-11]
DR RefSeq; NP_938199.1; NM_198385.2. [O43497-12]
DR RefSeq; NP_938200.1; NM_198386.2. [O43497-13]
DR RefSeq; NP_938201.1; NM_198387.2. [O43497-2]
DR RefSeq; NP_938202.1; NM_198388.2. [O43497-3]
DR RefSeq; NP_938406.1; NM_198396.2. [O43497-33]
DR PDB; 6KZO; EM; 3.30 A; A=1-2377.
DR PDB; 6KZP; EM; 3.10 A; A=2-2377.
DR PDBsum; 6KZO; -.
DR PDBsum; 6KZP; -.
DR AlphaFoldDB; O43497; -.
DR SMR; O43497; -.
DR BioGRID; 114427; 4.
DR IntAct; O43497; 3.
DR STRING; 9606.ENSP00000352011; -.
DR BindingDB; O43497; -.
DR ChEMBL; CHEMBL4641; -.
DR DrugBank; DB09231; Benidipine.
DR DrugBank; DB13746; Bioallethrin.
DR DrugBank; DB11148; Butamben.
DR DrugBank; DB11093; Calcium citrate.
DR DrugBank; DB11348; Calcium Phosphate.
DR DrugBank; DB14481; Calcium phosphate dihydrate.
DR DrugBank; DB09061; Cannabidiol.
DR DrugBank; DB00568; Cinnarizine.
DR DrugBank; DB00228; Enflurane.
DR DrugBank; DB00153; Ergocalciferol.
DR DrugBank; DB00593; Ethosuximide.
DR DrugBank; DB04841; Flunarizine.
DR DrugBank; DB09238; Manidipine.
DR DrugBank; DB14009; Medical Cannabis.
DR DrugBank; DB05246; Methsuximide.
DR DrugBank; DB01388; Mibefradil.
DR DrugBank; DB14011; Nabiximols.
DR DrugBank; DB01115; Nifedipine.
DR DrugBank; DB00421; Spironolactone.
DR DrugBank; DB09089; Trimebutine.
DR DrugBank; DB00347; Trimethadione.
DR DrugBank; DB00661; Verapamil.
DR DrugBank; DB00909; Zonisamide.
DR DrugCentral; O43497; -.
DR GuidetoPHARMACOLOGY; 535; -.
DR GlyGen; O43497; 8 sites.
DR iPTMnet; O43497; -.
DR PhosphoSitePlus; O43497; -.
DR BioMuta; CACNA1G; -.
DR jPOST; O43497; -.
DR MassIVE; O43497; -.
DR PaxDb; O43497; -.
DR PeptideAtlas; O43497; -.
DR PRIDE; O43497; -.
DR ProteomicsDB; 48982; -. [O43497-1]
DR ProteomicsDB; 48983; -. [O43497-10]
DR ProteomicsDB; 48984; -. [O43497-11]
DR ProteomicsDB; 48985; -. [O43497-12]
DR ProteomicsDB; 48986; -. [O43497-13]
DR ProteomicsDB; 48987; -. [O43497-2]
DR ProteomicsDB; 48988; -. [O43497-3]
DR ProteomicsDB; 48989; -. [O43497-4]
DR ProteomicsDB; 48990; -. [O43497-5]
DR ProteomicsDB; 48991; -. [O43497-6]
DR ProteomicsDB; 48992; -. [O43497-7]
DR ProteomicsDB; 48993; -. [O43497-8]
DR ProteomicsDB; 48994; -. [O43497-9]
DR ProteomicsDB; 61180; -.
DR ProteomicsDB; 61181; -.
DR ProteomicsDB; 61182; -.
DR ProteomicsDB; 61183; -.
DR ProteomicsDB; 61184; -.
DR ProteomicsDB; 61185; -.
DR ProteomicsDB; 61186; -.
DR ProteomicsDB; 61187; -.
DR ProteomicsDB; 61188; -.
DR ProteomicsDB; 61189; -.
DR ProteomicsDB; 61190; -.
