LinkDB: Q177V1_AEDAE Q177V4_AEDAE Q177V2_AEDAE Q177V3_AEDAE
Original site: Q177V1_AEDAE Q177V4_AEDAE Q177V2_AEDAE Q177V3_AEDAE
ID Q177V1_AEDAE Unreviewed; 1827 AA.
AC Q177V1;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
GN ORFNames=AAEL006019 {ECO:0000313|EMBL:EAT42416.1};
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159 {ECO:0000313|EMBL:EAT42416.1, ECO:0000313|Proteomes:UP000682892};
RN [1] {ECO:0000313|EMBL:EAT42416.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT42416.1};
RA Loftus B.J., Nene V.M., Hannick L.I., Bidwell S., Haas B., Amedeo P.,
RA Orvis J., Wortman J.R., White O.R., Salzberg S., Shumway M., Koo H.,
RA Zhao Y., Holmes M., Miller J., Schatz M., Pop M., Pai G., Utterback T.,
RA Rogers Y.-H., Kravitz S., Fraser C.M.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EAT42416.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT42416.1};
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
RN [3] {ECO:0000313|EMBL:EAT42416.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT42416.1};
RG VectorBase;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|RuleBase:RU361132}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|RuleBase:RU361132}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361132}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC {ECO:0000256|RuleBase:RU361132}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361132}.
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DR EMBL; CH477371; EAT42416.1; -; Genomic_DNA.
DR RefSeq; XP_001657360.1; XM_001657310.1.
DR SMR; Q177V1; -.
DR PaxDb; 7159-AAEL006019-PD; -.
DR VEuPathDB; VectorBase:AAEL023266; -.
DR HOGENOM; CLU_000540_5_0_1; -.
DR Proteomes; UP000682892; Unassembled WGS sequence.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IEA:InterPro.
DR CDD; cd13433; Na_channel_gate; 1.
DR Gene3D; 1.10.287.70; -; 4.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 3.
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_dom.
DR InterPro; IPR024583; Na_trans_cytopl.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037:SF288; SODIUM CHANNEL PROTEIN; 1.
DR PANTHER; PTHR10037; VOLTAGE-GATED CATION CHANNEL CALCIUM AND SODIUM; 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 SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|RuleBase:RU361132};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU361132};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361132};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sodium {ECO:0000256|ARBA:ARBA00023053, ECO:0000256|RuleBase:RU361132};
KW Sodium channel {ECO:0000256|ARBA:ARBA00022461,
KW ECO:0000256|RuleBase:RU361132};
KW Sodium transport {ECO:0000256|ARBA:ARBA00023201,
KW ECO:0000256|RuleBase:RU361132};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361132};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361132};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361132};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW ECO:0000256|RuleBase:RU361132}.
FT TRANSMEM 46..69
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 177..199
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 532..555
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 576..593
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 605..629
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 660..682
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 740..761
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1040..1062
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1068..1094
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1115..1146
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1233..1259
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1322..1340
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1352..1371
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1383..1402
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1446..1469
