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Q15878

- CAC1E_HUMAN

UniProt

Q15878 - CAC1E_HUMAN

Protein

Voltage-dependent R-type calcium channel subunit alpha-1E

Gene

CACNA1E

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 3 (14 Oct 2008)
      Previous versions | rss
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    Functioni

    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-1E gives 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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei309 – 3091Calcium ion selectivity and permeabilityBy similarity
    Sitei657 – 6571Calcium ion selectivity and permeabilityBy similarity
    Sitei1372 – 13721Calcium ion selectivity and permeabilityBy similarity
    Sitei1663 – 16631Calcium ion selectivity and permeabilityBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi426 – 43712PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi1752 – 176312PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. high voltage-gated calcium channel activity Source: RefGenome
    3. voltage-gated calcium channel activity Source: MGI

    GO - Biological processi

    1. behavioral fear response Source: Ensembl
    2. behavioral response to pain Source: Ensembl
    3. calcium ion import Source: RefGenome
    4. energy reserve metabolic process Source: Reactome
    5. glucose homeostasis Source: Ensembl
    6. locomotory behavior Source: Ensembl
    7. membrane depolarization Source: Reactome
    8. membrane depolarization during action potential Source: RefGenome
    9. regulation of heart rate Source: Ensembl
    10. regulation of insulin secretion Source: Reactome
    11. regulation of insulin secretion involved in cellular response to glucose stimulus Source: Ensembl
    12. regulation of somatostatin secretion Source: Ensembl
    13. sensory perception of pain Source: Ensembl
    14. small molecule metabolic process Source: Reactome
    15. sperm motility Source: Ensembl
    16. synaptic transmission Source: RefGenome
    17. transmission of nerve impulse Source: Ensembl
    18. transport Source: ProtInc
    19. visual learning Source: Ensembl

    Keywords - Molecular functioni

    Calcium channel, Ion channel, Voltage-gated channel

    Keywords - Biological processi

    Calcium transport, Ion transport, Transport

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_13606. Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels.
    REACT_18325. Regulation of insulin secretion.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:CACNA1E
    Synonyms:CACH6, CACNL1A6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1392. CACNA1E.

    Subcellular locationi

    GO - Cellular componenti

    1. plasma membrane Source: RefGenome
    2. voltage-gated calcium channel complex Source: ProtInc

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26009.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 23132313Voltage-dependent R-type calcium channel subunit alpha-1EPRO_0000053938Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi254 – 2541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1566 – 15661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1571 – 15711N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1734 – 17341Phosphoserine; by PKASequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ15878.
    PRIDEiQ15878.

    PTM databases

    PhosphoSiteiQ15878.

    Expressioni

    Tissue specificityi

    Expressed in neuronal tissues and in kidney.

    Gene expression databases

    ArrayExpressiQ15878.
    BgeeiQ15878.
    CleanExiHS_CACNA1E.
    GenevestigatoriQ15878.

    Organism-specific databases

    HPAiHPA042515.

    Interactioni

    Subunit structurei

    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.1 Publication

    Protein-protein interaction databases

    BioGridi107231. 3 interactions.
    STRINGi9606.ENSP00000356545.

