CAC1D_DROME
ID CAC1D_DROME Reviewed; 2516 AA.
AC Q24270; Q8IP23; Q8IP24; Q8IP25; Q95U73; Q9V3P7;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Voltage-dependent calcium channel type D subunit alpha-1;
DE Short=DmCa1D;
GN Name=Ca-alpha1D; Synonyms=DroCa1, l(2)35Fa; ORFNames=CG4894;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND ALTERNATIVE SPLICING.
RC STRAIN=Canton-S; TISSUE=Head;
RX PubMed=7869089; DOI=10.1523/jneurosci.15-02-01132.1995;
RA Zheng W., Feng G., Ren D., Eberl D.F., Hannan F., Dubald M., Hall L.M.;
RT "Cloning and characterization of a calcium channel alpha 1 subunit from
RT Drosophila melanogaster with similarity to the rat brain type D isoform.";
RL J. Neurosci. 15:1132-1143(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10471707; DOI=10.1093/genetics/153.1.179;
RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T.,
RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A.,
RA Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R.,
RA Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K.,
RA Celniker S.E., Rubin G.M.;
RT "An exploration of the sequence of a 2.9-Mb region of the genome of
RT Drosophila melanogaster: the Adh region.";
RL Genetics 153:179-219(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1895-2300 (ISOFORM D).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP MUTAGENESIS OF CYS-629.
RX PubMed=9502794; DOI=10.1523/jneurosci.18-07-02335.1998;
RA Ren D., Xu H., Eberl D.F., Chopra M., Hall L.M.;
RT "A mutation affecting dihydropyridine-sensitive current levels and
RT activation kinetics in Drosophila muscle and mammalian heart calcium
RT channels.";
RL J. Neurosci. 18:2335-2341(1998).
RN [7]
RP MUTAGENESIS OF CYS-629.
RX PubMed=9539432; DOI=10.1093/genetics/148.3.1159;
RA Eberl D.F., Ren D., Feng G., Lorenz L.J., van Vactor D., Hall L.M.;
RT "Genetic and developmental characterization of Dmca1D, a calcium channel
RT alpha-1 subunit gene in Drosophila melanogaster.";
RL Genetics 148:1159-1169(1998).
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. Encodes a dihydropyridine- and diltiazem-
CC sensitive current in larval body wall muscle. Vital for embryonic
CC development. {ECO:0000269|PubMed:7869089}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=A;
CC IsoId=Q24270-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q24270-3; Sequence=VSP_017568;
CC Name=C;
CC IsoId=Q24270-4; Sequence=VSP_017569;
CC Name=D;
CC IsoId=Q24270-2; Sequence=VSP_007604, VSP_007605;
CC -!- TISSUE SPECIFICITY: Expressed in the adult body, head and leg. Highly
CC expressed in the embryonic nervous system.
CC -!- DEVELOPMENTAL STAGE: Faintly expressed in embryos at 9-12 hours.
CC Expression increases rapidly as the nervous system matures, peaking
CC just prior to hatching. A second peak is observed in late pupal stages
CC around 73-108 hours postpuparium.
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}.
CC -!- CAUTION: It is uncertain whether Met-1, Met-494, Met-539, Met-544 or
CC Met-553 is the initiator. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL13497.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U00690; AAA81883.1; -; mRNA.
DR EMBL; AE014134; AAF53504.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10929.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10930.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10931.1; -; Genomic_DNA.
DR EMBL; AY058268; AAL13497.1; ALT_INIT; mRNA.
DR RefSeq; NP_525104.2; NM_080365.3.
DR RefSeq; NP_602305.1; NM_134429.3.
DR RefSeq; NP_723952.1; NM_165146.2.
DR RefSeq; NP_723953.1; NM_165147.2.
DR AlphaFoldDB; Q24270; -.
DR SMR; Q24270; -.
DR BioGRID; 60962; 3.
DR IntAct; Q24270; 7.
DR STRING; 7227.FBpp0089047; -.
DR GlyGen; Q24270; 2 sites.
