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

 CAC1E_RAT               Reviewed;        2222 AA.
Q07652;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
18-JUL-2018, entry version 137.
RecName: Full=Voltage-dependent R-type calcium channel subunit alpha-1E;
AltName: Full=BII;
AltName: Full=Brain calcium channel II;
AltName: Full=Calcium channel, L type, alpha-1 polypeptide, isoform 6;
AltName: Full=RBE-II;
AltName: Full=RBE2;
AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.3;
Name=Cacna1e; Synonyms=Cach6, Cacnl1a6;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=8388125; DOI=10.1126/science.8388125;
Soong T.W., Stea A., Hodson C.D., Dubel S.J., Vincent S.R.,
Snutch T.P.;
"Structure and functional expression of a member of the low voltage-
activated calcium channel family.";
Science 260:1133-1136(1993).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-687; SER-744; SER-806;
SER-898; SER-1049 AND SER-2022, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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. They are however insensitive to dihydropyridines (DHP).
Calcium channels containing alpha-1E subunit could be involved in
the modulation of firing patterns of neurons which is important
for information processing.
-!- SUBUNIT: 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.
-!- INTERACTION:
P62158:CALM3 (xeno); NbExp=2; IntAct=EBI-15734403, EBI-397435;
-!- 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.
-!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
1.A.1.11) family. CACNA1E subfamily. {ECO:0000305}.
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EMBL; L15453; AAA40855.1; -; mRNA.
PIR; A37490; A37490.
UniGene; Rn.10742; -.
PDB; 3DVK; X-ray; 2.30 A; B=1818-1837.
PDBsum; 3DVK; -.
ProteinModelPortal; Q07652; -.
SMR; Q07652; -.
DIP; DIP-46236N; -.
IntAct; Q07652; 2.
STRING; 10116.ENSRNOP00000003928; -.
GuidetoPHARMACOLOGY; 534; -.
CarbonylDB; Q07652; -.
iPTMnet; Q07652; -.
PhosphoSitePlus; Q07652; -.
PaxDb; Q07652; -.
PRIDE; Q07652; -.
UCSC; RGD:2246; rat.
RGD; 2246; Cacna1e.
eggNOG; ENOG410INF5; Eukaryota.
eggNOG; ENOG410YD06; LUCA.
HOGENOM; HOG000231530; -.
HOVERGEN; HBG050763; -.
InParanoid; Q07652; -.
PhylomeDB; Q07652; -.
EvolutionaryTrace; Q07652; -.
PRO; PR:Q07652; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0043204; C:perikaryon; IDA:RGD.
GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:RGD.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0008331; F:high voltage-gated calcium channel activity; IBA:GO_Central.
GO; GO:0008332; F:low voltage-gated calcium channel activity; TAS:RGD.
GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:RGD.
GO; GO:0070509; P:calcium ion import; IDA:RGD.
GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
Gene3D; 1.20.120.350; -; 4.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR031649; GPHH_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR014873; VDCC_a1su_IQ.
InterPro; IPR005449; VDCC_R_a1su.
InterPro; IPR002077; VDCCAlpha1.
InterPro; IPR027359; Volt_channel_dom_sf.
PANTHER; PTHR10037:SF57; PTHR10037:SF57; 2.
Pfam; PF08763; Ca_chan_IQ; 1.
Pfam; PF16905; GPHH; 1.
Pfam; PF00520; Ion_trans; 4.
PRINTS; PR00167; CACHANNEL.
PRINTS; PR01633; RVDCCALPHA1.
SMART; SM01062; Ca_chan_IQ; 1.
PROSITE; PS50222; EF_HAND_2; 1.
1: Evidence at protein level;
3D-structure; Calcium; Calcium channel; Calcium transport;
Complete proteome; Disulfide bond; Glycoprotein; Ion channel;
Ion transport; Membrane; Metal-binding; Phosphoprotein;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport; Voltage-gated channel.
CHAIN 1 2222 Voltage-dependent R-type calcium channel
subunit alpha-1E.
/FTId=PRO_0000053941.
TOPO_DOM 1 40 Cytoplasmic. {ECO:0000255}.
TRANSMEM 41 59 Helical; Name=S1 of repeat I.
{ECO:0000255}.
TOPO_DOM 60 78 Extracellular. {ECO:0000255}.
TRANSMEM 79 97 Helical; Name=S2 of repeat I.
{ECO:0000255}.
TOPO_DOM 98 109 Cytoplasmic. {ECO:0000255}.
TRANSMEM 110 124 Helical; Name=S3 of repeat I.
{ECO:0000255}.
TOPO_DOM 125 136 Extracellular. {ECO:0000255}.
TRANSMEM 137 156 Helical; Name=S4 of repeat I.
{ECO:0000255}.
TOPO_DOM 157 174 Cytoplasmic. {ECO:0000255}.
TRANSMEM 175 195 Helical; Name=S5 of repeat I.
{ECO:0000255}.
TOPO_DOM 196 277 Extracellular. {ECO:0000255}.
