Q15878 (CAC1E_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	CACNA1E
Synonyms:	CACH6, CACNL1A6

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2313 AA.
Sequence status	Complete.
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 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. Ref.4
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	Expressed in neuronal tissues and in kidney.
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.

Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding
Molecular function	Calcium channel Ion channel Voltage-gated channel
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	behavioral fear response Inferred from electronic annotation. Source: Compara behavioral response to pain Inferred from electronic annotation. Source: Compara energy reserve metabolic process Traceable author statement. Source: Reactome glucose homeostasis Inferred from electronic annotation. Source: Compara locomotory behavior Inferred from electronic annotation. Source: Compara membrane depolarization Traceable author statement. Source: Reactome regulation of heart rate Inferred from electronic annotation. Source: Compara regulation of insulin secretion Traceable author statement. Source: Reactome regulation of insulin secretion involved in cellular response to glucose stimulus Inferred from electronic annotation. Source: Compara regulation of somatostatin secretion Inferred from electronic annotation. Source: Compara sensory perception of pain Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome sperm motility Inferred from electronic annotation. Source: Compara synaptic transmission Traceable author statement. Source: Reactome visual learning Inferred from electronic annotation. Source: Compara
Cellular_component	voltage-gated calcium channel complex Traceable author statement Ref.2. Source: ProtInc
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro voltage-gated calcium channel activity Inferred from direct assay Ref.2. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q15878-1)

Also known as: Alpha-1E;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q15878-2)

Also known as: Alpha-1E-1;

The sequence of this isoform differs from the canonical sequence as follows:
     748-766: Missing.
     1967-2009: Missing.

Isoform 3 (identifier: Q15878-3)

Also known as: Alpha-1E-3;

The sequence of this isoform differs from the canonical sequence as follows:
     1967-2009: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2313

