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Protein

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

Gene

Cacna1e

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Sitei310Calcium ion selectivity and permeabilityBy similarity1
Sitei658Calcium ion selectivity and permeabilityBy similarity1
Sitei1375Calcium ion selectivity and permeabilityBy similarity1
Sitei1666Calcium ion selectivity and permeabilityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi427 – 438PROSITE-ProRule annotationAdd BLAST12
Calcium bindingi1755 – 1766PROSITE-ProRule annotationAdd BLAST12

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • high voltage-gated calcium channel activity Source: GO_Central
  • protein N-terminus binding Source: UniProtKB
  • voltage-gated calcium channel activity Source: MGI

GO - Biological processi

  • behavioral fear response Source: MGI
  • behavioral response to pain Source: MGI
  • calcium ion transmembrane transport Source: MGI
  • calcium ion transport Source: MGI
  • fear response Source: MGI
  • flagellated sperm motility Source: MGI
  • glucose homeostasis Source: MGI
  • locomotory behavior Source: MGI
  • membrane depolarization during action potential Source: GO_Central
  • neurological system process Source: MGI
  • regulation of heart rate Source: MGI
  • regulation of insulin secretion involved in cellular response to glucose stimulus Source: MGI
  • regulation of somatostatin secretion Source: MGI
  • response to pain Source: MGI
  • sensory perception of pain Source: MGI
  • transmission of nerve impulse Source: MGI
  • visual learning Source: MGI
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

Protein family/group databases

TCDBi1.A.1.11.3. the voltage-gated ion channel (vic) superfamily.

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, Cchra1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:106217. Cacna1e.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 90CytoplasmicSequence analysisAdd BLAST90
Transmembranei91 – 109Helical; Name=S1 of repeat ISequence analysisAdd BLAST19
Topological domaini110 – 128ExtracellularSequence analysisAdd BLAST19
Transmembranei129 – 147Helical; Name=S2 of repeat ISequence analysisAdd BLAST19
Topological domaini148 – 159CytoplasmicSequence analysisAdd BLAST12
Transmembranei160 – 174Helical; Name=S3 of repeat ISequence analysisAdd BLAST15
Topological domaini175 – 186ExtracellularSequence analysisAdd BLAST12
Transmembranei187 – 206Helical; Name=S4 of repeat ISequence analysisAdd BLAST20
Topological domaini207 – 224CytoplasmicSequence analysisAdd BLAST18
Transmembranei225 – 245Helical; Name=S5 of repeat ISequence analysisAdd BLAST21
Topological domaini246 – 327ExtracellularSequence analysisAdd BLAST82
Transmembranei328 – 351Helical; Name=S6 of repeat ISequence analysisAdd BLAST24
Topological domaini352 – 477CytoplasmicSequence analysisAdd BLAST126
Transmembranei478 – 497Helical; Name=S1 of repeat IISequence analysisAdd BLAST20
Topological domaini498 – 510ExtracellularSequence analysisAdd BLAST13
Transmembranei511 – 530Helical; Name=S2 of repeat IISequence analysisAdd BLAST20
Topological domaini531 – 539CytoplasmicSequence analysis9
Transmembranei540 – 558Helical; Name=S3 of repeat IISequence analysisAdd BLAST19
Topological domaini559 – 568ExtracellularSequence analysis10
Transmembranei569 – 587Helical; Name=S4 of repeat IISequence analysisAdd BLAST19
Topological domaini588 – 606CytoplasmicSequence analysisAdd BLAST19
Transmembranei607 – 626Helical; Name=S5 of repeat IISequence analysisAdd BLAST20
Topological domaini627 – 679ExtracellularSequence analysisAdd BLAST53
Transmembranei680 – 704Helical; Name=S6 of repeat IISequence analysisAdd BLAST25
Topological domaini705 – 1150CytoplasmicSequence analysisAdd BLAST446
Transmembranei1151 – 1167Helical; Name=S1 of repeat IIISequence analysisAdd BLAST17
Topological domaini1168 – 1191ExtracellularSequence analysisAdd BLAST24
Transmembranei1192 – 1211Helical; Name=S2 of repeat IIISequence analysisAdd BLAST20
Topological domaini1212 – 1219CytoplasmicSequence analysis8
Transmembranei1220 – 1242Helical; Name=S3 of repeat IIISequence analysisAdd BLAST23
Topological domaini1243 – 1256ExtracellularSequence analysisAdd BLAST14
Transmembranei1257 – 1274Helical; Name=S4 of repeat IIISequence analysisAdd BLAST18
Topological domaini1275 – 1293CytoplasmicSequence analysisAdd BLAST19
Transmembranei1294 – 1313Helical; Name=S5 of repeat IIISequence analysisAdd BLAST20
Topological domaini1314 – 1400ExtracellularSequence analysisAdd BLAST87
Transmembranei1401 – 1424Helical; Name=S6 of repeat IIISequence analysisAdd BLAST24
Topological domaini1425 – 1481CytoplasmicSequence analysisAdd BLAST57
Transmembranei1482 – 1500Helical; Name=S1 of repeat IVSequence analysisAdd BLAST19
Topological domaini1501 – 1515ExtracellularSequence analysisAdd BLAST15
Transmembranei1516 – 1535Helical; Name=S2 of repeat IVSequence analysisAdd BLAST20
Topological domaini1536 – 1543CytoplasmicSequence analysis8
Transmembranei1544 – 1562Helical; Name=S3 of repeat IVSequence analysisAdd BLAST19
Topological domaini1563 – 1573ExtracellularSequence analysisAdd BLAST11
Transmembranei1574 – 1592Helical; Name=S4 of repeat IVSequence analysisAdd BLAST19
Topological domaini1593 – 1611CytoplasmicSequence analysisAdd BLAST19
Transmembranei1612 – 1631Helical; Name=S5 of repeat IVSequence analysisAdd BLAST20
Topological domaini1632 – 1700ExtracellularSequence analysisAdd BLAST69
Transmembranei1701 – 1726Helical; Name=S6 of repeat IVSequence analysisAdd BLAST26
Topological domaini1727 – 2272CytoplasmicSequence analysisAdd BLAST546

GO - Cellular componenti

  • voltage-gated calcium channel complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000539391 – 2272Voltage-dependent R-type calcium channel subunit alpha-1EAdd BLAST2272

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei15PhosphoserineCombined sources1
Modified residuei20PhosphoserineCombined sources1
Glycosylationi255N-linked (GlcNAc...)Sequence analysis1
Modified residuei428PhosphoserineCombined sources1
Modified residuei441PhosphothreonineCombined sources1
Modified residuei737PhosphoserineBy similarity1
Modified residuei746PhosphoserineCombined sources1
Modified residuei794PhosphoserineBy similarity1
Modified residuei816PhosphoserineCombined sources1
Modified residuei856PhosphoserineCombined sources1
Modified residuei948PhosphoserineBy similarity1
Modified residuei1099PhosphoserineBy similarity1
Glycosylationi1569N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1692N-linked (GlcNAc...)Sequence analysis1
Modified residuei1737Phosphoserine; by PKASequence analysis1
Modified residuei2054PhosphoserineCombined sources1
Modified residuei2073PhosphoserineBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ61290.
MaxQBiQ61290.
PaxDbiQ61290.
PRIDEiQ61290.

PTM databases

iPTMnetiQ61290.
PhosphoSitePlusiQ61290.

Expressioni

Tissue specificityi

Expressed in neuronal tissues, retina, spleen, and pancreatic islet cells.

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.

GO - Molecular functioni

  • protein N-terminus binding Source: UniProtKB

Protein-protein interaction databases

IntActiQ61290. 2 interactors.
STRINGi10090.ENSMUSP00000004214.

Structurei

3D structure databases

ProteinModelPortaliQ61290.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati77 – 355IAdd BLAST279
Repeati463 – 707IIAdd BLAST245
Repeati1143 – 1429IIIAdd BLAST287
Repeati1466 – 1729IVAdd BLAST264
Domaini1742 – 1777EF-handPROSITE-ProRule annotationAdd BLAST36

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni375 – 392Binding to the beta subunitBy similarityAdd BLAST18

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi717 – 722Poly-Glu6
Compositional biasi751 – 754Poly-Arg4
Compositional biasi770 – 773Poly-Arg4
Compositional biasi1108 – 1112Poly-Glu5
Compositional biasi1115 – 1118Poly-Lys4
Compositional biasi1231 – 1234Poly-Val4
Compositional biasi2244 – 2247Poly-Arg4

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

eggNOGiKOG2301. Eukaryota.
ENOG410XNP6. LUCA.
HOVERGENiHBG050763.
InParanoidiQ61290.
PhylomeDBiQ61290.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR027359. Channel_four-helix_dom.
IPR002048. EF_hand_dom.
IPR031649. GPHH_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005449. VDCC_R_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PANTHERiPTHR10037:SF57. PTHR10037:SF57. 3 hits.
PfamiPF08763. Ca_chan_IQ. 1 hit.
PF16905. GPHH. 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.

Q61290-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARFGEAVVV GRPGSGDGDS DQSRNRQGTP VPASGPAAAY KQSKAQRART
60 70 80 90 100
MALYNPIPVR QNCFTVNRSL FIFGEDNIVR KYAKKLIDWP PFEYMILATI
110 120 130 140 150
IANCIVLALE QHLPEDDKTP MSRRLEKTEP YFIGIFCFEA GIKIVALGFI
160 170 180 190 200
FHKGSYLRNG WNVMDFIVVL SGILATAGTH FNTHVDLRAL RAVRVLRPLK
210 220 230 240 250
LVSGIPSLQI VLKSIMKAMV PLLQIGLLLF FAILMFAIIG LEFYSGKLHR
260 270 280 290 300
ACFMNNSGIL EGFDPPHPCG VQGCPAGYEC KDWIGPNDGI TQFDNILFAV
310 320 330 340 350
LTVFQCITME GWTTVLYNTN DALGATWNWL YFIPLIIIGS FFVLNLVLGV
360 370 380 390 400
LSGEFAKERE RVENRRAFMK LRRQQQIERE LNGYRAWIDK AEEVMLAEEN
410 420 430 440 450
KNSGTSALEV LRRATIKRSR TEAMTRDSSD EHCVDISSVG TPLARASIKS
460 470 480 490 500
TKVDGASYFR HKERLLRISI RHMVKSQVFY WIVLSVVALN TACVAIVHHN
510 520 530 540 550
QPQWLTHLLY YAEFLFLGLF LLEMSLKMYG MGPRLYFHSS FNCFDFGVTV
560 570 580 590 600
GSIFEVVWAI FRPGTSFGIS VLRALRLLRI FKITKYWASL RNLVVSLMSS
610 620 630 640 650
MKSIISLLFL LFLFIVVFAL LGMQLFGGRF NFNDGTPSAN FDTFPAAIMT
660 670 680 690 700
VFQILTGEDW NEVMYNGIRS QGGVSSGMWS AIYFIVLTLF GNYTLLNVFL
710 720 730 740 750
AIAVDNLANA QELTKDEQEE EEAFNQKHAL QKAKEVSPMS APNMPSIERD
760 770 780 790 800
RRRRHHMSMW EPRSSHLRER RRRHHMSVWE QRTSQLRRHM QMSSQEALNK
810 820 830 840 850
EEAPPMNPLN PLNPLSPLNP LNAHPSLYRR PRPIEGLALG LGLEKCEEER
860 870 880 890 900
ISRGGSLKGD IGGLTSALDN QRSPLSLGKR EPPWLPRSCH GNCDPIQQEA
910 920 930 940 950
GGGETVVTFE DRARHRQSQR RSRHRRVRTE GKDSASASRS RSASQERSLD
960 970 980 990 1000
EGVSVEGEKE HEPHSSHRSK EPTIHEEERT QDLRRTNSLM VPRGSGLVGA
1010 1020 1030 1040 1050
LDEAETPLVQ PQPELEVGKD AALTEQEAEG SSEQALLGDV QLDVGRGISQ
1060 1070 1080 1090 1100
SEPDLSCMTA NMDKATTEST SVTVAIPDVD PLVDSTVVNI SNKTDGEASP
1110 1120 1130 1140 1150
LKEAETKEEE EEVEKKKKQK KEKRETGKAM VPHSSMFIFS TTNPIRRACH
1160 1170 1180 1190 1200
YIVNLRYFEM CILLVIAASS IALAAEDPVL TNSERNKVLR YFDYVFTGVF
1210 1220 1230 1240 1250
TFEMVIKMID QGLILQDGSY FRDLWNILDF VVVVGALVAF ALANALGTNK
1260 1270 1280 1290 1300
GRDIKTIKSL RVLRVLRPLK TIKRLPKLKA VFDCVVTSLK NVFNILIVYK
1310 1320 1330 1340 1350
LFMFIFAVIA VQLFKGKFFY CTDSSKDTEK ECIGNYVDHE KNKMEVKGRE
1360 1370 1380 1390 1400
WKRHEFHYDN IIWALLTLFT VSTGEGWPQV LQHSVDVTEE DRGPSRSNRM
1410 1420 1430 1440 1450
EMSIFYVVYF VVFPFFFVNI FVALIIITFQ EQGDKMMEEC SLEKNERACI
1460 1470 1480 1490 1500
DFAISAKPLT RYMPQNRHTF QYRVWHFVVS PSFEYTIMAM IALNTVVLMM
1510 1520 1530 1540 1550
KYYTAPCTYE LALKYLNIAF TMVFSLECVL KVIAFGFLNY FRDTWNIFDF
1560 1570 1580 1590 1600
ITVIGSITEI ILTDSKLVNT SGFNMSFLKL FRAARLIKLL RQGYTIRILL
1610 1620 1630 1640 1650
WTFVQSFKAL PYVCLLIAML FFIYAIIGMQ VFGNIKLDEE SHINRHNNFR
1660 1670 1680 1690 1700
SFFGSLMLLF RSATGEAWQE IMLSCLGEKG CEPDTTAPSG QNESERCGTD
1710 1720 1730 1740 1750
LAYVYFVSFI FFCSFLMLNL FVAVIMDNFE YLTRDSSILG PHHLDEFVRV
1760 1770 1780 1790 1800
WAEYDRAACG RIHYTEMYEM LTLMSPPLGL GKRCPSKVAY KRLVLMNMPV
1810 1820 1830 1840 1850
AEDMTVHFTS TLMALIRTAL DIKIAKGGAD RQQLDSELQK ETLAIWPHLS
1860 1870 1880 1890 1900
QKMLDLLVPM PKASDLTVGK IYAAMMIMDY YKQSKVKKQR QQLEEQKNAP
1910 1920 1930 1940 1950
MFQRMEPSSL PQEIIANAKA LPYLQQDPVS GLSGRSGYPS MSPLSPQEIF
1960 1970 1980 1990 2000
QLACMDPADD GQFQEQQSLV VTDPSSMRRS FSTIRDKRSN SSWLEEFSME
2010 2020 2030 2040 2050
RSSENTYKSR RRSYHSSLRL SAHRLNSDSG HKSDTHRSGG RERGRSKERK
2060 2070 2080 2090 2100
HLLSPDVSRC NSEERGTQAD WESPERRQSR SPSEGRSQTP NRQGTGSLSE
2110 2120 2130 2140 2150
SSIPSISDTS TPRRSRRQLP PVPPKPRPLL SYSSLMRHTG GISPPPDGSE
2160 2170 2180 2190 2200
GGSPLASQAL ESNSACLTES SNSLHPQQGQ HPSPQHYISE PYLALHEDSH
2210 2220 2230 2240 2250
ASDCGEEETL TFEAAVATSL GRSNTIGSAP PLRHSWQMPN GHYRRRRWGA
2260 2270
WAGMMCGAVS DLLSDTEEDD KC
Length:2,272
Mass (Da):257,236
Last modified:November 1, 1996 - v1
Checksum:i70D9200B9E0C87A1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29346 mRNA. Translation: AAA59206.1.
PIRiC54972.
UniGeneiMm.267517.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29346 mRNA. Translation: AAA59206.1.
PIRiC54972.
UniGeneiMm.267517.

3D structure databases

ProteinModelPortaliQ61290.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ61290. 2 interactors.
STRINGi10090.ENSMUSP00000004214.

Protein family/group databases

TCDBi1.A.1.11.3. the voltage-gated ion channel (vic) superfamily.

PTM databases

iPTMnetiQ61290.
PhosphoSitePlusiQ61290.

Proteomic databases

EPDiQ61290.
MaxQBiQ61290.
PaxDbiQ61290.
PRIDEiQ61290.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:106217. Cacna1e.

Phylogenomic databases

eggNOGiKOG2301. Eukaryota.
ENOG410XNP6. LUCA.
HOVERGENiHBG050763.
InParanoidiQ61290.
PhylomeDBiQ61290.

Miscellaneous databases

ChiTaRSiCacna1e. mouse.
PROiQ61290.
SOURCEiSearch...

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR027359. Channel_four-helix_dom.
IPR002048. EF_hand_dom.
IPR031649. GPHH_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005449. VDCC_R_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PANTHERiPTHR10037:SF57. PTHR10037:SF57. 3 hits.
PfamiPF08763. Ca_chan_IQ. 1 hit.
PF16905. GPHH. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiCAC1E_MOUSE
AccessioniPrimary (citable) accession number: Q61290
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 145 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.