ID F8VPQ7_MOUSE Unreviewed; 1975 AA. AC F8VPQ7; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAR-2024, entry version 94. DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132}; GN Name=Scn9a {ECO:0000313|Ensembl:ENSMUSP00000097641.3, GN ECO:0000313|MGI:MGI:107636}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000097641.3, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000097641.3, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000097641.3, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] {ECO:0000313|Ensembl:ENSMUSP00000097641.3} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000097641.3}; 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 SMR; F8VPQ7; -. DR iPTMnet; F8VPQ7; -. DR MaxQB; F8VPQ7; -. DR ProteomicsDB; 361737; -. DR Antibodypedia; 33781; 562 antibodies from 39 providers. DR Ensembl; ENSMUST00000100063.9; ENSMUSP00000097641.3; ENSMUSG00000075316.13. DR UCSC; uc056zmv.1; mouse. DR AGR; MGI:107636; -. DR MGI; MGI:107636; Scn9a. DR VEuPathDB; HostDB:ENSMUSG00000075316; -. DR GeneTree; ENSGT00940000161368; -. DR ChiTaRS; Scn9a; mouse. DR Proteomes; UP000000589; Chromosome 2. DR Bgee; ENSMUSG00000075316; Expressed in lumbar dorsal root ganglion and 73 other cell types or tissues. DR ExpressionAtlas; F8VPQ7; baseline and differential. 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:0050877; P:nervous system process; IEA:UniProt. 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; IPR000048; IQ_motif_EF-hand-BS. 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:SF221; SODIUM CHANNEL PROTEIN TYPE 9 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 SMART; SM00015; IQ; 1. DR SUPFAM; SSF81324; Voltage-gated potassium channels; 4. DR Genevisible; F8VPQ7; MM. 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 Proteomics identification {ECO:0007829|MaxQB:F8VPQ7, KW ECO:0007829|ProteomicsDB:F8VPQ7}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; 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 Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}; KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882, KW ECO:0000256|RuleBase:RU361132}. FT TRANSMEM 122..145 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 190..209 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 221..242 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 248..268 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 380..407 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 727..753 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 765..783 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 803..824 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 845..873 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 935..958 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1182..1200 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1221..1237 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1249..1269 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1298..1324 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1423..1446 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1505..1523 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1535..1553 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1565..1585 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1622..1650 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1726..1749 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT DOMAIN 125..412 FT /note="Ion transport" FT /evidence="ECO:0000259|Pfam:PF00520" FT DOMAIN 536..684 FT /note="Voltage-gated Na+ ion channel cytoplasmic" FT /evidence="ECO:0000259|Pfam:PF11933" FT DOMAIN 734..965 FT /note="Ion transport" FT /evidence="ECO:0000259|Pfam:PF00520" FT DOMAIN 972..1176 FT /note="Sodium ion transport-associated" FT /evidence="ECO:0000259|Pfam:PF06512" FT DOMAIN 1180..1455 FT /note="Ion transport" FT /evidence="ECO:0000259|Pfam:PF00520" FT DOMAIN 1504..1759 FT /note="Ion transport" FT /evidence="ECO:0000259|Pfam:PF00520" FT REGION 26..55 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 456..542 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 578..611 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1006..1030 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1080..1136 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1924..1975 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 404..438 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 26..51 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 456..470 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 487..530 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 578..601 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1006..1022 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1099..1114 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1924..1950 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1952..1975 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1975 AA; 225087 MW; B63089B68F5E4210 CRC64; MAMLPPPGPQ SFVHFTKQSL ALIEQRISEE KAKGHKDEKK DDEEEGPKPS SDLEAGKQLP FIYGDIPPGM VSEPLEDLDP YYADKKTFIV LNKGKAIFRF NATPALYMLS PFSPLRRISI KILVHSLFSM LIMCTILTNC IFMTMSNPPD WTKNVEYTFT GIYTFESLIK ILARGFCVGE FTFLRDPWNW LDFVVIVFAY LTEFVNLGNV SALRTFRVLR ALKTISVIPG LKTIVGALIQ SVKKLSDVMI LTVFCLSVFA LIGLQLFMGN LKHKCFRKDL EQNETLENGH KGYQRKCKVK TMGYFYYLEG SKDALLCGFS TDSGQCPEGY ECVTAGRNPD YGYTSFDTFG WAFLALFRLM TQDYWENLYQ QTLRAAGKTY MIFFVVVIFL GSFYLINLIL AVVAMAYEEQ NQANIEEAKQ KELEFQQMLD RLKKEQEEAE VVFIITNTKA KQVGQRIMGL SESSSETSRL SSKSAKERRN RRKKKKQKLS SGEEKGDDEK LSKSGSEESI RKKSFHLGVE GHHRAREKRL STPNQSPLSI RGSLFSARRS SRTSLFSFKG RGRDLGSETE FADDEHSIFG DNESRRGSLF VPHRPRERRS SNISQASRSP PVLPVNGKMH SAVDCNGVVS LVDGPSALML PNGQLLPEGT TNQMRKKRLS SSYFLSEDML NDPHLRQRAM SRASILTNTV EELEESRQKC PPWWYRFAHT FLIWNCSPYW IKFKKFIYFI VMDPFVDLAI TICIVLNTLF MAMEHHPMTD EFKNVLAVGN LVFTGIFAAE MVLKLIAMDP YEYFQVGWNI FDSLIVTLSL VELFLADVEG LSVLRSFRLL RVFKLAKSWP TLNMLIKIIG NSVGALGNLT LVLAIIVFIF AVVGMQLFGK SYKECVCKIN ENCKLPRWHM NDFFHSFLIV FRVLCGEWIE TMWDCMEVAG QTMCLIVYMM VMVIGNLVVL NLFLALLLSS FSSDNLTAIE EDTDANNLQI AVARIKRGIN YVKQTLREFI LKSFSKKPKG SKDTKRTADP NNKRENYISN RTLAEISKDH NFLKEKDKIS GFSSSLDKSF MDENDYQSFI HNPSLTVTVP IAPGESDLEN MNTEELSSDS DSDYSKERRN RSSSSECSTV DNPLPGEEEA EAEPINADEP EACFTDGCVR RFPCCQVNID SGKGKVWWTI RKTCYRIVEH SWFESFIVLM ILLSSGALAF EDIYIEKKKT IKIILEYADK IFTYIFILEM LLKWVAYGYK TYFTNAWCWL DFLIVDVSLV TLVANTLGYS DLGPIKSLRT LRALRPLRAL SRFEGMRVVV NALIGAIPSI MNVLLVCLIF WLIFSIMGVN LFAGKFYECV NTTDGSRFSV SQVANRSECF ALMNVSGNVR WKNLKVNFDN VGLGYLSLLQ VATFKGWMDI MYAAVDSVNV NAQPIYEYNL YMYIYFVIFI IFGSFFTLNL FIGVIIDNFN QQKKKLGGQD IFMTEEQKKY YNAMKKLGSK KPQKPIPRPG NKFQGCIFDL VTNQAFDITI MVLICLNMVT MMVEKEGQTD YMSFVLYWIN VVFIILFTGE CVLKLISLRH YYFTVGWNIF DFVVVILSIV GMFLAEMIEK YFVSPTLFRV IRLARIGRIL RLIKGAKGIR TLLFALMMSL PALFNIGLLL FLVMFIYAIF GMSNFAYVKK EAGINDMFNF ETFGNSMICL FQITTSAGWD GLLAPILNSA PPDCDPKKVH PGSSVEGDCG NPSVGIFYFV SYIIISFLVV VNMYIAVILE NFSVATEEST EPLSEDDFEM FYEVWEKFDP DATQFIEFCK LSDFAAALDP PLLIAKPNKV QLIAMDLPMV SGDRIHCLDI LFAFTKRVLG ESGEMDSLRS QMEERFMSAN PSKVSYEPIT TTLKRKQEDV SATIIQRAYR RYRLRQNVKN ISSIYIKDGD RDDDLPNKED IVFDNVNENS SPEKTDATAS TISPPSYDSV TKPDQEKYET DKTEKEDKEK DESRK //