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1539..1559
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 1576..1611
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 286..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1699..1795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 203..238
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 352..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..924
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1749..1764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1780..1794
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1827 AA; 204977 MW; F2EC6CC99126F1FD CRC64;
MGIDLGNLAA LRTFRVLRAL KTVAIVPGLK TIVGAVIESV KNLRDVIILT MFSLSVFALM
GLQIYMGVLT QKCIREFPMD GSWGNLSDEN WERFNNNDSN WYFSETGDTP LCGNSSGAGQ
CEEGYICLQG YGDNPNYGYT SFDTFGWAFL SAFRLMTQDY WENLYQLVLR SAGPWHMLFF
IVIIFLGSFY LVNLILAIVA MSYDELQKKA EEEEAAEEEA LREAEEAAAA KAAKLEAQAA
AAAAAANPEI AKSPSDFSCH SYELFVNQEK GNDDNNKEKM SIRSEGLESA SLSLPGSPFN
LRRGSRGSHQ FTIRNGRGRF VGVPGSDRKP LVLSTYLDAQ EHLPYADDSN AVTPMSEENG
SRHSSYTSHQ SRISYTSHGD LLGGMTKESR LRNRSARNTN HSIVPPPNMS GPNMSYVDSN
HKGQRDFDMS QDCTDEAGKI KHNDNPFIEP SQTQTVVDMK DVMVLNDIIE QAAGRHSRAS
DHGVSVYYFP TEDDDEDGPT FKDKALEFTM RMIDVFCVWD CCWVWLKFQE WVAFIVFDPF
VELFITLCIV VNTLFMALDH HDMDPDMERA LKSGNYFFTA TFAIEATMKL IAMSPKYYFQ
EGWNIFDFII VALSLLELGL EGVQGLSVLR SFRLLRVFKL AKSWPTLNLL ISIMGRTMGA
LGNLTFVLCI IIFIFAVMGM QLFGKNYIDN VDRFPDKDLP RWNFTDFMHS FMIVFRVLCG
EWIESMWDCM LVGDVSCIPF FLATVVIGNL VVLNLFLALL LSNFGSSSLS APTADNETNK
IAEAFNRISR FSNWIKSNIA NALKFVKNKL TSQIASVQPA EHGENELELT PDDILADGLL
KKGVKEHNQL EVAIGDGMEF TIHGDLKNKG KKNKQLMNNS KDDDTASIKS YGSHKNRPFK
DESHKGSAET MEGEEKRDVS KEDLGIDEEL DDECDGEEGP LDGELIIHAD EDEVIEDSPA
DCCPDNCYKK FPVLAGDDDA PFWQGWANLR LKTFQLIENK YFETAVITMI LLSSLALALE
DVHLPHRPIL QDVLYYMDRI FTVIFFLEML IKWLALGFRV YFTNAWCWLD FIIVMVSLIN
FVASLCGAGG IQAFKTMRTL RALRPLRAMS RMQGMRVVVN ALVQAIPSIF NVLLVCLIFW
LIFAIMGVQL FAGKYFKCVD KNKTTLSHEI IPDVNACVAE NYTWENSPMN FDHVGKAYLC
LFQVATFKGW IQIMNDAIDS REVGKQPIRE TNIYMYLYFV FFIIFGSFFT LNLFIGVIID
NFNEQKKKAG GSLEMFMTED QKKYYNAMKK MGSKKPLKAI PRPRWRPQAI VFEIVTNKKF
DMIIMLFIGF NMLTMTLDHY KQTDTFSAVL DYLNMIFICI FSSECLMKIF ALRYHYFIEP
WNLFDFVVVI LSILGLVLSD LIEKYFVSPT LLRVVRVAKV GRVLRLVKGA KGIRTLLFAL
AMSLPALFNI CLLLFLVMFI FAIFGMSFFM HVKDKSGLDD VYNFKTFGQS MILLFQMSTS
AGWDGVLDGI INEDECLPPD NDKGYPGNCG SATIGITYLL AYLVISFLIV INMYIAVILE
NYSQATEDVQ EGLTDDDYDM YYEIWQQFDP DGTQYIRYDQ LSDFLDVLEP PLQIHKPNKY
KIISMDIPIC RGDMMFCVDI LDALTKDFFA RKGNPIEETA ELGEVQARPD EVGYEPVSST
LWRQREEYCA RVIQHAWRKH KERQAGGGGG DDTDADACDN DDGDDGGGGA GDGGSAGGGG
VTSPGVGSGS IVGGGTTPGS GGGGSQANLG IVVEHNLSPK ESPDGNNDPQ GRQTAVLVES
DGFVTKNGHR VVIHSRSPSI TSRSADV
//
ID Q177V4_AEDAE Unreviewed; 1851 AA.
AC Q177V4;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
GN ORFNames=AAEL006019 {ECO:0000313|EMBL:EAT42415.1};
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159 {ECO:0000313|EMBL:EAT42415.1, ECO:0000313|Proteomes:UP000682892};
RN [1] {ECO:0000313|EMBL:EAT42415.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT42415.1};
RA Loftus B.J., Nene V.M., Hannick L.I., Bidwell S., Haas B., Amedeo P.,
RA Orvis J., Wortman J.R., White O.R., Salzberg S., Shumway M., Koo H.,
RA Zhao Y., Holmes M., Miller J., Schatz M., Pop M., Pai G., Utterback T.,
RA Rogers Y.-H., Kravitz S., Fraser C.M.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EAT42415.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT42415.1};
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
RN [3] {ECO:0000313|EMBL:EAT42415.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT42415.1};
RG VectorBase;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|RuleBase:RU361132}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|RuleBase:RU361132}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361132}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC {ECO:0000256|RuleBase:RU361132}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361132}.
