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Q07652 (CAC1E_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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 names
Name:Cacna1e
Synonyms:Cach6, Cacnl1a6
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length2222 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-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.

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.

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Expressed in central nervous system and in insulinoma.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 22222222Voltage-dependent R-type calcium channel subunit alpha-1E
PRO_0000053941

Regions

Topological domain1 – 4040Cytoplasmic Potential
Transmembrane41 – 5919Helical; Name=S1 of repeat I; Potential
Topological domain60 – 7819Extracellular Potential
Transmembrane79 – 9719Helical; Name=S2 of repeat I; Potential
Topological domain98 – 10912Cytoplasmic Potential
Transmembrane110 – 12415Helical; Name=S3 of repeat I; Potential
Topological domain125 – 13612Extracellular Potential
Transmembrane137 – 15620Helical; Name=S4 of repeat I; Potential
Topological domain157 – 17418Cytoplasmic Potential
Transmembrane175 – 19521Helical; Name=S5 of repeat I; Potential
Topological domain196 – 27782Extracellular Potential
Transmembrane278 – 30124Helical; Name=S6 of repeat I; Potential
Topological domain302 – 427126Cytoplasmic Potential
Transmembrane428 – 44720Helical; Name=S1 of repeat II; Potential
Topological domain448 – 46013Extracellular Potential
Transmembrane461 – 48020Helical; Name=S2 of repeat II; Potential
Topological domain481 – 4899Cytoplasmic Potential
Transmembrane490 – 50819Helical; Name=S3 of repeat II; Potential
Topological domain509 – 51810Extracellular Potential
Transmembrane519 – 53719Helical; Name=S4 of repeat II; Potential
Topological domain538 – 55619Cytoplasmic Potential
Transmembrane557 – 57620Helical; Name=S5 of repeat II; Potential
Topological domain577 – 62953Extracellular Potential
Transmembrane630 – 65425Helical; Name=S6 of repeat II; Potential
Topological domain655 – 1100446Cytoplasmic Potential
Transmembrane1101 – 111717Helical; Name=S1 of repeat III; Potential
Topological domain1118 – 114124Extracellular Potential
Transmembrane1142 – 116120Helical; Name=S2 of repeat III; Potential
Topological domain1162 – 11698Cytoplasmic Potential
Transmembrane1170 – 119223Helical; Name=S3 of repeat III; Potential
Topological domain1193 – 120614Extracellular Potential
Transmembrane1207 – 122418Helical; Name=S4 of repeat III; Potential
Topological domain1225 – 124319Cytoplasmic Potential
Transmembrane1244 – 126320Helical; Name=S5 of repeat III; Potential
Topological domain1264 – 135087Extracellular Potential
Transmembrane1351 – 137424Helical; Name=S6 of repeat III; Potential
Topological domain1375 – 143157Cytoplasmic Potential
Transmembrane1432 – 145019Helical; Name=S1 of repeat IV; Potential
Topological domain1451 – 146717Extracellular Potential
Transmembrane1468 – 148518Helical; Name=S2 of repeat IV; Potential
Topological domain1486 – 14938Cytoplasmic Potential
Transmembrane1494 – 151219Helical; Name=S3 of repeat IV; Potential
Topological domain1513 – 152311Extracellular Potential
Transmembrane1524 – 154219Helical; Name=S4 of repeat IV; Potential
Topological domain1543 – 156119Cytoplasmic Potential
Transmembrane1562 – 158120Helical; Name=S5 of repeat IV; Potential
Topological domain1582 – 165069Extracellular Potential
Transmembrane1651 – 167626Helical; Name=S6 of repeat IV; Potential
Topological domain1677 – 2222546Cytoplasmic Potential
Repeat27 – 305279I
Repeat413 – 657245II
Repeat1092 – 1378287III
Repeat1415 – 1678264IV
Domain1691 – 172636EF-hand
Calcium binding377 – 38812 By similarity
Calcium binding1704 – 171512 By similarity
Region325 – 34218Binding to the beta subunit By similarity
Compositional bias667 – 6726Poly-Glu
Compositional bias699 – 7046Poly-Arg
Compositional bias718 – 7236Poly-Arg
Compositional bias1058 – 10647Poly-Glu
Compositional bias1180 – 11834Poly-Val
Compositional bias2193 – 21964Poly-Arg

Sites

Site2601Calcium ion selectivity and permeability By similarity
Site6081Calcium ion selectivity and permeability By similarity
Site13241Calcium ion selectivity and permeability By similarity
Site16151Calcium ion selectivity and permeability By similarity

