CAC1A_DROME
ID CAC1A_DROME Reviewed; 1851 AA.
AC P91645; O01713; O01714; Q76NR8; Q76NR9; Q76NS0; Q9VYR8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 3.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Voltage-dependent calcium channel type A subunit alpha-1;
DE AltName: Full=Protein cacophony;
DE AltName: Full=Protein nightblind A;
DE AltName: Full=Protein no-on-transient B;
DE Short=Dmca1A;
GN Name=cac; Synonyms=nbA, nonB; ORFNames=CG43368;
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 E), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=8987815; DOI=10.1523/jneurosci.16-24-07868.1996;
RA Smith L.A., Wang X.J., Peixoto A.A., Neumann E.K., Hall L.M., Hall J.C.;
RT "A Drosophila calcium channel alpha1 subunit gene maps to a genetic locus
RT associated with behavioral and visual defects.";
RL J. Neurosci. 16:7868-7879(1996).
RN [2]
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 [3]
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 [4]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=9093853; DOI=10.1093/genetics/145.4.1003;
RA Peixoto A.A., Smith L.A., Hall J.C.;
RT "Genomic organization and evolution of alternative exons in a Drosophila
RT calcium channel gene.";
RL Genetics 145:1003-1013(1997).
RN [5]
RP RNA EDITING.
RX PubMed=10966106; DOI=10.1016/s0092-8674(00)00049-0;
RA Palladino M.J., Keegan L.P., O'Connell M.A., Reenan R.A.;
RT "A-to-I pre-mRNA editing in Drosophila is primarily involved in adult
RT nervous system function and integrity.";
RL Cell 102:437-449(2000).
RN [6]
RP VARIANT ILE-1029, AND FUNCTION.
RX PubMed=9649530; DOI=10.1093/genetics/149.3.1407;
RA Smith L.A., Peixoto A.A., Kramer E.M., Villella A., Hall J.C.;
RT "Courtship and visual defects of cacophony mutants reveal functional
RT complexity of a calcium-channel alpha1 subunit in Drosophila.";
RL Genetics 149:1407-1426(1998).
RN [7]
RP VARIANTS 284-LEU--CYS-1851 DEL AND GLU-989 DELINS LYS-LYS, CHARACTERIZATION
RP OF VARIANTS 284-LEU--CYS-1851 DEL AND LYS-989, MUTAGENESIS OF ARG-1196 AND
RP ARG-1205, AND FUNCTION.
RX PubMed=28742085; DOI=10.1371/journal.pgen.1006905;
RG Members of the UDN;
RA Luo X., Rosenfeld J.A., Yamamoto S., Harel T., Zuo Z., Hall M.,
RA Wierenga K.J., Pastore M.T., Bartholomew D., Delgado M.R., Rotenberg J.,
RA Lewis R.A., Emrick L., Bacino C.A., Eldomery M.K., Coban Akdemir Z.,
RA Xia F., Yang Y., Lalani S.R., Lotze T., Lupski J.R., Lee B., Bellen H.J.,
RA Wangler M.F.;
RT "Clinically severe CACNA1A alleles affect synaptic function and
RT neurodegeneration differentially.";
RL PLoS Genet. 13:E1006905-E1006905(2017).
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,
CC neurotransmitter release, gene expression, cell motility, cell division
CC and cell death (By similarity). Probably encodes a dihydropyridine-
CC insensitive current. Vital for survival to adulthood.
CC {ECO:0000250|UniProtKB:O00555, ECO:0000269|PubMed:28742085,
CC ECO:0000269|PubMed:8987815, ECO:0000269|PubMed:9649530}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=At least 2 regions (Exon IS4 and Exon I/II) undergo
CC alternative splicing. The total number of isoforms is currently not
CC known. {ECO:0000269|PubMed:12537572, ECO:0000269|PubMed:9093853};
CC Name=E;
CC IsoId=P91645-1; Sequence=Displayed;
CC Name=A;
CC IsoId=P91645-2; Sequence=VSP_012741;
CC Name=B;
CC IsoId=P91645-3; Sequence=VSP_000952;
CC Name=C;
CC IsoId=P91645-4; Sequence=VSP_000953;
CC Name=D;
CC IsoId=P91645-5; Sequence=VSP_000952, VSP_000953, VSP_012741;
CC Name=F;
CC IsoId=P91645-6; Sequence=VSP_000952, VSP_000953;
CC -!- TISSUE SPECIFICITY: Expressed widely in the embryonic nervous system.
