ID F1LX08_RAT Unreviewed; 2016 AA. AC F1LX08; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 25-MAY-2022, sequence version 4. DT 27-MAR-2024, entry version 94. DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132}; GN Name=Scn3a {ECO:0000313|Ensembl:ENSRNOP00000006646.8, GN ECO:0000313|RGD:3635}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000006646.8, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000006646.8, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000006646.8, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0007829|PubMed:22673903} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). RN [3] {ECO:0000313|Ensembl:ENSRNOP00000006646.8} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000006646.8}; RG Ensembl; RL Submitted (NOV-2023) 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}. 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 Ensembl; ENSRNOT00000006646.8; ENSRNOP00000006646.8; ENSRNOG00000005007.8. DR RGD; 3635; Scn3a. DR VEuPathDB; HostDB:ENSRNOG00000005007; -. DR GeneTree; ENSGT00940000157130; -. DR HOGENOM; CLU_000540_5_0_1; -. DR OMA; CDAWLKI; -. DR OrthoDB; 1110761at2759; -. DR TreeFam; TF323985; -. DR Proteomes; UP000002494; Chromosome 3. DR Bgee; ENSRNOG00000005007; Expressed in Ammon's horn and 15 other cell types or tissues. DR GO; GO:0016528; C:sarcoplasm; IEA:Ensembl. DR GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:UniProtKB-UniRule. DR GO; GO:0005248; F:voltage-gated sodium channel activity; IEA:InterPro. DR GO; GO:0001508; P:action potential; IEA:UniProt. DR GO; GO:0048266; P:behavioral response to pain; IEA:Ensembl. 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; 1.20.5.1190; iswi atpase; 1. DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 4. 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:SF237; SODIUM CHANNEL PROTEIN TYPE 3 SUBUNIT ALPHA; 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. PE 1: Evidence at protein level; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; 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:UP000002494}; 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 254..274 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 404..431 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 778..796 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 808..831 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 888..916 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 978..1001 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1224..1242 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1263..1285 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1291..1311 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1340..1366 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1461..1485 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1543..1561 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1573..1591 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1598..1623 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1660..1688 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1764..1787 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT DOMAIN 136..437 FT /note="Ion transport" FT /evidence="ECO:0000259|Pfam:PF00520" FT DOMAIN 562..727 FT /note="Voltage-gated Na+ ion channel cytoplasmic" FT /evidence="ECO:0000259|Pfam:PF11933" FT DOMAIN 777..1008 