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Voltage-dependent T-type calcium channel subunit alpha-1H (Low-voltage-activated calcium channel alpha1 3.2 subunit) (Voltage-gated calcium channel subunit alpha Cav3.2)

 CAC1H_HUMAN             Reviewed;        2353 AA.
O95180; B5ME00; F8WFD1; O95802; Q8WWI6; Q96QI6; Q96RZ9; Q9NYY4;
Q9NYY5;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
19-SEP-2002, sequence version 4.
25-OCT-2017, entry version 169.
RecName: Full=Voltage-dependent T-type calcium channel subunit alpha-1H;
AltName: Full=Low-voltage-activated calcium channel alpha1 3.2 subunit;
AltName: Full=Voltage-gated calcium channel subunit alpha Cav3.2;
Name=CACNA1H;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-664, AND TISSUE
SPECIFICITY.
TISSUE=Heart;
PubMed=9670923; DOI=10.1161/01.RES.83.1.103;
Cribbs L.L., Lee J.-H., Yang J., Satin J., Zhang Y., Daud A.N.,
Barclay J., Wiliamson M.P., Fox M., Rees M., Perez-Reyes E.;
"Cloning and characterization of alpha1H from human heart, a member of
the T-type Ca2+ channel gene family.";
Circ. Res. 83:103-109(1998).
[2]
SEQUENCE REVISION.
Cribbs L.L., Lee J.-H., Yang J., Daud A.N., Perez-Reyes E.;
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT HIS-2077, AND TISSUE
SPECIFICITY.
TISSUE=Thyroid carcinoma;
PubMed=9930755; DOI=10.1046/j.1471-4159.1999.0720791.x;
Williams M.E., Washburn M.S., Hans M., Urrutia A., Brust P.F.,
Prodanovich P., Harpold M.M., Stauderman K.A.;
"Structure and functional characterization of a novel human low-
voltage activated calcium channel.";
J. Neurochem. 72:791-799(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ALA-664, AND TISSUE
SPECIFICITY.
TISSUE=Testis;
PubMed=11751928; DOI=10.1074/jbc.M105345200;
Jagannathan S., Punt E.L., Gu Y., Arnoult C., Sakkas D., Barratt C.L.,
Publicover S.J.;
"Identification and localization of T-type voltage-operated calcium
channel subunits in human male germ cells. Expression of multiple
isoforms.";
J. Biol. Chem. 277:8449-8456(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS VAL-313
AND HIS-2060.
PubMed=11157797; DOI=10.1093/hmg/10.4.339;
Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K.,
Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J.,
Higgs D.R.;
"Sequence, structure and pathology of the fully annotated terminal 2
Mb of the short arm of human chromosome 16.";
Hum. Mol. Genet. 10:339-352(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-313.
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 424-661 AND 838-2373 (ISOFORM 1),
AND VARIANTS LEU-640 AND HIS-2077.
Mittman S., Agnew W.S.;
"Organization and alternative splicing of CACNA1H.";
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
[8]
ZINC-BINDING SITES.
PubMed=19940152; DOI=10.1074/jbc.M109.067660;
Kang H.W., Vitko I., Lee S.S., Perez-Reyes E., Lee J.H.;
"Structural determinants of the high affinity extracellular zinc
binding site on Cav3.2 T-type calcium channels.";
J. Biol. Chem. 285:3271-3281(2010).
[9]
VARIANTS ECA6 LEU-161; LYS-282; SER-456; SER-499; LEU-648; GLN-744;
VAL-748; ASP-773; SER-784; MET-831; SER-848 AND ASN-1463, AND VARIANTS
VAL-313; LEU-640; ALA-664; SER-684; CYS-788; HIS-2060; HIS-2077 AND
SER-2173.
PubMed=12891677; DOI=10.1002/ana.10607;
Chen Y., Lu J., Pan H., Zhang Y., Wu H., Xu K., Liu X., Jiang Y.,
Bao X., Yao Z., Ding K., Lo W.H., Qiang B., Chan P., Shen Y., Wu X.;
"Association between genetic variation of CACNA1H and childhood
absence epilepsy.";
Ann. Neurol. 54:239-243(2003).
[10]
VARIANTS EIG6 LEU-618 AND ASP-755.