    Structurei

    Secondary structure

    1
    2313
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1868 – 188215

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BXLX-ray2.30B1867-1887[»]
    ProteinModelPortaliQ15878.
    SMRiQ15878. Positions 358-402, 1249-1276.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15878.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 8989CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini109 – 12719ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini147 – 15812CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini174 – 18512ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini206 – 22318CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini245 – 32682ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini351 – 476126CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini497 – 50913ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini530 – 5389CytoplasmicSequence Analysis
    Topological domaini558 – 56710ExtracellularSequence Analysis
    Topological domaini587 – 60519CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini626 – 67853ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini704 – 1148445CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1166 – 118924ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1210 – 12178CytoplasmicSequence Analysis
    Topological domaini1241 – 125414ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1273 – 129119CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1312 – 139887ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1423 – 147957CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1499 – 151315ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1534 – 15418CytoplasmicSequence Analysis
    Topological domaini1561 – 157111ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1591 – 160919CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1630 – 169869ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1725 – 2313589CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei90 – 10819Helical; Name=S1 of repeat IAdd
    BLAST
    Transmembranei128 – 14619Helical; Name=S2 of repeat IAdd
    BLAST
    Transmembranei159 – 17315Helical; Name=S3 of repeat IAdd
    BLAST
    Transmembranei186 – 20520Helical; Name=S4 of repeat IAdd
    BLAST
    Transmembranei224 – 24421Helical; Name=S5 of repeat IAdd
    BLAST
    Transmembranei327 – 35024Helical; Name=S6 of repeat IAdd
    BLAST
    Transmembranei477 – 49620Helical; Name=S1 of repeat IIAdd
    BLAST
    Transmembranei510 – 52920Helical; Name=S2 of repeat IIAdd
    BLAST
    Transmembranei539 – 55719Helical; Name=S3 of repeat IIAdd
    BLAST
    Transmembranei568 – 58619Helical; Name=S4 of repeat IIAdd
    BLAST
    Transmembranei606 – 62520Helical; Name=S5 of repeat IIAdd
    BLAST
    Transmembranei679 – 70325Helical; Name=S6 of repeat IIAdd
    BLAST
    Transmembranei1149 – 116517Helical; Name=S1 of repeat IIIAdd
    BLAST
    Transmembranei1190 – 120920Helical; Name=S2 of repeat IIIAdd
    BLAST
    Transmembranei1218 – 124023Helical; Name=S3 of repeat IIIAdd
    BLAST
    Transmembranei1255 – 127218Helical; Name=S4 of repeat IIIAdd
    BLAST
    Transmembranei1292 – 131120Helical; Name=S5 of repeat IIIAdd
    BLAST
    Transmembranei1399 – 142224Helical; Name=S6 of repeat IIIAdd
    BLAST
    Transmembranei1480 – 149819Helical; Name=S1 of repeat IVAdd
    BLAST
    Transmembranei1514 – 153320Helical; Name=S2 of repeat IVAdd
    BLAST
    Transmembranei1542 – 156019Helical; Name=S3 of repeat IVAdd
    BLAST
    Transmembranei1572 – 159019Helical; Name=S4 of repeat IVAdd
    BLAST
    Transmembranei1610 – 162920Helical; Name=S5 of repeat IVAdd
    BLAST
    Transmembranei1699 – 172426Helical; Name=S6 of repeat IVAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati76 – 354279IAdd
    BLAST
    Repeati462 – 706245IIAdd
    BLAST
    Repeati1140 – 1426287IIIAdd
    BLAST
    Repeati1463 – 1726264IVAdd
    BLAST
    Domaini1739 – 177436EF-handPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni374 – 39118Binding to the beta subunitBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi716 – 7216Poly-Glu
    Compositional biasi748 – 7536Poly-Arg
    Compositional biasi767 – 7726Poly-Arg
    Compositional biasi1228 – 12314Poly-Val
    Compositional biasi2284 – 22885Poly-Arg

    Domaini

    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 similaritiesi

    Contains 1 EF-hand domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1226.
    HOGENOMiHOG000231530.
    HOVERGENiHBG050763.
    InParanoidiQ15878.
    KOiK04852.
    OMAiHMQMSSQ.
    OrthoDBiEOG7T1RBQ.
    PhylomeDBiQ15878.
    TreeFamiTF312805.

