ID CAC1H_HUMAN Reviewed; 2353 AA. AC O95180; B5ME00; F8WFD1; O95802; Q8WWI6; Q96QI6; Q96RZ9; Q9NYY4; Q9NYY5; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 19-SEP-2002, sequence version 4. DT 27-MAR-2024, entry version 208. DE RecName: Full=Voltage-dependent T-type calcium channel subunit alpha-1H; DE AltName: Full=Low-voltage-activated calcium channel alpha1 3.2 subunit; DE AltName: Full=Voltage-gated calcium channel subunit alpha Cav3.2; GN Name=CACNA1H {ECO:0000312|HGNC:HGNC:1395}; 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 1), VARIANT ALA-664, FUNCTION, ACTIVITY RP REGULATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Heart; RX PubMed=9670923; DOI=10.1161/01.res.83.1.103; RA Cribbs L.L., Lee J.-H., Yang J., Satin J., Zhang Y., Daud A.N., Barclay J., RA Wiliamson M.P., Fox M., Rees M., Perez-Reyes E.; RT "Cloning and characterization of alpha1H from human heart, a member of the RT T-type Ca2+ channel gene family."; RL Circ. Res. 83:103-109(1998). RN [2] RP SEQUENCE REVISION. RA Cribbs L.L., Lee J.-H., Yang J., Daud A.N., Perez-Reyes E.; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, RP ACTIVITY REGULATION, VARIANT HIS-2077, AND TISSUE SPECIFICITY. RC TISSUE=Thyroid carcinoma; RX PubMed=9930755; DOI=10.1046/j.1471-4159.1999.0720791.x; RA Williams M.E., Washburn M.S., Hans M., Urrutia A., Brust P.F., RA Prodanovich P., Harpold M.M., Stauderman K.A.; RT "Structure and functional characterization of a novel human low-voltage RT activated calcium channel."; RL J. Neurochem. 72:791-799(1999). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ALA-664, AND TISSUE RP SPECIFICITY. RC TISSUE=Testis; RX PubMed=11751928; DOI=10.1074/jbc.m105345200; RA Jagannathan S., Punt E.L., Gu Y., Arnoult C., Sakkas D., Barratt C.L., RA Publicover S.J.; RT "Identification and localization of T-type voltage-operated calcium channel RT subunits in human male germ cells. Expression of multiple isoforms."; RL J. Biol. Chem. 277:8449-8456(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS VAL-313 AND RP HIS-2060. RX PubMed=11157797; DOI=10.1093/hmg/10.4.339; RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.; RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of RT the short arm of human chromosome 16."; RL Hum. Mol. Genet. 10:339-352(2001). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-313. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 424-661 AND 838-2373 (ISOFORM 1), AND RP VARIANTS LEU-640 AND HIS-2077. RA Mittman S., Agnew W.S.; RT "Organization and alternative splicing of CACNA1H."; RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases. RN [8] RP ZINC-BINDING SITES. RX PubMed=19940152; DOI=10.1074/jbc.m109.067660; RA Kang H.W., Vitko I., Lee S.S., Perez-Reyes E., Lee J.H.; RT "Structural determinants of the high affinity extracellular zinc binding RT site on Cav3.2 T-type calcium channels."; RL J. Biol. Chem. 285:3271-3281(2010). RN [9] RP INTERACTION WITH STAC, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=27149520; DOI=10.1080/19336950.2016.1186318; RA Rzhepetskyy Y., Lazniewska J., Proft J., Campiglio M., Flucher B.E., RA Weiss N.; RT "A Cav3.2/Stac1 molecular complex controls T-type channel expression at the RT plasma membrane."; RL Channels 10:346-354(2016). RN [10] RP VARIANTS ECA6 LEU-161; LYS-282; SER-456; SER-499; LEU-648; GLN-744; RP VAL-748; ASP-773; SER-784; MET-831; SER-848 AND ASN-1463, AND VARIANTS RP VAL-313; LEU-640; ALA-664; SER-684; CYS-788; HIS-2060; HIS-2077 AND RP SER-2173. RX PubMed=12891677; DOI=10.1002/ana.10607; RA Chen Y., Lu J., Pan H., Zhang Y., Wu H., Xu K., Liu X., Jiang Y., Bao X., RA Yao Z., Ding K., Lo W.H., Qiang B., Chan P., Shen Y., Wu X.; RT "Association between genetic variation of CACNA1H and childhood absence RT epilepsy."; RL Ann. Neurol. 