GenomeNet

Database: UniProt/SWISS-PROT
Entry: CAC1E_RABIT
LinkDB: CAC1E_RABIT
Original site: 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   07-OCT-2020, entry version 127.
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}.
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   STRING; 9986.ENSOCUP00000015082; -.
DR   PRIDE; Q02343; -.
DR   GeneID; 100009403; -.
DR   KEGG; ocu:100009403; -.
DR   CTD; 777; -.
DR   eggNOG; KOG2301; Eukaryota.
DR   InParanoid; Q02343; -.
DR   KO; K04852; -.
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   CA_BIND         426..437
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   CA_BIND         1742..1753
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          374..391
FT                   /note="Binding to the beta subunit"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        716..721
FT                   /note="Poly-Glu"
FT   COMPBIAS        748..753
FT                   /note="Poly-Arg"
FT   COMPBIAS        767..772
FT                   /note="Poly-Arg"
FT   COMPBIAS        1218..1221
FT                   /note="Poly-Val"
FT   COMPBIAS        1976..1979
FT                   /note="Poly-Ser"
FT   COMPBIAS        2231..2235
FT                   /note="Poly-Arg"
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
//
DBGET integrated database retrieval system