    Family and domain databases

    Gene3Di1.20.120.350. 4 hits.
    InterProiIPR027359. Channel_four-helix_dom.
    IPR002048. EF_hand_dom.
    IPR005821. Ion_trans_dom.
    IPR014873. VDCC_a1su_IQ.
    IPR005449. VDCC_R_a1su.
    IPR002077. VDCCAlpha1.
    [Graphical view]
    PANTHERiPTHR10037:SF57. PTHR10037:SF57. 1 hit.
    PfamiPF08763. Ca_chan_IQ. 1 hit.
    PF00520. Ion_trans. 4 hits.
    [Graphical view]
    PRINTSiPR00167. CACHANNEL.
    PR01633. RVDCCALPHA1.
    SMARTiSM01062. Ca_chan_IQ. 1 hit.
    [Graphical view]
    PROSITEiPS50222. EF_HAND_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15878-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MARFGEAVVA RPGSGDGDSD QSRNRQGTPV PASGQAAAYK QTKAQRARTM     50
    ALYNPIPVRQ NCFTVNRSLF IFGEDNIVRK YAKKLIDWPP FEYMILATII 100
    ANCIVLALEQ HLPEDDKTPM SRRLEKTEPY FIGIFCFEAG IKIVALGFIF 150
    HKGSYLRNGW NVMDFIVVLS GILATAGTHF NTHVDLRTLR AVRVLRPLKL 200
    VSGIPSLQIV LKSIMKAMVP LLQIGLLLFF AILMFAIIGL EFYSGKLHRA 250
    CFMNNSGILE GFDPPHPCGV QGCPAGYECK DWIGPNDGIT QFDNILFAVL 300
    TVFQCITMEG WTTVLYNTND ALGATWNWLY FIPLIIIGSF FVLNLVLGVL 350
    SGEFAKERER VENRRAFMKL RRQQQIEREL NGYRAWIDKA EEVMLAEENK 400
    NAGTSALEVL RRATIKRSRT EAMTRDSSDE HCVDISSVGT PLARASIKSA 450
    KVDGVSYFRH KERLLRISIR HMVKSQVFYW IVLSLVALNT ACVAIVHHNQ 500
    PQWLTHLLYY AEFLFLGLFL LEMSLKMYGM GPRLYFHSSF NCFDFGVTVG 550
    SIFEVVWAIF RPGTSFGISV LRALRLLRIF KITKYWASLR NLVVSLMSSM 600
    KSIISLLFLL FLFIVVFALL GMQLFGGRFN FNDGTPSANF DTFPAAIMTV 650
    FQILTGEDWN EVMYNGIRSQ GGVSSGMWSA IYFIVLTLFG NYTLLNVFLA 700
    IAVDNLANAQ ELTKDEQEEE EAFNQKHALQ KAKEVSPMSA PNMPSIERDR 750
    RRRHHMSMWE PRSSHLRERR RRHHMSVWEQ RTSQLRKHMQ MSSQEALNRE 800
    EAPTMNPLNP LNPLSSLNPL NAHPSLYRRP RAIEGLALGL ALEKFEEERI 850
    SRGGSLKGDG GDRSSALDNQ RTPLSLGQRE PPWLARPCHG NCDPTQQEAG 900
    GGEAVVTFED RARHRQSQRR SRHRRVRTEG KESSSASRSR SASQERSLDE 950
    AMPTEGEKDH ELRGNHGAKE PTIQEERAQD LRRTNSLMVS RGSGLAGGLD 1000
    EADTPLVLPH PELEVGKHVV LTEQEPEGSS EQALLGNVQL DMGRVISQSE 1050
    PDLSCITANT DKATTESTSV TVAIPDVDPL VDSTVVHISN KTDGEASPLK 1100
    EAEIREDEEE VEKKKQKKEK RETGKAMVPH SSMFIFSTTN PIRRACHYIV 1150
    NLRYFEMCIL LVIAASSIAL AAEDPVLTNS ERNKVLRYFD YVFTGVFTFE 1200
    MVIKMIDQGL ILQDGSYFRD LWNILDFVVV VGALVAFALA NALGTNKGRD 1250
    IKTIKSLRVL RVLRPLKTIK RLPKLKAVFD CVVTSLKNVF NILIVYKLFM 1300
    FIFAVIAVQL FKGKFFYCTD SSKDTEKECI GNYVDHEKNK MEVKGREWKR 1350
    HEFHYDNIIW ALLTLFTVST GEGWPQVLQH SVDVTEEDRG PSRSNRMEMS 1400
    IFYVVYFVVF PFFFVNIFVA LIIITFQEQG DKMMEECSLE KNERACIDFA 1450
    ISAKPLTRYM PQNRHTFQYR VWHFVVSPSF EYTIMAMIAL NTVVLMMKYY 1500
    SAPCTYELAL KYLNIAFTMV FSLECVLKVI AFGFLNYFRD TWNIFDFITV 1550
    IGSITEIILT DSKLVNTSGF NMSFLKLFRA ARLIKLLRQG YTIRILLWTF 1600
    VQSFKALPYV CLLIAMLFFI YAIIGMQVFG NIKLDEESHI NRHNNFRSFF 1650
    GSLMLLFRSA TGEAWQEIML SCLGEKGCEP DTTAPSGQNE NERCGTDLAY 1700
    VYFVSFIFFC SFLMLNLFVA VIMDNFEYLT RDSSILGPHH LDEFVRVWAE 1750
    YDRAACGRIH YTEMYEMLTL MSPPLGLGKR CPSKVAYKRL VLMNMPVAED 1800
    MTVHFTSTLM ALIRTALDIK IAKGGADRQQ LDSELQKETL AIWPHLSQKM 1850
    LDLLVPMPKA SDLTVGKIYA AMMIMDYYKQ SKVKKQRQQL EEQKNAPMFQ 1900
    RMEPSSLPQE IIANAKALPY LQQDPVSGLS GRSGYPSMSP LSPQDIFQLA 1950
    CMDPADDGQF QERQSLEPEV SELKSVQPSN HGIYLPSDTQ EHAGSGRASS 2000
    MPRLTVDPQV VTDPSSMRRS FSTIRDKRSN SSWLEEFSME RSSENTYKSR 2050
    RRSYHSSLRL SAHRLNSDSG HKSDTHRSGG RERGRSKERK HLLSPDVSRC 2100
    NSEERGTQAD WESPERRQSR SPSEGRSQTP NRQGTGSLSE SSIPSVSDTS 2150
    TPRRSRRQLP PVPPKPRPLL SYSSLIRHAG SISPPADGSE EGSPLTSQAL 2200
    ESNNACLTES SNSPHPQQSQ HASPQRYISE PYLALHEDSH ASDCGEEETL 2250
    TFEAAVATSL GRSNTIGSAP PLRHSWQMPN GHYRRRRRGG PGPGMMCGAV 2300
    NNLLSDTEED DKC 2313
    Length:2,313
    Mass (Da):261,731
    Last modified:October 14, 2008 - v3
    Checksum:iCCC7F309C27C42F1
    GO
    Isoform 2 (identifier: Q15878-2) [UniParc]FASTAAdd to Basket