Amino acid modifications

Modified residue6871Phosphoserine By similarity
Modified residue8061Phosphoserine By similarity
Modified residue16861Phosphoserine; by PKA Potential
Modified residue20221Phosphoserine By similarity
Modified residue20461Phosphoserine By similarity
Glycosylation2051N-linked (GlcNAc...) Potential
Glycosylation15181N-linked (GlcNAc...) Potential
Glycosylation15231N-linked (GlcNAc...) Potential
Glycosylation16411N-linked (GlcNAc...) Potential

Secondary structure

1 ... 2222
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q07652 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: DF6452A2175CEB19

FASTA2,222252,116
        10         20         30         40         50         60 
MALYNPIPVR QNCFTVNRSL FIFGEDNIVR KYAKKLIDWP PFEYMILATI IANCIVLALE 

        70         80         90        100        110        120 
QHLPEDDKTP MSRRLEKTEP YFIGIFCFEA GIKIVALGFI FHKGSYLRNG WNVMDFIVVL 

       130        140        150        160        170        180 
SGILATAGTH FNTHVDLRTL RAVRVLRPLK LVSGIPSLQI VLKSIMKAMV PLLQIGLLLF 

       190        200        210        220        230        240 
FAILMFAIIG LEFYSGKLHR ACFMNNSGIL EGFDPPHPCG VQGCPAGYEC KDWIGPNDGI 

       250        260        270        280        290        300 
TQFDNILFAV LTVFQCITME GWTTVLYNTN DALGATWNWL YFIPLIIIGS FFVLNLVLGV 

       310        320        330        340        350        360 
LSGEFAKERE RVENRRAFMK LRRQQQIERE LNGYRAWIDK AEEVMLAEEN KNSGTSALEV 

       370        380        390        400        410        420 
LRRATIKRSR TEAMTRDSSD EHCVDISSVG TPLARASIKS TKVDGASYFR HKERLLRISI 

       430        440        450        460        470        480 
RHMVKSQVFY WIVLSVVALN TACVAIVHHN QPQWLTHLLY YAEFLFLGLF LLEMSLKMYG 

       490        500        510        520        530        540 
MGPRLYFHSS FNCFDFGVTV GSIFEVVWAI FRPGTSFGIS VLRALRLLRI FKITKYWASL 

       550        560        570        580        590        600 
RNLVVSLMSS MKSIISLLFL LFLFIVVFAL LGMQLFGGRF NFNDGTPSAN FDTFPAAIMT 

       610        620        630        640        650        660 
VFQILTGEDW NEVMYNGIRS QGGVSSGMWS AIYFIVLTLF GNYTLLNVFL AIAVDNLANA 

       670        680        690        700        710        720 
QELTKDEQEE EEAFNQKHAL QKAKEVSPMS APNMPSIERD RRRRHHMSMW EPRSSHLRER 

       730        740        750        760        770        780 
RRRHHMSVWE QRTSQLRRHM QMSSQEALNK EEAPPMNPLN PLNPLSPLNP LNAHPSLYRR 

       790        800        810        820        830        840 
PRPIEGLALG LGLEKCEEER ISRGGSLKGD IGGLTSVLDN QRSPLSLGKR EPPWLPRSCH 

       850        860        870        880        890        900 
GNCDPTQQET GGGETVVTFE DRARHRQSQR RSRHRRVRTE GKESASASRS RSASQERSLD 

       910        920        930        940        950        960 
EGVSIDGEKE HEPQSSHRSK EPTIHEEERT QDLRRTNSLM VPRGSGLVGA LDEAETPLVQ 

       970        980        990       1000       1010       1020 
PQPELEVGKD AALTEQEAEG SSEQALLADV QLDVGRGISQ SEPDLSCMTT NMDKATTEST 

      1030       1040       1050       1060       1070       1080 
SVTVAIPDVD PLVDSTVVNI SNKTDGEASP LKEAETKEEE EEVEKKKQKK EKRETGKAMV 

      1090       1100       1110       1120       1130       1140 
PHSSMFIFST TNPIRKACHY IVNLRYFEMC ILLVIAASSI ALAAEDPVLT NSERNKVLRY 

      1150       1160       1170       1180       1190       1200 
FDYVFTGVFT FEMVIKMIDQ GLILQDGSYF RDLWNILDFV VVVGALVAFA LANALGTNKG 