DR PaxDb; Q24270; -.
DR EnsemblMetazoa; FBtr0479784; FBpp0428117; FBgn0001991.
DR GeneID; 34950; -.
DR KEGG; dme:Dmel_CG4894; -.
DR CTD; 34950; -.
DR FlyBase; FBgn0001991; Ca-alpha1D.
DR VEuPathDB; VectorBase:FBgn0001991; -.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00940000169312; -.
DR InParanoid; Q24270; -.
DR PhylomeDB; Q24270; -.
DR Reactome; R-DME-422356; Regulation of insulin secretion.
DR Reactome; R-DME-5576892; Phase 0 - rapid depolarisation.
DR Reactome; R-DME-5576893; Phase 2 - plateau phase.
DR SignaLink; Q24270; -.
DR BioGRID-ORCS; 34950; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Ca-alpha1D; fly.
DR GenomeRNAi; 34950; -.
DR PRO; PR:Q24270; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0001991; Expressed in oviduct (Drosophila) and 17 other tissues.
DR ExpressionAtlas; Q24270; baseline and differential.
DR Genevisible; Q24270; DM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:FlyBase.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IGI:FlyBase.
DR GO; GO:0008331; F:high voltage-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IMP:FlyBase.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IMP:FlyBase.
DR GO; GO:0006816; P:calcium ion transport; NAS:FlyBase.
DR GO; GO:0019722; P:calcium-mediated signaling; IMP:FlyBase.
DR GO; GO:0042045; P:epithelial fluid transport; IDA:FlyBase.
DR GO; GO:0040011; P:locomotion; IMP:FlyBase.
DR GO; GO:0006936; P:muscle contraction; TAS:FlyBase.
DR GO; GO:0016322; P:neuron remodeling; IMP:FlyBase.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR031649; GPHH_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR014873; VDCC_a1su_IQ.
DR InterPro; IPR005446; VDCC_L_a1su.
DR InterPro; IPR002077; VDCCAlpha1.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR Pfam; PF08763; Ca_chan_IQ; 1.
DR Pfam; PF16905; GPHH; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00167; CACHANNEL.
DR PRINTS; PR01630; LVDCCALPHA1.
DR SMART; SM01062; Ca_chan_IQ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..2516
FT /note="Voltage-dependent calcium channel type D subunit
FT alpha-1"
FT /id="PRO_0000053960"
FT TOPO_DOM 1..615
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 616..634
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 635..653
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..671
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 672..684
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 685..699
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 700..711
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 712..730
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 731..750
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 751..770
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 771..853
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 854..878
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 879..985
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 986..1005
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1006..1018
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1019..1038
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1039..1047
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1048..1066
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1067..1076
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1077..1095
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1096..1114
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1115..1134
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1135..1190
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1191..1215
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1216..1339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1340..1363
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1364..1380
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1381..1400
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1401..1408
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1409..1431
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1432..1439
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1440..1454
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1455..1475
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1476..1495
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1496..1584
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1585..1609
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1610..1664
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1665..1683
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1684..1697
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1698..1717
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1718..1726
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1727..1745
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1746..1777
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1778..1796
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1797..1815
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1816..1835
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1836..1902
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1903..1921
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1922..2516
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 602..883
FT /note="I"
FT REPEAT 971..1217
FT /note="II"
FT REPEAT 1331..1613
FT /note="III"
FT REPEAT 1648..1929
FT /note="IV"
FT REGION 19..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1226..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1533..1622
FT /note="Dihydropyridine binding"
FT /evidence="ECO:0000250"
FT REGION 1885..1948
FT /note="Dihydropyridine binding"
FT /evidence="ECO:0000250"
FT REGION 1896..1937
FT /note="Phenylalkylamine binding"
FT /evidence="ECO:0000250"
FT REGION 2423..2516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..432
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..467
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2423..2450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2458..2516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 836
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT BINDING 1168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT BINDING 1559
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 647
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1293..1329
FT /note="VDEEGMITARPRRMSEVNTATKILPIPPGTSFFLFSQ -> DSNSEVSARVT
FT ARPRRLSEVSMKKTKKPIPRGSAFFIFSY (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_017568"
FT VAR_SEQ 1496
FT /note="K -> KYVVKCVVVAIKTIGNIMLVTYLLQFMFAVIGVQLFK (in
FT isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_017569"
FT VAR_SEQ 2282..2300
FT /note="NRNRGILLHPYNNVYAPNG -> LRTQWCSSWPRTHDPIDTS (in
FT isoform D)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_007604"
FT VAR_SEQ 2301..2516
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_007605"
FT MUTAGEN 629
FT /note="C->Y: In AR66; slower channel activation and
FT reduction of peak current."
