SCNA_DROME
ID SCNA_DROME Reviewed; 2131 AA.
AC P35500; O15994; P92137; Q0KHR8; Q0KHR9; Q24082; Q24083; Q24084; Q24528;
AC Q24529; Q24530; Q24531; Q24532; Q9VXF7;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 3.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Sodium channel protein para;
DE AltName: Full=Protein paralytic;
DE AltName: Full=Sodium channel 1;
DE Short=DmNav1;
GN Name=para; ORFNames=CG9907;
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 [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Canton-S;
RX PubMed=8182428; DOI=10.1523/jneurosci.14-05-02569.1994;
RA Thackeray J.R., Ganetzky B.;
RT "Developmentally regulated alternative splicing generates a complex array
RT of Drosophila para sodium channel isoforms.";
RL J. Neurosci. 14:2569-2578(1994).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1862, FUNCTION, ALTERNATIVE
RP SPLICING, AND RNA EDITING OF POSITION 1587.
RC STRAIN=Canton-S; TISSUE=Head;
RX PubMed=2550145; DOI=10.1016/0092-8674(89)90512-6;
RA Loughney K., Kreber R., Ganetzky B.;
RT "Molecular analysis of the para locus, a sodium channel gene in
RT Drosophila.";
RL Cell 58:1143-1154(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 51-61.
RA Tanaka Y.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 51-61.
RA Tanaka Y., Yagi Y., Gamo S.;
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1683-1895.
RX PubMed=2538830; DOI=10.1073/pnas.86.6.2079;
RA Ramaswami M., Tanouye M.A.;
RT "Two sodium-channel genes in Drosophila: implications for channel
RT diversity.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:2079-2082(1989).
RN [8]
RP ALTERNATIVE SPLICING, AND DEVELOPMENTAL STAGE.
RX PubMed=8536968; DOI=10.1093/genetics/141.1.203;
RA Thackeray J.R., Ganetzky B.;
RT "Conserved alternative splicing patterns and splicing signals in the
RT Drosophila sodium channel gene para.";
RL Genetics 141:203-214(1995).
RN [9]
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 [10]
RP RNA EDITING OF POSITIONS 471; 1455 AND 1587.
RX PubMed=10880477; DOI=10.1093/genetics/155.3.1149;
RA Hanrahan C.J., Palladino M.J., Ganetzky B., Reenan R.A.;
RT "RNA editing of the Drosophila para Na(+) channel transcript. Evolutionary
RT conservation and developmental regulation.";
RL Genetics 155:1149-1160(2000).
CC -!- FUNCTION: Mediates the voltage-dependent sodium ion permeability of
CC excitable membranes. Assuming opened or closed conformations in
CC response to the voltage difference across the membrane, the protein
CC forms a sodium-selective channel through which Na(+) ions may pass in
CC accordance with their electrochemical gradient.
CC {ECO:0000305|PubMed:2550145}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:2550145};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Comment=Further isoforms have been identified but not yet sequenced.
CC These have different combinations of the optional exons A, B, C, D, E
CC and F. Isoforms always have either exon C or D as these encode
CC segment S4. Sequence identity to para from D.virilis suggests there
CC may also be optional exons H and I.;
CC Name=A;
CC IsoId=P35500-1; Sequence=Displayed;
CC Name=B;
CC IsoId=P35500-8; Sequence=VSP_026200;
CC Name=C;
CC IsoId=P35500-4; Sequence=VSP_001037;
CC Name=D;
CC IsoId=P35500-2; Sequence=VSP_001035;
CC Name=E;
CC IsoId=P35500-5; Sequence=VSP_001038;
CC Name=F24;
CC IsoId=P35500-6; Sequence=VSP_001039;
CC Name=F30;
CC IsoId=P35500-7; Sequence=VSP_001040;
CC Name=exonb;
CC IsoId=P35500-3; Sequence=VSP_001036;
CC Name=exond;
CC IsoId=P35500-9; Sequence=VSP_026199;
CC -!- DEVELOPMENTAL STAGE: Isoform exonb and isoform D are seen in embryos
CC and adults. Isoform A, isoform F24 and isoform F30 are predominant in
CC embryos and isoform C and isoform E predominant in adults.
