ID A7UUW1_ANOGA Unreviewed; 2092 AA.
AC A7UUW1;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
GN Name=1278521 {ECO:0000313|EnsemblMetazoa:AGAP004707-PL};
GN ORFNames=AgaP_AGAP004707 {ECO:0000313|EMBL:EDO63520.1};
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165 {ECO:0000313|EMBL:EDO63520.1};
RN [1] {ECO:0000313|EMBL:EDO63520.1, ECO:0000313|Proteomes:UP000007062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST {ECO:0000313|EMBL:EDO63520.1,
RC ECO:0000313|Proteomes:UP000007062};
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
RN [2] {ECO:0000313|EMBL:EDO63520.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EDO63520.1};
RG The Anopheles Genome Sequencing Consortium;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:EDO63520.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EDO63520.1};
RX PubMed=14747013; DOI=10.1016/j.pt.2003.11.003;
RA Mongin E., Louis C., Holt R.A., Birney E., Collins F.H.;
RT "The Anopheles gambiae genome: an update.";
RL Trends Parasitol. 20:49-52(2004).
RN [4] {ECO:0000313|EMBL:EDO63520.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EDO63520.1};
RX PubMed=17210077; DOI=10.1186/gb-2007-8-1-r5;
RA Sharakhova M.V., Hammond M.P., Lobo N.F., Krzywinski J., Unger M.F.,
RA Hillenmeyer M.E., Bruggner R.V., Birney E., Collins F.H.;
RT "Update of the Anopheles gambiae PEST genome assembly.";
RL Genome Biol. 8:R5.1-R5.13(2007).
RN [5] {ECO:0000313|EMBL:EDO63520.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EDO63520.1};
RG VectorBase;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EnsemblMetazoa:AGAP004707-PL}
RP IDENTIFICATION.
RC STRAIN=PEST {ECO:0000313|EnsemblMetazoa:AGAP004707-PL};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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; AAAB01008968; EDO63520.1; -; Genomic_DNA.
DR RefSeq; XP_001689103.1; XM_001689051.1.
DR EnsemblMetazoa; AGAP004707-RL; AGAP004707-PL; AGAP004707.
DR GeneID; 1278521; -.
DR KEGG; aga:AgaP_AGAP004707; -.
DR VEuPathDB; VectorBase:AGAP004707; -.
DR HOGENOM; CLU_006842_22_0_1; -.
DR OrthoDB; 1110761at2759; -.
DR Proteomes; UP000007062; Chromosome 2L.
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; 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_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 Reference proteome {ECO:0000313|Proteomes:UP000007062};
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 127..154
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 198..220
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 232..250
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 256..278
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 387..409
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 777..800
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 821..838
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 850..874
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 905..927
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 985..1006
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1295..1317
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1323..1349
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1370..1401
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1491..1517
