Reviewed, UniProtKB/Swiss-Prot Q61290 (CAC1E_MOUSE)

Names and origin

Protein names

Recommended name:
    Voltage-dependent R-type calcium channel subunit alpha-1E
Alternative name(s):
    Voltage-gated calcium channel subunit alpha Cav2.3
    Calcium channel, L type, alpha-1 polypeptide, isoform 6
    Brain calcium channel II
      Short name=BII

Gene names

Name:	Cacna1e
Synonyms:	Cach6, Cacnl1a6, Cchra1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	2272 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 contaning 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 neuronal tissues, retina, spleen, and pancreatic islet cells.
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. [View classification] Contains 1 EF-hand domain.

Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Membrane
Domain	Repeat Transmembrane
Ligand	Calcium
Molecular function	Calcium channel Ionic channel Voltage-gated channel
PTM	Disulfide bond Glycoprotein Phosphoprotein
Gene Ontology (GO)
Biological process	calcium ion transport Inferred from mutant phenotype. Source: MGI glucose homeostasis Inferred from mutant phenotype. Source: MGI
Cellular component	voltage-gated calcium channel complex Traceable author statement. Source: MGI
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein N-terminus binding Inferred from physical interaction. Source: UniProtKB voltage-gated calcium channel activity Inferred from mutant phenotype. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2272	2272	Voltage-dependent R-type calcium channel subunit alpha-1E		PRO_0000053939
Regions
	Topological domain	1 – 90	90	Cytoplasmic Potential
	Transmembrane	91 – 109	19	S1 of repeat I Potential
	Topological domain	110 – 128	19	Extracellular Potential
	Transmembrane	129 – 147	19	S2 of repeat I Potential
	Topological domain	148 – 159	12	Cytoplasmic Potential
	Transmembrane	160 – 174	15	S3 of repeat I Potential
	Topological domain	175 – 186	12	Extracellular Potential
	Transmembrane	187 – 206	20	S4 of repeat I Potential
	Topological domain	207 – 224	18	Cytoplasmic Potential
	Transmembrane	225 – 245	21	S5 of repeat I Potential
	Topological domain	246 – 327	82	Extracellular Potential
	Transmembrane	328 – 351	24	S6 of repeat I Potential
	Topological domain	352 – 477	126	Cytoplasmic Potential
	Transmembrane	478 – 497	20	S1 of repeat II Potential
	Topological domain	498 – 510	13	Extracellular Potential
	Transmembrane	511 – 530	20	S2 of repeat II Potential
	Topological domain	531 – 539	9	Cytoplasmic Potential
	Transmembrane	540 – 558	19	S3 of repeat II Potential
	Topological domain	559 – 568	10	Extracellular Potential
	Transmembrane	569 – 587	19	S4 of repeat II Potential
	Topological domain	588 – 606	19	Cytoplasmic Potential
	Transmembrane	607 – 626	20	S5 of repeat II Potential
