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Q15878 (CAC1E_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 R-type calcium channel subunit alpha-1E
Alternative name(s):
Brain calcium channel II
Short name=BII
Calcium channel, L type, alpha-1 polypeptide, isoform 6
Voltage-gated calcium channel subunit alpha Cav2.3
Gene names
Name:CACNA1E
Synonyms:CACH6, CACNL1A6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2313 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-1Egives rise to R-type calcium currents. R-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by nickel, and partially by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to dihydropyridines (DHP), omega-conotoxin-GVIA (omega-CTx-GVIA), and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing alpha-1E subunit could be involved in the modulation of firing patterns of neurons which is important for information processing.

Subunit structure

Interacts with EFHC1. Voltage-dependent calcium channels are multisubunit complexes, consisting of alpha-1, alpha-2, beta and delta subunits in a 1:1:1:1 ratio. The channel activity is directed by the pore-forming and voltage-sensitive alpha-1 subunit. In many cases, this subunit is sufficient to generate voltage-sensitive calcium channel activity. The auxiliary subunits beta and alpha-2/delta linked by a disulfide bridge regulate the channel activity. Ref.4

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Expressed in neuronal tissues and in kidney.

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.

Sequence similarities

Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family. CACNA1E subfamily. [View classification]

Contains 1 EF-hand domain.

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   Molecular functionCalcium channel
Ion channel
Voltage-gated channel
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbehavioral fear response

Inferred from electronic annotation. Source: Ensembl

behavioral response to pain

Inferred from electronic annotation. Source: Ensembl

calcium ion import

Inferred from Biological aspect of Ancestor. Source: RefGenome

energy reserve metabolic process

Traceable author statement. Source: Reactome

glucose homeostasis

Inferred from electronic annotation. Source: Ensembl

locomotory behavior

Inferred from electronic annotation. Source: Ensembl

membrane depolarization

Traceable author statement. Source: Reactome

membrane depolarization during action potential

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of heart rate

Inferred from electronic annotation. Source: Ensembl

regulation of insulin secretion

Traceable author statement. Source: Reactome

regulation of insulin secretion involved in cellular response to glucose stimulus

Inferred from electronic annotation. Source: Ensembl

regulation of somatostatin secretion

Inferred from electronic annotation. Source: Ensembl

sensory perception of pain

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

sperm motility

Inferred from electronic annotation. Source: Ensembl

synaptic transmission

Inferred from Biological aspect of Ancestor. Source: RefGenome

transmission of nerve impulse

Inferred from electronic annotation. Source: Ensembl

transport

Traceable author statement Ref.2. Source: ProtInc

visual learning

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentplasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

voltage-gated calcium channel complex

Traceable author statement Ref.2. Source: ProtInc

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

high voltage-gated calcium channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

voltage-gated calcium channel activity

Inferred from direct assay Ref.2. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15878-1)

Also known as: Alpha-1E;

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: Q15878-2)

Also known as: Alpha-1E-1;

The sequence of this isoform differs from the canonical sequence as follows:
     748-766: Missing.
     1967-2009: Missing.
Isoform 3 (identifier: Q15878-3)

Also known as: Alpha-1E-3;

The sequence of this isoform differs from the canonical sequence as follows:
     1967-2009: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 23132313Voltage-dependent R-type calcium channel subunit alpha-1E
PRO_0000053938

