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Q07652

- CAC1E_RAT

UniProt

Q07652 - CAC1E_RAT

Protein

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

Gene

Cacna1e

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      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
    Sitei260 – 2601Calcium ion selectivity and permeabilityBy similarity
    Sitei608 – 6081Calcium ion selectivity and permeabilityBy similarity
    Sitei1324 – 13241Calcium ion selectivity and permeabilityBy similarity
    Sitei1615 – 16151Calcium ion selectivity and permeabilityBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi377 – 38812PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi1704 – 171512PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. calcium ion import Source: RGD
    2. membrane depolarization during action potential Source: RefGenome
    3. synaptic transmission Source: RefGenome

    Keywords - Molecular functioni

    Calcium channel, Ion channel, Voltage-gated channel

    Keywords - Biological processi

    Calcium transport, Ion transport, Transport

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Voltage-dependent R-type calcium channel subunit alpha-1E
    Alternative name(s):
    BII
    Brain calcium channel II
    Calcium channel, L type, alpha-1 polypeptide, isoform 6
    RBE-II
    RBE2
    Voltage-gated calcium channel subunit alpha Cav2.3
    Gene namesi
    Name:Cacna1e
    Synonyms:Cach6, Cacnl1a6
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi2246. Cacna1e.

    Subcellular locationi

    GO - Cellular componenti

    1. perikaryon Source: RGD
    2. voltage-gated calcium channel complex Source: RGD

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 22222222Voltage-dependent R-type calcium channel subunit alpha-1EPRO_0000053941Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi205 – 2051N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1518 – 15181N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1523 – 15231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1641 – 16411N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1686 – 16861Phosphoserine; by PKASequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ07652.
    PRIDEiQ07652.

    PTM databases

    PhosphoSiteiQ07652.

    Expressioni

    Tissue specificityi

    Expressed in central nervous system and in insulinoma.

    Gene expression databases

    GenevestigatoriQ07652.

    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.

    Protein-protein interaction databases

    DIPiDIP-46236N.

    Structurei

    Secondary structure

    1
    2222
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1818 – 183518

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3DVKX-ray2.30B1818-1837[»]
    ProteinModelPortaliQ07652.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ07652.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4040CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini60 – 7819ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini98 – 10912CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini125 – 13612ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini157 – 17418CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini196 – 27782ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini302 – 427126CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini448 – 46013ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini481 – 4899CytoplasmicSequence Analysis
    Topological domaini509 – 51810ExtracellularSequence Analysis
    Topological domaini538 – 55619CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini577 – 62953ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini655 – 1100446CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1118 – 114124ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1162 – 11698CytoplasmicSequence Analysis
    Topological domaini1193 – 120614ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1225 – 124319CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1264 – 135087ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1375 – 143157CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1451 – 146717ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1486 – 14938CytoplasmicSequence Analysis
    Topological domaini1513 – 152311ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1543 – 156119CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1582 – 165069ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1677 – 2222546CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei41 – 5919Helical; Name=S1 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei79 – 9719Helical; Name=S2 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei110 – 12415Helical; Name=S3 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei137 – 15620Helical; Name=S4 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei175 – 19521Helical; Name=S5 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei278 – 30124Helical; Name=S6 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei428 – 44720Helical; Name=S1 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei461 – 48020Helical; Name=S2 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei490 – 50819Helical; Name=S3 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei519 – 53719Helical; Name=S4 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei557 – 57620Helical; Name=S5 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei630 – 65425Helical; Name=S6 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei1101 – 111717Helical; Name=S1 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1142 – 116120Helical; Name=S2 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1170 – 119223Helical; Name=S3 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1207 – 122418Helical; Name=S4 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1244 – 126320Helical; Name=S5 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1351 – 137424Helical; Name=S6 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1432 – 145019Helical; Name=S1 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1468 – 148518Helical; Name=S2 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1494 – 151219Helical; Name=S3 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1524 – 154219Helical; Name=S4 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1562 – 158120Helical; Name=S5 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1651 – 167626Helical; Name=S6 of repeat IVSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati27 – 305279IAdd
    BLAST
    Repeati413 – 657245IIAdd
    BLAST
    Repeati1092 – 1378287IIIAdd
    BLAST
    Repeati1415 – 1678264IVAdd
    BLAST
    Domaini1691 – 172636EF-handPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni325 – 34218Binding to the beta subunitBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi667 – 6726Poly-Glu
    Compositional biasi699 – 7046Poly-Arg
    Compositional biasi718 – 7236Poly-Arg
    Compositional biasi1058 – 10647Poly-Glu
    Compositional biasi1180 – 11834Poly-Val
    Compositional biasi2193 – 21964Poly-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.
    PhylomeDBiQ07652.