54:239-243(2003). RN [11] RP VARIANTS EIG6 LEU-618 AND ASP-755, AND FUNCTION. RX PubMed=15048902; DOI=10.1002/ana.20028; RA Heron S.E., Phillips H.A., Mulley J.C., Mazarib A., Neufeld M.Y., RA Berkovic S.F., Scheffer I.E.; RT "Genetic variation of CACNA1H in idiopathic generalized epilepsy."; RL Ann. Neurol. 55:595-596(2004). RN [12] RP CHARACTERIZATION OF VARIANT ECA6 SER-456, AND FUNCTION. RX PubMed=24277868; DOI=10.1113/jphysiol.2013.264176; RA Eckle V.S., Shcheglovitov A., Vitko I., Dey D., Yap C.C., Winckler B., RA Perez-Reyes E.; RT "Mechanisms by which a CACNA1H mutation in epilepsy patients increases RT seizure susceptibility."; RL J. Physiol. (Lond.) 592:795-809(2014). RN [13] RP VARIANT HALD4 VAL-1549, CHARACTERIZATION OF VARIANT HALD4 VAL-1549, RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=25907736; DOI=10.7554/elife.06315; RA Scholl U.I., Stoelting G., Nelson-Williams C., Vichot A.A., Choi M., RA Loring E., Prasad M.L., Goh G., Carling T., Juhlin C.C., Quack I., RA Rump L.C., Thiel A., Lande M., Frazier B.G., Rasoulpour M., Bowlin D.L., RA Sethna C.B., Trachtman H., Fahlke C., Lifton R.P.; RT "Recurrent gain of function mutation in calcium channel CACNA1H causes RT early-onset hypertension with primary aldosteronism."; RL Elife 4:E06315-E06315(2015). RN [14] RP VARIANT CYS-1970. RX PubMed=26637798; DOI=10.1016/j.neuron.2015.11.009; RA D'Gama A.M., Pochareddy S., Li M., Jamuar S.S., Reiff R.E., Lam A.T., RA Sestan N., Walsh C.A.; RT "Targeted DNA Sequencing from Autism Spectrum Disorder Brains Implicates RT Multiple Genetic Mechanisms."; RL Neuron 88:910-917(2015). RN [15] RP VARIANTS HALD4 LEU-196; ILE-1549 AND LEU-2083, VARIANT GLU-1951, RP CHARACTERIZATION OF VARIANTS HALD4 LEU-196; ILE-1549 AND LEU-2083, RP CHARACTERIZATION OF VARIANT GLU-1951, FUNCTION, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RX PubMed=27729216; DOI=10.1016/j.ebiom.2016.10.002; RA Daniil G., Fernandes-Rosa F.L., Chemin J., Blesneac I., Beltrand J., RA Polak M., Jeunemaitre X., Boulkroun S., Amar L., Strom T.M., Lory P., RA Zennaro M.C.; RT "CACNA1H mutations are associated with different forms of primary RT aldosteronism."; RL EBioMedicine 13:225-236(2016). RN [16] RP VARIANT GLN-1871. RX PubMed=28501589; DOI=10.1016/j.clim.2017.05.009; RA Sadovnick A.D., Traboulsee A.L., Zhao Y., Bernales C.Q., Encarnacion M., RA Ross J.P., Yee I.M., Criscuoli M.G., Vilarino-Gueell C.; RT "Genetic modifiers of multiple sclerosis progression, severity and onset."; RL Clin. Immunol. 180:100-105(2017). RN [17] RP VARIANT TYR-516. RX PubMed=27864847; DOI=10.1002/humu.23149; RG Clinical Study Group; RA Parrini E., Marini C., Mei D., Galuppi A., Cellini E., Pucatti D., RA Chiti L., Rutigliano D., Bianchini C., Virdo S., De Vita D., Bigoni S., RA Barba C., Mari F., Montomoli M., Pisano T., Rosati A., Guerrini R.; RT "Diagnostic targeted resequencing in 349 patients with drug-resistant RT pediatric epilepsies identifies causative mutations in 30 different RT genes."; RL Hum. Mutat. 38:216-225(2017). RN [18] RP CHARACTERIZATION OF VARIANT ECA6 LEU-648. RX PubMed=30197081; DOI=10.1016/j.cell.2018.08.019; RA Meyer K., Kirchner M., Uyar B., Cheng J.Y., Russo G., RA Hernandez-Miranda L.R., Szymborska A., Zauber H., Rudolph I.M., RA Willnow T.E., Akalin A., Haucke V., Gerhardt H., Birchmeier C., Kuehn R., RA Krauss M., Diecke S., Pascual J.M., Selbach M.; RT "Mutations in disordered regions can cause disease by creating dileucine RT motifs."; RL Cell 175:239-253(2018). CC -!