2313

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

PRO_0000053938

Regions

Topological domain

1 – 89

89

Cytoplasmic Potential

Transmembrane

90 – 108

19

Helical; Name=S1 of repeat I

Topological domain

109 – 127

19

Extracellular Potential

Transmembrane

128 – 146

19

Helical; Name=S2 of repeat I

Topological domain

147 – 158

12

Cytoplasmic Potential

Transmembrane

159 – 173

15

Helical; Name=S3 of repeat I

Topological domain

174 – 185

12

Extracellular Potential

Transmembrane

186 – 205

20

Helical; Name=S4 of repeat I

Topological domain

206 – 223

18

Cytoplasmic Potential

Transmembrane

224 – 244

21

Helical; Name=S5 of repeat I

Topological domain

245 – 326

82

Extracellular Potential

Transmembrane

327 – 350

24

Helical; Name=S6 of repeat I

Topological domain

351 – 476

126

Cytoplasmic Potential

Transmembrane

477 – 496

20

Helical; Name=S1 of repeat II

Topological domain

497 – 509

13

Extracellular Potential

Transmembrane

510 – 529

20

Helical; Name=S2 of repeat II

Topological domain

530 – 538

9

Cytoplasmic Potential

Transmembrane

539 – 557

19

Helical; Name=S3 of repeat II

Topological domain

558 – 567

10

Extracellular Potential

Transmembrane

568 – 586

19

Helical; Name=S4 of repeat II

Topological domain

587 – 605

19

Cytoplasmic Potential

Transmembrane

606 – 625

20

Helical; Name=S5 of repeat II

Topological domain

626 – 678

53

Extracellular Potential

Transmembrane

679 – 703

25

Helical; Name=S6 of repeat II

Topological domain

704 – 1148

445

Cytoplasmic Potential

Transmembrane

1149 – 1165

17

Helical; Name=S1 of repeat III

Topological domain

1166 – 1189

24

Extracellular Potential

Transmembrane

1190 – 1209

20

Helical; Name=S2 of repeat III

Topological domain

1210 – 1217

8

Cytoplasmic Potential

Transmembrane

1218 – 1240

23

Helical; Name=S3 of repeat III

Topological domain

1241 – 1254

14

Extracellular Potential

Transmembrane

1255 – 1272

18

Helical; Name=S4 of repeat III

Topological domain

1273 – 1291

19

Cytoplasmic Potential

Transmembrane

1292 – 1311

20

Helical; Name=S5 of repeat III

Topological domain

1312 – 1398

87

Extracellular Potential

Transmembrane

1399 – 1422

24

Helical; Name=S6 of repeat III

Topological domain

1423 – 1479

57

Cytoplasmic Potential

Transmembrane

1480 – 1498

19

Helical; Name=S1 of repeat IV

Topological domain

1499 – 1513

15

Extracellular Potential

Transmembrane

1514 – 1533

20

Helical; Name=S2 of repeat IV

Topological domain

1534 – 1541

8

Cytoplasmic Potential

Transmembrane

1542 – 1560

19

Helical; Name=S3 of repeat IV

Topological domain

1561 – 1571

11

Extracellular Potential

Transmembrane

1572 – 1590

19

Helical; Name=S4 of repeat IV

Topological domain

1591 – 1609

19

Cytoplasmic Potential

Transmembrane

1610 – 1629

20

Helical; Name=S5 of repeat IV

Topological domain

1630 – 1698

69

Extracellular Potential

Transmembrane

1699 – 1724

26

Helical; Name=S6 of repeat IV

Topological domain

1725 – 2313

589

Cytoplasmic Potential

Repeat

76 – 354

279

I

Repeat

462 – 706

245

II

Repeat

1140 – 1426

287

III

Repeat

1463 – 1726

264

IV

Domain

1739 – 1774

36

EF-hand

Calcium binding

426 – 437

12

By similarity

Calcium binding

1752 – 1763

12

By similarity

Region

374 – 391

18

Binding to the beta subunit By similarity

Compositional bias

716 – 721

6

Poly-Glu

Compositional bias

748 – 753

6

Poly-Arg

Compositional bias

767 – 772

6

Poly-Arg

Compositional bias

1228 – 1231

4

Poly-Val

Compositional bias

2284 – 2288

5

Poly-Arg

Sites

Site

309

1

Calcium ion selectivity and permeability By similarity

Site

657

1

Calcium ion selectivity and permeability By similarity

Site

1372

1

Calcium ion selectivity and permeability By similarity

Site

1663

1

Calcium ion selectivity and permeability By similarity

Amino acid modifications

Modified residue

14

1

Phosphoserine By similarity

Modified residue

28

1

Phosphothreonine By similarity

Modified residue

736

1

Phosphoserine By similarity

Modified residue

855

1

Phosphoserine By similarity

Modified residue

1734

1

Phosphoserine; by PKA Potential

Modified residue

2113

1

Phosphoserine By similarity

Modified residue

2137

1

Phosphoserine By similarity

Glycosylation

254

1

N-linked (GlcNAc...) Potential

Glycosylation

1566

1

N-linked (GlcNAc...) Potential

Glycosylation

1571

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

748 – 766

19

Missing in isoform 2.

VSP_000937

Alternative sequence

1967 – 2009

43

Missing in isoform 2 and isoform 3.

VSP_024817

Natural variant

859

1

D → E.
Corresponds to variant rs35737760 [ dbSNP | Ensembl ].

VAR_031912

Natural variant

1955

1

A → T. Ref.1
Corresponds to variant rs704326 [ dbSNP | Ensembl ].

VAR_046996

Experimental info

Sequence conflict

648

1

M → I in AAA72125. Ref.1

Sequence conflict

836 – 838

3

LAL → WP in AAA72125. Ref.1

Sequence conflict

2077

1

R → P in AAA59204. Ref.2

Sequence conflict

2077

1

R → P in AAA59205. Ref.2

Sequence conflict

2084

1

G → R in AAA59204. Ref.2

Sequence conflict

2084

1

G → R in AAA59205. Ref.2

Sequence conflict

2206

1

C → W in AAA59204. Ref.2

Sequence conflict

2206

1

C → W in AAA59205. Ref.2

Sequence conflict

2219

1

S → R in AAA59204. Ref.2

Sequence conflict

2219

1

S → R in AAA59205. Ref.2

Sequence conflict

2245

1

G → V in AAA59204. Ref.2

Sequence conflict

2245

1

G → V in AAA59205. Ref.2

Secondary structure

1

.

.

.

2313

Helix Strand Turn

Details...