TRANSMEM 278 301 Helical; Name=S6 of repeat I.
{ECO:0000255}.
TOPO_DOM 302 427 Cytoplasmic. {ECO:0000255}.
TRANSMEM 428 447 Helical; Name=S1 of repeat II.
{ECO:0000255}.
TOPO_DOM 448 460 Extracellular. {ECO:0000255}.
TRANSMEM 461 480 Helical; Name=S2 of repeat II.
{ECO:0000255}.
TOPO_DOM 481 489 Cytoplasmic. {ECO:0000255}.
TRANSMEM 490 508 Helical; Name=S3 of repeat II.
{ECO:0000255}.
TOPO_DOM 509 518 Extracellular. {ECO:0000255}.
TRANSMEM 519 537 Helical; Name=S4 of repeat II.
{ECO:0000255}.
TOPO_DOM 538 556 Cytoplasmic. {ECO:0000255}.
TRANSMEM 557 576 Helical; Name=S5 of repeat II.
{ECO:0000255}.
TOPO_DOM 577 629 Extracellular. {ECO:0000255}.
TRANSMEM 630 654 Helical; Name=S6 of repeat II.
{ECO:0000255}.
TOPO_DOM 655 1100 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1101 1117 Helical; Name=S1 of repeat III.
{ECO:0000255}.
TOPO_DOM 1118 1141 Extracellular. {ECO:0000255}.
TRANSMEM 1142 1161 Helical; Name=S2 of repeat III.
{ECO:0000255}.
TOPO_DOM 1162 1169 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1170 1192 Helical; Name=S3 of repeat III.
{ECO:0000255}.
TOPO_DOM 1193 1206 Extracellular. {ECO:0000255}.
TRANSMEM 1207 1224 Helical; Name=S4 of repeat III.
{ECO:0000255}.
TOPO_DOM 1225 1243 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1244 1263 Helical; Name=S5 of repeat III.
{ECO:0000255}.
TOPO_DOM 1264 1350 Extracellular. {ECO:0000255}.
TRANSMEM 1351 1374 Helical; Name=S6 of repeat III.
{ECO:0000255}.
TOPO_DOM 1375 1431 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1432 1450 Helical; Name=S1 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1451 1467 Extracellular. {ECO:0000255}.
TRANSMEM 1468 1485 Helical; Name=S2 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1486 1493 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1494 1512 Helical; Name=S3 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1513 1523 Extracellular. {ECO:0000255}.
TRANSMEM 1524 1542 Helical; Name=S4 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1543 1561 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1562 1581 Helical; Name=S5 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1582 1650 Extracellular. {ECO:0000255}.
TRANSMEM 1651 1676 Helical; Name=S6 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1677 2222 Cytoplasmic. {ECO:0000255}.
REPEAT 27 305 I.
REPEAT 413 657 II.
REPEAT 1092 1378 III.
REPEAT 1415 1678 IV.
DOMAIN 1691 1726 EF-hand. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 377 388 {ECO:0000255|PROSITE-ProRule:PRU00448}.
CA_BIND 1704 1715 {ECO:0000255|PROSITE-ProRule:PRU00448}.
REGION 325 342 Binding to the beta subunit.
{ECO:0000250}.
COMPBIAS 667 672 Poly-Glu.
COMPBIAS 699 704 Poly-Arg.
COMPBIAS 718 723 Poly-Arg.
COMPBIAS 1058 1064 Poly-Glu.
COMPBIAS 1180 1183 Poly-Val.
COMPBIAS 2193 2196 Poly-Arg.
SITE 260 260 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 608 608 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1324 1324 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1615 1615 Calcium ion selectivity and permeability.
{ECO:0000250}.
MOD_RES 378 378 Phosphoserine.
{ECO:0000250|UniProtKB:Q61290}.
MOD_RES 391 391 Phosphothreonine.
{ECO:0000250|UniProtKB:Q61290}.
MOD_RES 687 687 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 696 696 Phosphoserine.
{ECO:0000250|UniProtKB:Q61290}.
MOD_RES 744 744 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 766 766 Phosphoserine.
{ECO:0000250|UniProtKB:Q61290}.
MOD_RES 806 806 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 898 898 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1049 1049 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1686 1686 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 2003 2003 Phosphoserine.
{ECO:0000250|UniProtKB:Q61290}.
MOD_RES 2022 2022 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 205 205 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1518 1518 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1523 1523 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1641 1641 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
HELIX 1818 1835 {ECO:0000244|PDB:3DVK}.