- FUNCTION: Voltage-sensitive calcium channel that gives rise to T-type CC calcium currents. T-type calcium channels belong to the 'low-voltage CC activated (LVA)' group. A particularity of this type of channel is an CC opening at quite negative potentials, and a voltage-dependent CC inactivation (PubMed:9670923, PubMed:9930755, PubMed:27149520). T-type CC channels serve pacemaking functions in both central neurons and cardiac CC nodal cells and support calcium signaling in secretory cells and CC vascular smooth muscle (Probable). They may also be involved in the CC modulation of firing patterns of neurons (PubMed:15048902). In the CC adrenal zona glomerulosa, participates in the signaling pathway leading CC to aldosterone production in response to either AGT/angiotensin II, or CC hyperkalemia (PubMed:25907736, PubMed:27729216). CC {ECO:0000269|PubMed:24277868, ECO:0000269|PubMed:25907736, CC ECO:0000269|PubMed:27149520, ECO:0000269|PubMed:27729216, CC ECO:0000269|PubMed:9670923, ECO:0000269|PubMed:9930755, ECO:0000305, CC ECO:0000305|PubMed:15048902}. CC -!- ACTIVITY REGULATION: Channel activity is strongly inhibited by CC mibefradil (PubMed:9670923, PubMed:9930755). Channel activity is CC strongly inhibited by Ni(2+) ions (PubMed:9930755). CC {ECO:0000269|PubMed:9670923, ECO:0000269|PubMed:9930755}. CC -!- SUBUNIT: Interacts (via N-terminal cytoplasmic domain) with STAC. CC {ECO:0000269|PubMed:27149520}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25907736, CC ECO:0000269|PubMed:27149520, ECO:0000269|PubMed:27729216, CC ECO:0000269|PubMed:9670923, ECO:0000269|PubMed:9930755}; Multi-pass CC membrane protein {ECO:0000305}. Note=Interaction with STAC increases CC expression at the cell membrane. {ECO:0000269|PubMed:27149520}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=A1H-a; CC IsoId=O95180-1; Sequence=Displayed; CC Name=2; Synonyms=A1H-b; CC IsoId=O95180-2; Sequence=VSP_000949; CC -!- TISSUE SPECIFICITY: Expressed in the adrenal glomerulosa (at protein CC level) (PubMed:25907736, PubMed:27729216). In nonneuronal tissues, the CC highest expression levels are found in the kidney, liver, and heart. In CC the brain, most abundant in the amygdala, caudate nucleus, and putamen CC (PubMed:9670923, PubMed:9930755). In the heart, expressed in blood CC vessels. {ECO:0000269|PubMed:25907736, ECO:0000269|PubMed:27729216, CC ECO:0000269|PubMed:9670923, ECO:0000269|PubMed:9930755}. CC -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed in testis, primarily in the CC germ cells, but not in other portions of the reproductive tract, such CC as ductus deferens (PubMed:11751928). Expressed in the brain CC (PubMed:11751928). {ECO:0000269|PubMed:11751928}. CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in testis, primarily in the CC germ cells, but not in other portions of the reproductive tract, such CC as ductus deferens (PubMed:11751928). Not expressed in the brain CC (PubMed:11751928). {ECO:0000269|PubMed:11751928}. 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 -!- PTM: In response to raising of intracellular calcium, the T-type CC channels are activated by CaM-kinase II. CC -!- DISEASE: Epilepsy, idiopathic generalized 6 (EIG6) [MIM:611942]: A CC disorder characterized by recurring generalized seizures in the absence CC of detectable brain lesions and/or metabolic abnormalities. Generalized CC seizures arise diffusely and simultaneously from both hemispheres of CC the brain. {ECO:0000269|PubMed:15048902}. Note=Disease susceptibility CC may be associated with variants affecting the gene represented in this CC entry. CC -!- DISEASE: Epilepsy, childhood absence 6 (ECA6) [MIM:611942]: A subtype CC of idiopathic generalized epilepsy characterized by an onset at age 6-7 CC years, frequent absence seizures (several per day) and bilateral, CC synchronous, symmetric 3-Hz spike waves on EEG. Tonic-clonic seizures CC often develop in adolescence. Absence seizures may either remit or CC persist into adulthood. {ECO:0000269|PubMed:12891677, CC ECO:0000269|PubMed:24277868, ECO:0000269|PubMed:30197081}. Note=Disease CC susceptibility may be associated with variants affecting the gene CC represented in this entry. CC -!