PubMed=15048902; DOI=10.1002/ana.20028;
Heron S.E., Phillips H.A., Mulley J.C., Mazarib A., Neufeld M.Y.,
Berkovic S.F., Scheffer I.E.;
"Genetic variation of CACNA1H in idiopathic generalized epilepsy.";
Ann. Neurol. 55:595-596(2004).
[11]
VARIANT HALD4 VAL-1549, CHARACTERIZATION OF VARIANT HALD4 VAL-1549,
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=25907736; DOI=10.7554/eLife.06315;
Scholl U.I., Stoelting G., Nelson-Williams C., Vichot A.A., Choi M.,
Loring E., Prasad M.L., Goh G., Carling T., Juhlin C.C., Quack I.,
Rump L.C., Thiel A., Lande M., Frazier B.G., Rasoulpour M.,
Bowlin D.L., Sethna C.B., Trachtman H., Fahlke C., Lifton R.P.;
"Recurrent gain of function mutation in calcium channel CACNA1H causes
early-onset hypertension with primary aldosteronism.";
Elife 4:E06315-E06315(2015).
[12]
VARIANT CYS-1970.
PubMed=26637798; DOI=10.1016/j.neuron.2015.11.009;
D'Gama A.M., Pochareddy S., Li M., Jamuar S.S., Reiff R.E., Lam A.T.,
Sestan N., Walsh C.A.;
"Targeted DNA Sequencing from Autism Spectrum Disorder Brains
Implicates Multiple Genetic Mechanisms.";
Neuron 88:910-917(2015).
[13]
VARIANTS HALD4 LEU-196; ILE-1549 AND LEU-2083, VARIANT GLU-1951,
CHARACTERIZATION OF VARIANTS HALD4 LEU-196; ILE-1549 AND LEU-2083,
CHARACTERIZATION OF VARIANT GLU-1951, FUNCTION, AND TISSUE
SPECIFICITY.
PubMed=27729216; DOI=10.1016/j.ebiom.2016.10.002;
Daniil G., Fernandes-Rosa F.L., Chemin J., Blesneac I., Beltrand J.,
Polak M., Jeunemaitre X., Boulkroun S., Amar L., Strom T.M., Lory P.,
Zennaro M.C.;
"CACNA1H mutations are associated with different forms of primary
aldosteronism.";
EBioMedicine 13:225-236(2016).
[14]
VARIANT TYR-516.
PubMed=27864847; DOI=10.1002/humu.23149;
Clinical Study Group;
Parrini E., Marini C., Mei D., Galuppi A., Cellini E., Pucatti D.,
Chiti L., Rutigliano D., Bianchini C., Virdo S., De Vita D.,
Bigoni S., Barba C., Mari F., Montomoli M., Pisano T., Rosati A.,
Guerrini R.;
"Diagnostic targeted resequencing in 349 patients with drug-resistant
pediatric epilepsies identifies causative mutations in 30 different
genes.";
Hum. Mutat. 38:216-225(2017).
-!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the
entry of calcium ions into excitable cells and are also involved
in a variety of calcium-dependent processes, including muscle
contraction, hormone or neurotransmitter release, gene expression,
cell motility, cell division and cell death. The isoform alpha-1H
gives rise to T-type calcium currents. T-type calcium channels
belong to the "low-voltage activated (LVA)" group and are strongly
blocked by nickel and mibefradil. A particularity of this type of
channels is an opening at quite negative potentials, and a
voltage-dependent inactivation. T-type channels serve pacemaking
functions in both central neurons and cardiac nodal cells and
support calcium signaling in secretory cells and vascular smooth
muscle. They may also be involved in the modulation of firing
patterns of neurons which is important for information processing
as well as in cell growth processes. In the adrenal zona
glomerulosa, participates in the signaling pathway leading to
aldosterone production in response to either AGT/angiotensin II,
or hyperkalemia (PubMed:25907736, PubMed:27729216).
{ECO:0000269|PubMed:25907736, ECO:0000269|PubMed:27729216}.
