O95180 (CAC1H_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Voltage-dependent T-type calcium channel subunit alpha-1H

Alternative name(s):
Low-voltage-activated calcium channel alpha1 3.2 subunit
Voltage-gated calcium channel subunit alpha Cav3.2

Gene names

Name:

CACNA1H

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2353 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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.
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	Expressed in kidney, liver, heart, brain. Isoform 2 seems to be testis-specific.
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.
Post-translational modification	In response to raising of intracellular calcium, the T-type channels are activated by CaM-kinase II.
Involvement in 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. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. 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. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.9
Sequence similarities	Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family. CACNA1H subfamily. [View classification]
Sequence caution	The sequence AAK61268.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAC42094.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Epilepsy
Domain	Repeat Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding Zinc
Molecular function	Calcium channel Ion channel Voltage-gated channel
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aldosterone biosynthetic process Inferred from mutant phenotype PubMed 19342457. Source: UniProtKB axon guidance Traceable author statement. Source: Reactome calcium ion import Inferred from direct assay PubMed 21084288. Source: BHF-UCL cellular response to hormone stimulus Inferred from expression pattern PubMed 19342457. Source: UniProtKB cellular response to potassium ion Inferred from expression pattern PubMed 19342457. Source: UniProtKB cortisol biosynthetic process Inferred from mutant phenotype PubMed 19342457. Source: UniProtKB muscle contraction Traceable author statement Ref.1. Source: ProtInc myoblast fusion Traceable author statement PubMed 10861024. Source: ProtInc positive regulation of acrosome reaction Inferred from mutant phenotype PubMed 20394732. Source: UniProtKB regulation of heart contraction Traceable author statement Ref.1. Source: ProtInc regulation of membrane potential Inferred from direct assay PubMed 21084288. Source: BHF-UCL
Cellular_component	caveola Inferred from electronic annotation. Source: Compara sarcolemma Inferred from electronic annotation. Source: Compara voltage-gated calcium channel complex Traceable author statement PubMed 10861024. Source: ProtInc
Molecular_function	low voltage-gated calcium channel activity Inferred from direct assay PubMed 21084288. Source: BHF-UCL metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O95180-1)

Also known as: A1H-a;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O95180-2)

Also known as: A1H-b;

The sequence of this isoform differs from the canonical sequence as follows:
     1587-1593: STFPSPE → K