CC {ECO:0000269|PubMed:8536968}.
CC -!- DOMAIN: The sequence contains 4 internal repeats, each with 5
CC hydrophobic segments (S1, S2, S3, S5, S6) and one positively charged
CC segment (S4). Segments S4 are probably the voltage-sensors and are
CC characterized by a series of positively charged amino acids at every
CC third position. {ECO:0000305}.
CC -!- RNA EDITING: Modified_positions=471 {ECO:0000269|PubMed:10880477,
CC ECO:0000269|PubMed:10966106}, 1455 {ECO:0000269|PubMed:10880477,
CC ECO:0000269|PubMed:10966106}, 1587 {ECO:0000269|PubMed:10880477,
CC ECO:0000269|PubMed:10966106, ECO:0000269|PubMed:2550145};
CC Note=Partially edited. Further sites are edited by Adar. Positions 1455
CC and 1587 show minimal editing from embryos through to third larval
CC instar, then a 40-fold increase at pupation. Position 471 has slightly
CC higher levels during early development with only a four-fold increase
CC at pupation.;
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family. Para
CC subfamily. {ECO:0000305}.
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DR EMBL; U26713; AAA98541.1; -; Genomic_DNA.
DR EMBL; U26714; AAA98542.1; -; Genomic_DNA.
DR EMBL; U26715; AAA98543.1; -; Genomic_DNA.
DR EMBL; U26716; AAA98544.1; -; Genomic_DNA.
DR EMBL; U26716; AAA98545.1; -; Genomic_DNA.
DR EMBL; U26716; AAA98546.1; -; Genomic_DNA.
DR EMBL; U26716; AAA98547.1; -; Genomic_DNA.
DR EMBL; U26716; AAA98548.1; -; Genomic_DNA.
DR EMBL; U26717; AAA98549.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF48617.2; -; Genomic_DNA.
DR EMBL; AE014298; ABI30985.1; -; Genomic_DNA.
DR EMBL; AE014298; ABI30986.1; -; Genomic_DNA.
DR EMBL; M32078; AAB59190.1; -; Genomic_DNA.
DR EMBL; M32078; AAB59191.1; -; Genomic_DNA.
DR EMBL; M32078; AAB59192.1; -; Genomic_DNA.
DR EMBL; M32078; AAB59193.1; -; Genomic_DNA.
DR EMBL; M32078; AAB59194.1; -; Genomic_DNA.
DR EMBL; M32078; AAB59195.1; -; Genomic_DNA.
DR EMBL; AB008113; BAA22890.1; -; Genomic_DNA.
DR EMBL; AB035812; BAA88526.1; -; Genomic_DNA.
DR PIR; A30302; A30302.
DR PIR; A33299; A33299.
DR RefSeq; NP_001036280.1; NM_001042815.2. [P35500-8]
DR RefSeq; NP_001036281.1; NM_001042816.2. [P35500-4]
DR RefSeq; NP_001285332.1; NM_001298403.1. [P35500-1]
DR RefSeq; NP_523371.2; NM_078647.4. [P35500-1]
DR AlphaFoldDB; P35500; -.
DR SMR; P35500; -.
DR BioGRID; 58957; 35.
DR IntAct; P35500; 1.
DR STRING; 7227.FBpp0292707; -.
DR GlyGen; P35500; 6 sites.
DR PaxDb; P35500; -.
DR EnsemblMetazoa; FBtr0074298; FBpp0074073; FBgn0285944. [P35500-1]
DR EnsemblMetazoa; FBtr0111022; FBpp0110321; FBgn0285944. [P35500-8]
DR EnsemblMetazoa; FBtr0111023; FBpp0110322; FBgn0285944. [P35500-4]
DR EnsemblMetazoa; FBtr0303671; FBpp0292688; FBgn0285944. [P35500-5]
DR EnsemblMetazoa; FBtr0342746; FBpp0309614; FBgn0285944. [P35500-1]
DR GeneID; 32619; -.