DR ProteomicsDB; 61191; -.
DR ProteomicsDB; 61192; -.
DR ProteomicsDB; 61193; -.
DR ProteomicsDB; 61194; -.
DR ProteomicsDB; 61195; -.
DR ProteomicsDB; 61196; -.
DR ProteomicsDB; 61197; -.
DR ABCD; O43497; 1 sequenced antibody.
DR Antibodypedia; 1340; 326 antibodies from 35 providers.
DR DNASU; 8913; -.
DR Ensembl; ENST00000352832.9; ENSP00000339302.5; ENSG00000006283.18. [O43497-2]
DR Ensembl; ENST00000354983.8; ENSP00000347078.4; ENSG00000006283.18. [O43497-33]
DR Ensembl; ENST00000358244.9; ENSP00000350979.5; ENSG00000006283.18. [O43497-5]
DR Ensembl; ENST00000359106.10; ENSP00000352011.5; ENSG00000006283.18. [O43497-1]
DR Ensembl; ENST00000360761.8; ENSP00000353990.4; ENSG00000006283.18. [O43497-9]
DR Ensembl; ENST00000429973.6; ENSP00000414388.2; ENSG00000006283.18. [O43497-13]
DR Ensembl; ENST00000442258.6; ENSP00000409759.2; ENSG00000006283.18. [O43497-3]
DR Ensembl; ENST00000502264.5; ENSP00000425522.1; ENSG00000006283.18. [O43497-10]
DR Ensembl; ENST00000503436.5; ENSP00000427231.1; ENSG00000006283.18. [O43497-29]
DR Ensembl; ENST00000503485.5; ENSP00000427238.1; ENSG00000006283.18. [O43497-24]
DR Ensembl; ENST00000503607.5; ENSP00000426558.1; ENSG00000006283.18. [O43497-27]
DR Ensembl; ENST00000504076.5; ENSP00000425153.1; ENSG00000006283.18. [O43497-32]
DR Ensembl; ENST00000505165.5; ENSP00000422268.1; ENSG00000006283.18. [O43497-18]
DR Ensembl; ENST00000506406.5; ENSP00000426313.1; ENSG00000006283.18. [O43497-31]
DR Ensembl; ENST00000507336.5; ENSP00000420918.1; ENSG00000006283.18. [O43497-20]
DR Ensembl; ENST00000507510.6; ENSP00000423112.2; ENSG00000006283.18. [O43497-12]
DR Ensembl; ENST00000507609.5; ENSP00000423045.1; ENSG00000006283.18. [O43497-17]
DR Ensembl; ENST00000507896.5; ENSP00000421518.1; ENSG00000006283.18. [O43497-19]
DR Ensembl; ENST00000510115.5; ENSP00000427173.1; ENSG00000006283.18. [O43497-8]
DR Ensembl; ENST00000510366.5; ENSP00000426814.1; ENSG00000006283.18. [O43497-23]
DR Ensembl; ENST00000511765.5; ENSP00000427247.1; ENSG00000006283.18. [O43497-30]
DR Ensembl; ENST00000511768.5; ENSP00000424664.1; ENSG00000006283.18. [O43497-28]
DR Ensembl; ENST00000512389.5; ENSP00000426261.1; ENSG00000006283.18. [O43497-6]
DR Ensembl; ENST00000513689.6; ENSP00000426172.2; ENSG00000006283.18. [O43497-25]
DR Ensembl; ENST00000513964.5; ENSP00000425451.1; ENSG00000006283.18. [O43497-26]
DR Ensembl; ENST00000514079.5; ENSP00000423317.1; ENSG00000006283.18. [O43497-21]
DR Ensembl; ENST00000514181.5; ENSP00000425698.1; ENSG00000006283.18. [O43497-15]
DR Ensembl; ENST00000514717.5; ENSP00000422407.1; ENSG00000006283.18. [O43497-22]
DR Ensembl; ENST00000515165.5; ENSP00000426098.1; ENSG00000006283.18. [O43497-11]
DR Ensembl; ENST00000515411.5; ENSP00000423155.1; ENSG00000006283.18. [O43497-16]
DR Ensembl; ENST00000515765.5; ENSP00000426232.1; ENSG00000006283.18. [O43497-7]
DR GeneID; 8913; -.