CC {ECO:0000269|PubMed:8987815}.
CC -!- DEVELOPMENTAL STAGE: Expression peaks in the first larval instar,
CC midpupal, and late pupal stages. In late-stage embryos, it is expressed
CC preferentially in the nervous system. {ECO:0000269|PubMed:8987815}.
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 -!- RNA EDITING: Modified_positions=Undetermined; Note=Partially edited. 11
CC sites are edited by Adar. {ECO:0000269|PubMed:10966106};
CC -!- MISCELLANEOUS: [Isoform E]: Has exons IS4B and I/IIA.
CC -!- MISCELLANEOUS: [Isoform A]: Has exons IS4B and I/IIA. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform B]: Has exons IS4A and I/IIA. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform C]: Has exons IS4B and I/IIB. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform D]: Has exons IS4A and I/IIB. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform F]: Has exons IS4A and I/IIB. {ECO:0000305}.
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; U55776; AAC47406.1; -; mRNA.
DR EMBL; AE014298; AAF48120.2; -; Genomic_DNA.
DR EMBL; AE014298; AAS65322.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65323.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65324.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65325.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65326.1; -; Genomic_DNA.
DR EMBL; U88664; AAB53271.1; -; Genomic_DNA.
DR EMBL; U88665; AAB53272.1; -; Genomic_DNA.
DR PIR; T13980; T13980.
DR RefSeq; NP_001245639.1; NM_001258710.2. [P91645-1]
DR RefSeq; NP_511133.2; NM_078578.5. [P91645-2]
DR RefSeq; NP_996416.1; NM_206693.5. [P91645-6]
DR RefSeq; NP_996417.1; NM_206694.4. [P91645-1]
DR RefSeq; NP_996418.1; NM_206695.4. [P91645-5]
DR RefSeq; NP_996419.1; NM_206696.5.
DR RefSeq; NP_996420.1; NM_206697.4.
DR PDB; 4Z89; X-ray; 2.64 A; a/b/c/d/e/f/g/h/i/j=1688-1702.
DR PDB; 4Z8A; X-ray; 1.76 A; B=1688-1702.
DR PDBsum; 4Z89; -.
DR PDBsum; 4Z8A; -.
DR AlphaFoldDB; P91645; -.
DR SMR; P91645; -.
DR BioGRID; 58563; 20.
DR IntAct; P91645; 5.
DR STRING; 7227.FBpp0298326; -.
DR GlyGen; P91645; 3 sites.
DR PaxDb; P91645; -.
DR EnsemblMetazoa; FBtr0307318; FBpp0298319; FBgn0263111. [P91645-2]
DR EnsemblMetazoa; FBtr0307319; FBpp0298320; FBgn0263111. [P91645-5]
DR EnsemblMetazoa; FBtr0307320; FBpp0298321; FBgn0263111. [P91645-6]
DR EnsemblMetazoa; FBtr0307322; FBpp0298323; FBgn0263111. [P91645-1]
DR EnsemblMetazoa; FBtr0308609; FBpp0300833; FBgn0263111. [P91645-1]
DR GeneID; 32158; -.
DR KEGG; dme:Dmel_CG43368; -.
DR CTD; 12285; -.
DR FlyBase; FBgn0263111; cac.
DR VEuPathDB; VectorBase:FBgn0263111; -.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00940000170242; -.
DR InParanoid; P91645; -.
DR PhylomeDB; P91645; -.
DR Reactome; R-DME-112308; Presynaptic depolarization and calcium channel opening.
DR Reactome; R-DME-422356; Regulation of insulin secretion.
DR BioGRID-ORCS; 32158; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 32158; -.
DR PRO; PR:P91645; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0263111; Expressed in brain and 11 other tissues.
DR ExpressionAtlas; P91645; baseline and differential.
DR Genevisible; P91645; DM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:FlyBase.
DR GO; GO:0031594; C:neuromuscular junction; IMP:FlyBase.
DR GO; GO:0048786; C:presynaptic active zone; IDA:FlyBase.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IGI:FlyBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008331; F:high voltage-gated calcium channel activity; IMP:FlyBase.
DR GO; GO:0008332; F:low voltage-gated calcium channel activity; IMP:FlyBase.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:FlyBase.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:FlyBase.
DR GO; GO:0097352; P:autophagosome maturation; IMP:FlyBase.
DR GO; GO:0006914; P:autophagy; 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; IMP:FlyBase.
DR GO; GO:0019722; P:calcium-mediated signaling; IMP:FlyBase.
DR GO; GO:0007268; P:chemical synaptic transmission; IDA:FlyBase.
DR GO; GO:0007619; P:courtship behavior; IMP:FlyBase.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IMP:FlyBase.
DR GO; GO:0042045; P:epithelial fluid transport; IDA:FlyBase.
DR GO; GO:0006887; P:exocytosis; IMP:FlyBase.
DR GO; GO:0045433; P:male courtship behavior, veined wing generated song production; IMP:FlyBase.
DR GO; GO:0070050; P:neuron cellular homeostasis; IMP:FlyBase.
DR GO; GO:0016322; P:neuron remodeling; IMP:FlyBase.
DR GO; GO:0007269; P:neurotransmitter secretion; IMP:FlyBase.
DR GO; GO:0007602; P:phototransduction; NAS:FlyBase.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IMP:FlyBase.
DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0002027; P:regulation of heart rate; IMP:FlyBase.
DR GO; GO:0016057; P:regulation of membrane potential in photoreceptor cell; IGI:FlyBase.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; IGI:FlyBase.
DR GO; GO:0007632; P:visual behavior; NAS:FlyBase.
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; IPR002077; VDCCAlpha1.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037; PTHR10037; 2.
DR Pfam; PF08763; Ca_chan_IQ; 1.
DR Pfam; PF16905; GPHH; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00167; CACHANNEL.
DR SMART; SM01062; Ca_chan_IQ; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Calcium channel;
KW Calcium transport; Developmental protein; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; RNA editing; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..1851
FT /note="Voltage-dependent calcium channel type A subunit
FT alpha-1"
FT /id="PRO_0000053959"
FT TOPO_DOM 1..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..57
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..75
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..95
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..133
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..152
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..191
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..288
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..313
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..460
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 461..475
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 476..495
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 496..503
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 504..522
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 523..531
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..550
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 551..569
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 570..589
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 590..642
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 643..667
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 668..767