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=A1H-a;
IsoId=O95180-1; Sequence=Displayed;
Name=2; Synonyms=A1H-b;
IsoId=O95180-2; Sequence=VSP_000949;
Note=Ref.4 (CAD12646) sequence is in conflict in position:
1587:K->E. {ECO:0000305};
-!- TISSUE SPECIFICITY: In nonneuronal tissues, the highest expression
levels are found in the kidney, liver, and heart. In the brain,
most abundant in the amygdala, caudate nucleus, and putamen
(PubMed:9670923, PubMed:9930755). In the heart, expressed in blood
vessels. Isoform 1 and isoform 2 are expressed in testis,
primarily in the germ cells, but not in other portions of the
reproductive tract, such as ductus deferens. Isoform 2 is not
detected in brain (PubMed:11751928). Expressed in the adrenal
glomerulosa (at protein level) (PubMed:25907736, PubMed:27729216).
{ECO:0000269|PubMed:11751928, ECO:0000269|PubMed:25907736,
ECO:0000269|PubMed:27729216, ECO:0000269|PubMed:9670923,
ECO:0000269|PubMed:9930755}.
-!- DOMAIN: Each of the four internal repeats contains five
hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one
positively charged transmembrane segment (S4). S4 segments
probably represent the voltage-sensor and are characterized by a
series of positively charged amino acids at every third position.
-!- PTM: In response to raising of intracellular calcium, the T-type
channels are activated by CaM-kinase II.
-!- DISEASE: Epilepsy, idiopathic generalized 6 (EIG6) [MIM:611942]: A
disorder characterized by recurring generalized seizures in the
absence of detectable brain lesions and/or metabolic
abnormalities. Generalized seizures arise diffusely and
simultaneously from both hemispheres of the brain.
{ECO:0000269|PubMed:15048902}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- DISEASE: Epilepsy, childhood absence 6 (ECA6) [MIM:611942]: A
subtype of idiopathic generalized epilepsy characterized by an
onset at age 6-7 years, frequent absence seizures (several per
day) and bilateral, synchronous, symmetric 3-Hz spike waves on
EEG. Tonic-clonic seizures often develop in adolescence. Absence
seizures may either remit or persist into adulthood.
{ECO:0000269|PubMed:12891677}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- DISEASE: Hyperaldosteronism, familial, 4 (HALD4) [MIM:617027]: A
form of familial hyperaldosteronism, a disorder characterized by
hypertension, elevated aldosterone levels despite low plasma renin
activity, and abnormal adrenal steroid production. There is
significant phenotypic heterogeneity, and some individuals never
develop hypertension. {ECO:0000269|PubMed:25907736,
ECO:0000269|PubMed:27729216}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
1.A.1.11) family. CACNA1H subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAK61268.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAC42094.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AF051946; AAC67239.3; -; mRNA.
EMBL; AF073931; AAD17668.1; -; mRNA.
EMBL; AJ420779; CAD12646.1; -; mRNA.
EMBL; AE006466; AAK61268.1; ALT_SEQ; Genomic_DNA.
EMBL; AL031703; CAC42094.1; ALT_SEQ; Genomic_DNA.
EMBL; AC120498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF223562; AAF60162.1; -; Genomic_DNA.
EMBL; AF223563; AAF60163.1; -; Genomic_DNA.
CCDS; CCDS45375.1; -. [O95180-1]
CCDS; CCDS45376.1; -. [O95180-2]
RefSeq; NP_001005407.1; NM_001005407.1. [O95180-2]
RefSeq; NP_066921.2; NM_021098.2. [O95180-1]
UniGene; Hs.459642; -.
ProteinModelPortal; O95180; -.
BioGrid; 114426; 5.
IntAct; O95180; 2.
STRING; 9606.ENSP00000334198; -.
BindingDB; O95180; -.
ChEMBL; CHEMBL1859; -.
DrugBank; DB01118; Amiodarone.
DrugBank; DB01244; Bepridil.
DrugBank; DB00568; Cinnarizine.
DrugBank; DB01023; Felodipine.
DrugBank; DB04841; Flunarizine.
DrugBank; DB00270; Isradipine.
DrugBank; DB01388; Mibefradil.
DrugBank; DB01115; Nifedipine.
DrugBank; DB01054; Nitrendipine.
DrugBank; DB00421; Spironolactone.
DrugBank; DB00909; Zonisamide.