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2353	2353	Voltage-dependent T-type calcium channel subunit alpha-1H		PRO_0000053954
Regions
	Topological domain	1 – 100	100	Cytoplasmic Potential
	Transmembrane	101 – 119	19	Helical; Name=S1 of repeat I; Potential
	Topological domain	120 – 141	22	Extracellular Potential
	Transmembrane	142 – 160	19	Helical; Name=S2 of repeat I; Potential
	Topological domain	161 – 169	9	Cytoplasmic Potential
	Transmembrane	170 – 184	15	Helical; Name=S3 of repeat I; Potential
	Topological domain	185 – 193	9	Extracellular Potential
	Transmembrane	194 – 212	19	Helical; Name=S4 of repeat I; Potential
	Topological domain	213 – 232	20	Cytoplasmic Potential
	Transmembrane	233 – 253	21	Helical; Name=S5 of repeat I; Potential
	Topological domain	254 – 394	141	Extracellular Potential
	Transmembrane	395 – 419	25	Helical; Name=S6 of repeat I; Potential
	Topological domain	420 – 793	374	Cytoplasmic Potential
	Transmembrane	794 – 814	21	Helical; Name=S1 of repeat II; Potential
	Topological domain	815 – 827	13	Extracellular Potential
	Transmembrane	828 – 849	22	Helical; Name=S2 of repeat II; Potential
	Topological domain	850 – 855	6	Cytoplasmic Potential
	Transmembrane	856 – 874	19	Helical; Name=S3 of repeat II; Potential
	Topological domain	875 – 882	8	Extracellular Potential
	Transmembrane	883 – 906	24	Helical; Name=S4 of repeat II; Potential
	Topological domain	907 – 917	11	Cytoplasmic Potential
	Transmembrane	918 – 938	21	Helical; Name=S5 of repeat II; Potential
	Topological domain	939 – 990	52	Extracellular Potential
	Transmembrane	991 – 1015	25	Helical; Name=S6 of repeat II; Potential
	Topological domain	1016 – 1290	275	Cytoplasmic Potential
	Transmembrane	1291 – 1313	23	Helical; Name=S1 of repeat III; Potential
	Topological domain	1314 – 1331	18	Extracellular Potential
	Transmembrane	1332 – 1352	21	Helical; Name=S2 of repeat III; Potential
	Topological domain	1353 – 1362	10	Cytoplasmic Potential
	Transmembrane	1363 – 1382	20	Helical; Name=S3 of repeat III; Potential
	Topological domain	1383 – 1396	14	Extracellular Potential
	Transmembrane	1397 – 1418	22	Helical; Name=S4 of repeat III; Potential
	Topological domain	1419 – 1428	10	Cytoplasmic Potential
	Transmembrane	1429 – 1452	24	Helical; Name=S5 of repeat III; Potential
	Topological domain	1453 – 1529	77	Extracellular Potential
	Transmembrane	1530 – 1555	26	Helical; Name=S6 of repeat III; Potential
	Topological domain	1556 – 1616	61	Cytoplasmic Potential
	Transmembrane	1617 – 1637	21	Helical; Name=S1 of repeat IV; Potential
	Topological domain	1638 – 1651	14	Extracellular Potential
	Transmembrane	1652 – 1673	22	Helical; Name=S2 of repeat IV; Potential
	Topological domain	1674 – 1680	7	Cytoplasmic Potential
	Transmembrane	1681 – 1699	19	Helical; Name=S3 of repeat IV; Potential
	Topological domain	1700 – 1713	14	Extracellular Potential
	Transmembrane	1714 – 1737	24	Helical; Name=S4 of repeat IV; Potential
	Topological domain	1738 – 1751	14	Cytoplasmic Potential
	Transmembrane	1752 – 1772	21	Helical; Name=S5 of repeat IV; Potential
	Topological domain	1773 – 1835	63	Extracellular Potential
