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Voltage-dependent R-type calcium channel subunit alpha-1E (Brain calcium channel II) (BII) (Calcium channel, L type, alpha-1 polypeptide, isoform 6) (Voltage-gated calcium channel subunit alpha Cav2.3)

 CAC1E_MOUSE             Reviewed;        2272 AA.
Q61290;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
28-MAR-2018, entry version 153.
RecName: Full=Voltage-dependent R-type calcium channel subunit alpha-1E;
AltName: Full=Brain calcium channel II;
Short=BII;
AltName: Full=Calcium channel, L type, alpha-1 polypeptide, isoform 6;
AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.3;
Name=Cacna1e; Synonyms=Cach6, Cacnl1a6, Cchra1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=8071363;
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.;
"Structure and functional characterization of neuronal alpha 1E
calcium channel subtypes.";
J. Biol. Chem. 269:22347-22357(1994).
[2]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain cortex;
PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
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.;
"Qualitative and quantitative analyses of protein phosphorylation in
naive and stimulated mouse synaptosomal preparations.";
Mol. Cell. Proteomics 6:283-293(2007).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-20; SER-428;
THR-441; SER-746; SER-816; SER-856 AND SER-2054, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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: 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.
-!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
1.A.1.11) family. CACNA1E subfamily. {ECO:0000305}.
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EMBL; L29346; AAA59206.1; -; mRNA.
PIR; C54972; C54972.
UniGene; Mm.267517; -.
ProteinModelPortal; Q61290; -.
IntAct; Q61290; 3.
STRING; 10090.ENSMUSP00000004214; -.
TCDB; 1.A.1.11.3; the voltage-gated ion channel (vic) superfamily.
iPTMnet; Q61290; -.
PhosphoSitePlus; Q61290; -.
EPD; Q61290; -.
MaxQB; Q61290; -.
PaxDb; Q61290; -.
PRIDE; Q61290; -.
MGI; MGI:106217; Cacna1e.
eggNOG; KOG2301; Eukaryota.
eggNOG; ENOG410XNP6; LUCA.
HOVERGEN; HBG050763; -.
InParanoid; Q61290; -.
PhylomeDB; Q61290; -.
ChiTaRS; Cacna1e; mouse.
PRO; PR:Q61290; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0005891; C:voltage-gated calcium channel complex; TAS:MGI.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0008331; F:high voltage-gated calcium channel activity; IBA:GO_Central.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0005245; F:voltage-gated calcium channel activity; IMP:MGI.
GO; GO:0001662; P:behavioral fear response; IMP:MGI.
GO; GO:0048266; P:behavioral response to pain; IMP:MGI.
GO; GO:0070588; P:calcium ion transmembrane transport; IMP:MGI.
GO; GO:0006816; P:calcium ion transport; IMP:MGI.
GO; GO:0042596; P:fear response; IMP:MGI.
GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
GO; GO:0007626; P:locomotory behavior; IMP:MGI.
GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
GO; GO:0050877; P:nervous system process; IMP:MGI.
GO; GO:0002027; P:regulation of heart rate; IMP:MGI.
GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:MGI.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
GO; GO:0090273; P:regulation of somatostatin secretion; IMP:MGI.
GO; GO:0048265; P:response to pain; IMP:MGI.
GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
GO; GO:0019226; P:transmission of nerve impulse; IMP:MGI.
GO; GO:0008542; P:visual learning; IMP:MGI.
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;
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 2272 Voltage-dependent R-type calcium channel
subunit alpha-1E.
/FTId=PRO_0000053939.
TOPO_DOM 1 90 Cytoplasmic. {ECO:0000255}.
TRANSMEM 91 109 Helical; Name=S1 of repeat I.
{ECO:0000255}.
TOPO_DOM 110 128 Extracellular. {ECO:0000255}.
TRANSMEM 129 147 Helical; Name=S2 of repeat I.
{ECO:0000255}.
TOPO_DOM 148 159 Cytoplasmic. {ECO:0000255}.
TRANSMEM 160 174 Helical; Name=S3 of repeat I.
{ECO:0000255}.
TOPO_DOM 175 186 Extracellular. {ECO:0000255}.
TRANSMEM 187 206 Helical; Name=S4 of repeat I.
{ECO:0000255}.
TOPO_DOM 207 224 Cytoplasmic. {ECO:0000255}.
TRANSMEM 225 245 Helical; Name=S5 of repeat I.
{ECO:0000255}.
TOPO_DOM 246 327 Extracellular. {ECO:0000255}.
TRANSMEM 328 351 Helical; Name=S6 of repeat I.
{ECO:0000255}.
TOPO_DOM 352 477 Cytoplasmic. {ECO:0000255}.
TRANSMEM 478 497 Helical; Name=S1 of repeat II.
{ECO:0000255}.
TOPO_DOM 498 510 Extracellular. {ECO:0000255}.
TRANSMEM 511 530 Helical; Name=S2 of repeat II.
{ECO:0000255}.
TOPO_DOM 531 539 Cytoplasmic. {ECO:0000255}.
TRANSMEM 540 558 Helical; Name=S3 of repeat II.
{ECO:0000255}.
TOPO_DOM 559 568 Extracellular. {ECO:0000255}.
TRANSMEM 569 587 Helical; Name=S4 of repeat II.
{ECO:0000255}.
TOPO_DOM 588 606 Cytoplasmic. {ECO:0000255}.
TRANSMEM 607 626 Helical; Name=S5 of repeat II.
{ECO:0000255}.
TOPO_DOM 627 679 Extracellular. {ECO:0000255}.
TRANSMEM 680 704 Helical; Name=S6 of repeat II.
{ECO:0000255}.
TOPO_DOM 705 1150 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1151 1167 Helical; Name=S1 of repeat III.
{ECO:0000255}.
TOPO_DOM 1168 1191 Extracellular. {ECO:0000255}.
TRANSMEM 1192 1211 Helical; Name=S2 of repeat III.
{ECO:0000255}.
TOPO_DOM 1212 1219 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1220 1242 Helical; Name=S3 of repeat III.
{ECO:0000255}.
TOPO_DOM 1243 1256 Extracellular. {ECO:0000255}.
TRANSMEM 1257 1274 Helical; Name=S4 of repeat III.
{ECO:0000255}.
TOPO_DOM 1275 1293 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1294 1313 Helical; Name=S5 of repeat III.
{ECO:0000255}.
TOPO_DOM 1314 1400 Extracellular. {ECO:0000255}.
TRANSMEM 1401 1424 Helical; Name=S6 of repeat III.
{ECO:0000255}.
TOPO_DOM 1425 1481 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1482 1500 Helical; Name=S1 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1501 1515 Extracellular. {ECO:0000255}.
TRANSMEM 1516 1535 Helical; Name=S2 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1536 1543 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1544 1562 Helical; Name=S3 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1563 1573 Extracellular. {ECO:0000255}.
TRANSMEM 1574 1592 Helical; Name=S4 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1593 1611 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1612 1631 Helical; Name=S5 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1632 1700 Extracellular. {ECO:0000255}.
TRANSMEM 1701 1726 Helical; Name=S6 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1727 2272 Cytoplasmic. {ECO:0000255}.
REPEAT 77 355 I.
REPEAT 463 707 II.
REPEAT 1143 1429 III.
REPEAT 1466 1729 IV.
DOMAIN 1742 1777 EF-hand. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 427 438 {ECO:0000255|PROSITE-ProRule:PRU00448}.
CA_BIND 1755 1766 {ECO:0000255|PROSITE-ProRule:PRU00448}.
REGION 375 392 Binding to the beta subunit.
{ECO:0000250}.
COMPBIAS 717 722 Poly-Glu.
COMPBIAS 751 754 Poly-Arg.
COMPBIAS 770 773 Poly-Arg.
COMPBIAS 1108 1112 Poly-Glu.
COMPBIAS 1115 1118 Poly-Lys.
COMPBIAS 1231 1234 Poly-Val.
COMPBIAS 2244 2247 Poly-Arg.
SITE 310 310 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 658 658 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1375 1375 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1666 1666 Calcium ion selectivity and permeability.
{ECO:0000250}.
MOD_RES 15 15 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 20 20 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 428 428 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 441 441 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 737 737 Phosphoserine.
{ECO:0000250|UniProtKB:Q07652}.
MOD_RES 746 746 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 794 794 Phosphoserine.
{ECO:0000250|UniProtKB:Q07652}.
MOD_RES 816 816 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 856 856 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 948 948 Phosphoserine.
{ECO:0000250|UniProtKB:Q07652}.