    Also known as: Alpha-1E-1

    The sequence of this isoform differs from the canonical sequence as follows:
         748-766: Missing.
         1967-2009: Missing.

    Show »
    Length:2,251
    Mass (Da):254,604
    Checksum:i73640AD59C386BB2
    GO
    Isoform 3 (identifier: Q15878-3) [UniParc]FASTAAdd to Basket

    Also known as: Alpha-1E-3

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

    Show »
    Length:2,270
    Mass (Da):257,116
    Checksum:iD424C3592C9BD5F5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti648 – 6481M → I in AAA72125. (PubMed:7536609)Curated
    Sequence conflicti836 – 8383LAL → WP in AAA72125. (PubMed:7536609)Curated
    Sequence conflicti2077 – 20771R → P in AAA59204. (PubMed:8071363)Curated
    Sequence conflicti2077 – 20771R → P in AAA59205. (PubMed:8071363)Curated
    Sequence conflicti2084 – 20841G → R in AAA59204. (PubMed:8071363)Curated
    Sequence conflicti2084 – 20841G → R in AAA59205. (PubMed:8071363)Curated
    Sequence conflicti2206 – 22061C → W in AAA59204. (PubMed:8071363)Curated
    Sequence conflicti2206 – 22061C → W in AAA59205. (PubMed:8071363)Curated
    Sequence conflicti2219 – 22191S → R in AAA59204. (PubMed:8071363)Curated
    Sequence conflicti2219 – 22191S → R in AAA59205. (PubMed:8071363)Curated
    Sequence conflicti2245 – 22451G → V in AAA59204. (PubMed:8071363)Curated
    Sequence conflicti2245 – 22451G → V in AAA59205. (PubMed:8071363)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti859 – 8591D → E.
    Corresponds to variant rs35737760 [ dbSNP | Ensembl ].
    VAR_031912
    Natural varianti1955 – 19551A → T.1 Publication
    Corresponds to variant rs704326 [ dbSNP | Ensembl ].
    VAR_046996