    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]

    Sequencei

    Sequence statusi: Complete.

    Q07652-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALYNPIPVR QNCFTVNRSL FIFGEDNIVR KYAKKLIDWP PFEYMILATI     50
    IANCIVLALE QHLPEDDKTP MSRRLEKTEP YFIGIFCFEA GIKIVALGFI 100
    FHKGSYLRNG WNVMDFIVVL SGILATAGTH FNTHVDLRTL RAVRVLRPLK 150
    LVSGIPSLQI VLKSIMKAMV PLLQIGLLLF FAILMFAIIG LEFYSGKLHR 200
    ACFMNNSGIL EGFDPPHPCG VQGCPAGYEC KDWIGPNDGI TQFDNILFAV 250
    LTVFQCITME GWTTVLYNTN DALGATWNWL YFIPLIIIGS FFVLNLVLGV 300
    LSGEFAKERE RVENRRAFMK LRRQQQIERE LNGYRAWIDK AEEVMLAEEN 350
    KNSGTSALEV LRRATIKRSR TEAMTRDSSD EHCVDISSVG TPLARASIKS 400
    TKVDGASYFR HKERLLRISI RHMVKSQVFY WIVLSVVALN TACVAIVHHN 450
    QPQWLTHLLY YAEFLFLGLF LLEMSLKMYG MGPRLYFHSS FNCFDFGVTV 500
    GSIFEVVWAI FRPGTSFGIS VLRALRLLRI FKITKYWASL RNLVVSLMSS 550
    MKSIISLLFL LFLFIVVFAL LGMQLFGGRF NFNDGTPSAN FDTFPAAIMT 600
    VFQILTGEDW NEVMYNGIRS QGGVSSGMWS AIYFIVLTLF GNYTLLNVFL 650
    AIAVDNLANA QELTKDEQEE EEAFNQKHAL QKAKEVSPMS APNMPSIERD 700
    RRRRHHMSMW EPRSSHLRER RRRHHMSVWE QRTSQLRRHM QMSSQEALNK 750
    EEAPPMNPLN PLNPLSPLNP LNAHPSLYRR PRPIEGLALG LGLEKCEEER 800
    ISRGGSLKGD IGGLTSVLDN QRSPLSLGKR EPPWLPRSCH GNCDPTQQET 850
    GGGETVVTFE DRARHRQSQR RSRHRRVRTE GKESASASRS RSASQERSLD 900
    EGVSIDGEKE HEPQSSHRSK EPTIHEEERT QDLRRTNSLM VPRGSGLVGA 950
    LDEAETPLVQ PQPELEVGKD AALTEQEAEG SSEQALLADV QLDVGRGISQ 1000
    SEPDLSCMTT NMDKATTEST SVTVAIPDVD PLVDSTVVNI SNKTDGEASP 1050
    LKEAETKEEE EEVEKKKQKK EKRETGKAMV PHSSMFIFST TNPIRKACHY 1100
    IVNLRYFEMC ILLVIAASSI ALAAEDPVLT NSERNKVLRY FDYVFTGVFT 1150
    FEMVIKMIDQ GLILQDGSYF RDLWNILDFV VVVGALVAFA LANALGTNKG 1200
    RDIKTIKSLR VLRVLRPLKT IKRLPKLKAV FDCVVTSLKN VFNILIVYKL 1250
    FMFIFAVIAV QLFKGKFFYC TDSSKDTEKE CIGNYVDHEK NKMEVKGREW 1300
    KRHEFHYDNI IWALLTLFTV STGEGWPQVL QHSVDVTEED RGPSRSNRME 1350
    MSIFYVVYFV VFPFFFVNIF VALIIITFQE QGDKMMEECS LEKNERACID 1400
    FAISAKPLTR YMPQNRHTFQ YRVWHFVVSP SFEYTIMAMI ALNTVVLMMK 1450
    YYSAPWTYEL ALKYLNIAFT MVFSLECVLK VIAFGFLNYF RDTWNIFDFI 1500
    TVIGSITEII LTDSKLVNTS GFNMSFLKLF RAARLIKLLR QGYTIRILLW 1550
    TFVQSFKALP YVCLLIAMLF FIYAIIGMQV FGNIKLDEES HINRHNNFRS 1600
    FFGSLMLLFR SATGEAWQEI MLSCLGEKGC EPDTTAPSGQ NESERCGTDL 1650
    AYVYFVSFIF FCSFLMLNLF VAVIMDNFEY LTRDSSILGP HHLDEFVRVW 1700
    AEYDRAACGR IHYTEMYEML TLMSPPLGLG KRCPSKVAYK RLVLMNMPVA 1750
    EDMTVHFTST LMALIRTALD IKIAKGGADR QQLDSELQKE TLAIWPHLSQ 1800
    KMLDLLVPMP KASDLTVGKI YAAMMIMDYY KQSKVKKQRQ QLEEQKNAPM 1850
    FQRMEPSSLP QEIISNAKAL PYLQQDPVSG LSGRSGYPSM SPLSPQEIFQ 1900
    LACMDPADDG QFQEQQSLVV TDPSSMRRSF STIRDKRSNS SWLEEFSMER 1950
    SSENTYKSRR RSYHSSLRLS AHRLNSDSGH KSDTHRSGGR ERGRSKERKH 2000
    LLSPDVSRCN SEERGTQADW ESPERRQSRS PSEGRSQTPN RQGTGSLSES 2050
    SIPSISDTST PRRSRRQLPP VPPKPRPLLS YSSLMRHTGG ISPPPDGSEG 2100
    GSPLASQALE SNSACLTESS NSLHPQQGQH PSPQHYISEP YLALHEDSHA 2150
    SDCGEEETLT FEAAVATSLG RSNTIGSAPP LRHSWQMPNG HYRRRRLGGL 2200
    GLAMMCGAVS DLLSDTEEDD KC 2222
    Length:2,222
    Mass (Da):252,116
    Last modified:October 1, 1996 - v1
    Checksum:iDF6452A2175CEB19
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L15453 mRNA. Translation: AAA40855.1.
    PIRiA37490.
    UniGeneiRn.10742.