Regions

Topological domain1 – 8989Cytoplasmic Potential
Transmembrane90 – 10819Helical; Name=S1 of repeat I
Topological domain109 – 12719Extracellular Potential
Transmembrane128 – 14619Helical; Name=S2 of repeat I
Topological domain147 – 15812Cytoplasmic Potential
Transmembrane159 – 17315Helical; Name=S3 of repeat I
Topological domain174 – 18512Extracellular Potential
Transmembrane186 – 20520Helical; Name=S4 of repeat I
Topological domain206 – 22318Cytoplasmic Potential
Transmembrane224 – 24421Helical; Name=S5 of repeat I
Topological domain245 – 32682Extracellular Potential
Transmembrane327 – 35024Helical; Name=S6 of repeat I
Topological domain351 – 476126Cytoplasmic Potential
Transmembrane477 – 49620Helical; Name=S1 of repeat II
Topological domain497 – 50913Extracellular Potential
Transmembrane510 – 52920Helical; Name=S2 of repeat II
Topological domain530 – 5389Cytoplasmic Potential
Transmembrane539 – 55719Helical; Name=S3 of repeat II
Topological domain558 – 56710Extracellular Potential
Transmembrane568 – 58619Helical; Name=S4 of repeat II
Topological domain587 – 60519Cytoplasmic Potential
Transmembrane606 – 62520Helical; Name=S5 of repeat II
Topological domain626 – 67853Extracellular Potential
Transmembrane679 – 70325Helical; Name=S6 of repeat II
Topological domain704 – 1148445Cytoplasmic Potential
Transmembrane1149 – 116517Helical; Name=S1 of repeat III
Topological domain1166 – 118924Extracellular Potential
Transmembrane1190 – 120920Helical; Name=S2 of repeat III
Topological domain1210 – 12178Cytoplasmic Potential
Transmembrane1218 – 124023Helical; Name=S3 of repeat III
Topological domain1241 – 125414Extracellular Potential
Transmembrane1255 – 127218Helical; Name=S4 of repeat III
Topological domain1273 – 129119Cytoplasmic Potential
Transmembrane1292 – 131120Helical; Name=S5 of repeat III
Topological domain1312 – 139887Extracellular Potential
Transmembrane1399 – 142224Helical; Name=S6 of repeat III
Topological domain1423 – 147957Cytoplasmic Potential
Transmembrane1480 – 149819Helical; Name=S1 of repeat IV
Topological domain1499 – 151315Extracellular Potential
Transmembrane1514 – 153320Helical; Name=S2 of repeat IV
Topological domain1534 – 15418Cytoplasmic Potential
Transmembrane1542 – 156019Helical; Name=S3 of repeat IV
Topological domain1561 – 157111Extracellular Potential
Transmembrane1572 – 159019Helical; Name=S4 of repeat IV
Topological domain1591 – 160919Cytoplasmic Potential
Transmembrane1610 – 162920Helical; Name=S5 of repeat IV
Topological domain1630 – 169869Extracellular Potential
Transmembrane1699 – 172426Helical; Name=S6 of repeat IV
Topological domain1725 – 2313589Cytoplasmic Potential
Repeat76 – 354279I
Repeat462 – 706245II
Repeat1140 – 1426287III
Repeat1463 – 1726264IV
Domain1739 – 177436EF-hand
Calcium binding426 – 43712 By similarity
Calcium binding1752 – 176312 By similarity
Region374 – 39118Binding to the beta subunit By similarity
Compositional bias716 – 7216Poly-Glu
Compositional bias748 – 7536Poly-Arg
Compositional bias767 – 7726Poly-Arg
Compositional bias1228 – 12314Poly-Val
Compositional bias2284 – 22885Poly-Arg

Sites

Site3091Calcium ion selectivity and permeability By similarity
Site6571Calcium ion selectivity and permeability By similarity
Site13721Calcium ion selectivity and permeability By similarity
Site16631Calcium ion selectivity and permeability By similarity

Amino acid modifications

Modified residue17341Phosphoserine; by PKA Potential
Glycosylation2541N-linked (GlcNAc...) Potential
Glycosylation15661N-linked (GlcNAc...) Potential
Glycosylation15711N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence748 – 76619Missing in isoform 2.
VSP_000937
Alternative sequence1967 – 200943Missing in isoform 2 and isoform 3.
VSP_024817
Natural variant8591D → E.
Corresponds to variant rs35737760 [ dbSNP | Ensembl ].
VAR_031912
Natural variant19551A → T. Ref.1
Corresponds to variant rs704326 [ dbSNP | Ensembl ].
VAR_046996