DR KEGG; dme:Dmel_CG9907; -.
DR UCSC; CG9907-RA; d. melanogaster. [P35500-1]
DR CTD; 32619; -.
DR FlyBase; FBgn0285944; para.
DR VEuPathDB; VectorBase:FBgn0285944; -.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00940000167131; -.
DR InParanoid; P35500; -.
DR PhylomeDB; P35500; -.
DR BioGRID-ORCS; 32619; 0 hits in 3 CRISPR screens.
DR ChiTaRS; para; fly.
DR GenomeRNAi; 32619; -.
DR PRO; PR:P35500; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0285944; Expressed in brain and 11 other tissues.
DR ExpressionAtlas; P35500; baseline and differential.
DR Genevisible; P35500; DM.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005272; F:sodium channel activity; IMP:FlyBase.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IDA:FlyBase.
DR GO; GO:0045433; P:male courtship behavior, veined wing generated song production; IMP:FlyBase.
DR GO; GO:0007638; P:mechanosensory behavior; IMP:FlyBase.
DR GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0060078; P:regulation of postsynaptic membrane potential; IMP:FlyBase.
DR GO; GO:0001666; P:response to hypoxia; IDA:FlyBase.
DR GO; GO:0009612; P:response to mechanical stimulus; IMP:FlyBase.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IDA:FlyBase.
DR CDD; cd13433; Na_channel_gate; 1.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR001696; Na_channel_asu.
DR InterPro; IPR044564; Na_chnl_inactivation_gate.
DR InterPro; IPR010526; Na_trans_assoc.
DR InterPro; IPR024583; Na_trans_cytopl.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037; PTHR10037; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR Pfam; PF06512; Na_trans_assoc; 1.
DR Pfam; PF11933; Na_trans_cytopl; 1.
DR PRINTS; PR00170; NACHANNEL.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; RNA editing; Sodium; Sodium channel; Sodium transport;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..2131
FT /note="Sodium channel protein para"
FT /id="PRO_0000048515"
FT TOPO_DOM 1..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 149..172
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..180
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 181..199
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 213..231
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..237
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 238..257
FT /note="Helical; Voltage-sensor; Name=S4 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 274..297
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..373
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 374..398
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 399..405
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 406..427
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..812
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 813..837
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 838..848
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 849..873
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 874..880
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 881..900
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 901..906
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 907..926
FT /note="Helical; Voltage-sensor; Name=S4 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 927..941
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 942..963
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 964..985
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 986..1006
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1007..1013
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1014..1041
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1042..1296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1297..1320