Helix

1868 – 1882

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Alpha-1E) [UniParc]. Last modified October 14, 2008. Version 3. Checksum: CCC7F309C27C42F1	FASTA	2,313	261,731
	10 20 30 40 50 60 MARFGEAVVA RPGSGDGDSD QSRNRQGTPV PASGQAAAYK QTKAQRARTM ALYNPIPVRQ 70 80 90 100 110 120 NCFTVNRSLF IFGEDNIVRK YAKKLIDWPP FEYMILATII ANCIVLALEQ HLPEDDKTPM 130 140 150 160 170 180 SRRLEKTEPY FIGIFCFEAG IKIVALGFIF HKGSYLRNGW NVMDFIVVLS GILATAGTHF 190 200 210 220 230 240 NTHVDLRTLR AVRVLRPLKL VSGIPSLQIV LKSIMKAMVP LLQIGLLLFF AILMFAIIGL 250 260 270 280 290 300 EFYSGKLHRA CFMNNSGILE GFDPPHPCGV QGCPAGYECK DWIGPNDGIT QFDNILFAVL 310 320 330 340 350 360 TVFQCITMEG WTTVLYNTND ALGATWNWLY FIPLIIIGSF FVLNLVLGVL SGEFAKERER 370 380 390 400 410 420 VENRRAFMKL RRQQQIEREL NGYRAWIDKA EEVMLAEENK NAGTSALEVL RRATIKRSRT 430 440 450 460 470 480 EAMTRDSSDE HCVDISSVGT PLARASIKSA KVDGVSYFRH KERLLRISIR HMVKSQVFYW 490 500 510 520 530 540 IVLSLVALNT ACVAIVHHNQ PQWLTHLLYY AEFLFLGLFL LEMSLKMYGM GPRLYFHSSF 550 560 570 580 590 600 NCFDFGVTVG SIFEVVWAIF RPGTSFGISV LRALRLLRIF KITKYWASLR NLVVSLMSSM 610 620 630 640 650 660 KSIISLLFLL FLFIVVFALL GMQLFGGRFN FNDGTPSANF DTFPAAIMTV FQILTGEDWN 670 680 690 700 710 720 EVMYNGIRSQ GGVSSGMWSA IYFIVLTLFG NYTLLNVFLA IAVDNLANAQ ELTKDEQEEE 730 740 750 760 770 780 EAFNQKHALQ KAKEVSPMSA PNMPSIERDR RRRHHMSMWE PRSSHLRERR RRHHMSVWEQ 790 800 810 820 830 840 RTSQLRKHMQ MSSQEALNRE EAPTMNPLNP LNPLSSLNPL NAHPSLYRRP RAIEGLALGL 850 860 870 880 890 900 ALEKFEEERI SRGGSLKGDG GDRSSALDNQ RTPLSLGQRE PPWLARPCHG NCDPTQQEAG 910 920 930 940 950 960 GGEAVVTFED RARHRQSQRR SRHRRVRTEG KESSSASRSR SASQERSLDE AMPTEGEKDH 970 980 990 1000 1010 1020 ELRGNHGAKE PTIQEERAQD LRRTNSLMVS RGSGLAGGLD EADTPLVLPH PELEVGKHVV 1030 1040 1050 1060 1070 1080 LTEQEPEGSS EQALLGNVQL DMGRVISQSE PDLSCITANT DKATTESTSV TVAIPDVDPL 1090 1100 1110 1120 1130 1140 VDSTVVHISN KTDGEASPLK EAEIREDEEE VEKKKQKKEK RETGKAMVPH SSMFIFSTTN 1150 1160 1170 1180 1190 1200 PIRRACHYIV NLRYFEMCIL LVIAASSIAL AAEDPVLTNS ERNKVLRYFD YVFTGVFTFE 1210 1220 1230 1240 1250 1260 MVIKMIDQGL ILQDGSYFRD LWNILDFVVV VGALVAFALA NALGTNKGRD IKTIKSLRVL 1270 1280 1290 1300 1310 1320 RVLRPLKTIK RLPKLKAVFD CVVTSLKNVF NILIVYKLFM FIFAVIAVQL FKGKFFYCTD 1330 1340 1350 1360 1370 1380 SSKDTEKECI GNYVDHEKNK MEVKGREWKR HEFHYDNIIW ALLTLFTVST GEGWPQVLQH 1390 1400 1410 1420 1430 1440 SVDVTEEDRG PSRSNRMEMS IFYVVYFVVF PFFFVNIFVA LIIITFQEQG DKMMEECSLE 1450 1460 1470 1480 1490 1500 KNERACIDFA ISAKPLTRYM PQNRHTFQYR VWHFVVSPSF EYTIMAMIAL NTVVLMMKYY 1510 1520 1530 1540 1550 1560 SAPCTYELAL KYLNIAFTMV FSLECVLKVI AFGFLNYFRD TWNIFDFITV IGSITEIILT 1570 1580 1590 1600 1610 1620 DSKLVNTSGF NMSFLKLFRA ARLIKLLRQG YTIRILLWTF VQSFKALPYV CLLIAMLFFI 1630 1640 1650 