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 768..786
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 787..802
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 803..822
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 823..834
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 835..853
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 854..866
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 867..885
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 886..904
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 905..924
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 925..1013
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1014..1038
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1039..1093
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1094..1122
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1123..1127
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1128..1147
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1148..1155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1156..1174
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1175..1184
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1185..1203
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1204..1222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1223..1242
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1243..1308
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1309..1333
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1334..1851
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 25..316
FT /note="I"
FT REPEAT 427..670
FT /note="II"
FT REPEAT 762..1049
FT /note="III"
FT REPEAT 1086..1347
FT /note="IV"
FT DOMAIN 1353..1388
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 381..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1306..1348
FT /note="Phenylalkylamine binding"
FT /evidence="ECO:0000250"
FT REGION 1513..1572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1588..1653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1685..1764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1823..1851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1601..1651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1696..1726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1730..1764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1366
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 1368
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 1370
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 1372
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 1377
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT SITE 271
FT /note="Calcium ion selectivity and permeability"
FT SITE 621
FT /note="Calcium ion selectivity and permeability"
FT SITE 989
FT /note="Calcium ion selectivity and permeability"
FT SITE 1281
FT /note="Calcium ion selectivity and permeability"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 865
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 121..151
FT /note="FMTQYPQIGPEVDLRTLRAIRVLRPLKLVSG -> AMTIFAEANIDVDLRML
FT RSFRVLRPLKLVSR (in isoform F, isoform D and isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_000952"
FT VAR_SEQ 317..351
FT /note="SNERNRVERRMEFQKCRFRAMFQTAMVSYLDWITQ -> AKEREKVENRQEF
FT LKLRRQQQLERELNGYVEWICK (in isoform F, isoform D and isoform
FT C)"
FT /evidence="ECO:0000305"
FT /id="VSP_000953"
FT VAR_SEQ 1181..1183
FT /note="Missing (in isoform A and isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_012741"
FT VARIANT 284..1851
FT /note="Missing (in cac-J; lethal at an embryonic stage;
FT loss of synaptic transmission)"
FT /evidence="ECO:0000269|PubMed:28742085"
FT VARIANT 989
FT /note="E -> K (in cac-F; lethal at the larval stage 3; loss
FT of synaptic transmission)"
FT /evidence="ECO:0000269|PubMed:28742085"
