ID H3DCB7_TETNG Unreviewed; 1967 AA.
AC H3DCB7;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
GN Name=SCN8A {ECO:0000313|Ensembl:ENSTNIP00000018160.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000018160.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000018160.1}
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 STRING; 99883.ENSTNIP00000018160; -.
DR Ensembl; ENSTNIT00000018384.1; ENSTNIP00000018160.1; ENSTNIG00000015105.1.
DR GeneTree; ENSGT00940000156263; -.
DR InParanoid; H3DCB7; -.
DR OMA; ECSPMWI; -.
DR TreeFam; TF323985; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
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 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; IPR008054; Na_channel_a8su.
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:SF23; SODIUM CHANNEL PROTEIN TYPE 8 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 PRINTS; PR01667; NACHANNEL8.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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:UP000007303};
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 129..152
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 197..216
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 228..249
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 349..368
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 388..415
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 730..754
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 766..784
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 845..874
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 933..959
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..1240
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1252..1272
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1298..1324
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1421..1447
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1506..1524
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1536..1558
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1570..1589
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1633..1658
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1679..1698
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1726..1749
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 132..422
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 543..684
FT /note="Voltage-gated Na+ ion channel cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF11933"
FT DOMAIN 735..965
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 973..1175
FT /note="Sodium ion transport-associated"
FT /evidence="ECO:0000259|Pfam:PF06512"
FT DOMAIN 1180..1456
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1505..1759
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 26..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1094..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1908..1967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1908..1933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1935..1967
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1967 AA; 224043 MW; 6FA03863888CFC1B CRC64;
MAAPLLAPPG PDSFKKFTRE SLVALEQRIK EEKNKKPPKQ DSSYRDDDDE NKPRPNSDLE
AGKSLPYIYG DTPQGMVAVP LEDLDPYYLN TQKTFIVLNK GKTIFRFSAT SALYFISPFN
PVRRVAIKIL LHTLFSMIIM CTILTNCIFM TFSDPPEWSK QVEYTFTGIY TFESLVKITA
RGFCIDDFTF LRDPWNWLDF MVISMAYITE FVDLGNVSAL RTFRVLRALK TISVIPGLKT
IVGALIQSVK KLSDVMILTV FCLSVFALIG LQLFMGNLRQ KCVIWPINIT DSQLSNKSQP
FDWDEYITND TNFYFLPGQL DALLCGNSSD SGRCPEGYTC MKAGRNPNYG YTSFDSFGWA
FLALFRLMTQ DFWENLYMLT LRAAGKTYMI FFVLVIFVGS FYLVNLILAV VAMAYEEQNQ
ATMEEAQQKE EEFKAMLEQL KKQQEDAQAA AMATSAGTVS EDAVEDDGGG HLSCSSSEMS
KLSSKSAKER RNRKKKWRQK EQEKEKGDSE KFVKSESDDG SKRSRFRFPD NRLGRKSSIM
NQSLLSIPGS PFLSRHNSKS SIFSFKGRSK DVGSENEFAD DEHSTVEECE ERRGSLFSPY
RRSSYSGFHG KRNSTVDCNG VVSLIGPGPG GRLLPEVKID KAATDDSPTT EVEVKKKLSG
SLMVSVDQLN TSFGRKERAN SVMSVITNTL VEELEESQRK CPPCWYKFAN TFLIWECSPK
WIKIKEIVNL IVMDPFVDLA ITICIVLNTL FMAMEHYPMT PDFEHMLSVG NLVFTGIFAG
EMLFKLVAMD PYYYFQEAWN CFDGFIVTLS LVELALADVE GLSVLRSFRL LRVFKLAKSW
PTLNMLIKII GNSVGALGNL TLVLAIIVFI FAVVGMQLFG KNYKDCVCKI AQDCELPRWH
MNDFFHSFLI VFRVLCGEWI ETMWDCMEVA GQAMCLIVFM MVMVIGNLVV LNLFLALLLS
SFSADNLAAT DDDGEPNNLQ ISVMRFKKGI AWTKSKVRIL MASLLKKPPM EDEQKPLDDM
YDKKLNFIAN HTGVDINRDL DYAKNGNGTT SGIGSSVGKY MIDEDHMSFI HNPNLTVCVP
IAVGESDFEN LNTEDFSSES DIENSKELDD TSSSEGSTID IKPDVEEVVV VETVEEYMEP
EPCWTDACVA KYKCCDVDIT MGWGKSWWFL RKTCYVIVEH NWFETLIIFM ILLSSGALAF
EDVYIEQRKT IRIILEYADR VFTYIFILEM LLKWVAYGFV KYFTNAWCWL DFFIVDVSIV
SLVANALGYS DLGPIKSLRT LRALRPLRAL SRFEGMRVVV NALVGAIPSI MNVLLVCLIF
WLIFSIMGVN LFAGKYYYCF NETSEEMFSV DVVNNKTQCE ALIKDNFTEV RWKNVKINFD
NVGAGYLALL QVATFKGWMD IMYAAVDSRE VEDQPDYEVN IYMYIYFVVF IIFGSFFTLN
LFIGVIIDNF NQQKKKFGGQ DIFMTEEQKK YYNAMKKLGS KKPQKPIPRP QNKIQGMVFD
FVTQQVFDIS IMILICLNMV TMMVETDDQS DETETVLYWV NFIFIVVFTT EFLLKLFALR
HYYFTNGWNI FDVVVVILSI VGMFLADIIE KYFVSPTLFR VIRLARIGRI LRLIKGAKGI
RTLLFALMMS LPALFNIGLL LFLVMFIFSI FGMSNFGYVK HGAGIDDMYN FETFGNSMII
LFMITTSGGW DGLLLPILNY PPDCDPNSEN PGTSVKGNCG NPSVGIFFFV MYIIISFLIV
VNMYIAIILE NFSVATEESA DPLSEDDFET FYEIWEKFDP SASQFITFAK LSDFADALEH
PLRVPKPNTI ELIAMDMPMV SGDRIHCLDI LFAFTKRVLG DSGELDMLRQ QMEERFVAAN
PSKVSYEPIT TTLRRKQEDV SARIIQNAYR AHLIRRGIIF KRHTFTNNKL ENGGTNQEKK
ESTPSTASLP SYDSVTKPDK EKQDENKEEW ARKQKDKNQK DEWESKC
//