- DISEASE: Hyperaldosteronism, familial, 4 (HALD4) [MIM:617027]: A form CC of familial hyperaldosteronism, a disorder characterized by CC hypertension, elevated aldosterone levels despite low plasma renin CC activity, and abnormal adrenal steroid production. There is significant CC phenotypic heterogeneity, and some individuals never develop CC hypertension. {ECO:0000269|PubMed:25907736, CC ECO:0000269|PubMed:27729216}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit CC (TC 1.A.1.11) family. CACNA1H subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAK61268.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAC42094.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF051946; AAC67239.3; -; mRNA. DR EMBL; AF073931; AAD17668.1; -; mRNA. DR EMBL; AJ420779; CAD12646.1; -; mRNA. DR EMBL; AE006466; AAK61268.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL031703; CAC42094.1; ALT_SEQ; Genomic_DNA. DR EMBL; AC120498; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF223562; AAF60162.1; -; Genomic_DNA. DR EMBL; AF223563; AAF60163.1; -; Genomic_DNA. DR CCDS; CCDS45375.1; -. [O95180-1] DR CCDS; CCDS45376.1; -. [O95180-2] DR RefSeq; NP_001005407.1; NM_001005407.1. [O95180-2] DR RefSeq; NP_066921.2; NM_021098.2. [O95180-1] DR AlphaFoldDB; O95180; -. DR SMR; O95180; -. DR BioGRID; 114426; 12. DR IntAct; O95180; 5. DR MINT; O95180; -. DR STRING; 9606.ENSP00000334198; -. DR BindingDB; O95180; -. DR ChEMBL; CHEMBL1859; -. DR DrugBank; DB09229; Aranidipine. DR DrugBank; DB09227; Barnidipine. DR DrugBank; DB09231; Benidipine. DR DrugBank; DB01244; Bepridil. 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; DB09235; Efonidipine. DR DrugBank; DB00228; Enflurane. DR DrugBank; DB00153; Ergocalciferol. DR DrugBank; DB01023; Felodipine. DR DrugBank; DB04841; Flunarizine. DR DrugBank; DB00270; Isradipine. DR DrugBank; DB09238; Manidipine. DR DrugBank; DB14009; Medical Cannabis. DR DrugBank; DB01388; Mibefradil. DR DrugBank; DB14011; Nabiximols. DR DrugBank; DB00622; Nicardipine. DR DrugBank; DB01115; Nifedipine. DR DrugBank; DB06712; Nilvadipine. DR DrugBank; DB01054; Nitrendipine. DR DrugBank; DB00421; Spironolactone. DR DrugBank; DB09089; Trimebutine. DR DrugBank; DB00661; Verapamil. DR DrugBank; DB00909; Zonisamide. DR DrugCentral; O95180; -. DR GuidetoPHARMACOLOGY; 536; -. DR TCDB; 1.A.1.11.5; the voltage-gated ion channel (vic) superfamily. DR GlyCosmos; O95180; 3 sites, No reported glycans. DR GlyGen; O95180; 4 sites, 1 O-linked glycan (1 site). DR iPTMnet; O95180; -. DR PhosphoSitePlus; O95180; -. DR BioMuta; CACNA1H; -. DR jPOST; O95180; -. DR MassIVE; O95180; -. DR PaxDb; 9606-ENSP00000334198; -. DR PeptideAtlas; O95180; -. DR ProteomicsDB; 50690; -. [O95180-1] DR ProteomicsDB; 50691; -. [O95180-2] DR ABCD; O95180; 1 sequenced antibody. DR Antibodypedia; 22964; 340 antibodies from 32 providers. DR DNASU; 8912; -. DR Ensembl; ENST00000348261.11; ENSP00000334198.7; ENSG00000196557.13. [O95180-1] DR Ensembl; ENST00000358590.8; ENSP00000351401.4; ENSG00000196557.13. [O95180-2] DR Ensembl; ENST00000565831.6; ENSP00000455840.1; ENSG00000196557.13. [O95180-2] DR GeneID; 8912; -. DR KEGG; hsa:8912; -. DR MANE-Select; ENST00000348261.11; ENSP00000334198.7; NM_021098.3; NP_066921.2. DR UCSC; uc002cks.4; human. [O95180-1] DR AGR; HGNC:1395; -. DR CTD; 8912; -. DR DisGeNET; 8912; -. DR GeneCards; CACNA1H; -. DR HGNC; HGNC:1395; CACNA1H. DR HPA; ENSG00000196557; Tissue enhanced (intestine). DR MalaCards; CACNA1H; -. DR MIM; 607904; gene. DR MIM; 611942; phenotype. DR MIM; 