GuidetoPHARMACOLOGY; 536; -.
TCDB; 1.A.1.11.5; the voltage-gated ion channel (vic) superfamily.
iPTMnet; O95180; -.
PhosphoSitePlus; O95180; -.
BioMuta; CACNA1H; -.
PaxDb; O95180; -.
PeptideAtlas; O95180; -.
PRIDE; O95180; -.
Ensembl; ENST00000348261; ENSP00000334198; ENSG00000196557. [O95180-1]
Ensembl; ENST00000358590; ENSP00000351401; ENSG00000196557. [O95180-2]
Ensembl; ENST00000565831; ENSP00000455840; ENSG00000196557. [O95180-2]
GeneID; 8912; -.
KEGG; hsa:8912; -.
UCSC; uc002cks.4; human. [O95180-1]
CTD; 8912; -.
DisGeNET; 8912; -.
EuPathDB; HostDB:ENSG00000196557.10; -.
GeneCards; CACNA1H; -.
H-InvDB; HIX0038538; -.
HGNC; HGNC:1395; CACNA1H.
HPA; HPA039125; -.
MalaCards; CACNA1H; -.
MIM; 607904; gene.
MIM; 611942; phenotype.
MIM; 617027; phenotype.
neXtProt; NX_O95180; -.
OpenTargets; ENSG00000196557; -.
Orphanet; 64280; Childhood absence epilepsy.
PharmGKB; PA380; -.
eggNOG; ENOG410IP4J; Eukaryota.
eggNOG; COG1226; LUCA.
GeneTree; ENSGT00830000128242; -.
HOVERGEN; HBG050764; -.
InParanoid; O95180; -.
KO; K04855; -.
OMA; QSSWNLL; -.
OrthoDB; EOG091G02L1; -.
PhylomeDB; O95180; -.
TreeFam; TF313555; -.
Reactome; R-HSA-419037; NCAM1 interactions.
ChiTaRS; CACNA1H; human.
GeneWiki; CACNA1H; -.
GenomeRNAi; 8912; -.
PRO; PR:O95180; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000196557; -.
CleanEx; HS_CACNA1H; -.
ExpressionAtlas; O95180; baseline and differential.
Genevisible; O95180; HS.
GO; GO:0016021; C:integral component of membrane; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0005891; C:voltage-gated calcium channel complex; TAS:ProtInc.
GO; GO:0008332; F:low voltage-gated calcium channel activity; IDA:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
GO; GO:0005248; F:voltage-gated sodium channel activity; IBA:GO_Central.
GO; GO:0032342; P:aldosterone biosynthetic process; IMP:UniProtKB.
GO; GO:0070509; P:calcium ion import; IDA:BHF-UCL.
GO; GO:0032870; P:cellular response to hormone stimulus; IEP:UniProtKB.
GO; GO:0035865; P:cellular response to potassium ion; IEP:UniProtKB.
GO; GO:0034651; P:cortisol biosynthetic process; IMP:UniProtKB.
GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
GO; GO:0007517; P:muscle organ development; NAS:ProtInc.
GO; GO:0007520; P:myoblast fusion; TAS:ProtInc.
GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
GO; GO:2000344; P:positive regulation of acrosome reaction; IMP:UniProtKB.
GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; IBA:GO_Central.
GO; GO:0008016; P:regulation of heart contraction; TAS:ProtInc.
GO; GO:0042391; P:regulation of membrane potential; IDA:BHF-UCL.
GO; GO:0006810; P:transport; TAS:ProtInc.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR005445; VDCC_T_a1.
Pfam; PF00520; Ion_trans; 4.
PRINTS; PR01629; TVDCCALPHA1.
1: Evidence at protein level;
Alternative splicing; Calcium; Calcium channel; Calcium transport;
Complete proteome; Disease mutation; Epilepsy; Glycoprotein;
Ion channel; Ion transport; Membrane; Metal-binding; Polymorphism;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport; Voltage-gated channel; Zinc.
CHAIN 1 2353 Voltage-dependent T-type calcium channel
subunit alpha-1H.
/FTId=PRO_0000053954.
TOPO_DOM 1 100 Cytoplasmic. {ECO:0000255}.
TRANSMEM 101 119 Helical; Name=S1 of repeat I.