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei748 – 76619Missing in isoform 2. 1 PublicationVSP_000937Add
    BLAST
    Alternative sequencei1967 – 200943Missing in isoform 2 and isoform 3. 1 PublicationVSP_024817Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L27745 mRNA. Translation: AAA72125.1.
    L29384 mRNA. Translation: AAA59204.1.
    L29385 mRNA. Translation: AAA59205.1.
    AL161734
    , AL160059, AL359270, AL590998 Genomic DNA. Translation: CAH72675.1.
    AL161734
    , AL160059, AL359270, AL590998 Genomic DNA. Translation: CAH72676.1.
    AL161734
    , AL160059, AL359270, AL590998 Genomic DNA. Translation: CAH72677.1.
    AL359270
    , AL160059, AL161734, AL590998 Genomic DNA. Translation: CAI14653.1.
    AL359270
    , AL160059, AL161734, AL590998 Genomic DNA. Translation: CAI14654.1.
    AL359270
    , AL160059, AL161734, AL590998 Genomic DNA. Translation: CAI14655.1.
    AL160059
    , AL161734, AL359270, AL590998 Genomic DNA. Translation: CAI17081.1.
    AL160059
    , AL161734, AL359270, AL590998 Genomic DNA. Translation: CAI17082.1.
    AL160059
    , AL161734, AL359270, AL590998 Genomic DNA. Translation: CAI17083.1.
    AL590998
    , AL160059, AL161734, AL359270 Genomic DNA. Translation: CAI22327.1.
    AL590998
    , AL160059, AL161734, AL359270 Genomic DNA. Translation: CAI22328.1.
    AL590998
    , AL160059, AL161734, AL359270 Genomic DNA. Translation: CAI22329.1.
    CCDSiCCDS53443.1. [Q15878-3]
    CCDS55664.1. [Q15878-1]
    CCDS55665.1. [Q15878-2]
    PIRiA54972.
    B54972.
    RefSeqiNP_000712.2. NM_000721.3. [Q15878-3]
    NP_001192222.1. NM_001205293.1. [Q15878-1]
    NP_001192223.1. NM_001205294.1. [Q15878-2]
    UniGeneiHs.437444.

    Genome annotation databases

    EnsembliENST00000367570; ENSP00000356542; ENSG00000198216. [Q15878-3]
    ENST00000367573; ENSP00000356545; ENSG00000198216. [Q15878-1]
    GeneIDi777.
    KEGGihsa:777.
    UCSCiuc001gow.3. human. [Q15878-3]
    uc009wxs.3. human. [Q15878-2]
    uc009wxt.3. human. [Q15878-1]

    Polymorphism databases

    DMDMi209572758.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L27745 mRNA. Translation: AAA72125.1 .
    L29384 mRNA. Translation: AAA59204.1 .
    L29385 mRNA. Translation: AAA59205.1 .
    AL161734
    , AL160059 , AL359270 , AL590998 Genomic DNA. Translation: CAH72675.1 .
    AL161734
    , AL160059 , AL359270 , AL590998 Genomic DNA. Translation: CAH72676.1 .
    AL161734
    , AL160059 , AL359270 , AL590998 Genomic DNA. Translation: CAH72677.1 .
    AL359270
    , AL160059 , AL161734 , AL590998 Genomic DNA. Translation: CAI14653.1 .
    AL359270
    , AL160059 , AL161734 , AL590998 Genomic DNA. Translation: CAI14654.1 .
    AL359270
    , AL160059 , AL161734 , AL590998 Genomic DNA. Translation: CAI14655.1 .
    AL160059
    , AL161734 , AL359270 , AL590998 Genomic DNA. Translation: CAI17081.1 .
    AL160059
    , AL161734 , AL359270 , AL590998 Genomic DNA. Translation: CAI17082.1 .
    AL160059
    , AL161734 , AL359270 , AL590998 Genomic DNA. Translation: CAI17083.1 .
    AL590998
    , AL160059 , AL161734 , AL359270 Genomic DNA. Translation: CAI22327.1 .
    AL590998
    , AL160059 , AL161734 , AL359270 Genomic DNA. Translation: CAI22328.1 .
    AL590998
    , AL160059 , AL161734 , AL359270 Genomic DNA. Translation: CAI22329.1 .
    CCDSi CCDS53443.1. [Q15878-3 ]
    CCDS55664.1. [Q15878-1 ]
    CCDS55665.1. [Q15878-2 ]
    PIRi A54972.
    B54972.
    RefSeqi NP_000712.2. NM_000721.3. [Q15878-3 ]
    NP_001192222.1. NM_001205293.1. [Q15878-1 ]
    NP_001192223.1. NM_001205294.1. [Q15878-2 ]
    UniGenei Hs.437444.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3BXL X-ray 2.30 B 1867-1887 [» ]
    ProteinModelPortali Q15878.
    SMRi Q15878. Positions 358-402, 1249-1276.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107231. 3 interactions.
    STRINGi 9606.ENSP00000356545.

