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O95180 (CAC1H_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2353 AA.
Sequence statusComplete.
Protein existenceEvidence 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-1Hgives 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 processCalcium transport
Ion transport
Transport
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Epilepsy
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
Zinc
   Molecular functionCalcium channel
Ion channel
Voltage-gated channel
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaldosterone 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

membrane depolarization during action potential

Inferred from Biological aspect of Ancestor. Source: RefGenome

muscle contraction

Traceable author statement Ref.1. Source: ProtInc

muscle organ development

Non-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

transport

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcaveola

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from direct assay PubMed 21084288. Source: BHF-UCL

plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

sarcolemma

Inferred from electronic annotation. Source: Ensembl

voltage-gated calcium channel complex

Traceable author statement PubMed 10861024. Source: ProtInc

   Molecular_functionlow voltage-gated calcium channel activity

Inferred from direct assay PubMed 21084288. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

scaffold protein binding

Inferred from physical interaction PubMed 21084288. Source: BHF-UCL

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 23532353Voltage-dependent T-type calcium channel subunit alpha-1H
PRO_0000053954

Regions

Topological domain1 – 100100Cytoplasmic Potential
Transmembrane101 – 11919Helical; Name=S1 of repeat I; Potential
Topological domain120 – 14122Extracellular Potential
Transmembrane142 – 16019Helical; Name=S2 of repeat I; Potential
Topological domain161 – 1699Cytoplasmic Potential
Transmembrane170 – 18415Helical; Name=S3 of repeat I; Potential
Topological domain185 – 1939Extracellular Potential
Transmembrane194 – 21219Helical; Name=S4 of repeat I; Potential
Topological domain213 – 23220Cytoplasmic Potential
Transmembrane233 – 25321Helical; Name=S5 of repeat I; Potential
Topological domain254 – 394141Extracellular Potential
Transmembrane395 – 41925Helical; Name=S6 of repeat I; Potential
Topological domain420 – 793374Cytoplasmic Potential
Transmembrane794 – 81421Helical; Name=S1 of repeat II; Potential
Topological domain815 – 82713Extracellular Potential
Transmembrane828 – 84922Helical; Name=S2 of repeat II; Potential
Topological domain850 – 8556Cytoplasmic Potential
Transmembrane856 – 87419Helical; Name=S3 of repeat II; Potential
Topological domain875 – 8828Extracellular Potential
Transmembrane883 – 90624Helical; Name=S4 of repeat II; Potential
Topological domain907 – 91711Cytoplasmic Potential
Transmembrane918 – 93821Helical; Name=S5 of repeat II; Potential
Topological domain939 – 99052Extracellular Potential
Transmembrane991 – 101525Helical; Name=S6 of repeat II; Potential
Topological domain1016 – 1290275Cytoplasmic Potential
Transmembrane1291 – 131323Helical; Name=S1 of repeat III; Potential
Topological domain1314 – 133118Extracellular Potential
Transmembrane1332 – 135221Helical; Name=S2 of repeat III; Potential
Topological domain1353 – 136210Cytoplasmic Potential
Transmembrane1363 – 138220Helical; Name=S3 of repeat III; Potential
Topological domain1383 – 139614Extracellular Potential
Transmembrane1397 – 141822Helical; Name=S4 of repeat III; Potential
Topological domain1419 – 142810Cytoplasmic Potential
Transmembrane1429 – 145224Helical; Name=S5 of repeat III; Potential
Topological domain1453 – 152977Extracellular Potential
Transmembrane1530 – 155526Helical; Name=S6 of repeat III; Potential
Topological domain1556 – 161661Cytoplasmic Potential
Transmembrane1617 – 163721Helical; Name=S1 of repeat IV; Potential
Topological domain1638 – 165114Extracellular Potential
Transmembrane1652 – 167322Helical; Name=S2 of repeat IV; Potential
Topological domain1674 – 16807Cytoplasmic Potential
Transmembrane1681 – 169919Helical; Name=S3 of repeat IV; Potential
Topological domain1700 – 171314Extracellular Potential
Transmembrane1714 – 173724Helical; Name=S4 of repeat IV; Potential
Topological domain1738 – 175114Cytoplasmic Potential
Transmembrane1752 – 177221Helical; Name=S5 of repeat IV; Potential
Topological domain1773 – 183563Extracellular Potential
Transmembrane1836 – 186328Helical; Name=S6 of repeat IV; Potential
Topological domain1864 – 2353490Cytoplasmic Potential
Repeat87 – 422336I
Repeat779 – 1018240II
Repeat1281 – 1558278III
Repeat1602 – 1863262IV
Compositional bias520 – 53011Poly-His
Compositional bias1107 – 11104Poly-Ser
Compositional bias1583 – 15864Poly-Arg

Sites

Metal binding1401Zinc
Metal binding1891Zinc
Metal binding1911Zinc
Site3781Calcium ion selectivity and permeability By similarity
Site9741Calcium ion selectivity and permeability By similarity
Site15041Calcium ion selectivity and permeability By similarity
Site18081Calcium ion selectivity and permeability By similarity