{ECO:0000255}.
TOPO_DOM 120 141 Extracellular. {ECO:0000255}.
TRANSMEM 142 160 Helical; Name=S2 of repeat I.
{ECO:0000255}.
TOPO_DOM 161 169 Cytoplasmic. {ECO:0000255}.
TRANSMEM 170 184 Helical; Name=S3 of repeat I.
{ECO:0000255}.
TOPO_DOM 185 193 Extracellular. {ECO:0000255}.
TRANSMEM 194 212 Helical; Name=S4 of repeat I.
{ECO:0000255}.
TOPO_DOM 213 232 Cytoplasmic. {ECO:0000255}.
TRANSMEM 233 253 Helical; Name=S5 of repeat I.
{ECO:0000255}.
TOPO_DOM 254 394 Extracellular. {ECO:0000255}.
TRANSMEM 395 419 Helical; Name=S6 of repeat I.
{ECO:0000255}.
TOPO_DOM 420 793 Cytoplasmic. {ECO:0000255}.
TRANSMEM 794 814 Helical; Name=S1 of repeat II.
{ECO:0000255}.
TOPO_DOM 815 827 Extracellular. {ECO:0000255}.
TRANSMEM 828 849 Helical; Name=S2 of repeat II.
{ECO:0000255}.
TOPO_DOM 850 855 Cytoplasmic. {ECO:0000255}.
TRANSMEM 856 874 Helical; Name=S3 of repeat II.
{ECO:0000255}.
TOPO_DOM 875 882 Extracellular. {ECO:0000255}.
TRANSMEM 883 906 Helical; Name=S4 of repeat II.
{ECO:0000255}.
TOPO_DOM 907 917 Cytoplasmic. {ECO:0000255}.
TRANSMEM 918 938 Helical; Name=S5 of repeat II.
{ECO:0000255}.
TOPO_DOM 939 990 Extracellular. {ECO:0000255}.
TRANSMEM 991 1015 Helical; Name=S6 of repeat II.
{ECO:0000255}.
TOPO_DOM 1016 1290 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1291 1313 Helical; Name=S1 of repeat III.
{ECO:0000255}.
TOPO_DOM 1314 1331 Extracellular. {ECO:0000255}.
TRANSMEM 1332 1352 Helical; Name=S2 of repeat III.
{ECO:0000255}.
TOPO_DOM 1353 1362 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1363 1382 Helical; Name=S3 of repeat III.
{ECO:0000255}.
TOPO_DOM 1383 1396 Extracellular. {ECO:0000255}.
TRANSMEM 1397 1418 Helical; Name=S4 of repeat III.
{ECO:0000255}.
TOPO_DOM 1419 1428 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1429 1452 Helical; Name=S5 of repeat III.
{ECO:0000255}.
TOPO_DOM 1453 1529 Extracellular. {ECO:0000255}.
TRANSMEM 1530 1555 Helical; Name=S6 of repeat III.
{ECO:0000255}.
TOPO_DOM 1556 1616 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1617 1637 Helical; Name=S1 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1638 1651 Extracellular. {ECO:0000255}.
TRANSMEM 1652 1673 Helical; Name=S2 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1674 1680 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1681 1699 Helical; Name=S3 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1700 1713 Extracellular. {ECO:0000255}.
TRANSMEM 1714 1737 Helical; Name=S4 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1738 1751 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1752 1772 Helical; Name=S5 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1773 1835 Extracellular. {ECO:0000255}.
TRANSMEM 1836 1863 Helical; Name=S6 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1864 2353 Cytoplasmic. {ECO:0000255}.
REPEAT 87 422 I.
REPEAT 779 1018 II.
REPEAT 1281 1558 III.
REPEAT 1602 1863 IV.
COMPBIAS 520 530 Poly-His.
COMPBIAS 1107 1110 Poly-Ser.
COMPBIAS 1583 1586 Poly-Arg.
METAL 140 140 Zinc.
METAL 189 189 Zinc.
METAL 191 191 Zinc.
SITE 378 378 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 974 974 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1504 1504 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1808 1808 Calcium ion selectivity and permeability.
{ECO:0000250}.