DR KEGG; hsa:8913; -.
DR MANE-Select; ENST00000359106.10; ENSP00000352011.5; NM_018896.5; NP_061496.2.
DR UCSC; uc002irj.3; human. [O43497-1]
DR CTD; 8913; -.
DR DisGeNET; 8913; -.
DR GeneCards; CACNA1G; -.
DR HGNC; HGNC:1394; CACNA1G.
DR HPA; ENSG00000006283; Tissue enriched (brain).
DR MalaCards; CACNA1G; -.
DR MIM; 604065; gene.
DR MIM; 616795; phenotype.
DR MIM; 618087; phenotype.
DR neXtProt; NX_O43497; -.
DR OpenTargets; ENSG00000006283; -.
DR Orphanet; 458803; Spinocerebellar ataxia type 42.
DR PharmGKB; PA381; -.
DR VEuPathDB; HostDB:ENSG00000006283; -.
DR eggNOG; KOG2302; Eukaryota.
DR GeneTree; ENSGT00940000159664; -.
DR HOGENOM; CLU_000540_2_0_1; -.
DR InParanoid; O43497; -.
DR OMA; GQAWSCG; -.
DR OrthoDB; 172471at2759; -.
DR PhylomeDB; O43497; -.
DR TreeFam; TF313555; -.
DR PathwayCommons; O43497; -.
DR Reactome; R-HSA-419037; NCAM1 interactions.
DR SignaLink; O43497; -.
DR SIGNOR; O43497; -.
DR BioGRID-ORCS; 8913; 23 hits in 1067 CRISPR screens.
DR ChiTaRS; CACNA1G; human.
DR GeneWiki; CACNA1G; -.
DR GenomeRNAi; 8913; -.
DR Pharos; O43497; Tclin.
DR PRO; PR:O43497; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O43497; protein.
DR Bgee; ENSG00000006283; Expressed in lateral nuclear group of thalamus and 144 other tissues.
DR ExpressionAtlas; O43497; baseline and differential.
DR Genevisible; O43497; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; ISS:BHF-UCL.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IBA:GO_Central.
DR GO; GO:0008332; F:low voltage-gated calcium channel activity; IDA:UniProtKB.
DR GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
DR GO; GO:0086056; F:voltage-gated calcium channel activity involved in AV node cell action potential; ISS:BHF-UCL.
DR GO; GO:0086059; F:voltage-gated calcium channel activity involved SA node cell action potential; ISS:BHF-UCL.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IBA:GO_Central.
DR GO; GO:0086016; P:AV node cell action potential; ISS:BHF-UCL.
DR GO; GO:0086027; P:AV node cell to bundle of His cell signaling; ISS:BHF-UCL.
DR GO; GO:0070509; P:calcium ion import; IDA:BHF-UCL.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; ISS:BHF-UCL.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR GO; GO:0086045; P:membrane depolarization during AV node cell action potential; ISS:BHF-UCL.
DR GO; GO:0086046; P:membrane depolarization during SA node cell action potential; ISS:BHF-UCL.
DR GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; IBA:GO_Central.
DR GO; GO:0060371; P:regulation of atrial cardiac muscle cell membrane depolarization; IEA:Ensembl.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISS:BHF-UCL.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0042391; P:regulation of membrane potential; IDA:BHF-UCL.
DR GO; GO:0010045; P:response to nickel cation; IEA:Ensembl.
DR GO; GO:0086015; P:SA node cell action potential; ISS:BHF-UCL.
DR GO; GO:0086018; P:SA node cell to atrial cardiac muscle cell signaling; ISS:BHF-UCL.
DR GO; GO:0003163; P:sinoatrial node development; NAS:BHF-UCL.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR005445; VDCC_T_a1.
