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Database: UniProt
Entry: W5MUR5_LEPOC
LinkDB: W5MUR5_LEPOC
Original site: W5MUR5_LEPOC 
ID   W5MUR5_LEPOC            Unreviewed;      1961 AA.
AC   W5MUR5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000012124.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000012124.1}
RP   IDENTIFICATION.
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}.
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DR   EMBL; AHAT01010434; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01010435; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015209750.1; XM_015354264.1.
DR   STRING; 7918.ENSLOCP00000012124; -.
DR   Ensembl; ENSLOCT00000012145.1; ENSLOCP00000012124.1; ENSLOCG00000009914.1.
DR   GeneID; 102683457; -.
DR   CTD; 566868; -.
DR   eggNOG; KOG2301; Eukaryota.
DR   GeneTree; ENSGT00940000154992; -.
DR   InParanoid; W5MUR5; -.
DR   OMA; FTEMEQD; -.
DR   OrthoDB; 1110761at2759; -.
DR   Proteomes; UP000018468; Linkage group LG9.
DR   Bgee; ENSLOCG00000009914; Expressed in heart and 5 other cell types or tissues.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0001518; C:voltage-gated sodium channel complex; IBA:GO_Central.
DR   GO; GO:0005248; F:voltage-gated sodium channel activity; IEA:InterPro.
DR   GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR   GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
DR   GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
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: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   SMART; SM00015; IQ; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
DR   PROSITE; PS50096; IQ; 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   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:UP000018468};
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        126..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361132"
FT   TRANSMEM        225..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361132"
FT   TRANSMEM        252..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361132"
FT   TRANSMEM        392..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361132"
FT   TRANSMEM        715..733
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361132"
FT   TRANSMEM        745..768
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361132"
FT   TRANSMEM        825..853
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361132"
FT   TRANSMEM        913..938
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361132"
FT   TRANSMEM        1144..1163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361132"
FT   TRANSMEM        1184..1202
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361132"
FT   TRANSMEM        1270..1296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361132"
FT   TRANSMEM        1353..1372
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361132"
FT   TRANSMEM        1393..1416
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361132"
FT   TRANSMEM        1475..1493
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361132"
FT   TRANSMEM        1505..1527
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361132"
FT   TRANSMEM        1539..1558
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361132"
FT   TRANSMEM        1606..1628
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361132"
FT   TRANSMEM        1696..1719
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361132"
FT   DOMAIN          129..425
FT                   /note="Ion transport"
FT                   /evidence="ECO:0000259|Pfam:PF00520"
FT   DOMAIN          521..664
FT                   /note="Voltage-gated Na+ ion channel cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF11933"