    Chemistry

    BindingDBi Q15878.
    ChEMBLi CHEMBL1687682.
    GuidetoPHARMACOLOGYi 534.

    PTM databases

    PhosphoSitei Q15878.

    Polymorphism databases

    DMDMi 209572758.

    Proteomic databases

    PaxDbi Q15878.
    PRIDEi Q15878.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367570 ; ENSP00000356542 ; ENSG00000198216 . [Q15878-3 ]
    ENST00000367573 ; ENSP00000356545 ; ENSG00000198216 . [Q15878-1 ]
    GeneIDi 777.
    KEGGi hsa:777.
    UCSCi uc001gow.3. human. [Q15878-3 ]
    uc009wxs.3. human. [Q15878-2 ]
    uc009wxt.3. human. [Q15878-1 ]

    Organism-specific databases

    CTDi 777.
    GeneCardsi GC01P181382.
    HGNCi HGNC:1392. CACNA1E.
    HPAi HPA042515.
    MIMi 601013. gene.
    neXtProti NX_Q15878.
    PharmGKBi PA26009.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1226.
    HOGENOMi HOG000231530.
    HOVERGENi HBG050763.
    InParanoidi Q15878.
    KOi K04852.
    OMAi HMQMSSQ.
    OrthoDBi EOG7T1RBQ.
    PhylomeDBi Q15878.
    TreeFami TF312805.

    Enzyme and pathway databases

    Reactomei REACT_13606. Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels.
    REACT_18325. Regulation of insulin secretion.

    Miscellaneous databases

    EvolutionaryTracei Q15878.
    GeneWikii R-type_calcium_channel.
    GenomeRNAii 777.
    NextBioi 3140.
    PROi Q15878.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15878.
    Bgeei Q15878.
    CleanExi HS_CACNA1E.
    Genevestigatori Q15878.

    Family and domain databases

    Gene3Di 1.20.120.350. 4 hits.
    InterProi IPR027359. Channel_four-helix_dom.
    IPR002048. EF_hand_dom.
    IPR005821. Ion_trans_dom.
    IPR014873. VDCC_a1su_IQ.
    IPR005449. VDCC_R_a1su.
    IPR002077. VDCCAlpha1.
    [Graphical view ]
    PANTHERi PTHR10037:SF57. PTHR10037:SF57. 1 hit.
    Pfami PF08763. Ca_chan_IQ. 1 hit.
    PF00520. Ion_trans. 4 hits.
    [Graphical view ]
    PRINTSi PR00167. CACHANNEL.
    PR01633. RVDCCALPHA1.
    SMARTi SM01062. Ca_chan_IQ. 1 hit.
    [Graphical view ]
    PROSITEi PS50222. EF_HAND_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.

    Entry informationi

    Entry nameiCAC1E_HUMAN
    AccessioniPrimary (citable) accession number: Q15878
    Secondary accession number(s): B1AM12
    , B1AM13, B1AM14, Q14580, Q14581
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: October 14, 2008
    Last modified: October 1, 2014
    This is version 143 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3