	Topological domain	627 – 679	53	Extracellular Potential
	Transmembrane	680 – 704	25	S6 of repeat II Potential
	Topological domain	705 – 1150	446	Cytoplasmic Potential
	Transmembrane	1151 – 1167	17	S1 of repeat III Potential
	Topological domain	1168 – 1191	24	Extracellular Potential
	Transmembrane	1192 – 1211	20	S2 of repeat III Potential
	Topological domain	1212 – 1219	8	Cytoplasmic Potential
	Transmembrane	1220 – 1242	23	S3 of repeat III Potential
	Topological domain	1243 – 1256	14	Extracellular Potential
	Transmembrane	1257 – 1274	18	S4 of repeat III Potential
	Topological domain	1275 – 1293	19	Cytoplasmic Potential
	Transmembrane	1294 – 1313	20	S5 of repeat III Potential
	Topological domain	1314 – 1400	87	Extracellular Potential
	Transmembrane	1401 – 1424	24	S6 of repeat III Potential
	Topological domain	1425 – 1481	57	Cytoplasmic Potential
	Transmembrane	1482 – 1500	19	S1 of repeat IV Potential
	Topological domain	1501 – 1515	15	Extracellular Potential
	Transmembrane	1516 – 1535	20	S2 of repeat IV Potential
	Topological domain	1536 – 1543	8	Cytoplasmic Potential
	Transmembrane	1544 – 1562	19	S3 of repeat IV Potential
	Topological domain	1563 – 1573	11	Extracellular Potential
	Transmembrane	1574 – 1592	19	S4 of repeat IV Potential
	Topological domain	1593 – 1611	19	Cytoplasmic Potential
	Transmembrane	1612 – 1631	20	S5 of repeat IV Potential
	Topological domain	1632 – 1700	69	Extracellular Potential
	Transmembrane	1701 – 1726	26	S6 of repeat IV Potential
	Topological domain	1727 – 2272	546	Cytoplasmic Potential
	Repeat	77 – 355	279	I
	Repeat	463 – 707	245	II
	Repeat	1143 – 1429	287	III
	Repeat	1466 – 1729	264	IV
	Domain	1742 – 1777	36	EF-hand
	Calcium binding	427 – 438	12	By similarity
	Calcium binding	1755 – 1766	12	By similarity
	Region	375 – 392	18	Binding to the beta subunit By similarity
	Compositional bias	717 – 722	6	Poly-Glu
	Compositional bias	751 – 754	4	Poly-Arg
	Compositional bias	770 – 773	4	Poly-Arg
	Compositional bias	1108 – 1112	5	Poly-Glu
	Compositional bias	1115 – 1118	4	Poly-Lys
	Compositional bias	1231 – 1234	4	Poly-Val
	Compositional bias	2244 – 2247	4	Poly-Arg
Sites
	Site	310	1	Calcium ion selectivity and permeability By similarity
	Site	658	1	Calcium ion selectivity and permeability By similarity
	Site	1375	1	Calcium ion selectivity and permeability By similarity
	Site	1666	1	Calcium ion selectivity and permeability By similarity
Amino acid modifications
	Modified residue	15	1	Phosphoserine Ref.2
	Modified residue	29	1	Phosphothreonine Ref.3
	Modified residue	737	1	Phosphoserine Ref.3
	Modified residue	856	1	Phosphoserine Ref.3
	Modified residue	1737	1	Phosphoserine; by PKA Potential
	Modified residue	2073	1	Phosphoserine Ref.2 Ref.3
	Modified residue	2097	1	Phosphoserine Ref.3
	Glycosylation	255	1	N-linked (GlcNAc...) Potential