Experimental info

Sequence conflict6481M → I in AAA72125. Ref.1
Sequence conflict836 – 8383LAL → WP in AAA72125. Ref.1
Sequence conflict20771R → P in AAA59204. Ref.2
Sequence conflict20771R → P in AAA59205. Ref.2
Sequence conflict20841G → R in AAA59204. Ref.2
Sequence conflict20841G → R in AAA59205. Ref.2
Sequence conflict22061C → W in AAA59204. Ref.2
Sequence conflict22061C → W in AAA59205. Ref.2
Sequence conflict22191S → R in AAA59204. Ref.2
Sequence conflict22191S → R in AAA59205. Ref.2
Sequence conflict22451G → V in AAA59204. Ref.2
Sequence conflict22451G → V in AAA59205. Ref.2

Secondary structure

... 2313
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Alpha-1E) [UniParc].

Last modified October 14, 2008. Version 3.
Checksum: CCC7F309C27C42F1

FASTA2,313261,731
        10         20         30         40         50         60 
MARFGEAVVA RPGSGDGDSD QSRNRQGTPV PASGQAAAYK QTKAQRARTM ALYNPIPVRQ 

        70         80         90        100        110        120 
NCFTVNRSLF IFGEDNIVRK YAKKLIDWPP FEYMILATII ANCIVLALEQ HLPEDDKTPM 

       130        140        150        160        170        180 
SRRLEKTEPY FIGIFCFEAG IKIVALGFIF HKGSYLRNGW NVMDFIVVLS GILATAGTHF 

       190        200        210        220        230        240 
NTHVDLRTLR AVRVLRPLKL VSGIPSLQIV LKSIMKAMVP LLQIGLLLFF AILMFAIIGL 

       250        260        270        280        290        300 
EFYSGKLHRA CFMNNSGILE GFDPPHPCGV QGCPAGYECK DWIGPNDGIT QFDNILFAVL 

       310        320        330        340        350        360 
TVFQCITMEG WTTVLYNTND ALGATWNWLY FIPLIIIGSF FVLNLVLGVL SGEFAKERER 

       370        380        390        400        410        420 
VENRRAFMKL RRQQQIEREL NGYRAWIDKA EEVMLAEENK NAGTSALEVL RRATIKRSRT 

       430        440        450        460        470        480 
EAMTRDSSDE HCVDISSVGT PLARASIKSA KVDGVSYFRH KERLLRISIR HMVKSQVFYW 

       490        500        510        520        530        540 
IVLSLVALNT ACVAIVHHNQ PQWLTHLLYY AEFLFLGLFL LEMSLKMYGM GPRLYFHSSF 

       550        560        570        580        590        600 
NCFDFGVTVG SIFEVVWAIF RPGTSFGISV LRALRLLRIF KITKYWASLR NLVVSLMSSM 

       610        620        630        640        650        660 
KSIISLLFLL FLFIVVFALL GMQLFGGRFN FNDGTPSANF DTFPAAIMTV FQILTGEDWN 

       670        680        690        700        710        720 
EVMYNGIRSQ GGVSSGMWSA IYFIVLTLFG NYTLLNVFLA IAVDNLANAQ ELTKDEQEEE 

       730        740        750        760        770        780 
EAFNQKHALQ KAKEVSPMSA PNMPSIERDR RRRHHMSMWE PRSSHLRERR RRHHMSVWEQ 

       790        800        810        820        830        840 
RTSQLRKHMQ MSSQEALNRE EAPTMNPLNP LNPLSSLNPL NAHPSLYRRP RAIEGLALGL 

       850        860        870        880        890        900 
ALEKFEEERI SRGGSLKGDG GDRSSALDNQ RTPLSLGQRE PPWLARPCHG NCDPTQQEAG 