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1321..1334
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1335..1359
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1360..1365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1366..1387
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1388..1391
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1392..1413
FT /note="Helical; Voltage-sensor; Name=S4 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1414..1432
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1433..1454
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1455..1495
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1496..1517
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1518..1533
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1534..1560
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1561..1614
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1615..1638
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1639..1649
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1650..1673
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1674..1679
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1680..1703
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1704..1713
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1714..1735
FT /note="Helical; Voltage-sensor; Name=S4 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1736..1750
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1751..1773
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1774..1787
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1788..1810
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1811..1835
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1836..1860
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1861..2131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 134..467
FT /note="I"
FT /evidence="ECO:0000305"
FT REPEAT 799..1069
FT /note="II"
FT /evidence="ECO:0000305"
FT REPEAT 1284..1591
FT /note="III"
FT /evidence="ECO:0000305"
FT REPEAT 1601..1862
FT /note="IV"
FT /evidence="ECO:0000305"
FT DOMAIN 1877..1912
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 35..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1166..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2001..2096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1181..1195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1240
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2001..2024
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 553
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 570
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 982
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 301..350
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT DISULFID 1008..1016
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT VAR_SEQ 555..575
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_001035"
FT VAR_SEQ 763..770
FT /note="Missing (in isoform exonb)"
FT /evidence="ECO:0000305"
FT /id="VSP_001036"
FT VAR_SEQ 914..967
FT /note="Missing (in isoform exond)"
FT /evidence="ECO:0000305"
FT /id="VSP_026199"
FT VAR_SEQ 937..967
FT /note="MGALGNLTFVLCIIIFIFAVMGMQLFGKNYH -> VGALGNLTFVLCIIIFI
FT FAVMGMQLFGKNYT (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_001037"
FT VAR_SEQ 1100..1112
FT /note="Missing (in isoform E)"
FT /evidence="ECO:0000305"
FT /id="VSP_001038"
FT VAR_SEQ 1113..1122
FT /note="Missing (in isoform F24)"
FT /evidence="ECO:0000305"
FT /id="VSP_001039"
FT VAR_SEQ 1115..1122
FT /note="Missing (in isoform F30)"
FT /evidence="ECO:0000305"
FT /id="VSP_001040"
FT VAR_SEQ 1377..1417
FT /note="VSLINFVASLVGAGGIQAFKTMRTLRALRPLRAMSRMQGMR -> LSLINLA