	Glycosylation	1569	1	N-linked (GlcNAc...) Potential
	Glycosylation	1692	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q61290-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 70D9200B9E0C87A1	FASTA	2,272	257,236
	10 20 30 40 50 60 MARFGEAVVV GRPGSGDGDS DQSRNRQGTP VPASGPAAAY KQSKAQRART MALYNPIPVR 70 80 90 100 110 120 QNCFTVNRSL FIFGEDNIVR KYAKKLIDWP PFEYMILATI IANCIVLALE QHLPEDDKTP 130 140 150 160 170 180 MSRRLEKTEP YFIGIFCFEA GIKIVALGFI FHKGSYLRNG WNVMDFIVVL SGILATAGTH 190 200 210 220 230 240 FNTHVDLRAL RAVRVLRPLK LVSGIPSLQI VLKSIMKAMV PLLQIGLLLF FAILMFAIIG 250 260 270 280 290 300 LEFYSGKLHR ACFMNNSGIL EGFDPPHPCG VQGCPAGYEC KDWIGPNDGI TQFDNILFAV 310 320 330 340 350 360 LTVFQCITME GWTTVLYNTN DALGATWNWL YFIPLIIIGS FFVLNLVLGV LSGEFAKERE 370 380 390 400 410 420 RVENRRAFMK LRRQQQIERE LNGYRAWIDK AEEVMLAEEN KNSGTSALEV LRRATIKRSR 430 440 450 460 470 480 TEAMTRDSSD EHCVDISSVG TPLARASIKS TKVDGASYFR HKERLLRISI RHMVKSQVFY 490 500 510 520 530 540 WIVLSVVALN TACVAIVHHN QPQWLTHLLY YAEFLFLGLF LLEMSLKMYG MGPRLYFHSS 550 560 570 580 590 600 FNCFDFGVTV GSIFEVVWAI FRPGTSFGIS VLRALRLLRI FKITKYWASL RNLVVSLMSS 610 620 630 640 650 660 MKSIISLLFL LFLFIVVFAL LGMQLFGGRF NFNDGTPSAN FDTFPAAIMT VFQILTGEDW 670 680 690 700 710 720 NEVMYNGIRS QGGVSSGMWS AIYFIVLTLF GNYTLLNVFL AIAVDNLANA QELTKDEQEE 730 740 750 760 770 780 EEAFNQKHAL QKAKEVSPMS APNMPSIERD RRRRHHMSMW EPRSSHLRER RRRHHMSVWE 790 800 810 820 830 840 QRTSQLRRHM QMSSQEALNK EEAPPMNPLN PLNPLSPLNP LNAHPSLYRR PRPIEGLALG 850 860 870 880 890 900 LGLEKCEEER ISRGGSLKGD IGGLTSALDN QRSPLSLGKR EPPWLPRSCH GNCDPIQQEA 910 920 930 940 950 960 GGGETVVTFE DRARHRQSQR RSRHRRVRTE GKDSASASRS RSASQERSLD EGVSVEGEKE 970 980 990 1000 1010 1020 HEPHSSHRSK EPTIHEEERT QDLRRTNSLM VPRGSGLVGA LDEAETPLVQ PQPELEVGKD 1030 1040 1050 1060 1070 1080 AALTEQEAEG SSEQALLGDV QLDVGRGISQ SEPDLSCMTA NMDKATTEST SVTVAIPDVD 1090 1100 1110 1120 1130 1140 PLVDSTVVNI SNKTDGEASP LKEAETKEEE EEVEKKKKQK KEKRETGKAM VPHSSMFIFS 1150 1160 1170 1180 1190 1200 TTNPIRRACH YIVNLRYFEM CILLVIAASS IALAAEDPVL TNSERNKVLR YFDYVFTGVF 1210 1220 1230 1240 1250 1260 TFEMVIKMID QGLILQDGSY FRDLWNILDF VVVVGALVAF ALANALGTNK GRDIKTIKSL 1270 1280 1290 1300 1310 1320 RVLRVLRPLK TIKRLPKLKA VFDCVVTSLK NVFNILIVYK LFMFIFAVIA VQLFKGKFFY 1330 1340 1350 1360 1370 1380 CTDSSKDTEK ECIGNYVDHE KNKMEVKGRE WKRHEFHYDN IIWALLTLFT VSTGEGWPQV 1390 1400 1410 1420 1430 1440 LQHSVDVTEE DRGPSRSNRM EMSIFYVVYF VVFPFFFVNI FVALIIITFQ EQGDKMMEEC 1450 1460 1470 1480 1490 1500 SLEKNERACI DFAISAKPLT RYMPQNRHTF QYRVWHFVVS PSFEYTIMAM IALNTVVLMM 1510 1520 1530 1540 1550 1560 KYYTAPCTYE LALKYLNIAF TMVFSLECVL KVIAFGFLNY FRDTWNIFDF ITVIGSITEI 1570 1580 1590 1600 1610 1620 ILTDSKLVNT SGFNMSFLKL FRAARLIKLL RQGYTIRILL WTFVQSFKAL PYVCLLIAML 1630 1640 1650 1660 1670 1680 FFIYAIIGMQ VFGNIKLDEE SHINRHNNFR SFFGSLMLLF RSATGEAWQE IMLSCLGEKG 1690 1700 1710 1720 1730 