ID E9PW82_MOUSE Unreviewed; 1973 AA. AC E9PW82; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAR-2024, entry version 91. DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132}; GN Name=Scn9a {ECO:0000313|Ensembl:ENSMUSP00000131711.2, 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:ENSMUSP00000131711.2, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000131711.2, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000131711.2, 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:ENSMUSP00000131711.2} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000131711.2}; 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 RefSeq; NP_001277604.1; NM_001290675.1. DR SMR; E9PW82; -. DR MaxQB; E9PW82; -. DR ProteomicsDB; 312208; -. DR Antibodypedia; 33781; 562 antibodies from 39 providers. DR DNASU; 20274; -. DR Ensembl; ENSMUST00000169900.8; ENSMUSP00000131711.2; ENSMUSG00000075316.13. DR GeneID; 20274; -. DR UCSC; uc012bwi.3; mouse. DR AGR; MGI:107636; -. DR CTD; 6335; -. DR MGI; MGI:107636; Scn9a. DR VEuPathDB; HostDB:ENSMUSG00000075316; -. DR GeneTree; ENSGT00940000161368; -. DR HOGENOM; CLU_000540_5_0_1; -. DR OrthoDB; 1110761at2759; -. DR BioGRID-ORCS; 20274; 1 hit in 76 CRISPR screens. 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; E9PW82; 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. 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:E9PW82, KW ECO:0007829|ProteomicsDB:E9PW82}; 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 378..405 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 725..751 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 763..781 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 801..822 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 843..871 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 933..956 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1180..1198 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1219..1235 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1247..1267 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1296..1322 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1421..1444 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1503..1521 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1533..1551 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1563..1583 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1620..1648 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1724..1747 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT DOMAIN 125..410 FT /note="Ion transport" FT /evidence="ECO:0000259|Pfam:PF00520" FT DOMAIN 534..682 FT /note="Voltage-gated Na+ ion channel cytoplasmic" FT /evidence="ECO:0000259|Pfam:PF11933" FT DOMAIN 732..963 FT /note="Ion transport" FT /evidence="ECO:0000259|Pfam:PF00520" FT DOMAIN 970..1174 FT /note="Sodium ion transport-associated" FT /evidence="ECO:0000259|Pfam:PF06512" FT DOMAIN 1178..1453 FT /note="Ion transport" FT /evidence="ECO:0000259|Pfam:PF00520" FT DOMAIN 1502..1757 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 458..540 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 574..609 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1004..1028 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1078..1134 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1922..1973 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 402..447 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 485..528 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 574..599 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1004..1020 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1097..1112 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1922..1948 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1950..1973 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1973 AA; 224654 MW; A1E5422E899449E9 CRC64; MAMLPPPGPQ SFVHFTKQSL ALIEQRISEE KAKGHKDEKK DDEEEGPKPS SDLEAGKQLP FIYGDIPPGM VSEPLEDLDP YYADKKTFIV LNKGKAIFRF NATPALYMLS PFSPLRRISI KILVHSLFSM LIMCTILTNC IFMTMSNPPD WTKNVEYTFT GIYTFESLIK ILARGFCVGE FTFLRDPWNW LDFVVIVFAY VTEFVDLGNV SALRTFRVLR ALKTISVIPG LKTIVGALIQ SVKKLSDVMI LTVFCLSVFA LIGLQLFMGN LKHKCFRKDL EQNETLESIM STAESEEELK RYFYYLEGSK DALLCGFSTD SGQCPEGYEC VTAGRNPDYG YTSFDTFGWA FLALFRLMTQ DYWENLYQQT LRAAGKTYMI FFVVVIFLGS FYLINLILAV VAMAYEEQNQ ANIEEAKQKE LEFQQMLDRL KKEQEEAEAI AAAAAEYTSL GRSRIMGLSE SSSETSRLSS KSAKERRNRR KKKKQKLSSG EEKGDDEKLS KSGSEESIRK KSFHLGVEGH HRAREKRLST PNQSPLSIRG SLFSARRSSR TSLFSFKGRG RDLGSETEFA DDEHSIFGDN ESRRGSLFVP HRPRERRSSN ISQASRSPPV LPVNGKMHSA VDCNGVVSLV DGPSALMLPN GQLLPEGTTN QMRKKRLSSS YFLSEDMLND PHLRQRAMSR ASILTNTVEE LEESRQKCPP WWYRFAHTFL IWNCSPYWIK FKKFIYFIVM DPFVDLAITI CIVLNTLFMA MEHHPMTDEF KNVLAVGNLV FTGIFAAEMV LKLIAMDPYE YFQVGWNIFD SLIVTLSLVE LFLADVEGLS VLRSFRLLRV FKLAKSWPTL NMLIKIIGNS VGALGNLTLV LAIIVFIFAV VGMQLFGKSY KECVCKINEN CKLPRWHMND FFHSFLIVFR VLCGEWIETM WDCMEVAGQT MCLIVYMMVM VIGNLVVLNL FLALLLSSFS SDNLTAIEED TDANNLQIAV ARIKRGINYV KQTLREFILK SFSKKPKGSK DTKRTADPNN KRENYISNRT LAEISKDHNF LKEKDKISGF SSSLDKSFMD ENDYQSFIHN PSLTVTVPIA PGESDLENMN TEELSSDSDS DYSKERRNRS SSSECSTVDN PLPGEEEAEA EPINADEPEA CFTDGCVRRF PCCQVNIDSG KGKVWWTIRK TCYRIVEHSW FESFIVLMIL LSSGALAFED IYIEKKKTIK IILEYADKIF TYIFILEMLL KWVAYGYKTY FTNAWCWLDF LIVDVSLVTL VANTLGYSDL GPIKSLRTLR ALRPLRALSR FEGMRVVVNA LIGAIPSIMN VLLVCLIFWL IFSIMGVNLF AGKFYECVNT TDGSRFSVSQ VANRSECFAL MNVSGNVRWK NLKVNFDNVG LGYLSLLQVA TFKGWMDIMY AAVDSVNVNA QPIYEYNLYM YIYFVIFIIF GSFFTLNLFI GVIIDNFNQQ KKKLGGQDIF MTEEQKKYYN AMKKLGSKKP QKPIPRPGNK FQGCIFDLVT NQAFDITIMV LICLNMVTMM VEKEGQTDYM SFVLYWINVV FIILFTGECV LKLISLRHYY FTVGWNIFDF VVVILSIVGM FLAEMIEKYF VSPTLFRVIR LARIGRILRL IKGAKGIRTL LFALMMSLPA LFNIGLLLFL VMFIYAIFGM SNFAYVKKEA GINDMFNFET FGNSMICLFQ ITTSAGWDGL LAPILNSAPP DCDPKKVHPG SSVEGDCGNP SVGIFYFVSY IIISFLVVVN MYIAVILENF SVATEESTEP LSEDDFEMFY EVWEKFDPDA TQFIEFCKLS DFAAALDPPL LIAKPNKVQL IAMDLPMVSG DRIHCLDILF AFTKRVLGES GEMDSLRSQM EERFMSANPS KVSYEPITTT LKRKQEDVSA TIIQRAYRRY RLRQNVKNIS SIYIKDGDRD DDLPNKEDIV FDNVNENSSP EKTDATASTI SPPSYDSVTK PDQEKYETDK TEKEDKEKDE SRK //