617027; phenotype. DR neXtProt; NX_O95180; -. DR OpenTargets; ENSG00000196557; -. DR Orphanet; 64280; Childhood absence epilepsy. DR Orphanet; 642671; Familial hyperaldosteronism type IV. DR PharmGKB; PA380; -. DR VEuPathDB; HostDB:ENSG00000196557; -. DR eggNOG; KOG2302; Eukaryota. DR GeneTree; ENSGT00940000156666; -. DR HOGENOM; CLU_000540_2_0_1; -. DR InParanoid; O95180; -. DR OMA; RCLIAVY; -. DR OrthoDB; 1110761at2759; -. DR PhylomeDB; O95180; -. DR TreeFam; TF313555; -. DR PathwayCommons; O95180; -. DR Reactome; R-HSA-419037; NCAM1 interactions. DR Reactome; R-HSA-445355; Smooth Muscle Contraction. DR SignaLink; O95180; -. DR SIGNOR; O95180; -. DR BioGRID-ORCS; 8912; 15 hits in 1153 CRISPR screens. DR ChiTaRS; CACNA1H; human. DR GeneWiki; CACNA1H; -. DR GenomeRNAi; 8912; -. DR Pharos; O95180; Tclin. DR PRO; PR:O95180; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; O95180; Protein. DR Bgee; ENSG00000196557; Expressed in lower esophagus muscularis layer and 98 other cell types or tissues. DR ExpressionAtlas; O95180; baseline and differential. DR GO; GO:0016020; C:membrane; IDA:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005891; C:voltage-gated calcium channel complex; IBA:GO_Central. DR GO; GO:0008331; F:high voltage-gated calcium channel activity; IBA:GO_Central. DR GO; GO:0008332; F:low voltage-gated calcium channel activity; IDA:BHF-UCL. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL. DR GO; GO:0005244; F:voltage-gated monoatomic ion channel activity; IDA:UniProtKB. DR GO; GO:0032342; P:aldosterone biosynthetic process; IMP:UniProtKB. DR GO; GO:0070509; P:calcium ion import; IDA:BHF-UCL. DR GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central. DR GO; GO:0032870; P:cellular response to hormone stimulus; IEP:UniProtKB. DR GO; GO:0035865; P:cellular response to potassium ion; IEP:UniProtKB. DR GO; GO:0034651; P:cortisol biosynthetic process; IMP:UniProtKB. DR GO; GO:0098662; P:inorganic cation transmembrane transport; IDA:UniProtKB. DR GO; GO:0006936; P:muscle contraction; TAS:ProtInc. DR GO; GO:0007517; P:muscle organ development; NAS:ProtInc. DR GO; GO:0007520; P:myoblast fusion; TAS:ProtInc. DR GO; GO:2000344; P:positive regulation of acrosome reaction; IMP:UniProtKB. DR GO; GO:0008016; P:regulation of heart contraction; TAS:ProtInc. DR GO; GO:0042391; P:regulation of membrane potential; IDA:BHF-UCL. 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; IPR043203; VGCC_Ca_Na. DR InterPro; IPR027359; Volt_channel_dom_sf. DR PANTHER; PTHR10037:SF192; VOLTAGE-DEPENDENT T-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1H; 1. DR PANTHER; PTHR10037; VOLTAGE-GATED CATION CHANNEL CALCIUM AND SODIUM; 1. DR Pfam; PF00520; Ion_trans; 4. DR PRINTS; PR01629; TVDCCALPHA1. DR SUPFAM; SSF81324; Voltage-gated potassium channels; 4. DR Genevisible; O95180; HS. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Calcium channel; Calcium transport; KW Cell membrane; Disease variant; Epilepsy; Glycoprotein; Ion channel; KW Ion transport; Membrane; Metal-binding; Reference proteome; Repeat; KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel; Zinc. FT CHAIN 1..2353 FT /note="Voltage-dependent T-type calcium channel subunit FT alpha-1H" FT /id="PRO_0000053954" FT TOPO_DOM 1..100 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 101..119 FT /note="Helical; Name=S1 of repeat I" FT /evidence="ECO:0000255" FT TOPO_DOM 120..141 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 142..160 FT /note="Helical; Name=S2 of repeat I" FT /evidence="ECO:0000255" FT TOPO_DOM 161..169 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 170..184 FT /note="Helical; Name=S3 of repeat I" FT /evidence="ECO:0000255" FT TOPO_DOM 185..193 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 