FT /evidence="ECO:0000269|PubMed:9502794,
FT ECO:0000269|PubMed:9539432"
FT CONFLICT 134
FT /note="P -> A (in Ref. 1; AAA81883)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="F -> L (in Ref. 1; AAA81883)"
FT /evidence="ECO:0000305"
FT CONFLICT 678
FT /note="N -> D (in Ref. 1; AAA81883)"
FT /evidence="ECO:0000305"
FT CONFLICT 683
FT /note="R -> G (in Ref. 1; AAA81883)"
FT /evidence="ECO:0000305"
FT CONFLICT 696
FT /note="I -> M (in Ref. 1; AAA81883)"
FT /evidence="ECO:0000305"
FT CONFLICT 1390
FT /note="I -> M (in Ref. 1; AAA81883)"
FT /evidence="ECO:0000305"
FT CONFLICT 1433
FT /note="N -> D (in Ref. 1; AAA81883)"
FT /evidence="ECO:0000305"
FT CONFLICT 2479
FT /note="N -> S (in Ref. 1; AAA81883)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2516 AA; 276700 MW; 8CFC07499E750901 CRC64;
MGGGELVNCI AYDDNTLVIE RKPSPSSPST SRRYLKAETP TRGSRKYNRK SSAKSDLEVV
VVKPEHHHQH RSPTITLPVP ANPLTTSASA GSSPTGAGLA AGLGTASGTV LQQSCSALDP
PEDSNQPSGT RRRPTSTELA LSNVTSQIVN NATYKLDFKQ RRHKSNNGGS ESGSLTGIAT
GPATSPAGPT GPTSSSGKRR KSSCTSCGGG GISAPPPRLT PEEAWQLQPQ NSVTSAGSTN
SSFSSGGGRD DNSSYSAVGG DSSSSNSCNC DITGDNSTLH GFGVGDVCSF IADCDDNSED
DDGDPNNQDL SSQTLRTAAI VAAVAAAAKE QAQEQSLADC ESFSDRRQDA DEDVRIIQDC
CGGNNDSLED VGEVDDNADV VVRKNSRNRP SIRRTCRITE EDDDEDENAD YGDFDREDQE
LDDEEPEGTT IDIDEQEQQH DQGDSAEEED DDEDVDEYFE EEEDDTQAFS PFYSSSAELI
DNFGGGAGKF FNIMDFERGA SGEGGFSPNG NGGPGSGDVS RTARYDSGEG DLGGGNNIMG
IDSMGIANIP ETMNGTTIGP SGAGGQKGGA AAGAAGQKRQ QRRGKPQPDR PQRALFCLSV
KNPLRALCIR IVEWKPFEFL ILLTIFANCI ALAVYTPYPG SDSNVTNQTL EKVEYVFLVI
FTAECVMKIL AYGFVLHNGA YLRNGWNLLD FTIVVIGAIS TALSQLMKDA FDVKALRAFR
VLRPLRLVSG VPSLQVVLNS ILKAMVPLFH IALLVLFVII IYAIIGLELF SGKLHKACRD
EITGEYEENI RPCGVGYQCP PGYKCYGGWD GPNDGITNFD NFGLAMLTVF QCVTLEGWTD
VLYSIQDAMG SDWQWMYFIS MVILGAFFVM NLILGVLSGE FSKERNKAKN RGDFQKLREK