DR InterPro; IPR002077; VDCCAlpha1.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00167; CACHANNEL.
DR PRINTS; PR01629; TVDCCALPHA1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Calcium channel;
KW Calcium transport; Cell membrane; Cytoplasm; Disease variant; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Neurodegeneration; Phosphoprotein;
KW Reference proteome; Repeat; Spinocerebellar ataxia; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..2377
FT /note="Voltage-dependent T-type calcium channel subunit
FT alpha-1G"
FT /id="PRO_0000053952"
FT TOPO_DOM 1..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..119
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..141
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..170
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..175
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..193
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..370
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..395
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..743
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 744..764
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 765..777
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 778..799
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 800..805
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 806..824
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 825..832
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 833..856
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 857..867
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 868..888
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 889..939
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 940..964
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 965..1272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1273..1295
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1296..1313
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1314..1334
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1335..1344
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1345..1364
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1365..1378
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1379..1400
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1401..1410
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1411..1434
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1435..1511
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1512..1537
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1538..1610
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1611..1631
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1632..1645
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1646..1667
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1668..1674
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1675..1693
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1694..1707
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1708..1731
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1732..1745
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1746..1766
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1767..1826
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1827..1854
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1855..2377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 68..398
FT /note="I"
FT REPEAT 729..967
FT /note="II"
FT REPEAT 1263..1540
FT /note="III"
FT REPEAT 1596..1854
FT /note="IV"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 991..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1878..1917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2107..2129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2171..2244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2272..2377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1076