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DR EMBL; CH477371; EAT42415.1; -; Genomic_DNA.
DR RefSeq; XP_001657359.1; XM_001657309.1.
DR SMR; Q177V4; -.
DR VEuPathDB; VectorBase:AAEL023266; -.
DR Proteomes; UP000682892; Unassembled WGS sequence.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IEA:InterPro.
DR CDD; cd13433; Na_channel_gate; 1.
DR Gene3D; 1.10.287.70; -; 4.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 3.
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_dom.
DR InterPro; IPR024583; Na_trans_cytopl.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037:SF288; SODIUM CHANNEL PROTEIN; 1.
DR PANTHER; PTHR10037; VOLTAGE-GATED CATION CHANNEL CALCIUM AND SODIUM; 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 SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|RuleBase:RU361132};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU361132};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361132};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sodium {ECO:0000256|ARBA:ARBA00023053, ECO:0000256|RuleBase:RU361132};
KW Sodium channel {ECO:0000256|ARBA:ARBA00022461,
KW ECO:0000256|RuleBase:RU361132};
KW Sodium transport {ECO:0000256|ARBA:ARBA00023201,
KW ECO:0000256|RuleBase:RU361132};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361132};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361132};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361132};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW ECO:0000256|RuleBase:RU361132}.
FT TRANSMEM 46..69
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 177..199
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 556..579
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 600..617
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 629..653
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 684..706
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 764..785
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1064..1086
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1092..1118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1139..1170
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1257..1283
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1346..1364
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1376..1395
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1407..1426
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1470..1493
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1563..1583
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 1600..1635
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 377..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1723..1819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 203..238
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 384..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..948
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1773..1788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1804..1818
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1851 AA; 207163 MW; EC868187263CA40B CRC64;
MGIDLGNLAA LRTFRVLRAL KTVAIVPGLK TIVGAVIESV KNLRDVIILT MFSLSVFALM
GLQIYMGVLT QKCIREFPMD GSWGNLSDEN WERFNNNDSN WYFSETGDTP LCGNSSGAGQ
CEEGYICLQG YGDNPNYGYT SFDTFGWAFL SAFRLMTQDY WENLYQLVLR SAGPWHMLFF
IVIIFLGSFY LVNLILAIVA MSYDELQKKA EEEEAAEEEA LREAEEAAAA KAAKLEAQAA
AAAAAANPEI AKSPSDFSCH SYELFVNQEK GNDDNNKEKM SIRSEGLESV SEITRTTAPT
ATAAGTAKAR KVSAGVAAFQ KASLSLPGSP FNLRRGSRGS HQFTIRNGRG RFVGVPGSDR
KPLVLSTYLD AQEHLPYADD SNAVTPMSEE NGSRHSSYTS HQSRISYTSH GDLLGGMTKE
SRLRNRSARN TNHSIVPPPN MSGPNMSYVD SNHKGQRDFD MSQDCTDEAG KIKHNDNPFI
EPSQTQTVVD MKDVMVLNDI IEQAAGRHSR ASDHGEDDDE DGPTFKDKAL EFTMRMIDVF
CVWDCCWVWL KFQEWVAFIV FDPFVELFIT LCIVVNTLFM ALDHHDMDPD MERALKSGNY
FFTATFAIEA TMKLIAMSPK YYFQEGWNIF DFIIVALSLL ELGLEGVQGL SVLRSFRLLR
VFKLAKSWPT LNLLISIMGR TMGALGNLTF VLCIIIFIFA VMGMQLFGKN YIDNVDRFPD
KDLPRWNFTD FMHSFMIVFR VLCGEWIESM WDCMLVGDVS CIPFFLATVV IGNLVVLNLF