FT AVWSGADDVPAFRSMRTLRALRPLRAVSRWEGMK (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_026200"
FT VARIANT 471
FT /note="Q -> R (in RNA edited version)"
FT VARIANT 1455
FT /note="K -> R (in RNA edited version)"
FT VARIANT 1587
FT /note="N -> S (in RNA edited version)"
FT CONFLICT 52
FT /note="Q -> R (in Ref. 4; AAB59190/AAB59191/AAB59193/
FT AAB59194/AAB59195)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="Q -> E (in Ref. 4; AAB59190/AAB59191/AAB59193/
FT AAB59194/AAB59195)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="K -> E (in Ref. 1; AAA98542)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="K -> R (in Ref. 1; AAA98542 and 4; AAB59190/
FT AAB59191/AAB59193/AAB59194/AAB59195)"
FT /evidence="ECO:0000305"
FT CONFLICT 452..454
FT /note="EAE -> VSR (in Ref. 1; AAA98542)"
FT /evidence="ECO:0000305"
FT CONFLICT 1110..1111
FT /note="SE -> TK (in Ref. 1; AAA98543)"
FT /evidence="ECO:0000305"
FT CONFLICT 1296
FT /note="Q -> R (in Ref. 4; AAB59190/AAB59191/AAB59193/
FT AAB59194/AAB59195)"
FT /evidence="ECO:0000305"
FT CONFLICT 1300
FT /note="N -> D (in Ref. 4; AAB59190/AAB59191/AAB59193/
FT AAB59194/AAB59195)"
FT /evidence="ECO:0000305"
FT CONFLICT 1363
FT /note="F -> L (in Ref. 4; AAB59190/AAB59191/AAB59193/
FT AAB59194/AAB59195)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2131 AA; 239362 MW; D0B8AF6463EF4551 CRC64;
MTEDSDSISE EERSLFRPFT RESLVQIEQR IAAEHEKQKE LERKRAEGEV PQYGRKKKQK
EIRYDDEDED EGPQPDPTLE QGVPIPVRLQ GSFPPELAST PLEDIDPYYS NVLTFVVVSK
GKDIFRFSAS KAMWMLDPFN PIRRVAIYIL VHPLFSLFII TTILVNCILM IMPTTPTVES
TEVIFTGIYT FESAVKVMAR GFILCPFTYL RDAWNWLDFV VIALAYVTMG IDLGNLAALR
TFRVLRALKT VAIVPGLKTI VGAVIESVKN LRDVIILTMF SLSVFALMGL QIYMGVLTQK
CIKKFPLDGS WGNLTDENWD YHNRNSSNWY SEDEGISFPL CGNISGAGQC DDDYVCLQGF
GPNPNYGYTS FDSFGWAFLS AFRLMTQDFW EDLYQLVLRA AGPWHMLFFI VIIFLGSFYL
VNLILAIVAM SYDELQKKAE EEEAAEEEAI REAEEAAAAK AAKLEERANA QAQAAADAAA
AEEAALHPEM AKSPTYSCIS YELFVGGEKG NDDNNKEKMS IRSVEVESES VSVIQRQPAP
TTAHQATKVR KVSTTSLSLP GSPFNIRRGS RSSHKYTIRN GRGRFGIPGS DRKPLVLSTY
QDAQQHLPYA DDSNAVTPMS EENGAIIVPV YYGNLGSRHS SYTSHQSRIS YTSHGDLLGG
MAVMGVSTMT KESKLRNRNT RNQSVGATNG GTTCLDTNHK LDHRDYEIGL ECTDEAGKIK
HHDNPFIEPV QTQTVVDMKD VMVLNDIIEQ AAGRHSRASD RGVSVYYFPT EDDDEDGPTF
KDKALEVILK GIDVFCVWDC CWVWLKFQEW VSLIVFDPFV ELFITLCIVV NTMFMAMDHH
DMNKEMERVL KSGNYFFTAT FAIEATMKLM AMSPKYYFQE GWNIFDFIIV ALSLLELGLE
GVQGLSVLRS FRLLRVFKLA KSWPTLNLLI SIMGRTMGAL GNLTFVLCII IFIFAVMGMQ
LFGKNYHDHK DRFPDGDLPR WNFTDFMHSF MIVFRVLCGE WIESMWDCMY VGDVSCIPFF
LATVVIGNLV VLNLFLALLL SNFGSSSLSA PTADNDTNKI AEAFNRIGRF KSWVKRNIAD
CFKLIRNKLT NQISDQPSGE RTNQISWIWS EGKGVCRCIS AEHGDNELEL GHDEILADGL
IKKGIKEQTQ LEVAIGDGME FTIHGDMKNN KPKKSKYLNN ATDDDTASIN SYGSHKNRPF
KDESHKGSAE TMEGEEKRDA SKEDLGLDEE LDEEGECEEG PLDGDIIIHA HDEDILDEYP
ADCCPDSYYK KFPILAGDDD SPFWQGWGNL RLKTFQLIEN KYFETAVITM ILMSSLALAL
EDVHLPQRPI LQDILYYMDR IFTVIFFLEM LIKWLALGFK VYFTNAWCWL DFVIVMVSLI
NFVASLVGAG GIQAFKTMRT LRALRPLRAM SRMQGMRVVV NALVQAIPSI FNVLLVCLIF
WLIFAIMGVQ LFAGKYFKCE DMNGTKLSHE IIPNRNACES ENYTWVNSAM NFDHVGNAYL
CLFQVATFKG WIQIMNDAID SREVDKQPIR ETNIYMYLYF VFFIIFGSFF TLNLFIGVII
DNFNEQKKKA GGSLEMFMTE DQKKYYNAMK KMGSKKPLKA IPRPRWRPQA IVFEIVTDKK
FDIIIMLFIG LNMFTMTLDR YDASDTYNAV LDYLNAIFVV IFSSECLLKI FALRYHYFIE
PWNLFDVVVV ILSILGLVLS DIIEKYFVSP TLLRVVRVAK VGRVLRLVKG AKGIRTLLFA
LAMSLPALFN ICLLLFLVMF IFAIFGMSFF MHVKEKSGIN DVYNFKTFGQ SMILLFQMST
SAGWDGVLDA IINEEACDPP DNDKGYPGNC GSATVGITFL LSYLVISFLI VINMYIAVIL
ENYSQATEDV QEGLTDDDYD MYYEIWQQFD PEGTQYIRYD QLSEFLDVLE PPLQIHKPNK
YKIISMDIPI CRGDLMYCVD ILDALTKDFF ARKGNPIEET GEIGEIAARP DTEGYEPVSS
TLWRQREEYC ARLIQHAWRK HKARGEGGGS FEPDTDHGDG GDPDAGDPAP DEATDGDAPA
GGDGSVNGTA EGAADADESN VNSPGEDAAA AAAAAAAAAA AGTTTAGSPG AGSAGRQTAV
LVESDGFVTK NGHKVVIHSR SPSITSRTAD V