CARBOHYD 192 192 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 271 271 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1466 1466 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1587 1593 STFPSPE -> K (in isoform 2).
{ECO:0000303|PubMed:11751928}.
/FTId=VSP_000949.
VARIANT 161 161 F -> L (in ECA6; dbSNP:rs119454947).
{ECO:0000269|PubMed:12891677}.
/FTId=VAR_045935.
VARIANT 196 196 S -> L (in HALD4; changed calcium channel
activity; increased aldosterone
production in response to potassium ion
stimulation; increased expression of
genes involved in aldosterone
biosynthesis, with the strongest effect
observed on CYP11B2 expression in
response to potassium ion stimulation;
dbSNP:rs780596901).
{ECO:0000269|PubMed:27729216}.
/FTId=VAR_077064.
VARIANT 282 282 E -> K (in ECA6; dbSNP:rs119454948).
{ECO:0000269|PubMed:12891677}.
/FTId=VAR_045936.
VARIANT 313 313 M -> V (in dbSNP:rs36117280).
{ECO:0000269|PubMed:11157797,
ECO:0000269|PubMed:12891677,
ECO:0000269|PubMed:15616553}.
/FTId=VAR_045937.
VARIANT 456 456 C -> S (in ECA6).
{ECO:0000269|PubMed:12891677}.
/FTId=VAR_045938.
VARIANT 499 499 G -> S (in ECA6; dbSNP:rs560915333).
{ECO:0000269|PubMed:12891677}.
/FTId=VAR_045939.
VARIANT 516 516 H -> Y (found in a patient with drug-
resistant focal epilepsy; unknown
pathological significance).
{ECO:0000269|PubMed:27864847}.
/FTId=VAR_078237.
VARIANT 618 618 P -> L (in EIG6; dbSNP:rs60734921).
{ECO:0000269|PubMed:15048902}.
/FTId=VAR_066986.
VARIANT 640 640 P -> L (in dbSNP:rs61734410).
{ECO:0000269|PubMed:12891677,
ECO:0000269|Ref.7}.
/FTId=VAR_045940.
VARIANT 648 648 P -> L (in ECA6).
{ECO:0000269|PubMed:12891677}.
/FTId=VAR_045941.
VARIANT 664 664 V -> A (in dbSNP:rs4984636).
{ECO:0000269|PubMed:11751928,
ECO:0000269|PubMed:12891677,
ECO:0000269|PubMed:9670923}.
/FTId=VAR_045942.
VARIANT 684 684 P -> S (in dbSNP:rs762185083).
{ECO:0000269|PubMed:12891677}.
/FTId=VAR_045943.
VARIANT 744 744 R -> Q (in ECA6; dbSNP:rs373764821).
{ECO:0000269|PubMed:12891677}.
/FTId=VAR_045944.
VARIANT 748 748 A -> V (in ECA6; dbSNP:rs770371468).
{ECO:0000269|PubMed:12891677}.
/FTId=VAR_045945.
VARIANT 755 755 G -> D (in EIG6; dbSNP:rs142306293).
{ECO:0000269|PubMed:15048902}.
/FTId=VAR_066987.
VARIANT 773 773 G -> D (in ECA6; dbSNP:rs267606697).
{ECO:0000269|PubMed:12891677}.
/FTId=VAR_045946.
VARIANT 784 784 G -> S (in ECA6; dbSNP:rs779526640).
{ECO:0000269|PubMed:12891677}.
/FTId=VAR_045947.
VARIANT 788 788 R -> C (in dbSNP:rs3751664).
{ECO:0000269|PubMed:12891677}.
/FTId=VAR_045948.
VARIANT 812 812 V -> M (in dbSNP:rs28365119).
/FTId=VAR_045949.
VARIANT 831 831 V -> M (in ECA6; dbSNP:rs119454949).
{ECO:0000269|PubMed:12891677}.
/FTId=VAR_045950.
VARIANT 848 848 G -> S (in ECA6; dbSNP:rs374272094).
{ECO:0000269|PubMed:12891677}.
/FTId=VAR_045951.
VARIANT 1463 1463 D -> N (in ECA6; dbSNP:rs542245543).
{ECO:0000269|PubMed:12891677}.
/FTId=VAR_045952.