194..212 FT /note="Helical; Name=S4 of repeat I" FT /evidence="ECO:0000255" FT TOPO_DOM 213..232 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 233..253 FT /note="Helical; Name=S5 of repeat I" FT /evidence="ECO:0000255" FT TOPO_DOM 254..394 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 395..419 FT /note="Helical; Name=S6 of repeat I" FT /evidence="ECO:0000255" FT TOPO_DOM 420..793 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 794..814 FT /note="Helical; Name=S1 of repeat II" FT /evidence="ECO:0000255" FT TOPO_DOM 815..827 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 828..849 FT /note="Helical; Name=S2 of repeat II" FT /evidence="ECO:0000255" FT TOPO_DOM 850..855 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 856..874 FT /note="Helical; Name=S3 of repeat II" FT /evidence="ECO:0000255" FT TOPO_DOM 875..882 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 883..906 FT /note="Helical; Name=S4 of repeat II" FT /evidence="ECO:0000255" FT TOPO_DOM 907..917 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 918..938 FT /note="Helical; Name=S5 of repeat II" FT /evidence="ECO:0000255" FT TOPO_DOM 939..990 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 991..1015 FT /note="Helical; Name=S6 of repeat II" FT /evidence="ECO:0000255" FT TOPO_DOM 1016..1290 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 1291..1313 FT /note="Helical; Name=S1 of repeat III" FT /evidence="ECO:0000255" FT TOPO_DOM 1314..1331 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1332..1352 FT /note="Helical; Name=S2 of repeat III" FT /evidence="ECO:0000255" FT TOPO_DOM 1353..1362 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 1363..1382 FT /note="Helical; Name=S3 of repeat III" FT /evidence="ECO:0000255" FT TOPO_DOM 1383..1396 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1397..1418 FT /note="Helical; Name=S4 of repeat III" FT /evidence="ECO:0000255" FT TOPO_DOM 1419..1428 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 1429..1452 FT /note="Helical; Name=S5 of repeat III" FT /evidence="ECO:0000255" FT TOPO_DOM 1453..1529 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1530..1555 FT /note="Helical; Name=S6 of repeat III" FT /evidence="ECO:0000255" FT TOPO_DOM 1556..1616 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 1617..1637 FT /note="Helical; Name=S1 of repeat IV" FT /evidence="ECO:0000255" FT TOPO_DOM 1638..1651 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1652..1673 FT /note="Helical; Name=S2 of repeat IV" FT /evidence="ECO:0000255" FT TOPO_DOM 1674..1680 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 1681..1699 FT /note="Helical; Name=S3 of repeat IV" FT /evidence="ECO:0000255" FT TOPO_DOM 1700..1713 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1714..1737 FT /note="Helical; Name=S4 of repeat IV" FT /evidence="ECO:0000255" FT TOPO_DOM 1738..1751 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 1752..1772 FT /note="Helical; Name=S5 of repeat IV" FT /evidence="ECO:0000255" FT TOPO_DOM 1773..1835 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1836..1863 FT /note="Helical; Name=S6 of repeat IV" FT /evidence="ECO:0000255" FT TOPO_DOM 1864..2353 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REPEAT 87..422 FT /note="I" FT REPEAT 779..1018 FT /note="II" FT REPEAT 1281..1558 FT /note="III" FT REPEAT 1602..1863 FT /note="IV" FT REGION 1..64 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 490..571 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 621..646 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 708..772 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1083..1217 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1885..1911 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1989..2009 