	Transmembrane	1836 – 1863	28	Helical; Name=S6 of repeat IV; Potential
	Topological domain	1864 – 2353	490	Cytoplasmic Potential
	Repeat	87 – 422	336	I
	Repeat	779 – 1018	240	II
	Repeat	1281 – 1558	278	III
	Repeat	1602 – 1863	262	IV
	Compositional bias	520 – 530	11	Poly-His
	Compositional bias	1107 – 1110	4	Poly-Ser
	Compositional bias	1583 – 1586	4	Poly-Arg
Sites
	Metal binding	140	1	Zinc
	Metal binding	189	1	Zinc
	Metal binding	191	1	Zinc
	Site	378	1	Calcium ion selectivity and permeability By similarity
	Site	974	1	Calcium ion selectivity and permeability By similarity
	Site	1504	1	Calcium ion selectivity and permeability By similarity
	Site	1808	1	Calcium ion selectivity and permeability By similarity
Amino acid modifications
	Glycosylation	192	1	N-linked (GlcNAc...) Potential
	Glycosylation	271	1	N-linked (GlcNAc...) Potential
	Glycosylation	1466	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	1587 – 1593	7	STFPSPE → K in isoform 2.		VSP_000949
	Natural variant	161	1	F → L in ECA6. Ref.9		VAR_045935
	Natural variant	282	1	E → K in ECA6. Ref.9		VAR_045936
	Natural variant	313	1	M → V. Ref.5 Ref.6 Ref.9 Corresponds to variant rs36117280 [ dbSNP | Ensembl ].		VAR_045937
	Natural variant	456	1	C → S in ECA6. Ref.9		VAR_045938
	Natural variant	499	1	G → S in ECA6. Ref.9		VAR_045939
	Natural variant	618	1	P → L in IGE6. Ref.10		VAR_066986
	Natural variant	640	1	P → L. Ref.7 Ref.9		VAR_045940
	Natural variant	648	1	P → L in ECA6. Ref.9		VAR_045941
	Natural variant	664	1	V → A. Ref.1 Ref.4 Ref.9 Corresponds to variant rs4984636 [ dbSNP | Ensembl ].		VAR_045942
	Natural variant	684	1	P → S. Ref.9		VAR_045943
	Natural variant	744	1	R → Q in ECA6. Ref.9		VAR_045944
	Natural variant	748	1	A → V in ECA6. Ref.9		VAR_045945
	Natural variant	755	1	G → D in IGE6. Ref.10		VAR_066987
	Natural variant	773	1	G → D in ECA6. Ref.9		VAR_045946
	Natural variant	784	1	G → S in ECA6. Ref.9		VAR_045947
	Natural variant	788	1	R → C. Ref.9 Corresponds to variant rs3751664 [ dbSNP | Ensembl ].		VAR_045948
	Natural variant	812	1	V → M. Corresponds to variant rs28365119 [ dbSNP | Ensembl ].		VAR_045949
	Natural variant	831	1	V → M in ECA6. Ref.9		VAR_045950
	Natural variant	848	1	G → S in ECA6. Ref.9		VAR_045951
	Natural variant	1463	1	D → N in ECA6. Ref.9		VAR_045952
	Natural variant	1871	1	R → Q. Corresponds to variant rs58124832 [ dbSNP | Ensembl ].		VAR_061104
	Natural variant	1974	1	E → G. Corresponds to variant rs3751886 [ dbSNP | Ensembl ].		VAR_033698
	Natural variant	2060	1	R → H. Ref.5 Ref.9 Corresponds to variant rs1054644 [ dbSNP | Ensembl ].		VAR_045953
	Natural variant	2077	1	R → H. Ref.3 Ref.7 Ref.9 Corresponds to variant rs1054645 [ dbSNP | Ensembl ].		VAR_045954
	Natural variant	2173	1	P → S. Ref.9		VAR_045955
Experimental info
	Sequence conflict	7	1	A → S in AC120498. Ref.5
	Sequence conflict	31	1	E → K in AC120498. Ref.5
	Sequence conflict	55	1	A → S in AC120498. Ref.5
	Sequence conflict	94	1	L → V in AC120498. Ref.5
	Sequence conflict	215	1	S → T in CAC42094. Ref.6
Isoform 2:
	Sequence conflict	1587	1	K → E in CAD12646. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (A1H-a) [UniParc]. Last modified September 19, 2002. Version 4. Checksum: E13E270635173D98	FASTA	2,353	259,163
	10 20 30 40 50 60 MTEGARAADE VRVPLGAPPP GPAALVGASP ESPGAPGREA ERGSELGVSP SESPAAERGA 70 80 90 100 110 120 ELGADEEQRV PYPALAATVF FCLGQTTRPR SWCLRLVCNP WFEHVSMLVI MLNCVTLGMF 130 140 150 160 170 180 RPCEDVECGS ERCNILEAFD AFIFAFFAVE MVIKMVALGL FGQKCYLGDT WNRLDFFIVV 190 200 210 220 230 240 AGMMEYSLDG HNVSLSAIRT VRVLRPLRAI NRVPSMRILV TLLLDTLPML GNVLLLCFFV 250 260 270 280 290 300 FFIFGIVGVQ LWAGLLRNRC FLDSAFVRNN NLTFLRPYYQ TEEGEENPFI CSSRRDNGMQ 310 320 330 340 350 360 KCSHIPGRRE LRMPCTLGWE AYTQPQAEGV GAARNACINW NQYYNVCRSG DSNPHNGAIN 370 380 390 400 410 420 FDNIGYAWIA IFQVITLEGW VDIMYYVMDA HSFYNFIYFI LLIIVGSFFM INLCLVVIAT 430 440 450 460 470 480 QFSETKQRES QLMREQRARH LSNDSTLASF SEPGSCYEEL LKYVGHIFRK VKRRSLRLYA 490 500 510 520 530 540 RWQSRWRKKV DPSAVQGQGP GHRQRRAGRH TASVHHLVYH HHHHHHHHYH FSHGSPRRPG 550 560 570 580 590 600 PEPGACDTRL VRAGAPPSPP SPGRGPPDAE SVHSIYHADC HIEGPQERAR VAHAAATAAA 610 620 630 640 650 660 SLRLATGLGT MNYPTILPSG VGSGKGSTSP GPKGKWAGGP PGTGGHGPLS LNSPDPYEKI 670 680 690 700 710 720 PHVVGEHGLG QAPGHLSGLS VPCPLPSPPA GTLTCELKSC PYCTRALEDP EGELSGSESG 730 740 750 760 770 780 DSDGRGVYEF TQDVRHGDRW DPTRPPRATD TPGPGPGSPQ RRAQQRAAPG EPGWMGRLWV 790 800 810 820 830 840 TFSGKLRRIV DSKYFSRGIM MAILVNTLSM GVEYHEQPEE LTNALEISNI VFTSMFALEM 850 860 870 880 890 900 LLKLLACGPL GYIRNPYNIF DGIIVVISVW EIVGQADGGL SVLRTFRLLR VLKLVRFLPA 910 920 930 940 950 960 LRRQLVVLVK TMDNVATFCT LLMLFIFIFS ILGMHLFGCK FSLKTDTGDT VPDRKNFDSL 970 980 990 1000 1010 1020 LWAIVTVFQI LTQEDWNVVL YNGMASTSSW AALYFVALMT FGNYVLFNLL VAILVEGFQA 1030 1040 1050 1060 1070 1080 EGDANRSDTD EDKTSVHFEE DFHKLRELQT TELKMCSLAV TPNGHLEGRG SLSPPLIMCT 1090 1100 1110 1120 1130 1140 AATPMPTPKS SPFLDAAPSL PDSRRGSSSS GDPPLGDQKP PASLRSSPCA PWGPSGAWSS 1150 1160 1170 1180 1190 1200 RRSSWSSLGR APSLKRRGQC GERESLLSGE GKGSTDDEAE DGRAAPGPRA TPLRRAESLD 1210 1220 1230 1240 1250 1260 PRPLRPAALP PTKCRDRDGQ VVALPSDFFL RIDSHREDAA ELDDDSEDSC CLRLHKVLEP 1270 1280 1290 1300 1310 1320 YKPQWCRSRE AWALYLFSPQ NRFRVSCQKV ITHKMFDHVV LVFIFLNCVT IALERPDIDP 1330 1340 1350 1360 1370 1380 GSTERVFLSV SNYIFTAIFV AEMMVKVVAL GLLSGEHAYL QSSWNLLDGL LVLVSLVDIV 1390 1400 1410 1420 1430 1440 VAMASAGGAK ILGVLRVLRL LRTLRPLRVI SRAPGLKLVV ETLISSLRPI GNIVLICCAF 1450 1460 1470 1480 1490 1500 FIIFGILGVQ LFKGKFYYCE GPDTRNISTK AQCRAAHYRW VRRKYNFDNL GQALMSLFVL 1510 1520 1530 1540 1550 1560 SSKDGWVNIM YDGLDAVGVD QQPVQNHNPW MLLYFISFLL IVSFFVLNMF VGVVVENFHK 1570 1580 1590 1600 1610 1620 CRQHQEAEEA RRREEKRLRR LERRRRSTFP SPEAQRRPYY ADYSPTRRSI HSLCTSHYLD 1630 1640 1650 1660 1670 1680 LFITFIICVN VITMSMEHYN QPKSLDEALK YCNYVFTIVF VFEAALKLVA FGFRRFFKDR 1690 1700 1710 1720 1730 1740 WNQLDLAIVL LSLMGITLEE IEMSAALPIN PTIIRIMRVL RIARVLKLLK MATGMRALLD 1750 1760 1770 1780 1790 1800 TVVQALPQVG NLGLLFMLLF FIYAALGVEL FGRLECSEDN PCEGLSRHAT FSNFGMAFLT 1810 1820 1830 1840 1850 1860 LFRVSTGDNW NGIMKDTLRE CSREDKHCLS YLPALSPVYF VTFVLVAQFV LVNVVVAVLM 1870 1880 1890 1900 1910 1920 KHLEESNKEA REDAELDAEI ELEMAQGPGS ARRVDADRPP LPQESPGARD APNLVARKVS 1930 1940 1950 1960 1970 1980 VSRMLSLPND