       910        920        930        940        950        960 
GGEAVVTFED RARHRQSQRR SRHRRVRTEG KESSSASRSR SASQERSLDE AMPTEGEKDH 

       970        980        990       1000       1010       1020 
ELRGNHGAKE PTIQEERAQD LRRTNSLMVS RGSGLAGGLD EADTPLVLPH PELEVGKHVV 

      1030       1040       1050       1060       1070       1080 
LTEQEPEGSS EQALLGNVQL DMGRVISQSE PDLSCITANT DKATTESTSV TVAIPDVDPL 

      1090       1100       1110       1120       1130       1140 
VDSTVVHISN KTDGEASPLK EAEIREDEEE VEKKKQKKEK RETGKAMVPH SSMFIFSTTN 

      1150       1160       1170       1180       1190       1200 
PIRRACHYIV NLRYFEMCIL LVIAASSIAL AAEDPVLTNS ERNKVLRYFD YVFTGVFTFE 

      1210       1220       1230       1240       1250       1260 
MVIKMIDQGL ILQDGSYFRD LWNILDFVVV VGALVAFALA NALGTNKGRD IKTIKSLRVL 

      1270       1280       1290       1300       1310       1320 
RVLRPLKTIK RLPKLKAVFD CVVTSLKNVF NILIVYKLFM FIFAVIAVQL FKGKFFYCTD 

      1330       1340       1350       1360       1370       1380 
SSKDTEKECI GNYVDHEKNK MEVKGREWKR HEFHYDNIIW ALLTLFTVST GEGWPQVLQH 

      1390       1400       1410       1420       1430       1440 
SVDVTEEDRG PSRSNRMEMS IFYVVYFVVF PFFFVNIFVA LIIITFQEQG DKMMEECSLE 

      1450       1460       1470       1480       1490       1500 
KNERACIDFA ISAKPLTRYM PQNRHTFQYR VWHFVVSPSF EYTIMAMIAL NTVVLMMKYY 

      1510       1520       1530       1540       1550       1560 
SAPCTYELAL KYLNIAFTMV FSLECVLKVI AFGFLNYFRD TWNIFDFITV IGSITEIILT 

      1570       1580       1590       1600       1610       1620 
DSKLVNTSGF NMSFLKLFRA ARLIKLLRQG YTIRILLWTF VQSFKALPYV CLLIAMLFFI 

      1630       1640       1650       1660       1670       1680 
YAIIGMQVFG NIKLDEESHI NRHNNFRSFF GSLMLLFRSA TGEAWQEIML SCLGEKGCEP 

      1690       1700       1710       1720       1730       1740 
DTTAPSGQNE NERCGTDLAY VYFVSFIFFC SFLMLNLFVA VIMDNFEYLT RDSSILGPHH 

      1750       1760       1770       1780       1790       1800 
LDEFVRVWAE YDRAACGRIH YTEMYEMLTL MSPPLGLGKR CPSKVAYKRL VLMNMPVAED 

      1810       1820       1830       1840       1850       1860 
MTVHFTSTLM ALIRTALDIK IAKGGADRQQ LDSELQKETL AIWPHLSQKM LDLLVPMPKA 

      1870       1880       1890       1900       1910       1920 
SDLTVGKIYA AMMIMDYYKQ SKVKKQRQQL EEQKNAPMFQ RMEPSSLPQE IIANAKALPY 

      1930       1940       1950       1960       1970       1980 
LQQDPVSGLS GRSGYPSMSP LSPQDIFQLA CMDPADDGQF QERQSLEPEV SELKSVQPSN 

      1990       2000       2010       2020       2030       2040 
HGIYLPSDTQ EHAGSGRASS MPRLTVDPQV VTDPSSMRRS FSTIRDKRSN SSWLEEFSME 

      2050       2060       2070       2080       2090       2100 
RSSENTYKSR RRSYHSSLRL SAHRLNSDSG HKSDTHRSGG RERGRSKERK HLLSPDVSRC 