FT VARIANT 1029
FT /note="F -> I (in cac-S; exhibits defects in the patterning
FT of courtship lovesong and a subtle abnormality in visual
FT physiology)"
FT /evidence="ECO:0000269|PubMed:9649530"
FT MUTAGEN 1196
FT /note="R->Q: Homolog of Q-1664 variant in human. Partially
FT rescues the cac-F and cac-J lethal phenotypes. Does not
FT rescue the loss of synaptic transmission cac-F and cac-J
FT variants. No effect on photoreceptor morphology."
FT /evidence="ECO:0000269|PubMed:28742085"
FT MUTAGEN 1205
FT /note="R->P: Homolog of P-1673 variant in human. Does not
FT rescue cac-F and cac-J lethal phenotypes. Highly increases
FT amplitude on the synaptic transmission. Induces severe
FT neurodegeneration in both photoreceptor cell bodies and
FT terminals."
FT /evidence="ECO:0000269|PubMed:28742085"
FT CONFLICT 514
FT /note="S -> G (in Ref. 1; AAC47406)"
FT /evidence="ECO:0000305"
FT CONFLICT 815
FT /note="I -> M (in Ref. 1; AAC47406)"
FT /evidence="ECO:0000305"
FT CONFLICT 839
FT /note="N -> S (in Ref. 1; AAC47406)"
FT /evidence="ECO:0000305"
FT CONFLICT 906
FT /note="N -> S (in Ref. 1; AAC47406)"
FT /evidence="ECO:0000305"
FT CONFLICT 937
FT /note="S -> G (in Ref. 1; AAC47406)"
FT /evidence="ECO:0000305"
FT CONFLICT 1016
FT /note="M -> V (in Ref. 1; AAC47406)"
FT /evidence="ECO:0000305"
FT CONFLICT 1185
FT /note="N -> S (in Ref. 1; AAC47406)"
FT /evidence="ECO:0000305"
FT CONFLICT 1269
FT /note="Q -> H (in Ref. 1; AAC47406)"
FT /evidence="ECO:0000305"
FT CONFLICT 1368
FT /note="N -> G (in Ref. 1; AAC47406)"
FT /evidence="ECO:0000305"
FT CONFLICT 1580
FT /note="N -> D (in Ref. 1; AAC47406)"
FT /evidence="ECO:0000305"
FT CONFLICT 1602
FT /note="R -> G (in Ref. 1; AAC47406)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1851 AA; 212471 MW; 4CC958CFBAE05EC2 CRC64;
MGGPKKEENP PGGGPTSLFI LTEDNPIRKY TRFIIEWPPF EYAVLLTIIA NCVVLALEEH
LPGGDKTVLA QKLEKTEAYF LCIFCVEASL KILALGLVLH KHSYLRNIWN IMDFFVVVTG
FMTQYPQIGP EVDLRTLRAI RVLRPLKLVS GIPSLQVVLK SIIKAMAPLL QIGLLVLFAI
VIFAIIGLEF YSGALHKTCY SLEDPNKLVK EGESETPCNT DNILEKATGS FVCNNTTSMC
LEKWEGPNSG ITSFDNIGFA MLTVFQCITM EGWTAILYWT NDALGSAFNW IYFVPLIVIG
SFFMLNLVLG VLSGEFSNER NRVERRMEFQ KCRFRAMFQT AMVSYLDWIT QAEEVILAEE
RTTEEEKMHI MEARRRNAAK RKKLKSLGKS KSTDTEEEEA EEDYGDDGYL KTRSKPQGSC
TGFWRAEKRF RFWIRHTVKT QWFYWFVIVL VFLNTVCVAV EHYGQPSFLT EFLYYAEFIF
LGLFMSEMFI KMYALGPRIY FESSFNRFDC VVISGSIFEV IWSEVKGGSF GLSVLRALRL
LRIFKVTKYW SSLRNLVISL LNSMRSIISL LFLLFLFILI FALLGMQLFG GQFNLPGGTP
ETNFNTFPIA LLTVFQILTG EDWNEVMYQG IISQGGAQKG MIYSIYFIVL VLFGNYTLLN
VFLAIAVDNL ANAQELTAAE EEQVEEDKEK QLQELEKEME ALQADGVHVE NGDGAVAPSK
SKGKKKEEEK KEEEEVTEGP KPMLPYSSMF ILSPTNPIRR GAHWVVNLPY FDFFIMVVIS
MSSIALAAED PVRENSRRNK ILNYFDYAFT GVFTIEMLLK IVDLGVILHP GSYLREFWNI
MDAVVVICAA VSFGFDMSGS SAGQNLSTIK SLRVLRVLRP LKTIKRVPKL KAVFDCVVNS
LKNVVNILIV YILFQFIFSV IGVQLFNGKF FYCTDESKHT SAECQGSYFK YEEDELLPKQ
ELRVWKPRAF HYDNVAAAML TLFAVQTGEG WPQVLQHSMA ATYEDRGPIQ NFRIEMSIFY
IVYFIVFPFF FVNIFVALII ITFQEQGEAE LQDGEIDKNQ KSCIDFTIGA RPLERYMPKN
RNTFKYKVWR IVVSTPFEYF IMMLIVFNTL LLMMKYHNQG DMYEKSLKYI NMGFTGMFSV
ETVLKIIGFG VKNFFKDPWN IFDLITVLGS IVDALWMEFG HDDSNSINVG FLRLFRAARL
IKLLRQGYTI RILLWTFVQS FKALPYVCLL IAMLFFIYAI IGMQVFGNIK LGTVENSITR
HNNFQSFIQG VMLLFRCATG EAWPNIMLAC LKGKACDDDA EKAPGEYCGS TLAYAYFVSF
IFFCSFLMLN LFVAVIMDNF DYLTRDSSIL GAHHLDEFVR IWAEYDPNAT GKIHYTEMYD
MLKNMDPPLG FGNKCPNRLA YKKLIRMNMP LDDELRVQFT TTLFALIREN LSIKMRAPEE
MDQADMELRE TITNIWPLQA KKMLNLLVPP SDQLNKGKLS VGKIYAGFLI LESWRSTRFG
QLDSGMPMLE LQDASRHPSQ ESLTGADAGH LHPGHSYMNG HRRSPSLRHN GSPLARSPSP
RRRGHQYIHH DIGFSDTVSN VVEMVKETRH PRHGNSHPRY PRGSWSASTS PARSPSPSRY
GGHLSRSKRT QLPYPTYGTT SLCQRSRSPS PARLQEMRER DRLGYGIDMG VTHVQHSYPT
LASRRAGIGR RLPPTPSKPS TLQLKPTNIN FPKLNASPTH THHSTPHSVH SLPHHRDLLR
DPRDMYYSSR ERERDRERLR DRDRDRDRDR LHEYDLRYEY RDRERELYER ERDREREVER
ERLEYIAPLS FEQALAMGRT GRVLPSPVLN GFKPKSGLNP RHSDSDEEDW C