SYMFRPVVPA SAPHPRPLQE VEMETYGAGT PLGSVASVHS PPAESCASLQ 1990 2000 2010 2020 2030 2040 IPLAVSSPAR SGEPLHALSP RGTARSPSLS RLLCRQEAVH TDSLEGKIDS PRDTLDPAEP 2050 2060 2070 2080 2090 2100 GEKTPVRPVT QGGSLQSPPR SPRPASVRTR KHTFGQRCVS SRPAAPGGEE AEASDPADEE 2110 2120 2130 2140 2150 2160 VSHITSSACP WQPTAEPHGP EASPVAGGER DLRRLYSVDA QGFLDKPGRA DEQWRPSAEL 2170 2180 2190 2200 2210 2220 GSGEPGEAKA WGPEAEPALG ARRKKKMSPP CISVEPPAED EGSARPSAAE GGSTTLRRRT 2230 2240 2250 2260 2270 2280 PSCEATPHRD SLEPTEGSGA GGDPAAKGER WGQASCRAEH LTVPSFAFEP LDLGVPSGDP 2290 2300 2310 2320 2330 2340 FLDGSHSVTP ESRASSSGAI VPLEPPESEP PMPVGDPPEK RRGLYLTVPQ CPLEKPGSPS 2350 ATPAPGGGAD DPV
	Isoform 2 (A1H-b) [UniParc]. Checksum: 92C26CC4852C3E0A	FASTA	2,347	258,545
	10 20 30 40 50 60 MTEGARAADE VRVPLGAPPP GPAALVGASP ESPGAPGREA ERGSELGVSP SESPAAERGA 70 80 90 100 110 120 ELGADEEQRV PYPALAATVF FCLGQTTRPR SWCLRLVCNP WFEHVSMLVI MLNCVTLGMF 130 140 150 160 170 180 RPCEDVECGS ERCNILEAFD AFIFAFFAVE MVIKMVALGL FGQKCYLGDT WNRLDFFIVV 190 200 210 220 230 240 AGMMEYSLDG HNVSLSAIRT VRVLRPLRAI NRVPSMRILV TLLLDTLPML GNVLLLCFFV 250 260 270 280 290 300 FFIFGIVGVQ LWAGLLRNRC FLDSAFVRNN NLTFLRPYYQ TEEGEENPFI CSSRRDNGMQ 310 320 330 340 350 360 KCSHIPGRRE LRMPCTLGWE AYTQPQAEGV GAARNACINW NQYYNVCRSG DSNPHNGAIN 370 380 390 400 410 420 FDNIGYAWIA IFQVITLEGW VDIMYYVMDA HSFYNFIYFI LLIIVGSFFM INLCLVVIAT 430 440 450 460 470 480 QFSETKQRES QLMREQRARH LSNDSTLASF SEPGSCYEEL LKYVGHIFRK VKRRSLRLYA 490 500 510 520 530 540 RWQSRWRKKV DPSAVQGQGP GHRQRRAGRH TASVHHLVYH HHHHHHHHYH FSHGSPRRPG 550 560 570 580 590 600 PEPGACDTRL VRAGAPPSPP SPGRGPPDAE SVHSIYHADC HIEGPQERAR VAHAAATAAA 610 620 630 640 650 660 SLRLATGLGT MNYPTILPSG VGSGKGSTSP GPKGKWAGGP PGTGGHGPLS LNSPDPYEKI 670 680 690 700 710 720 PHVVGEHGLG QAPGHLSGLS VPCPLPSPPA GTLTCELKSC PYCTRALEDP EGELSGSESG 730 740 750 760 770 780 DSDGRGVYEF TQDVRHGDRW DPTRPPRATD TPGPGPGSPQ RRAQQRAAPG EPGWMGRLWV 790 800 810 820 830 840 TFSGKLRRIV DSKYFSRGIM MAILVNTLSM GVEYHEQPEE LTNALEISNI VFTSMFALEM 850 860 870 880 890 900 LLKLLACGPL GYIRNPYNIF DGIIVVISVW EIVGQADGGL SVLRTFRLLR VLKLVRFLPA 910 920 930 940 950 960 LRRQLVVLVK TMDNVATFCT LLMLFIFIFS ILGMHLFGCK FSLKTDTGDT VPDRKNFDSL 970 980 990 1000 1010 1020 LWAIVTVFQI LTQEDWNVVL YNGMASTSSW AALYFVALMT FGNYVLFNLL VAILVEGFQA 1030 1040 1050 1060 1070 1080 EGDANRSDTD EDKTSVHFEE DFHKLRELQT TELKMCSLAV TPNGHLEGRG SLSPPLIMCT 1090 1100 1110 1120 1130 1140 AATPMPTPKS SPFLDAAPSL PDSRRGSSSS GDPPLGDQKP PASLRSSPCA PWGPSGAWSS 1150 1160 1170 1180 1190 1200 RRSSWSSLGR APSLKRRGQC GERESLLSGE GKGSTDDEAE DGRAAPGPRA TPLRRAESLD 1210 1220 1230 1240 1250 1260 PRPLRPAALP PTKCRDRDGQ VVALPSDFFL RIDSHREDAA ELDDDSEDSC CLRLHKVLEP 1270 1280 1290 1300 1310 1320 YKPQWCRSRE AWALYLFSPQ NRFRVSCQKV ITHKMFDHVV LVFIFLNCVT IALERPDIDP 1330 1340 1350 1360 1370 1380 GSTERVFLSV SNYIFTAIFV AEMMVKVVAL GLLSGEHAYL QSSWNLLDGL LVLVSLVDIV 1390 1400 1410 1420 1430 1440 VAMASAGGAK ILGVLRVLRL LRTLRPLRVI SRAPGLKLVV ETLISSLRPI GNIVLICCAF 1450 1460 1470 1480 1490 1500 FIIFGILGVQ LFKGKFYYCE GPDTRNISTK AQCRAAHYRW VRRKYNFDNL GQALMSLFVL 1510 1520 1530 1540 1550 1560 SSKDGWVNIM YDGLDAVGVD QQPVQNHNPW MLLYFISFLL IVSFFVLNMF VGVVVENFHK 1570 