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2021..2255 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2269..2353 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 503..534 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 728..745 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1156..1184 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2021..2040 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2049..2063 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 140 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT BINDING 189 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT BINDING 191 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT SITE 378 FT /note="Calcium ion selectivity and permeability" FT /evidence="ECO:0000250" FT SITE 974 FT /note="Calcium ion selectivity and permeability" FT /evidence="ECO:0000250" FT SITE 1504 FT /note="Calcium ion selectivity and permeability" FT /evidence="ECO:0000250" FT SITE 1808 FT /note="Calcium ion selectivity and permeability" FT /evidence="ECO:0000250" FT CARBOHYD 192 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 271 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1466 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1587..1593 FT /note="STFPSPE -> K (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11751928" FT /id="VSP_000949" FT VARIANT 161 FT /note="F -> L (in ECA6; uncertain significance; FT dbSNP:rs119454947)" FT /evidence="ECO:0000269|PubMed:12891677" FT /id="VAR_045935" FT VARIANT 196 FT /note="S -> L (in HALD4; changed calcium channel activity; FT increased aldosterone production in response to potassium FT ion stimulation; increased expression of genes involved in FT aldosterone biosynthesis, with the strongest effect FT observed on CYP11B2 expression in response to potassium ion FT stimulation; dbSNP:rs780596901)" FT /evidence="ECO:0000269|PubMed:27729216" FT /id="VAR_077064" FT VARIANT 282 FT /note="E -> K (in ECA6; uncertain significance; FT dbSNP:rs119454948)" FT /evidence="ECO:0000269|PubMed:12891677" FT /id="VAR_045936" FT VARIANT 313 FT /note="M -> V (in dbSNP:rs36117280)" FT /evidence="ECO:0000269|PubMed:11157797, FT ECO:0000269|PubMed:12891677, ECO:0000269|PubMed:15616553" FT /id="VAR_045937" FT VARIANT 456 FT /note="C -> S (in ECA6; uncertain significance; results in FT increased T-current amplitude and lower threshold for FT spikes generation; results in increased neuronal FT excitability)" FT /evidence="ECO:0000269|PubMed:12891677, FT ECO:0000269|PubMed:24277868" FT /id="VAR_045938" FT VARIANT 499 FT /note="G -> S (in ECA6; likely benign; dbSNP:rs560915333)" FT /evidence="ECO:0000269|PubMed:12891677" FT /id="VAR_045939" FT VARIANT 516 FT /note="H -> Y (found in a patient with drug-resistant focal FT epilepsy; uncertain significance; dbSNP:rs1057519554)" FT /evidence="ECO:0000269|PubMed:27864847" FT /id="VAR_078237" FT VARIANT 618 FT /note="P -> L (in EIG6; uncertain significance; FT dbSNP:rs60734921)" FT /evidence="ECO:0000269|PubMed:15048902" FT /id="VAR_066986" FT VARIANT 640 FT /note="P -> L (in dbSNP:rs61734410)" FT /evidence="ECO:0000269|PubMed:12891677, ECO:0000269|Ref.7" FT /id="VAR_045940" FT VARIANT 648 FT /note="P -> L (in ECA6; uncertain significance; creates a FT dileucine internalization motif that promotes recruitment FT of clathrin; dbSNP:rs1288484976)" FT /evidence="ECO:0000269|PubMed:12891677, FT ECO:0000269|PubMed:30197081" FT /id="VAR_045941" FT VARIANT 664 FT /note="V -> A (in dbSNP:rs4984636)" FT /evidence="ECO:0000269|PubMed:11751928, FT ECO:0000269|PubMed:12891677, ECO:0000269|PubMed:9670923" FT /id="VAR_045942" FT VARIANT 684 FT /note="P -> S (in dbSNP:rs762185083)" FT /evidence="ECO:0000269|PubMed:12891677" FT /id="VAR_045943" FT