VARIANT 1549 1549 M -> I (in HALD4; changed calcium channel
activity; increased aldosterone
production in response to potassium ion
stimulation; increased expression of
genes involved in aldosterone
biosynthesis, with the strongest effect
observed on CYP11B2 expression in
response to potassium ion stimulation).
{ECO:0000269|PubMed:27729216}.
/FTId=VAR_077065.
VARIANT 1549 1549 M -> V (in HALD4; changed calcium channel
activity; dbSNP:rs786205050).
{ECO:0000269|PubMed:25907736}.
/FTId=VAR_077066.
VARIANT 1871 1871 R -> Q (in dbSNP:rs58124832).
/FTId=VAR_061104.
VARIANT 1951 1951 V -> E (probable disease-associated
mutation responsible for primary
aldosteronism found in a patient with
aldosterone-producing adenoma; changed
Ca(2+) channel activity;
dbSNP:rs746967306).
{ECO:0000269|PubMed:27729216}.
/FTId=VAR_077067.
VARIANT 1970 1970 S -> C (found in a patient with autism;
unknown pathological significance).
{ECO:0000269|PubMed:26637798}.
/FTId=VAR_078702.
VARIANT 1974 1974 E -> G (in dbSNP:rs3751886).
/FTId=VAR_033698.
VARIANT 2060 2060 R -> H (in dbSNP:rs1054644).
{ECO:0000269|PubMed:11157797,
ECO:0000269|PubMed:12891677}.
/FTId=VAR_045953.
VARIANT 2077 2077 R -> H (in dbSNP:rs1054645).
{ECO:0000269|PubMed:12891677,
ECO:0000269|PubMed:9930755,
ECO:0000269|Ref.7}.
/FTId=VAR_045954.
VARIANT 2083 2083 P -> L (in HALD4; changed calcium channel
activity; dbSNP:rs759924732).
{ECO:0000269|PubMed:27729216}.
/FTId=VAR_077068.
VARIANT 2173 2173 P -> S (in dbSNP:rs200675829).
{ECO:0000269|PubMed:12891677}.
/FTId=VAR_045955.
CONFLICT 7 7 A -> S (in Ref. 5; AC120498).
{ECO:0000305}.
CONFLICT 31 31 E -> K (in Ref. 5; AC120498).
{ECO:0000305}.
CONFLICT 55 55 A -> S (in Ref. 5; AC120498).
{ECO:0000305}.
CONFLICT 94 94 L -> V (in Ref. 5; AC120498).
{ECO:0000305}.
CONFLICT 215 215 S -> T (in Ref. 6; CAC42094).
{ECO:0000305}.
SEQUENCE 2353 AA; 259163 MW; E13E270635173D98 CRC64;
MTEGARAADE VRVPLGAPPP GPAALVGASP ESPGAPGREA ERGSELGVSP SESPAAERGA
ELGADEEQRV PYPALAATVF FCLGQTTRPR SWCLRLVCNP WFEHVSMLVI MLNCVTLGMF
RPCEDVECGS ERCNILEAFD AFIFAFFAVE MVIKMVALGL FGQKCYLGDT WNRLDFFIVV
AGMMEYSLDG HNVSLSAIRT VRVLRPLRAI NRVPSMRILV TLLLDTLPML GNVLLLCFFV
FFIFGIVGVQ LWAGLLRNRC FLDSAFVRNN NLTFLRPYYQ TEEGEENPFI CSSRRDNGMQ
KCSHIPGRRE LRMPCTLGWE AYTQPQAEGV GAARNACINW NQYYNVCRSG DSNPHNGAIN