QQIEEDLRGY LDWITQAEDI EPDAVGGLIS DGKGKQPNEM DSTENLGEEM PEVQMTESRW
RKMKKDFDRV NRRMRRACRK AVKSQAFYWL IIVLVFLNTG VLATEHYGQL DWLDNFQEYT
NVFFIGLFTC EMLLKMYSLG FQGYFVSLFN RFDCFVVIGS ITETLLTNTG MMPPLGVSVL
RCVRLLRVFK VTKYWRSLSN LVASLLNSIQ SIASLLLLLF LFIVIFALLG MQVFGGKFNF
DGKEEKYRMN FDCFWQALLT VFQIMTGEDW NAVMYVGINA YGGVSSYGAL ACIYFIILFI
CGNYILLNVF LAIAVDNLAD ADSLSEVEKE EEPHDESAQK KSHSPTPTID GMDDHLSIDI
DMEQQELDDE DKMDHETLSD EEVREMCEEE EEVDEEGMIT ARPRRMSEVN TATKILPIPP
GTSFFLFSQT NRFRVFCHWL CNHSNFGNII LCCIMFSSAM LAAENPLRAN DDLNKVLNKF
DYFFTAVFTI ELILKLISYG FVLHDGAFCR SAFNLLDLLV VCVSLISLVS SSNAISVVKI
LRVLRVLRPL RAINRAKGLK HVVQCVIVAV KTIGNIVLVT CLLQFMFAVI GVQLFKGKFF
KCTDGSKMTQ DECYGTYLVY DDGDVHKPRL REREWSNNRF HFDDVAKGML TLFTVSTFEG
WPGLLYVSID SNKENGGPIH NFRPIVAAYY IIYIIIIAFF MVNIFVGFVI VTFQNEGEQE
YKNCDLDKNQ RNCIEFALKA KPVRRYIPKH GIQYKVWWFV TSSSFEYTIF ILIMINTVTL
AMKFYNQPLW YTELLDALNM IFTAVFALEF VFKLAAFRFK NYFGDAWNVF DFIIVLGSFI
DIVYSEIKSK DTSQIAECDI VEGCKSTKKS AGSNLISINF FRLFRVMRLV KLLSKGEGIR
TLLWTFIKSF QALPYVALLI VLLFFIYAVV GMQVFGKIAL DGGNAITANN NFQTFQQAVL
VLFRSATGEA WQEIMMSCSA QPDVKCDMNS DTPGEPCGSS IAYPYFISFY VLCSFLIINL
FVAVIMDNFD YLTRDWSILG PHHLDEFIRL WSEYDPDAKG RIKHLDVVTL LRKISPPLGF
GKLCPHRMAC KRLVSMNMPL NSDGTVLFNA TLFAVVRTSL SIKTDGNIDD ANSELRATIK
QIWKRTNPKL LDQVVPPPGN DDEVTVGKFY ATYLIQDYFR RFKKRKEQEG KEGHPDSNTV
TLQAGLRTLH EVSPALKRAI SGNLDELDQE PEPMHRRHHT LFGSVWSSIR RHGNGTFRRS
AKATASQSNG ALAIGGSASA ALGVGGSSLV LGSSDPAGGD YLYDTLNRSV ADGVNNITRN
IMQARLAAAG KLQDELQGAG SGGELRTFGE SISMRPLAKN GGGAATVAGT LPPEANAINY
DNRNRGILLH PYNNVYAPNG ALPGHERMIQ STPASPYDQR RLPTSSDMNG LAESLIGGVL
AAEGLGKYCD SEFVGTAARE MREALDMTPE EMNLAAHQIL SNEHSLSLIG SSNGSIFGGS
AGGLGGAGSG GVGGLGGSSS IRNAFGGSGS GPSSLSPQHQ PYSGTLNSPP IPDNRLRRVA
TVTTTNNNNK SQVSQNNSNS LNVRANANSQ MNMSPTGQPV QQQSPLRGQG NQTYSS
