CAC1E_DIPOM
ID CAC1E_DIPOM Reviewed; 2223 AA.
AC P56699;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Probable voltage-dependent R-type calcium channel subunit alpha-1E;
DE AltName: Full=DOE-1;
DE AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.3;
OS Diplobatis ommata (Ocellated electric ray) (Discopyge ommata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Batoidea; Torpediniformes; Narcinidae; Diplobatis.
OX NCBI_TaxID=1870830;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Electric lobe;
RX PubMed=7683405; DOI=10.1073/pnas.90.9.3787;
RA Horne W.A., Ellinor P.T., Inman I., Zhou M., Tsien R.W., Schwarz T.L.;
RT "Molecular diversity of Ca2+ channel alpha 1 subunits from the marine ray
RT Discopyge ommata.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:3787-3791(1993).
CC -!- FUNCTION: The isoform alpha-1E gives rise to R-type calcium currents.
CC R-type calcium channels belong to the 'high-voltage activated' (HVA)
CC group (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Voltage-dependent calcium channels are multisubunit complexes,
CC consisting of alpha-1, alpha-2, beta and delta subunits in a 1:1:1:1
CC ratio. The channel activity is directed by the pore-forming and
CC voltage-sensitive alpha-1 subunit. In many cases, this subunit is
CC sufficient to generate voltage-sensitive calcium channel activity. The
CC auxiliary subunits beta and alpha-2/delta linked by a disulfide bridge
CC regulate the channel activity (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expression is higher in the forebrain than in the
CC electric lobe.
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. {ECO:0000305}.
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DR EMBL; L12531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A47447; A47447.
DR AlphaFoldDB; P56699; -.
DR BMRB; P56699; -.
DR SMR; P56699; -.
DR PRIDE; P56699; -.
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; 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 PROSITE; PS50222; EF_HAND_2; 1.
PE 2: Evidence at transcript level;
KW Calcium; Calcium channel; Calcium transport; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Metal-binding; Phosphoprotein;
KW Repeat; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..2223
FT /note="Probable voltage-dependent R-type calcium channel
FT subunit alpha-1E"
FT /id="PRO_0000053942"
FT TOPO_DOM 1..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..121
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..139
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..159
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..189
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..194
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..213
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..252
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..338
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..363
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..490
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 491..509
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 510..524
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 525..544
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 545..552
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 553..571
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 572..581
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 582..600
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 601..619
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 620..639
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 640..692
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 693..717
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 718..1105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1106..1124
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1125..1140
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1141..1160
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1161..1172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1173..1191
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1192..1205
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1206..1224
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1225..1243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1244..1263
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1264..1349
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1350..1374
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1375..1429
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1430..1448
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1449..1463
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1464..1483