VARIANT 744 FT /note="R -> Q (in ECA6; uncertain significance; FT dbSNP:rs373764821)" FT /evidence="ECO:0000269|PubMed:12891677" FT /id="VAR_045944" FT VARIANT 748 FT /note="A -> V (in ECA6; uncertain significance; FT dbSNP:rs770371468)" FT /evidence="ECO:0000269|PubMed:12891677" FT /id="VAR_045945" FT VARIANT 755 FT /note="G -> D (in EIG6; uncertain significance; FT dbSNP:rs142306293)" FT /evidence="ECO:0000269|PubMed:15048902" FT /id="VAR_066987" FT VARIANT 773 FT /note="G -> D (in ECA6; uncertain significance; FT dbSNP:rs267606697)" FT /evidence="ECO:0000269|PubMed:12891677" FT /id="VAR_045946" FT VARIANT 784 FT /note="G -> S (in ECA6; uncertain significance; FT dbSNP:rs779526640)" FT /evidence="ECO:0000269|PubMed:12891677" FT /id="VAR_045947" FT VARIANT 788 FT /note="R -> C (in dbSNP:rs3751664)" FT /evidence="ECO:0000269|PubMed:12891677" FT /id="VAR_045948" FT VARIANT 812 FT /note="V -> M (in dbSNP:rs28365119)" FT /id="VAR_045949" FT VARIANT 831 FT /note="V -> M (in ECA6; uncertain significance; FT dbSNP:rs119454949)" FT /evidence="ECO:0000269|PubMed:12891677" FT /id="VAR_045950" FT VARIANT 848 FT /note="G -> S (in ECA6; uncertain significance; FT dbSNP:rs374272094)" FT /evidence="ECO:0000269|PubMed:12891677" FT /id="VAR_045951" FT VARIANT 1463 FT /note="D -> N (in ECA6; uncertain significance; FT dbSNP:rs542245543)" FT /evidence="ECO:0000269|PubMed:12891677" FT /id="VAR_045952" FT VARIANT 1549 FT /note="M -> I (in HALD4; changed calcium channel activity; FT increased aldosterone production in response to potassium FT ion stimulation; increased expression of genes involved in FT aldosterone biosynthesis, with the strongest effect FT observed on CYP11B2 expression in response to potassium ion FT stimulation)" FT /evidence="ECO:0000269|PubMed:27729216" FT /id="VAR_077065" FT VARIANT 1549 FT /note="M -> V (in HALD4; changed calcium channel activity; FT dbSNP:rs786205050)" FT /evidence="ECO:0000269|PubMed:25907736" FT /id="VAR_077066" FT VARIANT 1871 FT /note="R -> Q (in dbSNP:rs58124832)" FT /evidence="ECO:0000269|PubMed:28501589" FT /id="VAR_061104" FT VARIANT 1951 FT /note="V -> E (found in a patient with FT aldosterone-producing adenoma and aldosterism; uncertain FT significance; changed Ca(2+) channel activity; FT dbSNP:rs746967306)" FT /evidence="ECO:0000269|PubMed:27729216" FT /id="VAR_077067" FT VARIANT 1970 FT /note="S -> C (found in a patient with autism; uncertain FT significance; dbSNP:rs1267377730)" FT /evidence="ECO:0000269|PubMed:26637798" FT /id="VAR_078702" FT VARIANT 1974 FT /note="E -> G (in dbSNP:rs3751886)" FT /id="VAR_033698" FT VARIANT 2060 FT /note="R -> H (in dbSNP:rs1054644)" FT /evidence="ECO:0000269|PubMed:11157797, FT ECO:0000269|PubMed:12891677" FT /id="VAR_045953" FT VARIANT 2077 FT /note="R -> H (in dbSNP:rs1054645)" FT /evidence="ECO:0000269|PubMed:12891677, FT ECO:0000269|PubMed:9930755, ECO:0000269|Ref.7" FT /id="VAR_045954" FT VARIANT 2083 FT /note="P -> L (in HALD4; changed calcium channel activity; FT dbSNP:rs759924732)" FT /evidence="ECO:0000269|PubMed:27729216" FT /id="VAR_077068" FT VARIANT 2173 FT /note="P -> S (in dbSNP:rs200675829)" FT /evidence="ECO:0000269|PubMed:12891677" FT /id="VAR_045955" FT CONFLICT 7 FT /note="A -> S (in Ref. 5; AC120498)" FT /evidence="ECO:0000305" FT CONFLICT 31 FT /note="E -> K (in Ref. 5; AC120498)" FT /evidence="ECO:0000305" FT CONFLICT 55 FT /note="A -> S (in Ref. 5; AC120498)" FT /evidence="ECO:0000305" FT CONFLICT 94 FT /note="L -> V (in Ref. 5; AC120498)" FT /evidence="ECO:0000305" FT CONFLICT 215 FT /note="S -> T (in Ref. 6; CAC42094)" FT /evidence="ECO:0000305" FT CONFLICT O95180-2:1587 FT /note="K -> E (in Ref. 4; CAD12646)" FT /evidence="ECO:0000305" SQ 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 //