      2110       2120       2130       2140       2150       2160 
NSEERGTQAD WESPERRQSR SPSEGRSQTP NRQGTGSLSE SSIPSVSDTS TPRRSRRQLP 

      2170       2180       2190       2200       2210       2220 
PVPPKPRPLL SYSSLIRHAG SISPPADGSE EGSPLTSQAL ESNNACLTES SNSPHPQQSQ 

      2230       2240       2250       2260       2270       2280 
HASPQRYISE PYLALHEDSH ASDCGEEETL TFEAAVATSL GRSNTIGSAP PLRHSWQMPN 

      2290       2300       2310 
GHYRRRRRGG PGPGMMCGAV NNLLSDTEED DKC 

« Hide

Isoform 2 (Alpha-1E-1) [UniParc].

Checksum: 73640AD59C386BB2
Show »

FASTA2,251254,604
Isoform 3 (Alpha-1E-3) [UniParc].

Checksum: D424C3592C9BD5F5
Show »

FASTA2,270257,116

References

« Hide 'large scale' references
[1]"Molecular analysis and functional expression of the human type E neuronal Ca2+ channel alpha 1 subunit."
Schneider T., Wei X., Olcese R., Costantin J.L., Neely A., Palade P., Perez-Reyes E., Qin N., Zhou J., Crawford G.D., Smith R.G., Appel S.H., Stefani E., Birnbaumer M.
Recept. Channels 2:255-270(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-1955.
Tissue: Brain.
[2]"Structure and functional characterization of neuronal alpha 1E calcium channel subtypes."
Williams M.E., Marubio L.M., Deal C.R., Hans M., Brust P.F., Philipson L.H., Miller R.J., Johnson E.C., Harpold M.M., Ellis S.B.
J. Biol. Chem. 269:22347-22357(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
Tissue: Hippocampus.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Mutations in EFHC1 cause juvenile myoclonic epilepsy."
Suzuki T., Delgado-Escueta A.V., Aguan K., Alonso M.E., Shi J., Hara Y., Nishida M., Numata T., Medina M.T., Takeuchi T., Morita R., Bai D., Ganesh S., Sugimoto Y., Inazawa J., Bailey J.N., Ochoa A., Jara-Prado A. expand/collapse author list , Rasmussen A., Ramos-Peek J., Cordova S., Rubio-Donnadieu F., Inoue Y., Osawa M., Kaneko S., Oguni H., Mori Y., Yamakawa K.
Nat. Genet. 36:842-849(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CACNA1E.
[5]"Crystal structure of the CaV2 IQ domain in complex with Ca2+/calmodulin: high-resolution mechanistic implications for channel regulation by Ca2+."
Mori M.X., Vander Kooi C.W., Leahy D.J., Yue D.T.
Structure 16:607-620(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1867-1885.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L27745 mRNA. Translation: AAA72125.1.
L29384 mRNA. Translation: AAA59204.1.
L29385 mRNA. Translation: AAA59205.1.
AL161734 expand/collapse EMBL AC list , AL160059, AL359270, AL590998 Genomic DNA. Translation: CAH72675.1.
AL161734 expand/collapse EMBL AC list , AL160059, AL359270, AL590998 Genomic DNA. Translation: CAH72676.1.
AL161734 expand/collapse EMBL AC list , AL160059, AL359270, AL590998 Genomic DNA. Translation: CAH72677.1.
AL359270 expand/collapse EMBL AC list , AL160059, AL161734, AL590998 Genomic DNA. Translation: CAI14653.1.
AL359270 expand/collapse EMBL AC list , AL160059, AL161734, AL590998 Genomic DNA. Translation: CAI14654.1.
AL359270 expand/collapse EMBL AC list , AL160059, AL161734, AL590998 Genomic DNA. Translation: CAI14655.1.
AL160059 expand/collapse EMBL AC list , AL161734, AL359270, AL590998 Genomic DNA. Translation: CAI17081.1.
AL160059 expand/collapse EMBL AC list , AL161734, AL359270, AL590998 Genomic DNA. Translation: CAI17082.1.
AL160059 expand/collapse EMBL AC list , AL161734, AL359270, AL590998 Genomic DNA. Translation: CAI17083.1.
AL590998 expand/collapse EMBL AC list , AL160059, AL161734, AL359270 Genomic DNA. Translation: CAI22327.1.
AL590998 expand/collapse EMBL AC list , AL160059, AL161734, AL359270 Genomic DNA. Translation: CAI22328.1.
AL590998 expand/collapse EMBL AC list , AL160059, AL161734, AL359270 Genomic DNA. Translation: CAI22329.1.
CCDSCCDS53443.1. [Q15878-3]
CCDS55664.1. [Q15878-1]
CCDS55665.1. [Q15878-2]
PIRA54972.
B54972.
RefSeqNP_000712.2. NM_000721.3. [Q15878-3]
NP_001192222.1. NM_001205293.1. [Q15878-1]
NP_001192223.1. NM_001205294.1. [Q15878-2]
UniGeneHs.437444.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BXLX-ray2.30B1867-1887[»]
ProteinModelPortalQ15878.
SMRQ15878. Positions 358-402, 1249-1276.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107231. 3 interactions.
STRING9606.ENSP00000356545.