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2272..2287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 354
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 924
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1465
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1770
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54898"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54898"
FT MOD_RES 1139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54898"
FT MOD_RES 1145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54898"
FT MOD_RES 1146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54898"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1698
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 971..993
FT /note="Missing (in isoform 1, isoform 2, isoform 3, isoform
FT 4, isoform 8, isoform 9, isoform 10, isoform 21, isoform
FT 26, isoform 27, isoform 28 and isoform 32)"
FT /evidence="ECO:0000303|PubMed:10493502,
FT ECO:0000303|PubMed:10648811, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16671074"
FT /id="VSP_000940"
FT VAR_SEQ 1505..1538
FT /note="Missing (in isoform 21, isoform 22, isoform 23,
FT isoform 24 and isoform 25)"
FT /evidence="ECO:0000303|PubMed:16671074"
FT /id="VSP_047545"
FT VAR_SEQ 1505..1531
FT /note="Missing (in isoform 33 and isoform 35)"
FT /evidence="ECO:0000303|PubMed:16671074"
FT /id="VSP_047546"
FT VAR_SEQ 1505..1529
FT /note="Missing (in isoform 34)"
FT /evidence="ECO:0000303|PubMed:16671074"
FT /id="VSP_047547"
FT VAR_SEQ 1569..1587
FT /note="NLMLDDVIASGSSASAASE -> K (in isoform 2, isoform 13,
FT isoform 14, isoform 15, isoform 22, isoform 26 and isoform
FT 29)"
FT /evidence="ECO:0000303|PubMed:10574461,
FT ECO:0000303|PubMed:16671074"
FT /id="VSP_000944"
FT VAR_SEQ 1569..1586
FT /note="NLMLDDVIASGSSASAAS -> SKEKQMA (in isoform 1, isoform
FT 4, isoform 6, isoform 7, isoform 8, isoform 18, isoform 19,
FT isoform 24, isoform 25, isoform 31, isoform 32, isoform 34
FT and isoform 35)"
FT /evidence="ECO:0000303|PubMed:10648811,
FT ECO:0000303|PubMed:16671074"
FT /id="VSP_000943"
FT VAR_SEQ 1569
FT /note="N -> SKEKQMAD (in isoform 20)"
FT /evidence="ECO:0000303|PubMed:16671074"
FT /id="VSP_047548"
FT VAR_SEQ 1736..1769
FT /note="VMQALPQVGNLGLLFMLLFFIFAALGVELFGDLE -> LWAWSSLETWSVTR
FT HTPVRAWAVMPPFGTLAWPS (in isoform 27)"
FT /evidence="ECO:0000303|PubMed:16671074"
FT /id="VSP_047549"
FT VAR_SEQ 1737..1743
FT /note="Missing (in isoform 14 and isoform 16)"
FT /evidence="ECO:0000303|PubMed:16671074"
FT /id="VSP_047550"
FT VAR_SEQ 1743..1776
FT /note="VGNLGLLFMLLFFIFAALGVELFGDLECDETHPC -> LWAWSSLETWSVTR
FT HTPVRAWAVMPPFGTLAWPS (in isoform 26, isoform 28, isoform
FT 29, isoform 30 and isoform 31)"
FT /evidence="ECO:0000303|PubMed:16671074"
FT /id="VSP_047551"
FT VAR_SEQ 1770..2377
FT /note="Missing (in isoform 27)"
FT /evidence="ECO:0000303|PubMed:16671074"
FT /id="VSP_047552"
FT VAR_SEQ 1777..2377
FT /note="Missing (in isoform 26, isoform 28, isoform 29,
FT isoform 30 and isoform 31)"
FT /evidence="ECO:0000303|PubMed:16671074"
FT /id="VSP_047553"
FT VAR_SEQ 1928..2020
FT /note="Missing (in isoform 1, isoform 2, isoform 4, isoform
FT 6, isoform 9, isoform 11, isoform 13, isoform 14, isoform
FT 16, isoform 17, isoform 18, isoform 20, isoform 21, isoform
FT 22, isoform 23, isoform 25, isoform 33, isoform 34 and
FT isoform 35)"
FT /evidence="ECO:0000303|PubMed:10574461,
FT ECO:0000303|PubMed:10648811, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16671074"
FT /id="VSP_000946"
FT VAR_SEQ 1928..1975
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000305"
FT /id="VSP_000945"
FT VAR_SEQ 1976..2020
FT /note="Missing (in isoform 7, isoform 8, isoform 12,
FT isoform 15 and isoform 24)"
FT /evidence="ECO:0000303|PubMed:16671074"
FT /id="VSP_000947"
FT VAR_SEQ 2156..2234
FT /note="Missing (in isoform 4, isoform 17 and isoform 18)"
FT /evidence="ECO:0000303|PubMed:16671074"
FT /id="VSP_000948"