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1484..1491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1492..1510
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1511..1519
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1520..1538
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1539..1557
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1558..1577
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1578..1638
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1639..1663
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1664..2223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 89..366
FT /note="I"
FT REPEAT 478..720
FT /note="II"
FT REPEAT 1092..1377
FT /note="III"
FT REPEAT 1414..1666
FT /note="IV"
FT DOMAIN 1679..1714
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..403
FT /note="Binding to the beta subunit"
FT /evidence="ECO:0000250"
FT REGION 742..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1880..1902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1978..2102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2116..2139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2178..2223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..973
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1024
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1040
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1067
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1995..2010
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2012..2083
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 441
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 443
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 445
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 1692
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 1698
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 1703
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT SITE 321
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 671
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1323
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1611
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 2223 AA; 251829 MW; 59722DC03E1CFC5B CRC64;
MARFGEAVGS LSADASSEQG RSRHQVPVTG ETAVAAAAAA VVAGAAQGSA GFKQTRAQRA
RTMALYNPIP VRHNCLTANR SLFLFGEDNI VRKSARRVIE WPPFEYMILA TIIANCVVLA
LEQHLPNGDK TPMAKSLEQT EPYFIGIFCF EAGIKIVALG FVFHKGSYLR NGWNVMDFIV
VLSGLLATAA THFNLRTLRA VRVLRPLKLV SGIPSLQIVL KSIMKAMVPL LQIGLLLFFA
ILMFAIIGLE FYYGKLHRTC YTDDAAAEEL DLQFPCGTQE PTRLCPNGTV CSYWIGPNDG
ITQFDNILFA LLTVFQCITM EGWTTILYNT DDALGAMWNW LYFIPLIIIG SFFVLNLVLG
VLSGEFAKER ERVENRRSFL KLRRQQQIER ELNGYRAWID KAEEVMLLEE NKNAGEKSAL
HVLRRATIKK GRMEMIQTES SEDQYTEISS VGSPLARASI KSTKLLEGSS YFRRKERMLR
ISIRHMVKSH AFYWIVLGLV ALNTVCVAVV HYDQPLWLSN FLYYAEFTFL GLFSSEMFLK
MYGCGPRLYF HSSFNCFDCG VIIGSIFDVV WTIIRPETSF GISVLRALRL LRIFKITKYW
ASLRNLVVSL MSSMKSIISL LFLLFLFIVV FALLGMQLFG GQFNFEEGTP PTNFDTFPAA
IITVFQILTG EDWNEVMYNG IKSQGGVNSG MWSSVYFIVL TLFGNYTLLN VFLAIAVDNL
ANAQELTKEE QEEEEAINQK HALQKAKEVS PMSAPGFPST EREFRRHKHM SIWEARTSQL
RRRMQMSSRE ALFTDALQGL EGSRYRRHRS RIFEAESLRR LAEQQAAESH QLGEVGRREA
FKSRSLRNSW QPAGPDKRSS SIKVNGEQGR ALGRSVEAGA SFRMAEPIRA RRRYRSLYKE
AKMGLEESAE TSLSRRPGKN KEGRLLQQLC EEQESGQLTQ TPEVMDAQGQ MKAFSWQGEP
HSSSMTRTPD VDTDPSGGNL EKESGRTPEN GKEESANTSE QVNEQSNWLN LQLNQQATPG
DRELTTGTRD TKQDKTQEQT EIDVDCENTE TPMDSLVTPG NAYSSSSSVK EDEKKSKAII
PYTSMFLFRK TNPIRRVCHF IVNLRYFEMC ILLVIAASSV ALAAEDPIHK DSARNQVLRY
FDYVFTGVFT FEMVIKMIDI GLVFHEGSYF RDVWNILDFI VVSGALVAFA FTNLIGGSSG
KDINTIKSLR VLRVLRPLKT IKRLPKLKAV FDCVVTSLKN VFNILIVYKL FMFIFAVIAV
QLFKGKFFYC TDSSKMTKQD CRGQFVLYRQ RTKLSIENGN VTTFHYDNVV WALLTLFTVS
TGEGWPQVLQ HSVDVTEADQ GPIPGNRMEM SIFYIVYFVV FPFFFVNIFV ALIIITFQEQ
GDKMLEESSL EKNERACIDF AISAKPLTRY MPQNRQTFQY RVWQFVVSPS FEYTILTMIA
LNTVVLMMKH HSPPPGFASV LKLMNIAFTI TFTLECILKI IAFGFLNYFR DSWNVFDFVT
VVGSISEIIV TECNLKFVNL SFLKLFRAAR LIKLLRQGIT IRILLWTFVQ SFKALPYVCL
LIAMLFFIYA IIGMQLFGNI GLDDHTPINR HNNFHTFFNA LMLLFRSATG ESWQEIMLAC
LSGKECEGTR EPSCGTDVAY FYFVSFIFLC SFLMLNLFVA VIMDNFEYLT RDSSILGPHH
LDEFVRVWAE YDRAACGRIH YTDMYQMLTL MSPPLGLGKK CPSKVAYKRL VLMNMPVTED
KTVHFTSTLM GLIRTALQIK LARGGADKQQ LDAELRKEIM TIWPHLSQKT LDLLVPMHTY
SDLTVGKIYA AMMIMDYYKQ SKNKKYQKLQ EEQSRTPMFQ RMEASSLPPQ IISSTKGLPY
LQTGTGPDVD SRSEFTPLVP LPPVMFQQGR TSSQGEEIHK QRPKELKKIK LEYPHYGHYL
PIENQGRAVS MPRLEIESAE DTSPLKRSLS TFAANHSNST WLNEYSLERA GPEDLYKRWS
RRPLRPPSRS SNAGSRERGR SRERKHLLSP ERSVCSTGQC AHPSQHRGLD QRLSRSPSPG
YSHRPREQVN SSVSESPVPS SSGTSPPKQG QRQLPQTPSK PRPLVSYSPV AQRGDVSGHC
SPMCKETRYQ SLRVQPSKAL WSESPGRSRE SESQHSTPLR YISEPSLTLH DGPGSLDQAL
GEETLTFEAA VATSLGRSHT ISSAPPLRQG WHLPNGSYRT RMMQSGAPST PDPYTHAEED
DRC
