CAC1E_RABIT
ID CAC1E_RABIT Reviewed; 2259 AA.
AC Q02343; Q02344;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Voltage-dependent R-type calcium channel subunit alpha-1E;
DE AltName: Full=Brain calcium channel II;
DE Short=BII;
DE AltName: Full=Calcium channel, L type, alpha-1 polypeptide, isoform 6;
DE AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.3;
GN Name=CACNA1E; Synonyms=CACH6, CACNL1A6;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BII-1 AND BII-2).
RC TISSUE=Brain;
RX PubMed=1379552; DOI=10.1016/0014-5793(92)81038-n;
RA Niidome T., Kim M.S., Friedrich T., Mori Y.;
RT "Molecular cloning and characterization of a novel calcium channel from
RT rabbit brain.";
RL FEBS Lett. 308:7-13(1992).
CC -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry
CC of calcium ions into excitable cells and are also involved in a variety
CC of calcium-dependent processes, including muscle contraction, hormone
CC or neurotransmitter release, gene expression, cell motility, cell
CC division and cell death. The isoform alpha-1E gives rise to R-type
CC calcium currents. R-type calcium channels belong to the 'high-voltage
CC activated' (HVA) group and are blocked by nickel. They are however
CC insensitive to dihydropyridines (DHP). Calcium channels containing
CC alpha-1E subunit could be involved in the modulation of firing patterns
CC of neurons which is important for information processing.
CC -!- SUBUNIT: Interacts with EFHC1. Voltage-dependent calcium channels are
CC multisubunit complexes, consisting of alpha-1, alpha-2, beta and delta
CC subunits in a 1:1:1:1 ratio. The channel activity is directed by the
CC pore-forming and voltage-sensitive alpha-1 subunit. In many cases, this
CC subunit is sufficient to generate voltage-sensitive calcium channel
CC activity. The auxiliary subunits beta and alpha-2/delta linked by a
CC disulfide bridge regulate the channel activity.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=BII-1;
CC IsoId=Q02343-1; Sequence=Displayed;
CC Name=BII-2;
CC IsoId=Q02343-2; Sequence=VSP_000938;
CC -!- TISSUE SPECIFICITY: Abundant in the cerebral cortex, hippocampus, and
CC corpus striatum.
CC -!- DOMAIN: Each of the four internal repeats contains five hydrophobic
CC transmembrane segments (S1, S2, S3, S5, S6) and one positively charged
CC transmembrane segment (S4). S4 segments probably represent the voltage-
CC sensor and are characterized by a series of positively charged amino
CC acids at every third position.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. CACNA1E subfamily. {ECO:0000305}.
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DR EMBL; X67855; CAA48040.1; -; mRNA.
DR EMBL; X67856; CAA48041.1; -; mRNA.
DR PIR; S29236; S29236.
DR PIR; S29237; S29237.
DR RefSeq; NP_001095186.1; NM_001101716.1. [Q02343-1]
DR AlphaFoldDB; Q02343; -.
DR SMR; Q02343; -.
DR STRING; 9986.ENSOCUP00000015082; -.
DR PRIDE; Q02343; -.
DR GeneID; 100009403; -.
DR KEGG; ocu:100009403; -.
DR CTD; 777; -.
DR eggNOG; KOG2301; Eukaryota.
DR InParanoid; Q02343; -.
DR OrthoDB; 172471at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR031649; GPHH_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR014873; VDCC_a1su_IQ.
DR InterPro; IPR005449; VDCC_R_a1su.
DR InterPro; IPR002077; VDCCAlpha1.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR45628:SF5; PTHR45628:SF5; 2.
DR Pfam; PF08763; Ca_chan_IQ; 1.
DR Pfam; PF16905; GPHH; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00167; CACHANNEL.
DR PRINTS; PR01633; RVDCCALPHA1.