Amino acid modifications

Glycosylation1921N-linked (GlcNAc...) Potential
Glycosylation2711N-linked (GlcNAc...) Potential
Glycosylation14661N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1587 – 15937STFPSPE → K in isoform 2.
VSP_000949
Natural variant1611F → L in ECA6. Ref.9
VAR_045935
Natural variant2821E → K in ECA6. Ref.9
VAR_045936
Natural variant3131M → V. Ref.5 Ref.6 Ref.9
Corresponds to variant rs36117280 [ dbSNP | Ensembl ].
VAR_045937
Natural variant4561C → S in ECA6. Ref.9
VAR_045938
Natural variant4991G → S in ECA6. Ref.9
VAR_045939
Natural variant6181P → L in IGE6. Ref.10
Corresponds to variant rs60734921 [ dbSNP | Ensembl ].
VAR_066986
Natural variant6401P → L. Ref.7 Ref.9
Corresponds to variant rs61734410 [ dbSNP | Ensembl ].
VAR_045940
Natural variant6481P → L in ECA6. Ref.9
VAR_045941
Natural variant6641V → A. Ref.1 Ref.4 Ref.9
Corresponds to variant rs4984636 [ dbSNP | Ensembl ].
VAR_045942
Natural variant6841P → S. Ref.9
VAR_045943
Natural variant7441R → Q in ECA6. Ref.9
VAR_045944
Natural variant7481A → V in ECA6. Ref.9
VAR_045945
Natural variant7551G → D in IGE6. Ref.10
Corresponds to variant rs142306293 [ dbSNP | Ensembl ].
VAR_066987
Natural variant7731G → D in ECA6. Ref.9
VAR_045946
Natural variant7841G → S in ECA6. Ref.9
VAR_045947
Natural variant7881R → C. Ref.9
Corresponds to variant rs3751664 [ dbSNP | Ensembl ].
VAR_045948
Natural variant8121V → M.
Corresponds to variant rs28365119 [ dbSNP | Ensembl ].
VAR_045949
Natural variant8311V → M in ECA6. Ref.9
VAR_045950
Natural variant8481G → S in ECA6. Ref.9
VAR_045951
Natural variant14631D → N in ECA6. Ref.9
VAR_045952
Natural variant18711R → Q.
Corresponds to variant rs58124832 [ dbSNP | Ensembl ].
VAR_061104
Natural variant19741E → G.
Corresponds to variant rs3751886 [ dbSNP | Ensembl ].
VAR_033698
Natural variant20601R → H. Ref.5 Ref.9
Corresponds to variant rs1054644 [ dbSNP | Ensembl ].
VAR_045953
Natural variant20771R → H. Ref.3 Ref.7 Ref.9
Corresponds to variant rs1054645 [ dbSNP | Ensembl ].
VAR_045954
Natural variant21731P → S. Ref.9
Corresponds to variant rs200675829 [ dbSNP | Ensembl ].
VAR_045955

Experimental info

Sequence conflict71A → S in AC120498. Ref.5
Sequence conflict311E → K in AC120498. Ref.5
Sequence conflict551A → S in AC120498. Ref.5
Sequence conflict941L → V in AC120498. Ref.5
Sequence conflict2151S → T in CAC42094. Ref.6
Isoform 2:
Sequence conflict15871K → E in CAD12646. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (A1H-a) [UniParc].

Last modified September 19, 2002. Version 4.
Checksum: E13E270635173D98

FASTA2,353259,163
        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 

« Hide

Isoform 2 (A1H-b) [UniParc].

Checksum: 92C26CC4852C3E0A
Show »

FASTA2,347258,545

References

« Hide '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. expand/collapse author list , 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.
CCDSCCDS45375.1. [O95180-1]
CCDS45376.1. [O95180-2]
RefSeqNP_001005407.1. NM_001005407.1. [O95180-2]
NP_066921.2. NM_021098.2. [O95180-1]
UniGeneHs.459642.

3D structure databases

ProteinModelPortalO95180.
SMRO95180. Positions 96-253, 361-431, 795-1031, 1296-1583, 1623-1875.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114426. 3 interactions.
IntActO95180. 2 interactions.
STRING9606.ENSP00000334198.

Chemistry

BindingDBO95180.
ChEMBLCHEMBL2363032.
DrugBankDB04841. Flunarizine.
DB01388. Mibefradil.
GuidetoPHARMACOLOGY536.

Protein family/group databases

TCDB1.A.1.11.5. the voltage-gated ion channel (vic) superfamily.

PTM databases

PhosphoSiteO95180.

Proteomic databases

PaxDbO95180.
PRIDEO95180.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000348261; ENSP00000334198; ENSG00000196557. [O95180-1]
ENST00000358590; ENSP00000351401; ENSG00000196557. [O95180-2]
ENST00000565831; ENSP00000455840; ENSG00000196557. [O95180-2]
GeneID8912.
KEGGhsa:8912.
UCSCuc002cks.3. human. [O95180-1]
uc002ckt.3. human. [O95180-2]

Organism-specific databases

CTD8912.
GeneCardsGC16P001203.
H-InvDBHIX0038538.
HGNCHGNC:1395. CACNA1H.
HPAHPA039125.
MIM607904. gene.
611942. phenotype.
neXtProtNX_O95180.
Orphanet64280. Childhood absence epilepsy.
PharmGKBPA380.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1226.
HOVERGENHBG050764.
InParanoidO95180.
KOK04855.
OMAGRADEQW.
OrthoDBEOG7MKW55.
PhylomeDBO95180.
TreeFamTF313555.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.

Gene expression databases

ArrayExpressO95180.
BgeeO95180.
CleanExHS_CACNA1H.
GenevestigatorO95180.

Family and domain databases

Gene3D1.20.120.350. 4 hits.
InterProIPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR005445. VDCC_T_a1su.
[Graphical view]
PfamPF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSPR01629. TVDCCALPHA1.
ProtoNetSearch...

Other

ChiTaRSCACNA1H. human.
GeneWikiCACNA1H.
GenomeRNAi8912.
NextBio33494.
PROO95180.
SOURCESearch...

Entry information

Entry nameCAC1H_HUMAN
AccessionPrimary (citable) accession number: O95180
Secondary accession number(s): B5ME00 expand/collapse secondary AC list , 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: July 9, 2014
This is version 139 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM