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Q61290

- CAC1E_MOUSE

UniProt

Q61290 - CAC1E_MOUSE

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Protein

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

Gene

Cacna1e

Organism
Mus musculus (Mouse)
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
Sitei310 – 3101Calcium ion selectivity and permeabilityBy similarity
Sitei658 – 6581Calcium ion selectivity and permeabilityBy similarity
Sitei1375 – 13751Calcium ion selectivity and permeabilityBy similarity
Sitei1666 – 16661Calcium ion selectivity and permeabilityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi427 – 43812PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi1755 – 176612PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. high voltage-gated calcium channel activity Source: RefGenome
  3. protein N-terminus binding Source: UniProtKB
  4. voltage-gated calcium channel activity Source: MGI

GO - Biological processi

  1. behavioral fear response Source: MGI
  2. behavioral response to pain Source: MGI
  3. calcium ion import Source: RefGenome
  4. calcium ion transmembrane transport Source: MGI
  5. calcium ion transport Source: MGI
  6. fear response Source: MGI
  7. glucose homeostasis Source: MGI
  8. locomotory behavior Source: MGI
  9. membrane depolarization during action potential Source: RefGenome
  10. neurological system process Source: MGI
  11. regulation of heart rate Source: MGI
  12. regulation of insulin secretion involved in cellular response to glucose stimulus Source: MGI
  13. regulation of somatostatin secretion Source: MGI
  14. response to pain Source: MGI
  15. sensory perception of pain Source: MGI
  16. sperm motility Source: MGI
  17. synaptic transmission Source: RefGenome
  18. transmission of nerve impulse Source: MGI
  19. 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
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:106217. Cacna1e.

Subcellular locationi

GO - Cellular componenti

  1. plasma membrane Source: RefGenome
  2. voltage-gated calcium channel complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 22722272Voltage-dependent R-type calcium channel subunit alpha-1EPRO_0000053939Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi255 – 2551N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1569 – 15691N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1692 – 16921N-linked (GlcNAc...)Sequence Analysis
Modified residuei1737 – 17371Phosphoserine; by PKASequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ61290.
PaxDbiQ61290.
PRIDEiQ61290.

PTM databases

PhosphoSiteiQ61290.

Expressioni

Tissue specificityi

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

Gene expression databases

GenevestigatoriQ61290.

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

IntActiQ61290. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ61290.
SMRiQ61290. Positions 359-403, 1252-1279.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 9090CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini110 – 12819ExtracellularSequence AnalysisAdd
BLAST
Topological domaini148 – 15912CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini175 – 18612ExtracellularSequence AnalysisAdd
BLAST
Topological domaini207 – 22418CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini246 – 32782ExtracellularSequence AnalysisAdd
BLAST
Topological domaini352 – 477126CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini498 – 51013ExtracellularSequence AnalysisAdd
BLAST
Topological domaini531 – 5399CytoplasmicSequence Analysis
Topological domaini559 – 56810ExtracellularSequence Analysis
Topological domaini588 – 60619CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini627 – 67953ExtracellularSequence AnalysisAdd
BLAST
Topological domaini705 – 1150446CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1168 – 119124ExtracellularSequence AnalysisAdd
BLAST
Topological domaini1212 – 12198CytoplasmicSequence Analysis
Topological domaini1243 – 125614ExtracellularSequence AnalysisAdd
BLAST
Topological domaini1275 – 129319CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1314 – 140087ExtracellularSequence AnalysisAdd
BLAST
Topological domaini1425 – 148157CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1501 – 151515ExtracellularSequence AnalysisAdd
BLAST
Topological domaini1536 – 15438CytoplasmicSequence Analysis
Topological domaini1563 – 157311ExtracellularSequence AnalysisAdd
BLAST
Topological domaini1593 – 161119CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1632 – 170069ExtracellularSequence AnalysisAdd
BLAST
Topological domaini1727 – 2272546CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei91 – 10919Helical; Name=S1 of repeat ISequence AnalysisAdd
BLAST
Transmembranei129 – 14719Helical; Name=S2 of repeat ISequence AnalysisAdd
BLAST
Transmembranei160 – 17415Helical; Name=S3 of repeat ISequence AnalysisAdd
BLAST
Transmembranei187 – 20620Helical; Name=S4 of repeat ISequence AnalysisAdd
BLAST
Transmembranei225 – 24521Helical; Name=S5 of repeat ISequence AnalysisAdd
BLAST
Transmembranei328 – 35124Helical; Name=S6 of repeat ISequence AnalysisAdd
BLAST
Transmembranei478 – 49720Helical; Name=S1 of repeat IISequence AnalysisAdd
BLAST
Transmembranei511 – 53020Helical; Name=S2 of repeat IISequence AnalysisAdd
BLAST
Transmembranei540 – 55819Helical; Name=S3 of repeat IISequence AnalysisAdd
BLAST
Transmembranei569 – 58719Helical; Name=S4 of repeat IISequence AnalysisAdd
BLAST
Transmembranei607 – 62620Helical; Name=S5 of repeat IISequence AnalysisAdd
BLAST
Transmembranei680 – 70425Helical; Name=S6 of repeat IISequence AnalysisAdd
BLAST
Transmembranei1151 – 116717Helical; Name=S1 of repeat IIISequence AnalysisAdd
BLAST
Transmembranei1192 – 121120Helical; Name=S2 of repeat IIISequence AnalysisAdd
BLAST
Transmembranei1220 – 124223Helical; Name=S3 of repeat IIISequence AnalysisAdd
BLAST
Transmembranei1257 – 127418Helical; Name=S4 of repeat IIISequence AnalysisAdd
BLAST
Transmembranei1294 – 131320Helical; Name=S5 of repeat IIISequence AnalysisAdd
BLAST
Transmembranei1401 – 142424Helical; Name=S6 of repeat IIISequence AnalysisAdd
BLAST
Transmembranei1482 – 150019Helical; Name=S1 of repeat IVSequence AnalysisAdd
BLAST
Transmembranei1516 – 153520Helical; Name=S2 of repeat IVSequence AnalysisAdd
BLAST
Transmembranei1544 – 156219Helical; Name=S3 of repeat IVSequence AnalysisAdd
BLAST
Transmembranei1574 – 159219Helical; Name=S4 of repeat IVSequence AnalysisAdd
BLAST
Transmembranei1612 – 163120Helical; Name=S5 of repeat IVSequence AnalysisAdd
BLAST
Transmembranei1701 – 172626Helical; Name=S6 of repeat IVSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati77 – 355279IAdd
BLAST
Repeati463 – 707245IIAdd
BLAST
Repeati1143 – 1429287IIIAdd
BLAST
Repeati1466 – 1729264IVAdd
BLAST
Domaini1742 – 177736EF-handPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni375 – 39218Binding to the beta subunitBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi717 – 7226Poly-Glu
Compositional biasi751 – 7544Poly-Arg
Compositional biasi770 – 7734Poly-Arg
Compositional biasi1108 – 11125Poly-Glu
Compositional biasi1115 – 11184Poly-Lys
Compositional biasi1231 – 12344Poly-Val
Compositional biasi2244 – 22474Poly-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.
HOVERGENiHBG050763.
InParanoidiQ61290.
PhylomeDBiQ61290.

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.

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:
EMBL
GenBank
DDBJ
Links Updated
L29346 mRNA. Translation: AAA59206.1.
PIRiC54972.
UniGeneiMm.267517.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L29346 mRNA. Translation: AAA59206.1 .
PIRi C54972.
UniGenei Mm.267517.

3D structure databases

ProteinModelPortali Q61290.
SMRi Q61290. Positions 359-403, 1252-1279.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q61290. 2 interactions.

Protein family/group databases

TCDBi 1.A.1.11.3. the voltage-gated ion channel (vic) superfamily.

PTM databases

PhosphoSitei Q61290.

Proteomic databases

MaxQBi Q61290.
PaxDbi Q61290.
PRIDEi Q61290.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

MGIi MGI:106217. Cacna1e.

Phylogenomic databases

eggNOGi COG1226.
HOVERGENi HBG050763.
InParanoidi Q61290.
PhylomeDBi Q61290.

Miscellaneous databases

PROi Q61290.
SOURCEi Search...

Gene expression databases

Genevestigatori Q61290.

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

« Hide 'large scale' publications
  1. "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].
    Strain: BALB/c.
    Tissue: Brain.
  2. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
    Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
    Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.

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: October 29, 2014
This is version 131 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

External Data

Dasty 3