1580 1590 1600 1610 1620 CRQHQEAEEA RRREEKRLRR LERRRRKAQR RPYYADYSPT RRSIHSLCTS HYLDLFITFI 1630 1640 1650 1660 1670 1680 ICVNVITMSM EHYNQPKSLD EALKYCNYVF TIVFVFEAAL KLVAFGFRRF FKDRWNQLDL 1690 1700 1710 1720 1730 1740 AIVLLSLMGI TLEEIEMSAA LPINPTIIRI MRVLRIARVL KLLKMATGMR ALLDTVVQAL 1750 1760 1770 1780 1790 1800 PQVGNLGLLF MLLFFIYAAL GVELFGRLEC SEDNPCEGLS RHATFSNFGM AFLTLFRVST 1810 1820 1830 1840 1850 1860 GDNWNGIMKD TLRECSREDK HCLSYLPALS PVYFVTFVLV AQFVLVNVVV AVLMKHLEES 1870 1880 1890 1900 1910 1920 NKEAREDAEL DAEIELEMAQ GPGSARRVDA DRPPLPQESP GARDAPNLVA RKVSVSRMLS 1930 1940 1950 1960 1970 1980 LPNDSYMFRP VVPASAPHPR PLQEVEMETY GAGTPLGSVA SVHSPPAESC ASLQIPLAVS 1990 2000 2010 2020 2030 2040 SPARSGEPLH ALSPRGTARS PSLSRLLCRQ EAVHTDSLEG KIDSPRDTLD PAEPGEKTPV 2050 2060 2070 2080 2090 2100 RPVTQGGSLQ SPPRSPRPAS VRTRKHTFGQ RCVSSRPAAP GGEEAEASDP ADEEVSHITS 2110 2120 2130 2140 2150 2160 SACPWQPTAE PHGPEASPVA GGERDLRRLY SVDAQGFLDK PGRADEQWRP SAELGSGEPG 2170 2180 2190 2200 2210 2220 EAKAWGPEAE PALGARRKKK MSPPCISVEP PAEDEGSARP SAAEGGSTTL RRRTPSCEAT 2230 2240 2250 2260 2270 2280 PHRDSLEPTE GSGAGGDPAA KGERWGQASC RAEHLTVPSF AFEPLDLGVP SGDPFLDGSH 2290 2300 2310 2320 2330 2340 SVTPESRASS SGAIVPLEPP ESEPPMPVGD PPEKRRGLYL TVPQCPLEKP GSPSATPAPG GGADDPV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of alpha1H from human heart, a member of the T-type Ca2+ channel gene family." 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. Circ. Res. 83:103-109(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-664. Tissue: Heart.
[2]	Cribbs L.L., Lee J.-H., Yang J., Daud A.N., Perez-Reyes E. Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Structure and functional characterization of a novel human low-voltage activated calcium channel." Williams M.E., Washburn M.S., Hans M., Urrutia A., Brust P.F., Prodanovich P., Harpold M.M., Stauderman K.A. J. Neurochem. 72:791-799(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT HIS-2077. Tissue: Thyroid carcinoma.
[4]	"Identification and localization of T-type voltage-operated calcium channel subunits in human male germ cells. Expression of multiple isoforms." Jagannathan S., Punt E.L., Gu Y., Arnoult C., Sakkas D., Barratt C.L., Publicover S.J. J. Biol. Chem. 277:8449-8456(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ALA-664. Tissue: Testis.
[5]	"Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16." 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. Hum. Mol. Genet. 10:339-352(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS VAL-313 AND HIS-2060.
[6]	"The sequence and analysis of duplication-rich human chromosome 16." 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. Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-313.
[7]	"Organization and alternative splicing of CACNA1H." Mittman S., Agnew W.S. Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 424-661 AND 838-2373 (ISOFORM 1), VARIANTS LEU-640 AND HIS-2077.
[8]	"Structural determinants of the high affinity extracellular zinc binding site on Cav3.2 T-type calcium channels." Kang H.W., Vitko I., Lee S.S., Perez-Reyes E., Lee J.H. J. Biol. Chem. 285:3271-3281(2010) [PubMed] [Europe PMC] [Abstract] Cited for: ZINC-BINDING SITES.