LALLLSNFGS SSLSAPTADN ETNKIAEAFN RISRFSNWIK SNIANALKFV KNKLTSQIAS
VQPAEHGENE LELTPDDILA DGLLKKGVKE HNQLEVAIGD GMEFTIHGDL KNKGKKNKQL
MNNSKDDDTA SIKSYGSHKN RPFKDESHKG SAETMEGEEK RDVSKEDLGI DEELDDECDG
EEGPLDGELI IHADEDEVIE DSPADCCPDN CYKKFPVLAG DDDAPFWQGW ANLRLKTFQL
IENKYFETAV ITMILLSSLA LALEDVHLPH RPILQDVLYY MDRIFTVIFF LEMLIKWLAL
GFRVYFTNAW CWLDFIIVMV SLINFVASLC GAGGIQAFKT MRTLRALRPL RAMSRMQGMR
VVVNALVQAI PSIFNVLLVC LIFWLIFAIM GVQLFAGKYF KCVDKNKTTL SHEIIPDVNA
CVAENYTWEN SPMNFDHVGK AYLCLFQVAT FKGWIQIMND AIDSREVGKQ PIRETNIYMY
LYFVFFIIFG SFFTLNLFIG VIIDNFNEQK KKAGGSLEMF MTEDQKKYYN AMKKMGSKKP
LKAIPRPRWR PQAIVFEIVT NKKFDMIIML FIGFNMLTMT LDHYKQTDTF SAVLDYLNMI
FICIFSSECL MKIFALRYHY FIEPWNLFDF VVVILSILGL VLSDLIEKYF VSPTLLRVVR
VAKVGRVLRL VKGAKGIRTL LFALAMSLPA LFNICLLLFL VMFIFAIFGM SFFMHVKDKS
GLDDVYNFKT FGQSMILLFQ MSTSAGWDGV LDGIINEDEC LPPDNDKGYP GNCGSATIGI
TYLLAYLVIS FLIVINMYIA VILENYSQAT EDVQEGLTDD DYDMYYEIWQ QFDPDGTQYI
RYDQLSDFLD VLEPPLQIHK PNKYKIISMD IPICRGDMMF CVDILDALTK DFFARKGNPI
EETAELGEVQ ARPDEVGYEP VSSTLWRQRE EYCARVIQHA WRKHKERQAG GGGGDDTDAD
ACDNDDGDDG GGGAGDGGSA GGGGVTSPGV GSGSIVGGGT TPGSGGGGSQ ANLGIVVEHN
LSPKESPDGN NDPQGRQTAV LVESDGFVTK NGHRVVIHSR SPSITSRSAD V
//
ID Q177V2_AEDAE Unreviewed; 1835 AA.
AC Q177V2;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
GN ORFNames=AAEL006019 {ECO:0000313|EMBL:EAT42417.1};
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159 {ECO:0000313|EMBL:EAT42417.1, ECO:0000313|Proteomes:UP000682892};
RN [1] {ECO:0000313|EMBL:EAT42417.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT42417.1};
RA Loftus B.J., Nene V.M., Hannick L.I., Bidwell S., Haas B., Amedeo P.,
RA Orvis J., Wortman J.R., White O.R., Salzberg S., Shumway M., Koo H.,
RA Zhao Y., Holmes M., Miller J., Schatz M., Pop M., Pai G., Utterback T.,
RA Rogers Y.-H., Kravitz S., Fraser C.M.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EAT42417.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT42417.1};
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
RN [3] {ECO:0000313|EMBL:EAT42417.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT42417.1};
RG VectorBase;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|RuleBase:RU361132}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|RuleBase:RU361132}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361132}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC {ECO:0000256|RuleBase:RU361132}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361132}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH477371; EAT42417.1; -; Genomic_DNA.
DR RefSeq; XP_001657361.1; XM_001657311.1.
DR SMR; Q177V2; -.
DR VEuPathDB; VectorBase:AAEL023266; -.
DR Proteomes; UP000682892; Unassembled WGS sequence.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IEA:InterPro.
DR CDD; cd13433; Na_channel_gate; 1.
DR Gene3D; 1.10.287.70; -; 4.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 3.
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_dom.
DR InterPro; IPR024583; Na_trans_cytopl.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037:SF288; SODIUM CHANNEL PROTEIN; 1.
DR PANTHER; PTHR10037; VOLTAGE-GATED CATION CHANNEL CALCIUM AND SODIUM; 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 SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|RuleBase:RU361132};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU361132};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361132};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sodium {ECO:0000256|ARBA:ARBA00023053, ECO:0000256|RuleBase:RU361132};
KW Sodium channel {ECO:0000256|ARBA:ARBA00022461,
KW ECO:0000256|RuleBase:RU361132};
KW Sodium transport {ECO:0000256|ARBA:ARBA00023201,
KW ECO:0000256|RuleBase:RU361132};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361132};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361132};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361132};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW ECO:0000256|RuleBase:RU361132}.