FT VARIANT 961
FT /note="A -> T (in SCA42ND; gain-of-function mutation;
FT results in slower channel inactivation and negatively
FT shifted potential for half-inactivation;
FT dbSNP:rs886041505)"
FT /evidence="ECO:0000269|PubMed:29878067"
FT /id="VAR_081177"
FT VARIANT 1531
FT /note="M -> V (in SCA42ND; gain-of-function mutation;
FT results in slower channel inactivation and negatively
FT shifted potential for half-inactivation;
FT dbSNP:rs1555558553)"
FT /evidence="ECO:0000269|PubMed:29878067"
FT /id="VAR_081178"
FT VARIANT 1715
FT /note="R -> H (in SCA42; changed voltage-gated calcium
FT channel activity; membrane potential dependency is shifted
FT toward more positive potentials; dbSNP:rs755221106)"
FT /evidence="ECO:0000269|PubMed:26456284,
FT ECO:0000269|PubMed:26715324"
FT /id="VAR_076292"
FT CONFLICT 1345
FT /note="S -> I (in Ref. 10; AAD12731)"
FT /evidence="ECO:0000305"
FT HELIX 81..99
FT /evidence="ECO:0007829|PDB:6KZP"
FT TURN 103..107
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 112..135
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 152..171
FT /evidence="ECO:0007829|PDB:6KZP"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 180..189
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 195..207
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 212..233
FT /evidence="ECO:0007829|PDB:6KZP"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:6KZP"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:6KZO"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:6KZO"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:6KZP"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:6KZP"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 330..333
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 340..351
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 356..366
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 372..381
FT /evidence="ECO:0007829|PDB:6KZP"
FT TURN 382..386
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 387..404
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 744..760
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 770..795
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 799..802
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 806..822
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 832..835
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 836..844
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 850..864
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 866..886
FT /evidence="ECO:0007829|PDB:6KZP"
FT TURN 887..889
FT /evidence="ECO:0007829|PDB:6KZP"
FT STRAND 906..908
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 910..920
FT /evidence="ECO:0007829|PDB:6KZP"
FT TURN 921..924
FT /evidence="ECO:0007829|PDB:6KZO"
FT HELIX 925..935
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 938..940
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 941..952
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 955..967
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 1266..1274
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 1276..1294
FT /evidence="ECO:0007829|PDB:6KZP"
FT STRAND 1302..1304
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 1307..1331
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 1345..1366
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 1373..1384
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 1385..1390
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 1391..1394
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 1396..1408
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 1413..1434
FT /evidence="ECO:0007829|PDB:6KZP"
FT STRAND 1439..1442
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 1452..1458
FT /evidence="ECO:0007829|PDB:6KZP"
FT STRAND 1461..1464
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 1472..1483
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 1488..1497