FDNIGYAWIA IFQVITLEGW VDIMYYVMDA HSFYNFIYFI LLIIVGSFFM INLCLVVIAT
QFSETKQRES QLMREQRARH LSNDSTLASF SEPGSCYEEL LKYVGHIFRK VKRRSLRLYA
RWQSRWRKKV DPSAVQGQGP GHRQRRAGRH TASVHHLVYH HHHHHHHHYH FSHGSPRRPG
PEPGACDTRL VRAGAPPSPP SPGRGPPDAE SVHSIYHADC HIEGPQERAR VAHAAATAAA
SLRLATGLGT MNYPTILPSG VGSGKGSTSP GPKGKWAGGP PGTGGHGPLS LNSPDPYEKI
PHVVGEHGLG QAPGHLSGLS VPCPLPSPPA GTLTCELKSC PYCTRALEDP EGELSGSESG
DSDGRGVYEF TQDVRHGDRW DPTRPPRATD TPGPGPGSPQ RRAQQRAAPG EPGWMGRLWV
TFSGKLRRIV DSKYFSRGIM MAILVNTLSM GVEYHEQPEE LTNALEISNI VFTSMFALEM
LLKLLACGPL GYIRNPYNIF DGIIVVISVW EIVGQADGGL SVLRTFRLLR VLKLVRFLPA
LRRQLVVLVK TMDNVATFCT LLMLFIFIFS ILGMHLFGCK FSLKTDTGDT VPDRKNFDSL
LWAIVTVFQI LTQEDWNVVL YNGMASTSSW AALYFVALMT FGNYVLFNLL VAILVEGFQA
EGDANRSDTD EDKTSVHFEE DFHKLRELQT TELKMCSLAV TPNGHLEGRG SLSPPLIMCT
AATPMPTPKS SPFLDAAPSL PDSRRGSSSS GDPPLGDQKP PASLRSSPCA PWGPSGAWSS
RRSSWSSLGR APSLKRRGQC GERESLLSGE GKGSTDDEAE DGRAAPGPRA TPLRRAESLD
PRPLRPAALP PTKCRDRDGQ VVALPSDFFL RIDSHREDAA ELDDDSEDSC CLRLHKVLEP
YKPQWCRSRE AWALYLFSPQ NRFRVSCQKV ITHKMFDHVV LVFIFLNCVT IALERPDIDP
GSTERVFLSV SNYIFTAIFV AEMMVKVVAL GLLSGEHAYL QSSWNLLDGL LVLVSLVDIV
VAMASAGGAK ILGVLRVLRL LRTLRPLRVI SRAPGLKLVV ETLISSLRPI GNIVLICCAF
FIIFGILGVQ LFKGKFYYCE GPDTRNISTK AQCRAAHYRW VRRKYNFDNL GQALMSLFVL
SSKDGWVNIM YDGLDAVGVD QQPVQNHNPW MLLYFISFLL IVSFFVLNMF VGVVVENFHK
CRQHQEAEEA RRREEKRLRR LERRRRSTFP SPEAQRRPYY ADYSPTRRSI HSLCTSHYLD
LFITFIICVN VITMSMEHYN QPKSLDEALK YCNYVFTIVF VFEAALKLVA FGFRRFFKDR
WNQLDLAIVL LSLMGITLEE IEMSAALPIN PTIIRIMRVL RIARVLKLLK MATGMRALLD
TVVQALPQVG NLGLLFMLLF FIYAALGVEL FGRLECSEDN PCEGLSRHAT FSNFGMAFLT
LFRVSTGDNW NGIMKDTLRE CSREDKHCLS YLPALSPVYF VTFVLVAQFV LVNVVVAVLM
KHLEESNKEA REDAELDAEI ELEMAQGPGS ARRVDADRPP LPQESPGARD APNLVARKVS
VSRMLSLPND SYMFRPVVPA SAPHPRPLQE VEMETYGAGT PLGSVASVHS PPAESCASLQ
IPLAVSSPAR SGEPLHALSP RGTARSPSLS RLLCRQEAVH TDSLEGKIDS PRDTLDPAEP
GEKTPVRPVT QGGSLQSPPR SPRPASVRTR KHTFGQRCVS SRPAAPGGEE AEASDPADEE
VSHITSSACP WQPTAEPHGP EASPVAGGER DLRRLYSVDA QGFLDKPGRA DEQWRPSAEL
GSGEPGEAKA WGPEAEPALG ARRKKKMSPP CISVEPPAED EGSARPSAAE GGSTTLRRRT
PSCEATPHRD SLEPTEGSGA GGDPAAKGER WGQASCRAEH LTVPSFAFEP LDLGVPSGDP
FLDGSHSVTP ESRASSSGAI VPLEPPESEP PMPVGDPPEK RRGLYLTVPQ CPLEKPGSPS
ATPAPGGGAD DPV


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