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1580..1598
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1610..1629
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1641..1660
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1704..1727
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1797..1817
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 1834..1869
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 27..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1126..1196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1984..2028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 413..451
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 27..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1195
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1991..2012
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2092 AA; 234689 MW; 2940AE37086CD107 CRC64;
MTEDSDSISE EERSLFRPFT RESLQAIEAR IADEEAKQRE LERKRAEGED EDEGPQPDPT
LEQGVPVPVR MQGSFPPELA STPLEDIDSF YSNQRTFVVI SKGKDIFRFS ATNALYVLDP
FNPIRRVAIY ILVHPLFSLF IITTILVNCI LMIMPTTPTV ESTEVIFTGI YTFESAVKVM
ARGFILQPFT YLRDAWNWLD FVVIALAYVT MGIDLGNLAA LRTFRVLRAL KTVAIVPGLK
TIVGAVIESV KNLRDVIILT MFSLSVFALM GLQIYMGVLT QKCIKEFPLD GSWGNLTDES
WELFNSNDTN WFYSESGDIP LCGNSSGAGQ CDEGYICLQG YGKNPNYGYT SFDTFGWAFL
SAFRLMTQDY WENLYQLVLR SAGPWHMLFF IVIIFLGSFY LVNLILAIVA MSYDELQKKA
EEEEAAEEEA LREAEEAAAA KAAKLEAQQA AAAAAANPEI AKSPSDFSCH SYELFVGQEK
GNDDNNKEKM SIRSEGLESV SEITRTTAPT ATAAGTAKAR KVSAASLSLP GSPFNLRRGS
RGSHQFTIRN GRGRFVGVPG SDRKPLVLST YLDAQEHLPY ADDSNAVTPM SEENGAIIVP
VYYANLGSRH SSYTSHQSRI SYTSHGDLLG GMTKESRLRN RSARNTNHSI VPPPNANNLS
YAETNHKGQR DFDLTQDCTD DAGKIKHNDN PFIEPAQTQT VVDMKDVMVL NDIIEQAAGR
HSRASDHGVS VYYFPTEDDD EDGPTFKDKA LEFLMKMIDI FCVWDCCWVW LKFQEWVAFI
VFDPFVELFI TLCIVVNTLF MALDHHDMDP DMEKALKSGN YFFTATFAIE ATMKLIAMSP
KYYFQEGWNI FDFIIVALSL LELGLEGVQG LSVLRSFRLL RVFKLAKSWP TLNLLISIMG
RTMGALGNLT FVLCIIIFIF AVMGMQLFGK NYVDNVDRFP DHDLPRWNFT DFMHSFMIVF
RVLCGEWIES MWDCMLVGDV SCIPFFLATV VIGNLVVLNL FLALLLSNFG SSSLSAPTAD
NETNKIAEAF NRISRFSNWI KMNLANALKF VKNKLTSQIA SVQPTGKGVC PCISSEHGEN
ELELTPDDIL ADGLLKKGIK EHNQLEVAIG DGMEFTIHGD LKNKAKKNKQ IMNNSKDDDT
ASIKSYGSHK NRPFKDESHK GSAETMEGEE KRDASKEDLG IDEELDDEGE GDEGPLDGEL
IIHAEEDEVI EDSPADCCPD NCYKKFPVLA GDDDAPFWQG WGNLRLKTFQ LIENKYFETA
VITMILLSSL ALALEDVHLP QRPILQDILY YMDRIFTVIF FLEMLIKWLA LGFKVYFTNA
WCWLDFIIVM VSLINFVASL CGAGGIQAFK TMRTLRALRP LRAMSRMQGM RVVVNALVQA
IPSIFNVLLV CLIFWLIFAI MGVQLFAGKY FKCVDKNKTT LPHEIIPDVN ACKAENYSWE
NSPMNFDHVG KAYLCLFQVA TFKGWIQIMN DAIDSRDVSF VGKQPIRETN IYMYLYFVFF
IIFGSFFTLN LFIGVIIDNF NEQKKKAGGS LEMFMTEDQK KYYNAMKKMG SKKPLKAIPR
PRWRPQAIVF EIVTNKKFDM IIMLFIGFNM LTMTLDHYKQ SETFSAVLDY LNMIFICIFS
SECLMKIFAL RYHYFIEPWN LFDFVVVILS ILGLVLSDII EKYFVSPTLL RVVRVAKVGR
VLRLVKGAKG IRTLLFALAM SLPALFNICL LLFLVMFIFA IFGMSFFMHV KDKSGLDDVY
NFKTFGQSMI LLFQMSTSAG WDGVLDGIIN EEDCLPPDND KGYPGNCGSS TIGITYLLAY
LVISFLIVIN MYIAVILENY SQATEDVQEG LTDDDYDMYY EIWQQFDPDG TQYVRYDQLS
DFLDVLEPPL QIHKPNRYKI ISMDIPICRG DMMFCVDILD ALTKDFFARK GNPIEETAEL
GEVQQRPDEV GYEPVSSTLW RQREEYCARL IQHAWKRYKQ RHGGGTDASG DDLEIDACDN
GCGGGNGNEN DDSGDGATGS GDNGSQHGGG SISGGGGTPG GGKSKGIIGS TQANIGIVDS
NISPKESPDS IGDPQGRQTA VLVESDGFVT KNGHRVVIHS RSPSITSRTA DV
//