FT /evidence="ECO:0007829|PDB:6KZP"
FT STRAND 1501..1503
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 1511..1513
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 1514..1540
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 1613..1629
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 1637..1665
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 1669..1672
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 1675..1690
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 1693..1698
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 1705..1714
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 1715..1722
FT /evidence="ECO:0007829|PDB:6KZP"
FT TURN 1723..1725
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 1727..1738
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 1740..1765
FT /evidence="ECO:0007829|PDB:6KZP"
FT STRAND 1772..1774
FT /evidence="ECO:0007829|PDB:6KZP"
FT STRAND 1780..1782
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 1788..1799
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 1804..1811
FT /evidence="ECO:0007829|PDB:6KZP"
FT HELIX 1823..1854
FT /evidence="ECO:0007829|PDB:6KZP"
FT TURN 1855..1858
FT /evidence="ECO:0007829|PDB:6KZP"
SQ SEQUENCE 2377 AA; 262472 MW; 1C9F7C557D9D32DF CRC64;
MDEEEDGAGA EESGQPRSFM RLNDLSGAGG RPGPGSAEKD PGSADSEAEG LPYPALAPVV
FFYLSQDSRP RSWCLRTVCN PWFERISMLV ILLNCVTLGM FRPCEDIACD SQRCRILQAF
DDFIFAFFAV EMVVKMVALG IFGKKCYLGD TWNRLDFFIV IAGMLEYSLD LQNVSFSAVR
TVRVLRPLRA INRVPSMRIL VTLLLDTLPM LGNVLLLCFF VFFIFGIVGV QLWAGLLRNR
CFLPENFSLP LSVDLERYYQ TENEDESPFI CSQPRENGMR SCRSVPTLRG DGGGGPPCGL
DYEAYNSSSN TTCVNWNQYY TNCSAGEHNP FKGAINFDNI GYAWIAIFQV ITLEGWVDIM
YFVMDAHSFY NFIYFILLII VGSFFMINLC LVVIATQFSE TKQRESQLMR EQRVRFLSNA
STLASFSEPG SCYEELLKYL VYILRKAARR LAQVSRAAGV RVGLLSSPAP LGGQETQPSS
SCSRSHRRLS VHHLVHHHHH HHHHYHLGNG TLRAPRASPE IQDRDANGSR RLMLPPPSTP
ALSGAPPGGA ESVHSFYHAD CHLEPVRCQA PPPRSPSEAS GRTVGSGKVY PTVHTSPPPE
TLKEKALVEV AASSGPPTLT SLNIPPGPYS SMHKLLETQS TGACQSSCKI SSPCLKADSG
ACGPDSCPYC ARAGAGEVEL ADREMPDSDS EAVYEFTQDA QHSDLRDPHS RRQRSLGPDA
EPSSVLAFWR LICDTFRKIV DSKYFGRGIM IAILVNTLSM GIEYHEQPEE LTNALEISNI
VFTSLFALEM LLKLLVYGPF GYIKNPYNIF DGVIVVISVW EIVGQQGGGL SVLRTFRLMR
VLKLVRFLPA LQRQLVVLMK TMDNVATFCM LLMLFIFIFS ILGMHLFGCK FASERDGDTL
PDRKNFDSLL WAIVTVFQIL TQEDWNKVLY NGMASTSSWA ALYFIALMTF GNYVLFNLLV
AILVEGFQAE EISKREDASG QLSCIQLPVD SQGGDANKSE SEPDFFSPSL DGDGDRKKCL
ALVSLGEHPE LRKSLLPPLI IHTAATPMSL PKSTSTGLGE ALGPASRRTS SSGSAEPGAA
HEMKSPPSAR SSPHSPWSAA SSWTSRRSSR NSLGRAPSLK RRSPSGERRS LLSGEGQESQ
DEEESSEEER ASPAGSDHRH RGSLEREAKS SFDLPDTLQV PGLHRTASGR GSASEHQDCN
GKSASGRLAR ALRPDDPPLD GDDADDEGNL SKGERVRAWI RARLPACCLE RDSWSAYIFP
PQSRFRLLCH RIITHKMFDH VVLVIIFLNC ITIAMERPKI DPHSAERIFL TLSNYIFTAV
FLAEMTVKVV ALGWCFGEQA YLRSSWNVLD GLLVLISVID ILVSMVSDSG TKILGMLRVL
RLLRTLRPLR VISRAQGLKL VVETLMSSLK PIGNIVVICC AFFIIFGILG VQLFKGKFFV
CQGEDTRNIT NKSDCAEASY RWVRHKYNFD NLGQALMSLF VLASKDGWVD IMYDGLDAVG
VDQQPIMNHN PWMLLYFISF LLIVAFFVLN MFVGVVVENF HKCRQHQEEE EARRREEKRL
RRLEKKRRNL MLDDVIASGS SASAASEAQC KPYYSDYSRF RLLVHHLCTS HYLDLFITGV
IGLNVVTMAM EHYQQPQILD EALKICNYIF TVIFVLESVF KLVAFGFRRF FQDRWNQLDL
AIVLLSIMGI TLEEIEVNAS LPINPTIIRI MRVLRIARVL KLLKMAVGMR ALLDTVMQAL
PQVGNLGLLF MLLFFIFAAL GVELFGDLEC DETHPCEGLG RHATFRNFGM AFLTLFRVST
GDNWNGIMKD TLRDCDQEST CYNTVISPIY FVSFVLTAQF VLVNVVIAVL MKHLEESNKE
AKEEAELEAE LELEMKTLSP QPHSPLGSPF LWPGVEGPDS PDSPKPGALH PAAHARSASH
FSLEHPTDRQ LFDTISLLIQ GSLEWELKLM DELAGPGGQP SAFPSAPSLG GSDPQIPLAE
MEALSLTSEI VSEPSCSLAL TDDSLPDDMH TLLLSALESN MQPHPTELPG PDLLTVRKSG
VSRTHSLPND SYMCRHGSTA EGPLGHRGWG LPKAQSGSVL SVHSQPADTS YILQLPKDAP
HLLQPHSAPT WGTIPKLPPP GRSPLAQRPL RRQAAIRTDS LDVQGLGSRE DLLAEVSGPS
PPLARAYSFW GQSSTQAQQH SRSHSKISKH MTPPAPCPGP EPNWGKGPPE TRSSLELDTE
LSWISGDLLP PGGQEEPPSP RDLKKCYSVE AQSCQRRPTS WLDEQRRHSI AVSCLDSGSQ
PHLGTDPSNL GGQPLGGPGS RPKKKLSPPS ITIDPPESQG PRTPPSPGIC LRRRAPSSDS
KDPLASGPPD SMAASPSPKK DVLSLSGLSS DPADLDP