1660 1670 1680 YAIIGMQVFG NIKLDEESHI NRHNNFRSFF GSLMLLFRSA TGEAWQEIML SCLGEKGCEP 1690 1700 1710 1720 1730 1740 DTTAPSGQNE NERCGTDLAY VYFVSFIFFC SFLMLNLFVA VIMDNFEYLT RDSSILGPHH 1750 1760 1770 1780 1790 1800 LDEFVRVWAE YDRAACGRIH YTEMYEMLTL MSPPLGLGKR CPSKVAYKRL VLMNMPVAED 1810 1820 1830 1840 1850 1860 MTVHFTSTLM ALIRTALDIK IAKGGADRQQ LDSELQKETL AIWPHLSQKM LDLLVPMPKA 1870 1880 1890 1900 1910 1920 SDLTVGKIYA AMMIMDYYKQ SKVKKQRQQL EEQKNAPMFQ RMEPSSLPQE IIANAKALPY 1930 1940 1950 1960 1970 1980 LQQDPVSGLS GRSGYPSMSP LSPQDIFQLA CMDPADDGQF QERQSLEPEV SELKSVQPSN 1990 2000 2010 2020 2030 2040 HGIYLPSDTQ EHAGSGRASS MPRLTVDPQV VTDPSSMRRS FSTIRDKRSN SSWLEEFSME 2050 2060 2070 2080 2090 2100 RSSENTYKSR RRSYHSSLRL SAHRLNSDSG HKSDTHRSGG RERGRSKERK HLLSPDVSRC 2110 2120 2130 2140 2150 2160 NSEERGTQAD WESPERRQSR SPSEGRSQTP NRQGTGSLSE SSIPSVSDTS TPRRSRRQLP 2170 2180 2190 2200 2210 2220 PVPPKPRPLL SYSSLIRHAG SISPPADGSE EGSPLTSQAL ESNNACLTES SNSPHPQQSQ 2230 2240 2250 2260 2270 2280 HASPQRYISE PYLALHEDSH ASDCGEEETL TFEAAVATSL GRSNTIGSAP PLRHSWQMPN 2290 2300 2310 GHYRRRRRGG PGPGMMCGAV NNLLSDTEED DKC
	Isoform 2 (Alpha-1E-1) [UniParc]. Checksum: 73640AD59C386BB2	FASTA	2,251	254,604
	10 20 30 40 50 60 MARFGEAVVA RPGSGDGDSD QSRNRQGTPV PASGQAAAYK QTKAQRARTM ALYNPIPVRQ 70 80 90 100 110 120 NCFTVNRSLF IFGEDNIVRK YAKKLIDWPP FEYMILATII ANCIVLALEQ HLPEDDKTPM 130 140 150 160 170 180 SRRLEKTEPY FIGIFCFEAG IKIVALGFIF HKGSYLRNGW NVMDFIVVLS GILATAGTHF 190 200 210 220 230 240 NTHVDLRTLR AVRVLRPLKL VSGIPSLQIV LKSIMKAMVP LLQIGLLLFF AILMFAIIGL 250 260 270 280 290 300 EFYSGKLHRA CFMNNSGILE GFDPPHPCGV QGCPAGYECK DWIGPNDGIT QFDNILFAVL 310 320 330 340 350 360 TVFQCITMEG WTTVLYNTND ALGATWNWLY FIPLIIIGSF FVLNLVLGVL SGEFAKERER 370 380 390 400 410 420 VENRRAFMKL RRQQQIEREL NGYRAWIDKA EEVMLAEENK NAGTSALEVL RRATIKRSRT 430 440 450 460 470 480 EAMTRDSSDE HCVDISSVGT PLARASIKSA KVDGVSYFRH KERLLRISIR HMVKSQVFYW 490 500 510 520 530 540 IVLSLVALNT ACVAIVHHNQ PQWLTHLLYY AEFLFLGLFL LEMSLKMYGM GPRLYFHSSF 550 560 570 580 590 600 NCFDFGVTVG SIFEVVWAIF RPGTSFGISV LRALRLLRIF KITKYWASLR NLVVSLMSSM 610 620 630 640 650 660 KSIISLLFLL FLFIVVFALL GMQLFGGRFN FNDGTPSANF DTFPAAIMTV FQILTGEDWN 670 680 690 700 710 720 EVMYNGIRSQ GGVSSGMWSA IYFIVLTLFG NYTLLNVFLA IAVDNLANAQ ELTKDEQEEE 730 740 750 760 770 780 EAFNQKHALQ KAKEVSPMSA PNMPSIERER RRRHHMSVWE QRTSQLRKHM QMSSQEALNR 790 800 810 820 830 840 EEAPTMNPLN PLNPLSSLNP LNAHPSLYRR PRAIEGLALG LALEKFEEER ISRGGSLKGD 850 860 870 880 890 900 GGDRSSALDN QRTPLSLGQR EPPWLARPCH GNCDPTQQEA GGGEAVVTFE DRARHRQSQR 910 920 930 940 950 960 RSRHRRVRTE GKESSSASRS RSASQERSLD EAMPTEGEKD HELRGNHGAK EPTIQEERAQ 970 980 990 1000 1010 1020 DLRRTNSLMV SRGSGLAGGL DEADTPLVLP HPELEVGKHV