FT   DOMAIN          714..944
FT                   /note="Ion transport"
FT                   /evidence="ECO:0000259|Pfam:PF00520"
FT   DOMAIN          952..1139
FT                   /note="Sodium ion transport-associated"
FT                   /evidence="ECO:0000259|Pfam:PF06512"
FT   DOMAIN          1143..1425
FT                   /note="Ion transport"
FT                   /evidence="ECO:0000259|Pfam:PF00520"
FT   DOMAIN          1474..1729
FT                   /note="Ion transport"
FT                   /evidence="ECO:0000259|Pfam:PF00520"
FT   REGION          32..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          462..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1048..1091
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1907..1926
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1938..1961
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          427..457
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        485..510
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1063..1091
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1909..1926
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1947..1961
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1961 AA;  223485 MW;  C4F9D674B5031679 CRC64;
     MATLLLPPGP DSLRRFTRES LAAIENRIAE EQARNAKQEY REDLGDVEPP KPRADLEAGK
     QLPRIFGDIP SELVGVPLDD FDSYYYNNQK TFIVLNKGKA IFRFSATPAL YIFSPFHPVR
     RASIKILVHS LFSLFIMCTI LTNCVFMAMS EPAQWAKYVE YTFTGIYTFE SLIKILARGF
     CIGPFTFLRD PWNWLDFSVI VMAYVTEFVD LGNVSALRTF RVLRALKTIS VIPGLKTIVG
     ALIQSVKKLA DVMILTVFCL SVFALIGLQL FMGNLRQKCV QNITDCYHNT STNGTNYYCK
     NKTWPSYQDF ISDEENYYKL EGAKDPLLCG NGSDAGRCPD GAVCLKIGKN PDYGYTSFDT
     FGWAFLALFR LMTQDYWENL YHQTLRSVGK TYMIFFVLVI FLGSFYLINL ILAVVAMAYE
     EQNQATIAEA WQKEKEFQEA MEQLRKEQQA IVNKVQETDS VLSPEMSPFP MKDTKERRNR
     KKKHKTLSEG AEDDAEDKTA KQDTEDRQRG NVFLARTLSS ANRRESQCSI FNFRSRNKES
     ETDFADDECS ANGDNASRTG SLVIPWSRRR TSAHSTSSHC SQGNTPTLNI NGKLNITVDR
     NGVSSLGPPS ALTLPVVMVD KVNTEDHMLN CTNETSNMLN PRRFSAAEFL EEPFQRERAL
     SAASVLTNAM EELEESHQKC HPCWYRFAQH YLIWDCCPLW LKIKEWVKFG VMDPFLDLAI
     TICIVLNTLF MALEHHPMTD DFNSMLSVGN LVFTGIFTAE MVFKIIALDP YYYFQQGWNI
     FDSIIVSLSL MELGLSNVEG LSVLRSFRLL RVFKLAKSWP TLNTLIKIIG NSVGALGNLT
     LVLAIIVFIF AVVGMQLFGK SYQDCVCKIS KDCTLPRWHM KDFFHSFLIV FRVLCGEWIE
     TMWDCMEVAG QPLCILVFML VMVIGNLVVL NLFLALLLSS FSADNLSAPD DDGEMNNLQI
     AIARIQRGIN WLKIAICDFF NGNFKKRRQK AKEAKAMTKL QRLGNHIEGN GTMGIIGRNG
     EKYVISDGDS YMTNPNLTIN VPIAPGESDV EFPEEDERSE CSEDEEVKQK DEISLSEGST
     VDLRKPGEEE DEFSEMAEEA MDPEDCFPEM CVRRFPCCDI NTTQGVGSIW WRLRKTCYRI
     VEHSWFETFI IFMILLSSGA LAFEDINIEK RKVIKVILEY ADKVFTYVFV LEMLLKWVAY
     GFKKYFTNYW CWLDFLIVDI STDTAFDRVS LISLIANTLG YSDFAAIKSL RTLRALRPLR
     ALSRFEGMRV VVNALIGAIP SIMNVLLVCL IFWLIFSIMG VNLFAGKFGK CVSKAGYQYN
     ASHINNRSEC LAMNNMTLYY WTKVKVNFDN VGAGYLALLQ VATFKGWMEI MYAAVDSRGL
     EEQPIKESNL YMYLYFVIFI IFGSFFTLNL FIGVIIDNFN QQKRKLGGQD IFMTEEQKKY
     YNAMKKLGSK KPQKPIPRPL NPFQGFFFDV VSKQAFDIII MILICLNMVT MMVETDDQSK
     RMEDILNKIN LAFIVIFTGE CCIKIMALRC YFFTVGWNIF DFVVVILSIV GIVLADIIEK
     YFVSPTLFRV IRLARIGRVL RLIRGAKGIR TLLFALMMSL PALFNIGLLL FLVMFIYAIF
     GMANFAYVKK QGGIDDMFNF ETFGNSMICL FQITTSAGWD SLLSPILNNS PEECDANKTH
     TGTNAKGDCG NPSVGITFFV SYIIISFLIV VNMYIAIILE NFSVATEEST EPLSEDDFEM
     FYEVWEKFDP EATQFIEYAK LSDFADSLEE PLRIAKPNKI KLISMDLPMV SGDKIHCLDI
     LFAFTKRVLG ESGEMDALKQ QMEEKFMMAN PSKISYEPIT TTLRRKQEEV SAVIIQRAYR
     RHLLRRSMRQ ASFLYRHINS DGNIDVEDPP EKEGLIASMI KENYGHETEM TETLSSTSSP
     PSYDSVTRAT SDIFQVVISD PRNTDQSEPF IHPDRDRESF L
//
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