1740 CEPDTTAPSG QNESERCGTD LAYVYFVSFI FFCSFLMLNL FVAVIMDNFE YLTRDSSILG 1750 1760 1770 1780 1790 1800 PHHLDEFVRV WAEYDRAACG RIHYTEMYEM LTLMSPPLGL GKRCPSKVAY KRLVLMNMPV 1810 1820 1830 1840 1850 1860 AEDMTVHFTS TLMALIRTAL DIKIAKGGAD RQQLDSELQK ETLAIWPHLS QKMLDLLVPM 1870 1880 1890 1900 1910 1920 PKASDLTVGK IYAAMMIMDY YKQSKVKKQR QQLEEQKNAP MFQRMEPSSL PQEIIANAKA 1930 1940 1950 1960 1970 1980 LPYLQQDPVS GLSGRSGYPS MSPLSPQEIF QLACMDPADD GQFQEQQSLV VTDPSSMRRS 1990 2000 2010 2020 2030 2040 FSTIRDKRSN SSWLEEFSME RSSENTYKSR RRSYHSSLRL SAHRLNSDSG HKSDTHRSGG 2050 2060 2070 2080 2090 2100 RERGRSKERK HLLSPDVSRC NSEERGTQAD WESPERRQSR SPSEGRSQTP NRQGTGSLSE 2110 2120 2130 2140 2150 2160 SSIPSISDTS TPRRSRRQLP PVPPKPRPLL SYSSLMRHTG GISPPPDGSE GGSPLASQAL 2170 2180 2190 2200 2210 2220 ESNSACLTES SNSLHPQQGQ HPSPQHYISE PYLALHEDSH ASDCGEEETL TFEAAVATSL 2230 2240 2250 2260 2270 GRSNTIGSAP PLRHSWQMPN GHYRRRRWGA WAGMMCGAVS DLLSDTEEDD KC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8071363] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Brain.
[2]	"Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed: 16452087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-2073, MASS SPECTROMETRY. Tissue: Brain.
[3]	"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: 17114649] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-29; SER-737; SER-856; SER-2073 AND SER-2097, MASS SPECTROMETRY. Tissue: Brain cortex.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L29346 mRNA. Translation: AAA59206.1.
IPI	IPI00331064.
PIR	C54972.
UniGene	Mm.267517
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q61290.
Protein family/group databases
TCDB	1.A.1.11.3. voltage-gated ion channel (VIC) superfamily.
PTM databases
PhosphoSite	Q61290.
Proteomic databases
PRIDE	Q61290.
Genome annotation databases
Ensembl	ENSMUST00000004214; ENSMUSP00000004214; ENSMUSG00000004110; Mus musculus. [Genome view]
UCSC	uc007dav.1. mouse.
Organism-specific databases
MGI	MGI:106217. Cacna1e.
Phylogenomic databases
HOGENOM	Q61290.
HOVERGEN	Q61290.
Gene expression databases
ArrayExpress	Q61290.
Bgee	Q61290.
Genevestigator	Q61290.
GermOnline	ENSMUSG00000004110. Mus musculus.
Family and domain databases
InterPro	IPR018249. EF_HAND_2. IPR005821. Ion_trans. IPR014873. VDCC_a1su_IQ. IPR005449. VDCC_R_a1su. IPR002077. VDCCAlpha1. [Graphical view]
PANTHER	PTHR10037:SF57. RVDCCAlpha1. 1 hit.
Pfam	PF08763. Ca_chan_IQ. 1 hit. PF00520. Ion_trans. 4 hits. [Graphical view]
PRINTS	PR00167. CACHANNEL. PR01633. RVDCCALPHA1.
PROSITE	PS50222. EF_HAND_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

CAC1E_MOUSE

Accession

Primary (citable) accession number: Q61290

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	November 1, 1996
Last modified:	October 13, 2009
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)