MOD_RES 1099 1099 Phosphoserine.
{ECO:0000250|UniProtKB:Q07652}.
MOD_RES 1737 1737 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 2054 2054 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2073 2073 Phosphoserine.
{ECO:0000250|UniProtKB:Q07652}.
CARBOHYD 255 255 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1569 1569 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1692 1692 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 2272 AA; 257236 MW; 70D9200B9E0C87A1 CRC64;
MARFGEAVVV GRPGSGDGDS DQSRNRQGTP VPASGPAAAY KQSKAQRART MALYNPIPVR
QNCFTVNRSL FIFGEDNIVR KYAKKLIDWP PFEYMILATI IANCIVLALE QHLPEDDKTP
MSRRLEKTEP YFIGIFCFEA GIKIVALGFI FHKGSYLRNG WNVMDFIVVL SGILATAGTH
FNTHVDLRAL 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 IGGLTSALDN QRSPLSLGKR EPPWLPRSCH GNCDPIQQEA
GGGETVVTFE DRARHRQSQR RSRHRRVRTE GKDSASASRS RSASQERSLD EGVSVEGEKE
HEPHSSHRSK EPTIHEEERT QDLRRTNSLM VPRGSGLVGA LDEAETPLVQ PQPELEVGKD
AALTEQEAEG SSEQALLGDV QLDVGRGISQ SEPDLSCMTA NMDKATTEST SVTVAIPDVD
PLVDSTVVNI SNKTDGEASP LKEAETKEEE EEVEKKKKQK KEKRETGKAM VPHSSMFIFS
TTNPIRRACH YIVNLRYFEM CILLVIAASS IALAAEDPVL TNSERNKVLR YFDYVFTGVF
TFEMVIKMID QGLILQDGSY FRDLWNILDF VVVVGALVAF ALANALGTNK GRDIKTIKSL
RVLRVLRPLK TIKRLPKLKA VFDCVVTSLK NVFNILIVYK LFMFIFAVIA VQLFKGKFFY
CTDSSKDTEK ECIGNYVDHE KNKMEVKGRE WKRHEFHYDN IIWALLTLFT VSTGEGWPQV
LQHSVDVTEE DRGPSRSNRM EMSIFYVVYF VVFPFFFVNI FVALIIITFQ EQGDKMMEEC
SLEKNERACI DFAISAKPLT RYMPQNRHTF QYRVWHFVVS PSFEYTIMAM IALNTVVLMM
KYYTAPCTYE LALKYLNIAF TMVFSLECVL KVIAFGFLNY FRDTWNIFDF ITVIGSITEI
ILTDSKLVNT SGFNMSFLKL FRAARLIKLL RQGYTIRILL WTFVQSFKAL PYVCLLIAML
FFIYAIIGMQ VFGNIKLDEE SHINRHNNFR SFFGSLMLLF RSATGEAWQE IMLSCLGEKG
CEPDTTAPSG QNESERCGTD LAYVYFVSFI FFCSFLMLNL FVAVIMDNFE YLTRDSSILG
PHHLDEFVRV WAEYDRAACG RIHYTEMYEM LTLMSPPLGL GKRCPSKVAY KRLVLMNMPV
AEDMTVHFTS TLMALIRTAL DIKIAKGGAD RQQLDSELQK ETLAIWPHLS QKMLDLLVPM
PKASDLTVGK IYAAMMIMDY YKQSKVKKQR QQLEEQKNAP MFQRMEPSSL PQEIIANAKA
LPYLQQDPVS GLSGRSGYPS MSPLSPQEIF QLACMDPADD GQFQEQQSLV VTDPSSMRRS
FSTIRDKRSN SSWLEEFSME RSSENTYKSR RRSYHSSLRL SAHRLNSDSG HKSDTHRSGG
RERGRSKERK HLLSPDVSRC NSEERGTQAD WESPERRQSR SPSEGRSQTP NRQGTGSLSE
SSIPSISDTS TPRRSRRQLP PVPPKPRPLL SYSSLMRHTG GISPPPDGSE GGSPLASQAL
ESNSACLTES SNSLHPQQGQ HPSPQHYISE PYLALHEDSH ASDCGEEETL TFEAAVATSL
GRSNTIGSAP PLRHSWQMPN GHYRRRRWGA WAGMMCGAVS DLLSDTEEDD KC


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Genprice Inc, Invoices and accounting
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