ID A0A2I3S8Y1_PANTR Unreviewed; 1957 AA.
AC A0A2I3S8Y1;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Voltage-dependent R-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1E {ECO:0000313|Ensembl:ENSPTRP00000073286.1,
GN ECO:0000313|VGNC:VGNC:11749};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000073286.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000073286.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000073286.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|RuleBase:RU003808}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU003808}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. {ECO:0000256|RuleBase:RU003808}.
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DR EMBL; AACZ04056183; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSPTRT00000079052.1; ENSPTRP00000073286.1; ENSPTRG00000001749.6.
DR VGNC; VGNC:11749; CACNA1E.
DR GeneTree; ENSGT00940000155601; -.
DR Proteomes; UP000002277; Chromosome 1.
DR Bgee; ENSPTRG00000001749; Expressed in temporal lobe and 10 other cell types or tissues.
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 Gene3D; 1.10.287.70; -; 4.
DR Gene3D; 6.10.250.2180; -; 1.
DR Gene3D; 6.10.250.2500; -; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 3.
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; VOLTAGE-DEPENDENT CALCIUM CHANNEL TYPE A SUBUNIT ALPHA-1; 1.
DR PANTHER; PTHR45628:SF5; VOLTAGE-DEPENDENT R-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1E; 1.
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 SUPFAM; SSF81324; Voltage-gated potassium channels; 3.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR602077-1};
KW Calcium channel {ECO:0000256|ARBA:ARBA00022673,
KW ECO:0000256|RuleBase:RU003808};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW ECO:0000256|RuleBase:RU003808}; Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602077-1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW ECO:0000256|RuleBase:RU003808}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 371..394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 843..862
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 915..932
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 976..998
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1088..1113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1169..1187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1199..1222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1228..1246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1293..1311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1386..1410
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1426..1461
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 420..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1705..1814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1850..1869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1907..1938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 390..417
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 436..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1709..1766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1767..1800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 348
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1059
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 1957 AA; 222510 MW; 65A04C40836D389F CRC64;
MEPWGTLLET CLWGATWNWL YFIPLIIIGS FFVLNLVLGV LSGEFAKERE RVENRRAFMK
LRRQQQIERE LNGYRAWIDK AEEVMLAEEN KNAGTSALEV LRRATIKRSR TEAMTRDSSD
EHCVDISSVG TPLARASIKS AKVDGVSYFR HKERLLRISI RHMVKSQVFY WIVLSLVALN
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 QRTSQLRKHM
QMSSQEALNR EEAPTMNPLN PLNPLSSLNP LNAHPSLYRR PRAIEGLALG LALEKFEEER
ISRGGSLKGD GGDRSSALDN QRTPLSLGQR EPPWLARPCH GNCDPTQQEA GGGEAVVTFE
DRARHRQSQR RSRHRRVRTE GKESSSASRS RSASQERSLD EAMPTEGEKD HELRGNHGAK
EPTIQEERAQ DLRRTNSLMV SRGSGLAGGL DEADTPLVLP HPELEVGKHV VLTEQEPEGS
SEQALLGNVQ LDMGRVISQS EPDLSCITAN TDKATTESTS VTVAIPDVDP LVDSTVVHIS
NKTDGEASPL KEAEIREDEE EVEKKKQKKE KRETGKAMVP HSSMFIFSTT NPIRRACHYI
VNLRYFEMCI LLVIAASSIA LAAEDPVLTN SERNKVLRYF DYVFTGVFTF EMVIKMIDQG
LILQDGSYFR DLWNILDFVV VVGALVAFAL ATNKGRDIKT IKSLRVLRVL RPLKTIKRLP
KLKAVFDCVV TSLKNVFNIL IVYKLFMFIF AVIAVQLFKG KFFYCTDSSK DTEKECIGNY
VDHEKNKMEV KGREWKRHEF HYDNIIWALL TLFTVSTGEG WPQVLQHSVD VTEEDRGPSR
SNRMEMSIFY VVYFVVFPFF FVNIFVALII ITFQEQGDKM MEECSLEKNE RACIDFAISA
KPLTRYMPQN RHTFQYRVWH FVVSPSFEYT IMAMIALNTV VLMMKYYSAP CTYELALKYL
NIAFTMVFSL ECVLKVIAFG FLNYFRDTWN IFDFITVIGS ITEIILTDSK LVNTSGFNMS
FLKLFRAARL IKLLRQGYTI RILLWTFVQS FKALPYVCLL IAMLFFIYAI IGMQVFGNIK
LDEESHINRH NNFRSFFGSL MLLFRSATGE AWQEIMLSCL GEKGCEPDTT APSGQNENER
CGTDLAYVYF VSFIFFCSFL MLNLFVAVIM DNFEYLTRDS SILGPHHLDE FVRVWAEYDR
AACGRIHYTE MYEMLTLMSP PLGLGKRCPS KVAYKRLVLM NMPVAEDMTV HFTSTLMALI
RTALDIKIAK GGADRQQLDS ELQKETLAIW PHLSQKMLDL LVPMPKASDL TVGKIYAAMM
IMDYYKQSKV KKQRQQLEEQ KNAPMFQRME PSSLPQEIIA NAKALPYLQQ DPVSGLSGRS
GYPSMSPLSP QDIFQLACMD PADDGQFQER QSLVVTDPSS MRRSFSTIRD KRSNSSWLEE
FSMERSSENT YKSRRRSYHS SLRLSAHRLN SDSGHKSDTH RSGGRERGRS KERKHLLSPD
VSRCNSEERG TQADWESPER RQSRSPSEGR SQTPNRQGTG SLSESSIPSV SDTSTPRRSR
RQLPPVPPKP RPLLSYSSLI RHAGSISPPA DGSEEGSPLT SQALESNNAC LTESSNSPHP
QQSQHASPQR YISEPYLALH EDSHASDCGE EETLTFEAAV ATSLGRSNTI GSAPPLRHSW
QMPNGHYRRR RRGGPGPGMM CGAVNNLLSD TEEDDKC
//