VLTEQEPEGS SEQALLGNVQ 1030 1040 1050 1060 1070 1080 LDMGRVISQS EPDLSCITAN TDKATTESTS VTVAIPDVDP LVDSTVVHIS NKTDGEASPL 1090 1100 1110 1120 1130 1140 KEAEIREDEE EVEKKKQKKE KRETGKAMVP HSSMFIFSTT NPIRRACHYI VNLRYFEMCI 1150 1160 1170 1180 1190 1200 LLVIAASSIA LAAEDPVLTN SERNKVLRYF DYVFTGVFTF EMVIKMIDQG LILQDGSYFR 1210 1220 1230 1240 1250 1260 DLWNILDFVV VVGALVAFAL ANALGTNKGR DIKTIKSLRV LRVLRPLKTI KRLPKLKAVF 1270 1280 1290 1300 1310 1320 DCVVTSLKNV FNILIVYKLF MFIFAVIAVQ LFKGKFFYCT DSSKDTEKEC IGNYVDHEKN 1330 1340 1350 1360 1370 1380 KMEVKGREWK RHEFHYDNII WALLTLFTVS TGEGWPQVLQ HSVDVTEEDR GPSRSNRMEM 1390 1400 1410 1420 1430 1440 SIFYVVYFVV FPFFFVNIFV ALIIITFQEQ GDKMMEECSL EKNERACIDF AISAKPLTRY 1450 1460 1470 1480 1490 1500 MPQNRHTFQY RVWHFVVSPS FEYTIMAMIA LNTVVLMMKY YSAPCTYELA LKYLNIAFTM 1510 1520 1530 1540 1550 1560 VFSLECVLKV IAFGFLNYFR DTWNIFDFIT VIGSITEIIL TDSKLVNTSG FNMSFLKLFR 1570 1580 1590 1600 1610 1620 AARLIKLLRQ GYTIRILLWT FVQSFKALPY VCLLIAMLFF IYAIIGMQVF GNIKLDEESH 1630 1640 1650 1660 1670 1680 INRHNNFRSF FGSLMLLFRS ATGEAWQEIM LSCLGEKGCE PDTTAPSGQN ENERCGTDLA 1690 1700 1710 1720 1730 1740 YVYFVSFIFF CSFLMLNLFV AVIMDNFEYL TRDSSILGPH HLDEFVRVWA EYDRAACGRI 1750 1760 1770 1780 1790 1800 HYTEMYEMLT LMSPPLGLGK RCPSKVAYKR LVLMNMPVAE DMTVHFTSTL MALIRTALDI 1810 1820 1830 1840 1850 1860 KIAKGGADRQ QLDSELQKET LAIWPHLSQK MLDLLVPMPK ASDLTVGKIY AAMMIMDYYK 1870 1880 1890 1900 1910 1920 QSKVKKQRQQ LEEQKNAPMF QRMEPSSLPQ EIIANAKALP YLQQDPVSGL SGRSGYPSMS 1930 1940 1950 1960 1970 1980 PLSPQDIFQL ACMDPADDGQ FQERQSLVVT DPSSMRRSFS TIRDKRSNSS WLEEFSMERS 1990 2000 2010 2020 2030 2040 SENTYKSRRR SYHSSLRLSA HRLNSDSGHK SDTHRSGGRE RGRSKERKHL LSPDVSRCNS 2050 2060 2070 2080 2090 2100 EERGTQADWE SPERRQSRSP SEGRSQTPNR QGTGSLSESS IPSVSDTSTP RRSRRQLPPV 2110 2120 2130 2140 2150 2160 PPKPRPLLSY SSLIRHAGSI SPPADGSEEG SPLTSQALES NNACLTESSN SPHPQQSQHA 2170 2180 2190 2200 2210 2220 SPQRYISEPY LALHEDSHAS DCGEEETLTF EAAVATSLGR SNTIGSAPPL RHSWQMPNGH 2230 2240 2250 YRRRRRGGPG PGMMCGAVNN LLSDTEEDDK C
	Isoform 3 (Alpha-1E-3) [UniParc]. Checksum: D424C3592C9BD5F5	FASTA	2,270	257,116
	10 20 30 40 50 60 MARFGEAVVA RPGSGDGDSD QSRNRQGTPV PASGQAAAYK QTKAQRARTM ALYNPIPVRQ 70 80 90 100 110 120 NCFTVNRSLF IFGEDNIVRK YAKKLIDWPP FEYMILATII ANCIVLALEQ HLPEDDKTPM 130 140 150 160 170 180 SRRLEKTEPY FIGIFCFEAG IKIVALGFIF HKGSYLRNGW NVMDFIVVLS GILATAGTHF 190 200 210 220 230 240 NTHVDLRTLR AVRVLRPLKL VSGIPSLQIV LKSIMKAMVP LLQIGLLLFF AILMFAIIGL 250 260 270 280 290 300 EFYSGKLHRA CFMNNSGILE GFDPPHPCGV QGCPAGYECK DWIGPNDGIT QFDNILFAVL 310 320 330 340 350 360 TVFQCITMEG WTTVLYNTND ALGATWNWLY FIPLIIIGSF FVLNLVLGVL SGEFAKERER 370 380 390 400 410 420 VENRRAFMKL RRQQQIEREL NGYRAWIDKA EEVMLAEENK NAGTSALEVL