Chemistry

BindingDBQ15878.
ChEMBLCHEMBL1687682.
GuidetoPHARMACOLOGY534.

PTM databases

PhosphoSiteQ15878.

Polymorphism databases

DMDM209572758.

Proteomic databases

PaxDbQ15878.
PRIDEQ15878.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367570; ENSP00000356542; ENSG00000198216. [Q15878-3]
ENST00000367573; ENSP00000356545; ENSG00000198216. [Q15878-1]
ENST00000526775; ENSP00000434814; ENSG00000198216. [Q15878-2]
GeneID777.
KEGGhsa:777.
UCSCuc001gow.3. human. [Q15878-3]
uc009wxs.3. human. [Q15878-2]
uc009wxt.3. human. [Q15878-1]

Organism-specific databases

CTD777.
GeneCardsGC01P181382.
HGNCHGNC:1392. CACNA1E.
HPAHPA042515.
MIM601013. gene.
neXtProtNX_Q15878.
PharmGKBPA26009.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1226.
HOGENOMHOG000231530.
HOVERGENHBG050763.
InParanoidQ15878.
KOK04852.
OMAHMQMSSQ.
OrthoDBEOG7T1RBQ.
PhylomeDBQ15878.
TreeFamTF312805.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_13685. Neuronal System.

Gene expression databases

ArrayExpressQ15878.
BgeeQ15878.
CleanExHS_CACNA1E.
GenevestigatorQ15878.

Family and domain databases

Gene3D1.20.120.350. 4 hits.
InterProIPR027359. Channel_four-helix_dom.
IPR002048. EF_hand_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005449. VDCC_R_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PANTHERPTHR10037:SF57. PTHR10037:SF57. 1 hit.
PfamPF08763. Ca_chan_IQ. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSPR00167. CACHANNEL.
PR01633. RVDCCALPHA1.
SMARTSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]
PROSITEPS50222. EF_HAND_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ15878.
GeneWikiR-type_calcium_channel.
GenomeRNAi777.
NextBio3140.
PROQ15878.
SOURCESearch...

Entry information

Entry nameCAC1E_HUMAN
AccessionPrimary (citable) accession number: Q15878
Secondary accession number(s): B1AM12 expand/collapse secondary AC list , B1AM13, B1AM14, Q14580, Q14581
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: October 14, 2008
Last modified: July 9, 2014
This is version 141 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 1

Human chromosome 1: entries, gene names and cross-references to MIM