FT TRANSMEM 46..69
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 177..199
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 540..563
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 584..601
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 613..637
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 668..690
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 748..769
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1048..1070
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1076..1102
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1123..1154
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1241..1267
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1330..1348
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1360..1379
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1391..1410
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1454..1477
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1547..1567
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 1584..1619
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 877..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1707..1803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 203..238
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 895..932
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1757..1772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1788..1802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1835 AA; 205530 MW; FE6D1B0FCF87C465 CRC64;
MGIDLGNLAA LRTFRVLRAL KTVAIVPGLK TIVGAVIESV KNLRDVIILT MFSLSVFALM
GLQIYMGVLT QKCIREFPMD GSWGNLSDEN WERFNNNDSN WYFSETGDTP LCGNSSGAGQ
CEEGYICLQG YGDNPNYGYT SFDTFGWAFL SAFRLMTQDY WENLYQLVLR SAGPWHMLFF
IVIIFLGSFY LVNLILAIVA MSYDELQKKA EEEEAAEEEA LREAEEAAAA KAAKLEAQAA
AAAAAANPEI AKSPSDFSCH SYELFVNQEK GNDDNNKEKM SIRSEGLESV SEITRTTAPT
ATAAGTAKAR KVSAFTIRNG RGRFVGVPGS DRKPLVLSTY LDAQEHLPYA DDSNAVTPMS
EENGAIIVPV YYANLGSRHS SYTSHQSRIS YTSHGDLLGG MTKESRLRNR SARNTNHSIV
PPPNMSGPNM SYVDSNHKGQ RDFDMSQDCT DEAGKIKHND NPFIEPSQTQ TVVDMKDVMV
LNDIIEQAAG RHSRASDHGE DDDEDGPTFK DKALEFTMRM IDVFCVWDCC WVWLKFQEWV
AFIVFDPFVE LFITLCIVVN TLFMALDHHD MDPDMERALK SGNYFFTATF AIEATMKLIA
MSPKYYFQEG WNIFDFIIVA LSLLELGLEG VQGLSVLRSF RLLRVFKLAK SWPTLNLLIS
IMGRTMGALG NLTFVLCIII FIFAVMGMQL FGKNYIDNVD RFPDKDLPRW NFTDFMHSFM
IVFRVLCGEW IESMWDCMLV GDVSCIPFFL ATVVIGNLVV LNLFLALLLS NFGSSSLSAP
TADNETNKIA EAFNRISRFS NWIKSNIANA LKFVKNKLTS QIASVQPAEH GENELELTPD
DILADGLLKK GVKEHNQLEV AIGDGMEFTI HGDLKNKGKK NKQLMNNSKD DDTASIKSYG
SHKNRPFKDE SHKGSAETME GEEKRDVSKE DLGIDEELDD ECDGEEGPLD GELIIHADED
EVIEDSPADC CPDNCYKKFP VLAGDDDAPF WQGWANLRLK TFQLIENKYF ETAVITMILL
SSLALALEDV HLPHRPILQD VLYYMDRIFT VIFFLEMLIK WLALGFRVYF TNAWCWLDFI
IVMVSLINFV ASLCGAGGIQ AFKTMRTLRA LRPLRAMSRM QGMRVVVNAL VQAIPSIFNV
LLVCLIFWLI FAIMGVQLFA GKYFKCVDKN KTTLSHEIIP DVNACVAENY TWENSPMNFD
HVGKAYLCLF QVATFKGWIQ IMNDAIDSRE VGKQPIRETN IYMYLYFVFF IIFGSFFTLN
LFIGVIIDNF NEQKKKAGGS LEMFMTEDQK KYYNAMKKMG SKKPLKAIPR PRWRPQAIVF
EIVTNKKFDM IIMLFIGFNM LTMTLDHYKQ TDTFSAVLDY LNMIFICIFS SECLMKIFAL
RYHYFIEPWN LFDFVVVILS ILGLVLSDLI EKYFVSPTLL RVVRVAKVGR VLRLVKGAKG
IRTLLFALAM SLPALFNICL LLFLVMFIFA IFGMSFFMHV KDKSGLDDVY NFKTFGQSMI
LLFQMSTSAG WDGVLDGIIN EDECLPPDND KGYPGNCGSA TIGITYLLAY LVISFLIVIN
MYIAVILENY SQATEDVQEG LTDDDYDMYY EIWQQFDPDG TQYIRYDQLS DFLDVLEPPL
QIHKPNKYKI ISMDIPICRG DMMFCVDILD ALTKDFFARK GNPIEETAEL GEVQARPDEV
GYEPVSSTLW RQREEYCARV IQHAWRKHKE RQAGGGGGDD TDADACDNDD GDDGGGGAGD
GGSAGGGGVT SPGVGSGSIV GGGTTPGSGG GGSQANLGIV VEHNLSPKES PDGNNDPQGR
QTAVLVESDG FVTKNGHRVV IHSRSPSITS RSADV
//
ID Q177V3_AEDAE Unreviewed; 1900 AA.