RRATIKRSRT 430 440 450 460 470 480 EAMTRDSSDE HCVDISSVGT PLARASIKSA KVDGVSYFRH KERLLRISIR HMVKSQVFYW 490 500 510 520 530 540 IVLSLVALNT ACVAIVHHNQ PQWLTHLLYY AEFLFLGLFL LEMSLKMYGM GPRLYFHSSF 550 560 570 580 590 600 NCFDFGVTVG SIFEVVWAIF RPGTSFGISV LRALRLLRIF KITKYWASLR NLVVSLMSSM 610 620 630 640 650 660 KSIISLLFLL FLFIVVFALL GMQLFGGRFN FNDGTPSANF DTFPAAIMTV FQILTGEDWN 670 680 690 700 710 720 EVMYNGIRSQ GGVSSGMWSA IYFIVLTLFG NYTLLNVFLA IAVDNLANAQ ELTKDEQEEE 730 740 750 760 770 780 EAFNQKHALQ KAKEVSPMSA PNMPSIERDR RRRHHMSMWE PRSSHLRERR RRHHMSVWEQ 790 800 810 820 830 840 RTSQLRKHMQ MSSQEALNRE EAPTMNPLNP LNPLSSLNPL NAHPSLYRRP RAIEGLALGL 850 860 870 880 890 900 ALEKFEEERI SRGGSLKGDG GDRSSALDNQ RTPLSLGQRE PPWLARPCHG NCDPTQQEAG 910 920 930 940 950 960 GGEAVVTFED RARHRQSQRR SRHRRVRTEG KESSSASRSR SASQERSLDE AMPTEGEKDH 970 980 990 1000 1010 1020 ELRGNHGAKE PTIQEERAQD LRRTNSLMVS RGSGLAGGLD EADTPLVLPH PELEVGKHVV 1030 1040 1050 1060 1070 1080 LTEQEPEGSS EQALLGNVQL DMGRVISQSE PDLSCITANT DKATTESTSV TVAIPDVDPL 1090 1100 1110 1120 1130 1140 VDSTVVHISN KTDGEASPLK EAEIREDEEE VEKKKQKKEK RETGKAMVPH SSMFIFSTTN 1150 1160 1170 1180 1190 1200 PIRRACHYIV NLRYFEMCIL LVIAASSIAL AAEDPVLTNS ERNKVLRYFD YVFTGVFTFE 1210 1220 1230 1240 1250 1260 MVIKMIDQGL ILQDGSYFRD LWNILDFVVV VGALVAFALA NALGTNKGRD IKTIKSLRVL 1270 1280 1290 1300 1310 1320 RVLRPLKTIK RLPKLKAVFD CVVTSLKNVF NILIVYKLFM FIFAVIAVQL FKGKFFYCTD 1330 1340 1350 1360 1370 1380 SSKDTEKECI GNYVDHEKNK MEVKGREWKR HEFHYDNIIW ALLTLFTVST GEGWPQVLQH 1390 1400 1410 1420 1430 1440 SVDVTEEDRG PSRSNRMEMS IFYVVYFVVF PFFFVNIFVA LIIITFQEQG DKMMEECSLE 1450 1460 1470 1480 1490 1500 KNERACIDFA ISAKPLTRYM PQNRHTFQYR VWHFVVSPSF EYTIMAMIAL NTVVLMMKYY 1510 1520 1530 1540 1550 1560 SAPCTYELAL KYLNIAFTMV FSLECVLKVI AFGFLNYFRD TWNIFDFITV IGSITEIILT 1570 1580 1590 1600 1610 1620 DSKLVNTSGF NMSFLKLFRA ARLIKLLRQG YTIRILLWTF VQSFKALPYV CLLIAMLFFI 1630 1640 1650 1660 1670 1680 YAIIGMQVFG NIKLDEESHI NRHNNFRSFF GSLMLLFRSA TGEAWQEIML SCLGEKGCEP 1690 1700 1710 1720 1730 1740 DTTAPSGQNE NERCGTDLAY VYFVSFIFFC SFLMLNLFVA VIMDNFEYLT RDSSILGPHH 1750 1760 1770 1780 1790 1800 LDEFVRVWAE YDRAACGRIH YTEMYEMLTL MSPPLGLGKR CPSKVAYKRL VLMNMPVAED 1810 1820 1830 1840 1850 1860 MTVHFTSTLM ALIRTALDIK IAKGGADRQQ LDSELQKETL AIWPHLSQKM LDLLVPMPKA 1870 1880 1890 1900 1910 1920 SDLTVGKIYA AMMIMDYYKQ SKVKKQRQQL EEQKNAPMFQ RMEPSSLPQE IIANAKALPY 1930 1940 1950 1960 1970 1980 LQQDPVSGLS GRSGYPSMSP LSPQDIFQLA CMDPADDGQF QERQSLVVTD PSSMRRSFST 1990 2000 2010 2020 2030 2040 IRDKRSNSSW LEEFSMERSS ENTYKSRRRS YHSSLRLSAH RLNSDSGHKS DTHRSGGRER 2050 2060 2070 2080 2090 2100 GRSKERKHLL SPDVSRCNSE ERGTQADWES PERRQSRSPS EGRSQTPNRQ GTGSLSESSI 2110 2120 2130 2140 2150 2160 PSVSDTSTPR