[9]	"Association between genetic variation of CACNA1H and childhood absence epilepsy." 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. Ann. Neurol. 54:239-243(2003) [PubMed] [Europe PMC] [Abstract] Cited for: 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, VARIANTS VAL-313; LEU-640; ALA-664; SER-684; CYS-788; HIS-2060; HIS-2077 AND SER-2173.
[10]	"Genetic variation of CACNA1H in idiopathic generalized epilepsy." Heron S.E., Phillips H.A., Mulley J.C., Mazarib A., Neufeld M.Y., Berkovic S.F., Scheffer I.E. Ann. Neurol. 55:595-596(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS IGE6 LEU-618 AND ASP-755.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF051946 mRNA. Translation: AAC67239.3. AF073931 mRNA. Translation: AAD17668.1. AJ420779 mRNA. Translation: CAD12646.1. AE006466 Genomic DNA. Translation: AAK61268.1. Sequence problems. AL031703 Genomic DNA. Translation: CAC42094.1. Sequence problems. AC120498 Genomic DNA. No translation available. AF223562 Genomic DNA. Translation: AAF60162.1. AF223563 Genomic DNA. Translation: AAF60163.1.
IPI	IPI00028915. IPI00288892.
RefSeq	NP_001005407.1. NM_001005407.1. NP_066921.2. NM_021098.2.
UniGene	Hs.459642.
3D structure databases
ProteinModelPortal	O95180.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000334198.
Protein family/group databases
TCDB	1.A.1.11.5. voltage-gated ion channel (VIC) superfamily.
PTM databases
PhosphoSite	O95180.
Proteomic databases
PaxDb	O95180.
PRIDE	O95180.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000348261; ENSP00000334198; ENSG00000196557. ENST00000358590; ENSP00000351401; ENSG00000196557. ENST00000565831; ENSP00000455840; ENSG00000196557.
GeneID	8912.
KEGG	hsa:8912.
UCSC	uc002cks.3. human.
Organism-specific databases
CTD	8912.
GeneCards	GC16P001203.
H-InvDB	HIX0038538.
HGNC	HGNC:1395. CACNA1H.
HPA	HPA039125.
MIM	607904. gene. 611942. phenotype.
neXtProt	NX_O95180.
Orphanet	64280. Childhood absence epilepsy.
PharmGKB	PA380.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1226.
HOVERGEN	HBG050764.
InParanoid	O95180.
KO	K04855.
OMA	PDPYEKI.
Enzyme and pathway databases
Reactome	REACT_111045. Developmental Biology.
Gene expression databases
ArrayExpress	O95180.
Bgee	O95180.
CleanEx	HS_CACNA1H.
Genevestigator	O95180.
GermOnline	ENSG00000196557. Homo sapiens.
Family and domain databases
InterPro	IPR005821. Ion_trans_dom. IPR005445. VDCC_T_a1su. [Graphical view]
Pfam	PF00520. Ion_trans. 4 hits. [Graphical view]
PRINTS	PR01629. TVDCCALPHA1.
ProtoNet	Search...
Other
BindingDB	O95180.
ChEMBL	CHEMBL1859.
ChiTaRS	CACNA1H. human.
DrugBank	DB04841. Flunarizine. DB01388. Mibefradil.
GenomeRNAi	8912.
NextBio	33494.
SOURCE	Search...

Entry information

Entry name

CAC1H_HUMAN

Accession

Primary (citable) accession number: O95180
Secondary accession number(s): B5ME00 , F8WFD1, O95802, Q8WWI6, Q96QI6, Q96RZ9, Q9NYY4, Q9NYY5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	September 19, 2002
Last modified:	May 1, 2013
This is version 125 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.