ID A6N7T8_RAT Unreviewed; 1963 AA.
AC A6N7T8;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
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|EMBL:ABR14546.1};
RN [1] {ECO:0000313|EMBL:ABR14546.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W {ECO:0000313|EMBL:ABR14546.1};
RC TISSUE=Brain {ECO:0000313|EMBL:ABR14546.1};
RX PubMed=16115203; DOI=10.1111/j.1460-9568.2005.04280.x;
RA Ou S.-W., Kameyama A., Hao L.-Y., Horiuchi M., Minobe E., Wang W.-Y.,
RA Makita N., Kameyama M.;
RT "Tetrodotoxin-resistant Na+ channels in human neuroblastoma cells are
RT encoded by new variants of Nav1.5/SCN5A.";
RL Eur. J. Neurosci. 22:793-801(2005).
RN [2] {ECO:0000313|EMBL:ABR14546.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W {ECO:0000313|EMBL:ABR14546.1};
RC TISSUE=Brain {ECO:0000313|EMBL:ABR14546.1};
RA Ren C.-T., Ou S.-W., Wang Y.-J., Wang J., Lin Y., Zong Z.-H.;
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; EF618550; ABR14546.1; -; mRNA.
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 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; IPR008053; Na_channel_a5su.
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:SF206; SODIUM CHANNEL PROTEIN TYPE 5 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; PR01666; NACHANNEL5.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
PE 2: Evidence at transcript 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, ECO:0000313|EMBL:ABR14546.1};
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 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 127..149
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 388..416
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 721..739
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 751..769
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 781..798
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 838..861
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 914..939
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1151..1170
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1191..1207
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1219..1240
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1268..1294
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1390..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..1523
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1535..1555
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1592..1620
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1695..1718
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 130..422
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 508..667
FT /note="Voltage-gated Na+ ion channel cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF11933"
FT DOMAIN 719..945
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 953..1146
FT /note="Sodium ion transport-associated"
FT /evidence="ECO:0000259|Pfam:PF06512"
FT DOMAIN 1150..1425
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1474..1728
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 27..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1908..1963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 413..451
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 480..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1037
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1068
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1094
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1908..1939
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1963 AA; 221304 MW; FADEB8D16CFEA93E CRC64;
MANFLLPRGT SSFRRFTRES LAAIEKRMAE KQARGSTTLQ ESREGLPEEE APRPQLDLQA
SKKLPDLYGN PPQELIGEPL EDLDPFYSTQ KTFIVPNKGK TIFRFSATNA LYVLSPFHPI
RRAAVKILVH SLFNTLIMCT ILTNCVFMAQ HDPPPWTKYV EHTFTAIYTF ESLVKILARG
SCLHAFTFLR GPWNWLDFSV IIMAYVSENI KLGNLSALRT FRVLRALKTI SVIPGLKTIV
GALIQSVKKL ADVMVLTVFC LSVFALIGLQ LFMGNLRHKR VRNFTALNGI NGSVEADGLV
WESLDLYLSD PENYLLKNGT SDVLLCGNSS DAGTCLEGYR CLKAGENPDH GYTSFDSFAW
AFLALFRLMT QDCWERLYQQ TLRSAGKIYM IFFMLVIFLG SFYLVNLILA VVAMAYEEQN
QATIAETEEK EKRFQEAMEM LKKEHEALTI RGADTVSRSS LEMSPLAPVN SHERRSKRRK
RMSSGTEECG EDRLPKSDSE DGPRAMNHLS LTRGLSRTSM KPRSSRGSIF TFRRRDLGSE
ADFADDENST AGESESHHTS LLVPWPLRRT SAQGQPSPGT SAPGHALHGK KNSTVDCNGV
VSLLGAGDPE ATSPGSHLLR PVMLEHPPDT TTPSEEPGGP QMLTSQAPCV DGFEEPGARQ
RALSAVSVLT SALEELEESR HKCPPCWNRL AQRYLIWECC PLWMSIKQGV KLVVMDPXTD
LTITXCIVLN TLFMALEHYN MTSEFEEMLQ VGNLVFTGIF TAEMTFKIIA LDPYYYFQQG
WNIFDSIIVI LSLMELGLSR MSNLSVLRSF RLLRVFKLAK SWPTLNTLIK IIGNSVGALG
NLTLVLAIIV FIFAVVGMQL FGKNYSELRD SDSGLLPRWH MMDFFHAFLX IFRILCGEWI
ETMWDCMEVS GQSLCLLVFL LVMVIGNLVV LNLFLALLLS SFSADNLTAP DEDGEMNNLQ
LALARIQRGL RFVKRTTWDF CCGILRRRPK KPAALATHSQ LPSCITAPRS PPPPEVEKVP
PARKETRFEE DKRPGQGTPG DSEPVCVPIA VAESDTEDQE EDEENSLGTE EESSKQTPED
SYSEGSTADM TNTADLLEQI PDLGEDVKDP EDCFTEGCVR RCPCCMVDTT QSPGKVWWRL
RKTCYHIVEH SWFETFIIFM ILLSSGALAF EDIYLEERKT IKVLLEYADK MFTYVFVLEM
LLKWVAYGFK KYFTNAWCWL DFLIVDVSLV SLVANTLGFA EMGPIKSLRT LRALRPLRAL
SRFEGMRVVV NALVGAIPSI MNVLLVCLIF WLIFSIMGVN LFAGKFGRCI NQTEGDLPLN
YTIVNNKSEC ESFNVTGELY WTKVKVNFDN VGAGYLALLQ VATFKGWMDI MYAAVDSRGY
EEQPQWEDNL YMYIYFVVFI IFGSFFTLNL FIGVIIDNFN QQKKKLGGQD IFMTEEQKKY
YNAMKKLGSK KPQKPIPRPL NKYQGFIFDI VTKQAFDVTI MFLICLNMVT MMVETDDQSP
EKVNILAKIN LLFVAIFTGE CIVKMAALRH YYFTNSWNIF DFVVVILSIV GTVLSDIIQK
YFFSPTLFRV IRLARIGRIL RLIRGAKGIR TLLFALMMSL PALFNIGLLL FLVMFIYSIF
GMANFAYVKW EAGIDDMFNF QTFANSMLCL FQITTSAGWD GLLSPILNTG PPYCDPNLPN
SNGSRGNCGS PAVGILFFTT YIIISFLIVV NMYIAIILEN FSVATEESTE PLSEDDFDMF
YEIWEKFDPE ATQFIEYLAL SDFADALSEP LRIAKPNQIS LINMDLPMVS GDRIHCMDIL
FAFTKRVLGE SGEMDALKIQ MEEKFMAANP SKISYEPITT TLRRKHEEVS ATVIQRAFRR
HLLQRSVKHA SFLFRQQAGG SGLSDEDAPE REGLIAYMMN GNFSRRSAPL SSSSISSTSF
PPSYDSVTRA TSDNLPVRAS DYSRSEDLAD FPPSPDRDRE SIV
//