RSRRQLPPVP PKPRPLLSYS SLIRHAGSIS PPADGSEEGS PLTSQALESN 2170 2180 2190 2200 2210 2220 NACLTESSNS PHPQQSQHAS PQRYISEPYL ALHEDSHASD CGEEETLTFE AAVATSLGRS 2230 2240 2250 2260 2270 NTIGSAPPLR HSWQMPNGHY RRRRRGGPGP GMMCGAVNNL LSDTEEDDKC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular analysis and functional expression of the human type E neuronal Ca2+ channel alpha 1 subunit." Schneider T., Wei X., Olcese R., Costantin J.L., Neely A., Palade P., Perez-Reyes E., Qin N., Zhou J., Crawford G.D., Smith R.G., Appel S.H., Stefani E., Birnbaumer M. Recept. Channels 2:255-270(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-1955. Tissue: Brain.
[2]	"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] (ISOFORMS 2 AND 3). Tissue: Hippocampus.
[3]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Mutations in EFHC1 cause juvenile myoclonic epilepsy." Suzuki T., Delgado-Escueta A.V., Aguan K., Alonso M.E., Shi J., Hara Y., Nishida M., Numata T., Medina M.T., Takeuchi T., Morita R., Bai D., Ganesh S., Sugimoto Y., Inazawa J., Bailey J.N., Ochoa A., Jara-Prado A. , Rasmussen A., Ramos-Peek J., Cordova S., Rubio-Donnadieu F., Inoue Y., Osawa M., Kaneko S., Oguni H., Mori Y., Yamakawa K. Nat. Genet. 36:842-849(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CACNA1E.
[5]	"Crystal structure of the CaV2 IQ domain in complex with Ca2+/calmodulin: high-resolution mechanistic implications for channel regulation by Ca2+." Mori M.X., Vander Kooi C.W., Leahy D.J., Yue D.T. Structure 16:607-620(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1867-1885.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L27745 mRNA. Translation: AAA72125.1.
L29384 mRNA. Translation: AAA59204.1.
L29385 mRNA. Translation: AAA59205.1.
AL161734 , AL160059, AL359270, AL590998 Genomic DNA. Translation: CAH72675.1.
AL161734 , AL160059, AL359270, AL590998 Genomic DNA. Translation: CAH72676.1.
AL161734 , AL160059, AL359270, AL590998 Genomic DNA. Translation: CAH72677.1.
AL359270 , AL160059, AL161734, AL590998 Genomic DNA. Translation: CAI14653.1.
AL359270 , AL160059, AL161734, AL590998 Genomic DNA. Translation: CAI14654.1.
AL359270 , AL160059, AL161734, AL590998 Genomic DNA. Translation: CAI14655.1.
AL160059 , AL161734, AL359270, AL590998 Genomic DNA. Translation: CAI17081.1.
AL160059 , AL161734, AL359270, AL590998 Genomic DNA. Translation: CAI17082.1.
AL160059 , AL161734, AL359270, AL590998 Genomic DNA. Translation: CAI17083.1.
AL590998 , AL160059, AL161734, AL359270 Genomic DNA. Translation: CAI22327.1.
AL590998 , AL160059, AL161734, AL359270 Genomic DNA. Translation: CAI22328.1.
AL590998 , AL160059, AL161734, AL359270 Genomic DNA. Translation: CAI22329.1.