FT /note="Ion transport" FT /evidence="ECO:0000259|Pfam:PF00520" FT DOMAIN 1015..1217 FT /note="Sodium ion transport-associated" FT /evidence="ECO:0000259|Pfam:PF06512" FT DOMAIN 1222..1494 FT /note="Ion transport" FT /evidence="ECO:0000259|Pfam:PF00520" FT DOMAIN 1542..1797 FT /note="Ion transport" FT /evidence="ECO:0000259|Pfam:PF00520" FT REGION 28..60 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 497..533 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 592..635 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1134..1178 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1963..2016 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 428..469 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 28..53 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 501..515 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 516..533 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 592..620 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1967..1988 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1989..2016 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 2016 AA; 228177 MW; E2242C5308741055 CRC64; MAQALLVPPG PESFRLFTRE SLAAIEKRAA EEKAKKPKKE QDIDDENKPK PNSDLEAGKN LPFIYGDIPP EMVSEPLEDL DPYYVSKKTF VVLNKGKAIF RFSATSALYI LTPLNPVRKI AIKILVHSYP FHAKIMLIMC TILTNCVFMT LSNPPDWTKN VEYTFTGIYT FESLIKILAR GFCLEDFTFL RDPWNWLDFS VIVMAYVTEF VDLGNVSALR TFRVLRALKT ISVIPGLKTI VGALIQSVKK LSDVMILTVF CLSVFALIGL QLFMGNLRNK CLQWPPSDSA FETNTTSYFN GTMDSNGTFV NVTMSTFNWK DYIADDSHFY VLDGQKDPLL CGNGSDAGQC PEGYICVKAG RNPNYGYTSF DTFSWAFLSL FRLMTQDYWE NLYQLTLRAA GKTYMIFFVL VIFLGSFYLV NLILAVVAMA YEEQNQATLE EAEQKEAEFQ QMLEQLKKQQ EEAQAVAAAS AASRDFSGIG GLGELLESSS EASKLSSKSA KEWRNRRKKR RQREHLEGNH RADGDRFPKS ESEDSVKRRS FLLSLDGNPL TGDKKLCSPH QSLLSIRGSL FSPRRNSKTS IFSFRGRAKD VGSENDFADD EHSTFEDSES RRDSLFVPHR PGERRNSNVS QASMSSRMVP GLPANGKMHS TVDCNGVVSL VGGLSALTSP TGWLAPEVII HKPATIFGLQ GTTTETEVRK RRLSSYQISM EMLEDSSGRQ RAMSIASILT NTMEELEESR QKCPPCWYRF ANVFLIWDCC DAWLKVKHLV NLIVMDPFVD LAITICIVLN TLFMAMEHYP MTQQFSSVLT VGNLVFTGIF TAEMVLKIIA MDPYYYFQEG WNIFDGIIVS LSLMELGLAN VEGLSVLRSF RLLRVFKLAK SWPTLNMLIK IIGNSVGALG NLTLVLAIIV FIFAVVGMQL FGKSYKECVC KINVDCKLPR WHMNDFFHSF LIVFRVLCGE WIETMWDCME VAGQTMCLIV FMLVMVIGNL VVLNLFLALL LSSFSSDNLA ATDDDNEMNN LQIAVGRMQK GIDFVKNKIR ECFRKAFFRK PKVIEIQEGN KIDSCMSNNT GIEISKELNY LKDGNGTTSG VGTGSSVEKY VIDENDYMSF INNPSLTVTV PIAVGESDFE NLNTEEFSSE SELEESKEKL NATSSSEGST VDVAPPREGE QAEIEPEEDL KPEACFTEGC IKKFPFCQVS TEEGKGKIWW NLRKTCYSIV EHNWFETFIV FMILLSSGAL AFEDIYIEQR KTIKTMLEYA DKVFTYIFIL EMLLKWVAYG FQTYFTNAWC WLDFLIVDVS LVSLVANALG YSELGAIKSL RTLRALRPLR ALSRFEGMRV VVNALVGAIP SIMNVLLVCL IFWLIFSIMG VNLFAGKFYH CVNTTTGNMF EIKEVNNFSD CQALGKQARW KNVKVNFDNV GAGYLALLQV ATFKGWMDIM YAAVDSRDVK LQPIYEENLY MYLYFVIFII FGSFFTLNLF IGVIIDNFNQ QKKKMSQDIF MTEEQKKYYN AMKKLGSKKP QKPIPRPANK FQGMVFDFVT RQVFDISIMI LICLNMVTMM VETDDQSKYM TLVLSRINLV FIVLFTGEFL LKLISLRYYY FTIGWNIFDF VVVILSIVGM FLAELIEKYF VSPTLFRVIR LARIGRILRL IKGAKGIRTL LFALMMSLPA LFNIGLLLFL VMFIYAIFGM SNFAYVKKEA GIDDMFNFET FGNSMICLFQ ITTSAGWDGL LAPILNSAPP DCDPDAIHPG SSVKGDCGNP SVGIFFFVSY IIISFLVVVN MYIAVILENF SVATEESAEP LSEDDFEMFY EVWEKFDPDA TQFIEFCKLS DFAAALDPPL LIAKPNKVQL IAMDLPMVSG DRIHCLDILF AFTKRVLGES GEMDALRIQM EERFMASNPS KVSYEPITTT LKRKQEEVSA AIIQRNYRCY LLKQRLKNIS SKYDKETIKG RIDLPIKGDM VIDKLNGNST PEKTDGSSST TSPPSYDSVT KPDKEKFEKD KPEKEIKGKE VRENQK //