DR SMART; SM01062; Ca_chan_IQ; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..2259
FT /note="Voltage-dependent R-type calcium channel subunit
FT alpha-1E"
FT /id="PRO_0000053940"
FT TOPO_DOM 1..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..108
FT /note="Helical; Name=S1 of repeat I"
FT TOPO_DOM 109..126
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..146
FT /note="Helical; Name=S2 of repeat I"
FT TOPO_DOM 147..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..176
FT /note="Helical; Name=S3 of repeat I"
FT TOPO_DOM 177..185
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..204
FT /note="Helical; Name=S4 of repeat I"
FT TOPO_DOM 205..223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..243
FT /note="Helical; Name=S5 of repeat I"
FT TOPO_DOM 244..326
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..351
FT /note="Helical; Name=S6 of repeat I"
FT TOPO_DOM 352..476
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..495
FT /note="Helical; Name=S1 of repeat II"
FT TOPO_DOM 496..510
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 511..530
FT /note="Helical; Name=S2 of repeat II"
FT TOPO_DOM 531..538
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 539..557
FT /note="Helical; Name=S3 of repeat II"
FT TOPO_DOM 558..567
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 568..586
FT /note="Helical; Name=S4 of repeat II"
FT TOPO_DOM 587..605
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..625
FT /note="Helical; Name=S5 of repeat II"
FT TOPO_DOM 626..678
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 679..703
FT /note="Helical; Name=S6 of repeat II"
FT TOPO_DOM 704..1143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1144..1162
FT /note="Helical; Name=S1 of repeat III"
FT TOPO_DOM 1163..1178
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1179..1198
FT /note="Helical; Name=S2 of repeat III"
FT TOPO_DOM 1199..1210
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1211..1229
FT /note="Helical; Name=S3 of repeat III"
FT TOPO_DOM 1230..1243
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1244..1262
FT /note="Helical; Name=S4 of repeat III"
FT TOPO_DOM 1263..1281
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1282..1301
FT /note="Helical; Name=S5 of repeat III"
FT TOPO_DOM 1302..1388
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1389..1413
FT /note="Helical; Name=S6 of repeat III"
FT TOPO_DOM 1414..1468
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1469..1487
FT /note="Helical; Name=S1 of repeat IV"
FT TOPO_DOM 1488..1502
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1503..1522
FT /note="Helical; Name=S2 of repeat IV"
FT TOPO_DOM 1523..1530
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1531..1549
FT /note="Helical; Name=S3 of repeat IV"
FT TOPO_DOM 1550..1561
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1562..1580
FT /note="Helical; Name=S4 of repeat IV"
FT TOPO_DOM 1581..1599
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1600..1619
FT /note="Helical; Name=S5 of repeat IV"
FT TOPO_DOM 1620..1688
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1689..1712
FT /note="Helical; Name=S6 of repeat IV"
FT TOPO_DOM 1713..2259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 76..354
FT /note="I"
FT REPEAT 464..706
FT /note="II"
FT REPEAT 1130..1414
FT /note="III"
FT REPEAT 1453..1716
FT /note="IV"
FT DOMAIN 1729..1764
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..391
FT /note="Binding to the beta subunit"
FT /evidence="ECO:0000250"
FT REGION 720..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1979..2176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2209..2242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..765
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..940
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..976
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2012..2069
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2070..2103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2118..2137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2151..2172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 426
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 428
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 430
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 432
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 1742