IPI

IPI00165045.
IPI00218338.
IPI00472283.

PIR

A54972.
B54972.

RefSeq

NP_000712.2. NM_000721.3.
NP_001192222.1. NM_001205293.1.
NP_001192223.1. NM_001205294.1.

UniGene

Hs.437444.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3BXL	X-ray	2.30	B	1867-1887	[»]

ProteinModelPortal

Q15878.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000356545.

PTM databases

PhosphoSite

Q15878.

Polymorphism databases

DMDM

209572758.

Proteomic databases

PaxDb

Q15878.

PRIDE

Q15878.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000367570; ENSP00000356542; ENSG00000198216.
ENST00000367573; ENSP00000356545; ENSG00000198216.
ENST00000526775; ENSP00000434814; ENSG00000198216.

GeneID

777.

KEGG

hsa:777.

UCSC

uc001gow.3. human.
uc009wxs.3. human.
uc009wxt.3. human.

Organism-specific databases

CTD

777.

GeneCards

GC01P181382.

HGNC

HGNC:1392. CACNA1E.

HPA

HPA042515.

MIM

601013. gene.

neXtProt

NX_Q15878.

PharmGKB

PA26009.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1226.

HOGENOM

HOG000231530.

HOVERGEN

HBG050763.

InParanoid

Q15878.

KO

K04852.

OMA

HHMSVWE.

OrthoDB

EOG45B1DN.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.
REACT_13685. Neuronal System.

Gene expression databases

ArrayExpress

Q15878.

Bgee

Q15878.

CleanEx

HS_CACNA1E.

Genevestigator

Q15878.

GermOnline

ENSG00000198216. Homo sapiens.

Family and domain databases

InterPro

IPR002048. EF_hand_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005449. VDCC_R_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]

PANTHER

PTHR10037:SF57. PTHR10037:SF57. 1 hit.

Pfam

PF08763. Ca_chan_IQ. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]

PRINTS

PR00167. CACHANNEL.
PR01633. RVDCCALPHA1.

SMART

SM01062. Ca_chan_IQ. 1 hit.
[Graphical view]

PROSITE

PS50222. EF_HAND_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q15878.

ChEMBL

CHEMBL1687682.

EvolutionaryTrace

Q15878.

GenomeRNAi

777.

NextBio

3140.

SOURCE

Search...

Entry information

Entry name

CAC1E_HUMAN

Accession

Primary (citable) accession number: Q15878
Secondary accession number(s): B1AM12 , B1AM13, B1AM14, Q14580, Q14581

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	October 14, 2008
Last modified:	May 1, 2013
This is version 128 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.