      1210       1220       1230       1240       1250       1260 
RDIKTIKSLR VLRVLRPLKT IKRLPKLKAV FDCVVTSLKN VFNILIVYKL FMFIFAVIAV 

      1270       1280       1290       1300       1310       1320 
QLFKGKFFYC TDSSKDTEKE CIGNYVDHEK NKMEVKGREW KRHEFHYDNI IWALLTLFTV 

      1330       1340       1350       1360       1370       1380 
STGEGWPQVL QHSVDVTEED RGPSRSNRME MSIFYVVYFV VFPFFFVNIF VALIIITFQE 

      1390       1400       1410       1420       1430       1440 
QGDKMMEECS LEKNERACID FAISAKPLTR YMPQNRHTFQ YRVWHFVVSP SFEYTIMAMI 

      1450       1460       1470       1480       1490       1500 
ALNTVVLMMK YYSAPWTYEL ALKYLNIAFT MVFSLECVLK VIAFGFLNYF RDTWNIFDFI 

      1510       1520       1530       1540       1550       1560 
TVIGSITEII LTDSKLVNTS GFNMSFLKLF RAARLIKLLR QGYTIRILLW TFVQSFKALP 

      1570       1580       1590       1600       1610       1620 
YVCLLIAMLF FIYAIIGMQV FGNIKLDEES HINRHNNFRS FFGSLMLLFR SATGEAWQEI 

      1630       1640       1650       1660       1670       1680 
MLSCLGEKGC EPDTTAPSGQ NESERCGTDL AYVYFVSFIF FCSFLMLNLF VAVIMDNFEY 

      1690       1700       1710       1720       1730       1740 
LTRDSSILGP HHLDEFVRVW AEYDRAACGR IHYTEMYEML TLMSPPLGLG KRCPSKVAYK 

      1750       1760       1770       1780       1790       1800 
RLVLMNMPVA EDMTVHFTST LMALIRTALD IKIAKGGADR QQLDSELQKE TLAIWPHLSQ 

      1810       1820       1830       1840       1850       1860 
KMLDLLVPMP KASDLTVGKI YAAMMIMDYY KQSKVKKQRQ QLEEQKNAPM FQRMEPSSLP 

      1870       1880       1890       1900       1910       1920 
QEIISNAKAL PYLQQDPVSG LSGRSGYPSM SPLSPQEIFQ LACMDPADDG QFQEQQSLVV 

      1930       1940       1950       1960       1970       1980 
TDPSSMRRSF STIRDKRSNS SWLEEFSMER SSENTYKSRR RSYHSSLRLS AHRLNSDSGH 

      1990       2000       2010       2020       2030       2040 
KSDTHRSGGR ERGRSKERKH LLSPDVSRCN SEERGTQADW ESPERRQSRS PSEGRSQTPN 

      2050       2060       2070       2080       2090       2100 
RQGTGSLSES SIPSISDTST PRRSRRQLPP VPPKPRPLLS YSSLMRHTGG ISPPPDGSEG 

      2110       2120       2130       2140       2150       2160 
GSPLASQALE SNSACLTESS NSLHPQQGQH PSPQHYISEP YLALHEDSHA SDCGEEETLT 

      2170       2180       2190       2200       2210       2220 
FEAAVATSLG RSNTIGSAPP LRHSWQMPNG HYRRRRLGGL GLAMMCGAVS DLLSDTEEDD 


KC

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References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L15453 mRNA. Translation: AAA40855.1.
IPIIPI00201157.
PIRA37490.
UniGeneRn.10742.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3DVKX-ray2.30B1818-1837[»]
ProteinModelPortalQ07652.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-46236N.

PTM databases

PhosphoSiteQ07652.

Proteomic databases

PaxDbQ07652.
PRIDEQ07652.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:2246. rat.

Organism-specific databases

RGD2246. Cacna1e.

Phylogenomic databases

eggNOGCOG1226.
HOGENOMHOG000231530.
HOVERGENHBG050763.
OrthoDBEOG45B1DN.

Gene expression databases

ArrayExpressQ07652.
GenevestigatorQ07652.
GermOnlineENSRNOG00000002863. Rattus norvegicus.

Family and domain databases

Gene3D1.20.120.350. 4 hits.
InterProIPR002048. EF_hand_dom.
IPR005821. Ion_trans_dom.
IPR027359. K_channel_four-helix_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

BindingDBQ07652.
ChEMBLCHEMBL4115.
EvolutionaryTraceQ07652.

Entry information

Entry nameCAC1E_RAT
AccessionPrimary (citable) accession number: Q07652
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 29, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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