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 1748
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 1753
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT SITE 309
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 657
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1362
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1653
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61290"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61290"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61290"
FT MOD_RES 440
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q61290"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07652"
FT MOD_RES 745
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61290"
FT MOD_RES 793
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07652"
FT MOD_RES 815
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61290"
FT MOD_RES 853
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61290"
FT MOD_RES 938
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07652"
FT MOD_RES 1088
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07652"
FT MOD_RES 2041
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61290"
FT MOD_RES 2060
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07652"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1556
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1561
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 2101..2259
FT /note="HSRRQLPPVPPKPRPLLSYSSLKQQPSNFSPPADGSQGGSLLASPALESAQV
FT GLPESSDSPRRAQGSHASPQRYISEPYLALHEDSHASDCGEEETLTFEAAVATSLGRSN
FT TIGSAPPLRHSWQMPNGHYRRRRRGGPGAGALCGAVGDLLSDTEEDKC -> QQWGPQE
FT EGVLLHPHQGCGWPCRDRRWMPGRRGWSGEKSHSPLPHCGRDSTGGAGQGPPRYCGSGA
FT GDAGGTCDSLSP (in isoform BII-2)"
FT /evidence="ECO:0000303|PubMed:1379552"
FT /id="VSP_000938"
SQ SEQUENCE 2259 AA; 254252 MW; E4A757076E38779E CRC64;
MARFGEAAAG RPASGEGDSD QGRNLPGTPV PASGSAAAYK QSKAQRARTM ALYNPIPVRQ
NCFTVNRSLF IFGEDNIVRK YAKKLIDWPP FEYMILATII ANCIVLALEQ HLPEDDKTPM
SRRLEKTEPY FIGIFCFEAG IKIVALGFIF HKGSYLRNGW NVMDFIVVLS GILATAGTHF
NTHVDLRTLR AVRVLRPLKL VSGIPSLQIV LKSIMKAMVP LLQIGLLLFF AILMFAIIGL
EFYSGKLHRA CFVNNSGVLE GFDPPHPCGV QGCPAGYECK DWIGPNDGIT QFDNILFAVL
TVFQCITMEG WTTVLYNTND ALGATWNWLY FIPLIIIGSF FVLNLVLGVL SGEFAKERER
VENRRAFMKL RRQQQIEREL NGYRAWIDKA EEVMLAEENK NSGTSALEVL RRATIKRSRT
EAMTRDSSDE HCVDISSVGT PLARASIKSA KVDGASYFRH KERLLRISVR HAVKSQVFYW
IVLSLVALNT ACVAIVHHNQ PQWLTHLLYY AEFLFLGLFL LEMSLKMYGM GPRLYFHSSF
NCFDFGVTVG SIFEVVWAIF RPGTSFGISV LRALRLLRIF KITKYWASLR NLVVSLMSSM
KSIISLLFLL FLFIVVFALL GMQLFGGRFN FNDGTPSANF DTFPAAIMTV FQILTGEDWN
EVMYNGIRSQ GGVSSGMWSA VYFIVLTLFG NYTLLNVFLA IAVDNLANAQ ELTKDEQEEE
EAFNQKHALQ KAKEVSPMSA PNVPSIERDR RRRHHMSMWE PRSSHLRERR RRHHMSVWEQ
RTSQLRRHMQ MSSQEALNKE EAPPMNPLNP LNPLSPLNPL NAHPSLYRRP RPMEGLALGL
EKCEEEHVSR GGSLKGALDC QRSPLSLGRR EPPWLARPCH GNCEPALQET AGGETVVTFE
DRARHRQSQR RSRHRRVRTE AKESSSASRS RSVSQERSLD EGASTEGERD HEARGSHGGK
EPTIHEEERA QDLRRTDSLM VPKGSGLAGG LDEAGTPLVL SSPEGVGKEA APTEQHADGS
GEPALLGHVQ LDVGRAISQS EPDLSCVTAT TDKVTTESTD VTVAIPDAEP LVDSTVVHIG
NKTDGEASPF QEAEMKEAEQ ETEKQKKKER PASGKAMVPH SSMFIFSTSN PIRRACHYVV
NLRYFEMCIL LVIAASSIAL AAEDPVLTNS ERNRVLRYFD YVFTGVFTFE MVIKMIDQGL
ILQDGSYFRD LWNILDFVVV VGALVAFALA NALGTNKGRD IKTIKSLRVL RVLRPLKTIK
RLPKLKAVFD CVVTSLKNVF NILIVYKLFM FIFAVIAVQL FKGKFFYCTD SSKDTEKECI
GNYVDHEKNK MEVKGREWKR HEFHYDNIIW ALLTLFTVST GEGWPQVLQH SVDVTEEDRG
PSRSNRMEMS IFYVVYFVVF PFFFVNIFVA LIIITFQEQG DKMMEECSLE KNERACIDFA
ISAKPLTRYM PQNRHTFQYR VWHFVVSPSF EYTIMAMIAL NTVVLMMKYY SAPCTYELAL
KYLNIAFTMV FSLECVLKVI AFGFVNYFRD TWNIFDFITV IGSITEIVLT DSKLVNTTGF
NMSFLKLFRA ARLIKLLRQG YTIRILLWTF VQSFKALPYV CLLIAMLFFI YAIIGMQVFG
NIRLDEESHI NRHNNFRSFF GSLMLLFRSA TGEAWQEIML SCLGEKGCEP DTTAPSGQQE
SERCGTDLAY VYFVSFIFFC SFLMLNLFVA VIMDNFEYLT RDSSILGPHH LDEFVRVWAE
YDRAACGRIH YTEMYEMLTL MSPPLGLGKR CPSKVAYKRL VLMNMPVAED MTVHFTSTLM
ALIRTALDIK IAKGGADRQQ LDSELQKETL AIWPHLSQKM LDLLVPMPKA SDLTVGKIYA
AMMIMDYYKQ SKVKKQRRQL EEQKNAPMFQ RMEPSSLPQE IIANAKALPC LPQGPPAGLG
GRSGCPAMSP LSPQIFQLTC MDPADDDGQF QEQRSLVVTD PGSMRRSFST IRDKRSSSSW
LEEFSMERSS DNTYKSRRRS YHSSLRLSAH RLNSDSGHKS DTHRSGGRER GRSKEREHLL
SADVSRCSSE ERGAQADWDS PERHPSRSPS EGRSQSPSRQ GTGSLSESSI PSVSDTSTPR
HSRRQLPPVP PKPRPLLSYS SLKQQPSNFS PPADGSQGGS LLASPALESA QVGLPESSDS
PRRAQGSHAS PQRYISEPYL ALHEDSHASD CGEEETLTFE AAVATSLGRS NTIGSAPPLR
HSWQMPNGHY RRRRRGGPGA GALCGAVGDL LSDTEEDKC
