Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q07652

- CAC1E_RAT

UniProt

Q07652 - CAC1E_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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
Complete GO annotation...

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
Complete GO annotation...

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.
InParanoidiQ07652.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALYNPIPVR QNCFTVNRSL FIFGEDNIVR KYAKKLIDWP PFEYMILATI
60 70 80 90 100
IANCIVLALE QHLPEDDKTP MSRRLEKTEP YFIGIFCFEA GIKIVALGFI
110 120 130 140 150
FHKGSYLRNG WNVMDFIVVL SGILATAGTH FNTHVDLRTL RAVRVLRPLK
160 170 180 190 200
LVSGIPSLQI VLKSIMKAMV PLLQIGLLLF FAILMFAIIG LEFYSGKLHR
210 220 230 240 250
ACFMNNSGIL EGFDPPHPCG VQGCPAGYEC KDWIGPNDGI TQFDNILFAV
260 270 280 290 300
LTVFQCITME GWTTVLYNTN DALGATWNWL YFIPLIIIGS FFVLNLVLGV
310 320 330 340 350
LSGEFAKERE RVENRRAFMK LRRQQQIERE LNGYRAWIDK AEEVMLAEEN
360 370 380 390 400
KNSGTSALEV LRRATIKRSR TEAMTRDSSD EHCVDISSVG TPLARASIKS
410 420 430 440 450
TKVDGASYFR HKERLLRISI RHMVKSQVFY WIVLSVVALN TACVAIVHHN
460 470 480 490 500
QPQWLTHLLY YAEFLFLGLF LLEMSLKMYG MGPRLYFHSS FNCFDFGVTV
510 520 530 540 550
GSIFEVVWAI FRPGTSFGIS VLRALRLLRI FKITKYWASL RNLVVSLMSS
560 570 580 590 600
MKSIISLLFL LFLFIVVFAL LGMQLFGGRF NFNDGTPSAN FDTFPAAIMT
610 620 630 640 650
VFQILTGEDW NEVMYNGIRS QGGVSSGMWS AIYFIVLTLF GNYTLLNVFL
660 670 680 690 700
AIAVDNLANA QELTKDEQEE EEAFNQKHAL QKAKEVSPMS APNMPSIERD
710 720 730 740 750
RRRRHHMSMW EPRSSHLRER RRRHHMSVWE QRTSQLRRHM QMSSQEALNK
760 770 780 790 800
EEAPPMNPLN PLNPLSPLNP LNAHPSLYRR PRPIEGLALG LGLEKCEEER
810 820 830 840 850
ISRGGSLKGD IGGLTSVLDN QRSPLSLGKR EPPWLPRSCH GNCDPTQQET
860 870 880 890 900
GGGETVVTFE DRARHRQSQR RSRHRRVRTE GKESASASRS RSASQERSLD
910 920 930 940 950
EGVSIDGEKE HEPQSSHRSK EPTIHEEERT QDLRRTNSLM VPRGSGLVGA
960 970 980 990 1000
LDEAETPLVQ PQPELEVGKD AALTEQEAEG SSEQALLADV QLDVGRGISQ
1010 1020 1030 1040 1050
SEPDLSCMTT NMDKATTEST SVTVAIPDVD PLVDSTVVNI SNKTDGEASP
1060 1070 1080 1090 1100
LKEAETKEEE EEVEKKKQKK EKRETGKAMV PHSSMFIFST TNPIRKACHY
1110 1120 1130 1140 1150
IVNLRYFEMC ILLVIAASSI ALAAEDPVLT NSERNKVLRY FDYVFTGVFT
1160 1170 1180 1190 1200
FEMVIKMIDQ GLILQDGSYF RDLWNILDFV VVVGALVAFA LANALGTNKG
1210 1220 1230 1240 1250
RDIKTIKSLR VLRVLRPLKT IKRLPKLKAV FDCVVTSLKN VFNILIVYKL
1260 1270 1280 1290 1300
FMFIFAVIAV QLFKGKFFYC TDSSKDTEKE CIGNYVDHEK NKMEVKGREW
1310 1320 1330 1340 1350
KRHEFHYDNI IWALLTLFTV STGEGWPQVL QHSVDVTEED RGPSRSNRME
1360 1370 1380 1390 1400
MSIFYVVYFV VFPFFFVNIF VALIIITFQE QGDKMMEECS LEKNERACID
1410 1420 1430 1440 1450
FAISAKPLTR YMPQNRHTFQ YRVWHFVVSP SFEYTIMAMI ALNTVVLMMK
1460 1470 1480 1490 1500
YYSAPWTYEL ALKYLNIAFT MVFSLECVLK VIAFGFLNYF RDTWNIFDFI
1510 1520 1530 1540 1550
TVIGSITEII LTDSKLVNTS GFNMSFLKLF RAARLIKLLR QGYTIRILLW
1560 1570 1580 1590 1600
TFVQSFKALP YVCLLIAMLF FIYAIIGMQV FGNIKLDEES HINRHNNFRS
1610 1620 1630 1640 1650
FFGSLMLLFR SATGEAWQEI MLSCLGEKGC EPDTTAPSGQ NESERCGTDL
1660 1670 1680 1690 1700
AYVYFVSFIF FCSFLMLNLF VAVIMDNFEY LTRDSSILGP HHLDEFVRVW
1710 1720 1730 1740 1750
AEYDRAACGR IHYTEMYEML TLMSPPLGLG KRCPSKVAYK RLVLMNMPVA
1760 1770 1780 1790 1800
EDMTVHFTST LMALIRTALD IKIAKGGADR QQLDSELQKE TLAIWPHLSQ
1810 1820 1830 1840 1850
KMLDLLVPMP KASDLTVGKI YAAMMIMDYY KQSKVKKQRQ QLEEQKNAPM
1860 1870 1880 1890 1900
FQRMEPSSLP QEIISNAKAL PYLQQDPVSG LSGRSGYPSM SPLSPQEIFQ
1910 1920 1930 1940 1950
LACMDPADDG QFQEQQSLVV TDPSSMRRSF STIRDKRSNS SWLEEFSMER
1960 1970 1980 1990 2000
SSENTYKSRR RSYHSSLRLS AHRLNSDSGH KSDTHRSGGR ERGRSKERKH
2010 2020 2030 2040 2050
LLSPDVSRCN SEERGTQADW ESPERRQSRS PSEGRSQTPN RQGTGSLSES
2060 2070 2080 2090 2100
SIPSISDTST PRRSRRQLPP VPPKPRPLLS YSSLMRHTGG ISPPPDGSEG
2110 2120 2130 2140 2150
GSPLASQALE SNSACLTESS NSLHPQQGQH PSPQHYISEP YLALHEDSHA
2160 2170 2180 2190 2200
SDCGEEETLT FEAAVATSLG RSNTIGSAPP LRHSWQMPNG HYRRRRLGGL
2210 2220
GLAMMCGAVS DLLSDTEEDD KC
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.
InParanoidi Q07652.
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 29, 2014
This is version 114 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