SEQUENCE 2222 AA; 252116 MW; DF6452A2175CEB19 CRC64;
MALYNPIPVR QNCFTVNRSL FIFGEDNIVR KYAKKLIDWP PFEYMILATI IANCIVLALE
QHLPEDDKTP MSRRLEKTEP YFIGIFCFEA GIKIVALGFI FHKGSYLRNG WNVMDFIVVL
SGILATAGTH FNTHVDLRTL RAVRVLRPLK LVSGIPSLQI VLKSIMKAMV PLLQIGLLLF
FAILMFAIIG LEFYSGKLHR ACFMNNSGIL EGFDPPHPCG VQGCPAGYEC KDWIGPNDGI
TQFDNILFAV LTVFQCITME GWTTVLYNTN DALGATWNWL YFIPLIIIGS FFVLNLVLGV
LSGEFAKERE RVENRRAFMK LRRQQQIERE LNGYRAWIDK AEEVMLAEEN KNSGTSALEV
LRRATIKRSR TEAMTRDSSD EHCVDISSVG TPLARASIKS TKVDGASYFR HKERLLRISI
RHMVKSQVFY WIVLSVVALN TACVAIVHHN QPQWLTHLLY YAEFLFLGLF LLEMSLKMYG
MGPRLYFHSS FNCFDFGVTV GSIFEVVWAI FRPGTSFGIS VLRALRLLRI FKITKYWASL
RNLVVSLMSS MKSIISLLFL LFLFIVVFAL LGMQLFGGRF NFNDGTPSAN FDTFPAAIMT
VFQILTGEDW NEVMYNGIRS QGGVSSGMWS AIYFIVLTLF GNYTLLNVFL AIAVDNLANA
QELTKDEQEE EEAFNQKHAL QKAKEVSPMS APNMPSIERD RRRRHHMSMW EPRSSHLRER
RRRHHMSVWE QRTSQLRRHM QMSSQEALNK EEAPPMNPLN PLNPLSPLNP LNAHPSLYRR
PRPIEGLALG LGLEKCEEER ISRGGSLKGD IGGLTSVLDN QRSPLSLGKR EPPWLPRSCH
GNCDPTQQET GGGETVVTFE DRARHRQSQR RSRHRRVRTE GKESASASRS RSASQERSLD
EGVSIDGEKE HEPQSSHRSK EPTIHEEERT QDLRRTNSLM VPRGSGLVGA LDEAETPLVQ
PQPELEVGKD AALTEQEAEG SSEQALLADV QLDVGRGISQ SEPDLSCMTT NMDKATTEST
SVTVAIPDVD PLVDSTVVNI SNKTDGEASP LKEAETKEEE EEVEKKKQKK EKRETGKAMV
PHSSMFIFST TNPIRKACHY IVNLRYFEMC ILLVIAASSI ALAAEDPVLT NSERNKVLRY
FDYVFTGVFT FEMVIKMIDQ GLILQDGSYF RDLWNILDFV VVVGALVAFA LANALGTNKG
RDIKTIKSLR VLRVLRPLKT IKRLPKLKAV FDCVVTSLKN VFNILIVYKL FMFIFAVIAV
QLFKGKFFYC TDSSKDTEKE CIGNYVDHEK NKMEVKGREW KRHEFHYDNI IWALLTLFTV
STGEGWPQVL QHSVDVTEED RGPSRSNRME MSIFYVVYFV VFPFFFVNIF VALIIITFQE
QGDKMMEECS LEKNERACID FAISAKPLTR YMPQNRHTFQ YRVWHFVVSP SFEYTIMAMI
ALNTVVLMMK YYSAPWTYEL ALKYLNIAFT MVFSLECVLK VIAFGFLNYF RDTWNIFDFI
TVIGSITEII LTDSKLVNTS GFNMSFLKLF RAARLIKLLR QGYTIRILLW TFVQSFKALP
YVCLLIAMLF FIYAIIGMQV FGNIKLDEES HINRHNNFRS FFGSLMLLFR SATGEAWQEI
MLSCLGEKGC EPDTTAPSGQ NESERCGTDL AYVYFVSFIF FCSFLMLNLF VAVIMDNFEY
LTRDSSILGP HHLDEFVRVW AEYDRAACGR IHYTEMYEML TLMSPPLGLG KRCPSKVAYK
RLVLMNMPVA EDMTVHFTST LMALIRTALD IKIAKGGADR QQLDSELQKE TLAIWPHLSQ
KMLDLLVPMP KASDLTVGKI YAAMMIMDYY KQSKVKKQRQ QLEEQKNAPM FQRMEPSSLP
QEIISNAKAL PYLQQDPVSG LSGRSGYPSM SPLSPQEIFQ LACMDPADDG QFQEQQSLVV
TDPSSMRRSF STIRDKRSNS SWLEEFSMER SSENTYKSRR RSYHSSLRLS AHRLNSDSGH
KSDTHRSGGR ERGRSKERKH LLSPDVSRCN SEERGTQADW ESPERRQSRS PSEGRSQTPN
RQGTGSLSES SIPSISDTST PRRSRRQLPP VPPKPRPLLS YSSLMRHTGG ISPPPDGSEG
GSPLASQALE SNSACLTESS NSLHPQQGQH PSPQHYISEP YLALHEDSHA SDCGEEETLT
FEAAVATSLG RSNTIGSAPP LRHSWQMPNG HYRRRRLGGL GLAMMCGAVS DLLSDTEEDD
KC


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