AC Q177V3;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
GN ORFNames=AAEL006019 {ECO:0000313|EMBL:EAT42414.1};
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159 {ECO:0000313|EMBL:EAT42414.1, ECO:0000313|Proteomes:UP000682892};
RN [1] {ECO:0000313|EMBL:EAT42414.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT42414.1};
RA Loftus B.J., Nene V.M., Hannick L.I., Bidwell S., Haas B., Amedeo P.,
RA Orvis J., Wortman J.R., White O.R., Salzberg S., Shumway M., Koo H.,
RA Zhao Y., Holmes M., Miller J., Schatz M., Pop M., Pai G., Utterback T.,
RA Rogers Y.-H., Kravitz S., Fraser C.M.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EAT42414.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT42414.1};
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
RN [3] {ECO:0000313|EMBL:EAT42414.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT42414.1};
RG VectorBase;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|RuleBase:RU361132}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|RuleBase:RU361132}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361132}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC {ECO:0000256|RuleBase:RU361132}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361132}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH477371; EAT42414.1; -; Genomic_DNA.
DR RefSeq; XP_001657358.1; XM_001657308.1.
DR SMR; Q177V3; -.
DR STRING; 7159.Q177V3; -.
DR VEuPathDB; VectorBase:AAEL023266; -.
DR eggNOG; KOG2301; Eukaryota.
DR OMA; YNDSNFY; -.
DR PhylomeDB; Q177V3; -.
DR Proteomes; UP000682892; Unassembled WGS sequence.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IEA:InterPro.
DR CDD; cd13433; Na_channel_gate; 1.
DR Gene3D; 1.10.287.70; -; 4.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 3.
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_dom.
DR InterPro; IPR024583; Na_trans_cytopl.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037:SF288; SODIUM CHANNEL PROTEIN; 1.
DR PANTHER; PTHR10037; VOLTAGE-GATED CATION CHANNEL CALCIUM AND SODIUM; 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 SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|RuleBase:RU361132};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU361132};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361132};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sodium {ECO:0000256|ARBA:ARBA00023053, ECO:0000256|RuleBase:RU361132};
KW Sodium channel {ECO:0000256|ARBA:ARBA00022461,
KW ECO:0000256|RuleBase:RU361132};
KW Sodium transport {ECO:0000256|ARBA:ARBA00023201,
KW ECO:0000256|RuleBase:RU361132};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361132};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361132};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361132};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW ECO:0000256|RuleBase:RU361132}.