    Genome annotation databases

    UCSCiRGD:2246. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L15453 mRNA. Translation: AAA40855.1 .
    PIRi A37490.
    UniGenei Rn.10742.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3DVK X-ray 2.30 B 1818-1837 [» ]
    ProteinModelPortali Q07652.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-46236N.

    Chemistry

    BindingDBi Q07652.
    GuidetoPHARMACOLOGYi 534.

    PTM databases

    PhosphoSitei Q07652.

    Proteomic databases

    PaxDbi Q07652.
    PRIDEi Q07652.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi RGD:2246. rat.

    Organism-specific databases

    RGDi 2246. Cacna1e.

    Phylogenomic databases

    eggNOGi COG1226.
    HOGENOMi HOG000231530.
    HOVERGENi HBG050763.
    PhylomeDBi Q07652.

    Miscellaneous databases

    EvolutionaryTracei Q07652.
    PROi Q07652.

    Gene expression databases

    Genevestigatori Q07652.

    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. "Structure and functional expression of a member of the low voltage-activated calcium channel family."
      Soong T.W., Stea A., Hodson C.D., Dubel S.J., Vincent S.R., Snutch T.P.
      Science 260:1133-1136(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
      Tissue: Brain.

    Entry informationi

    Entry nameiCAC1E_RAT
    AccessioniPrimary (citable) accession number: Q07652
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 113 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3