FT TRANSMEM 46..69
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 177..199
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 569..592
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 613..630
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 642..666
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 697..719
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 777..798
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1113..1135
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1141..1167
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1188..1219
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1306..1332
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1395..1413
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1425..1444
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1456..1475
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1519..1542
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1612..1632
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 1649..1684
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 956..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1772..1868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 203..238
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 961..997
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1012
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1822..1837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1853..1867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1900 AA; 212563 MW; D1FF8257FB48053E CRC64;
MGIDLGNLAA LRTFRVLRAL KTVAIVPGLK TIVGAVIESV KNLRDVIILT MFSLSVFALM
GLQIYMGVLT QKCIREFPMD GSWGNLSDEN WERFNNNDSN WYFSETGDTP LCGNSSGAGQ
CEEGYICLQG YGDNPNYGYT SFDTFGWAFL SAFRLMTQDY WENLYQLVLR SAGPWHMLFF
IVIIFLGSFY LVNLILAIVA MSYDELQKKA EEEEAAEEEA LREAEEAAAA KAAKLEAQAA
AAAAAANPEI AKSPSDFSCH SYELFVNQEK GNDDNNKEKM SIRSEGLESV SEITRTTAPT
ATAAGTAKAR KVSAASLSLP GSPFNLRRGS RGSHQFTIRN GRGRFVGVPG SDRKPLVLST
YLDAQEHLPY ADDSNAVTPM SEENGAIIVP VYYANLGSRH SSYTSHQSRI SYTSHGDLLG
GMTKESRLRN RSARNTNHSI VPPPNMSGPN MSYVDSNHKG QRDFDMSQDC TDEAGKIKHN
DNPFIEPSQT QTVVDMKDVM VLNDIIEQAA GRHSRASDHG VSVYYFPTED DDEDGPTFKD
KALEFTMRMI DVFCVWDCCW VWLKFQEWVA FIVFDPFVEL FITLCIVVNT LFMALDHHDM
DPDMERALKS GNYFFTATFA IEATMKLIAM SPKYYFQEGW NIFDFIIVAL SLLELGLEGV
QGLSVLRSFR LLRVFKLAKS WPTLNLLISI MGRTMGALGN LTFVLCIIIF IFAVMGMQLF
GKNYIDNVDR FPDKDLPRWN FTDFMHSFMI VFRVLCGEWI ESMWDCMLVG DVSCIPFFLA
TVVIGNLVVL NLFLALLLSN FGSSSLSAPT ADNETNKIAE AFNRISRFSN WIKSNIANAL
KFVKNKLTSQ IASVQPAGKG VCPCISAEHG ENELELTPDD ILADGLLKKG VKEHNQLEVA
IGDGMEFTIH GDLKNKGKKN KQLMNNSKVI GNSISNHQDN KLEHELNHRG MSLQDDDTAS
IKSYGSHKNR PFKDESHKGS AETMEGEEKR DVSKEDLGID EELDDECDGE EGPLDGELII
HADEDEVIED SPADCCPDNC YKKFPVLAGD DDAPFWQGWA NLRLKTFQLI ENKYFETAVI
TMILLSSLAL ALEDVHLPHR PILQDVLYYM DRIFTVIFFL EMLIKWLALG FRVYFTNAWC
WLDFIIVMVS LINFVASLCG AGGIQAFKTM RTLRALRPLR AMSRMQGMRV VVNALVQAIP
SIFNVLLVCL IFWLIFAIMG VQLFAGKYFK CVDKNKTTLS HEIIPDVNAC VAENYTWENS
PMNFDHVGKA YLCLFQVATF KGWIQIMNDA IDSREVGKQP IRETNIYMYL YFVFFIIFGS
FFTLNLFIGV IIDNFNEQKK KAGGSLEMFM TEDQKKYYNA MKKMGSKKPL KAIPRPRWRP
QAIVFEIVTN KKFDMIIMLF IGFNMLTMTL DHYKQTDTFS AVLDYLNMIF ICIFSSECLM
KIFALRYHYF IEPWNLFDFV VVILSILGLV LSDLIEKYFV SPTLLRVVRV AKVGRVLRLV
KGAKGIRTLL FALAMSLPAL FNICLLLFLV MFIFAIFGMS FFMHVKDKSG LDDVYNFKTF
GQSMILLFQM STSAGWDGVL DGIINEDECL PPDNDKGYPG NCGSATIGIT YLLAYLVISF
LIVINMYIAV ILENYSQATE DVQEGLTDDD YDMYYEIWQQ FDPDGTQYIR YDQLSDFLDV
LEPPLQIHKP NKYKIISMDI PICRGDMMFC VDILDALTKD FFARKGNPIE ETAELGEVQA
RPDEVGYEPV SSTLWRQREE YCARVIQHAW RKHKERQAGG GGGDDTDADA CDNDDGDDGG
GGAGDGGSAG GGGVTSPGVG SGSIVGGGTT PGSGGGGSQA NLGIVVEHNL SPKESPDGNN
DPQGRQTAVL VESDGFVTKN GHRVVIHSRS PSITSRSADV
//