ID A0A093HH83_STRCA Unreviewed; 2005 AA.
AC A0A093HH83;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
DE Flags: Fragment;
GN ORFNames=N308_12688 {ECO:0000313|EMBL:KFV81983.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV81983.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV81983.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV81983.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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; KL206404; KFV81983.1; -; Genomic_DNA.
DR STRING; 441894.ENSSCUP00000014367; -.
DR Proteomes; UP000053584; 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; IPR008051; Na_channel_a1su.
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:SF280; SODIUM CHANNEL PROTEIN TYPE 1 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; PR01664; NACHANNEL1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
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, ECO:0000313|EMBL:KFV81983.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000053584};
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 125..147
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 400..427
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 764..788
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 800..821
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 883..911
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 970..996
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1222..1240
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1261..1280
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1336..1364
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1462..1486
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1544..1562
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1574..1592
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1604..1624
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1661..1689
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1765..1788
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 129..433
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 559..722
FT /note="Voltage-gated Na+ ion channel cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF11933"
FT DOMAIN 772..1001
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1010..1216
FT /note="Sodium ion transport-associated"
FT /evidence="ECO:0000259|Pfam:PF06512"
FT DOMAIN 1220..1495
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1543..1798
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 28..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1978..2005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 424..458
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 31..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1991..2005
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 2005
FT /evidence="ECO:0000313|EMBL:KFV81983.1"
SQ SEQUENCE 2005 AA; 227714 MW; 2B0A97B8D6028AC9 CRC64;
MEQSVLVPPG PDSFQYFTRE SLAAIEQRIA AEKAKNPKQD RKDNDNENGP KPNSDLEAGK
TLPFIYGDIP PGMVSEPLED MDPYYINKKT FIVLNKGKAI FRFSATSALY ILTPFNPLRK
IAIKILFTLF SMLIMCTILT NCVFMTMSNP PDWTKNVEYT FTGIYTFESL IKIIARGFCL
EDFTFLRDPW NWLDFTVITF AYVTEFVDLG NVSALRTFRV LRALKTISVI PGLKTIVGAL
IQSVKKLSDV MILTVFCLSV FALIGLQLFM GNLRNKCLQW PPENFTLETN ITSQFNTTIG
ENGTLVNATV TPFDWKGYIE DESHFYFLEG QNDALLCGNS SDAGQCPEGY TCVKAGRNPN
YGYTSFDTFS WAFLSLFRLM TQDFWENLYQ LTLRAAGKTY MIFFVLVIFL GSFYLINLIL
AVVAMAYEEQ NQATLEEAEQ KEAEFQQMLE QLKKQQEAAA AAAAVTASAE SREPSVGEGA
GGLSESSSQA SKLSSKSAKE RRNRRKKRKQ KEQSGGEEKD EDEFHKSESE DSIRRKGFRL
SIEGNRLTYE KKYSSPHQSL LSIRGSLFSP RRNSRTSLFS FRGRAKDIGS ENDFADDEHS
TFEDNDSRRD SLFVPRRHGE RRNSNISQAS RSSRMLAVFP VNGKMHSTVD CNGVVSLVGG
PSAPTSPVGQ LLPEVIIDKP ATDDNGTTTE TEMRKRISSS FHVSMDFLED PALRERAMSI
ASILTNTVEE LEESRQKCPP CWYKFANIFL IWDCSPHWLK VKHIVNLVVM DPFVDLAITI
CIVLNTLFMA MEHYPMTDEF NSVLSVGNLV FTGIFTAEMF LKIIAMDPYY YFQEGWNIFD
GFIVTLSLVE LGLADVEGLS VLRSFRLLRV FKLAKSWPTL NMLIKIIGNS VGALGNLTLV
LAIIVFIFAV VGMQLFGKNY KECVCKIASD CVLPRWHMQD FFHSFLIVFR VLCGEWIETM
WDCMEVAGQA MCLTVFMMVM VIGNLVVLNL FLALLLSSFS ADNLAVTDDD NEMNNLQIAV
ARMQKGIDYV KRKAREFLQK AFVKKQKALD EIKPLEDLNN KNSCISNHTN VEISKDHDFI
KDGNGTTSGI GTGSSVEKYI IDESDYMSFI NNPSLTVTVP IAVGESDFEN LNTEEFSSES
DLEESKEKLN LSSSSEGSTV DIGLPAEEQP EIEPEEAQEP EACFTEGCVR RFKCCQVSVE
EGRGKQWWNL RKTCFRIVEH NWFETFIVFM ILLSSGALAF EDIYIEQRKT IKTMLEYADK
VFTYIFILEM LLKWVAYGYQ TYFTNAWCWL DFLIVDVSLV SLTANALGYS ELGAIKSLRT
LRALRPLRAL SRFEGMRVVV NALLGAIPSI MNVLLVCLIF WLIFSIMGVN LFAGKFYYCV
NTTTDERFEV DQINNFSQCE ELIKNNQSAR WKNVKVNFDN VGFGYLSLLQ VATFKGWMDI
MYAAIDSRDV LLQPKYEDNL YMYLYFVIFI IFGSFFTLNL FIGVIIDNFN QQKKKISQDI
FMTEEQKKYY NAMKKLGSKK PQKPIPRPGN KFQGMVFDFV TQQVFDISIM ILICLNMVTM
MVETDDQSDE MENILYWINL VFIVLFTGEC VLKLISLRHY YFTIGWNIFD FVVVILSIVG
MFLAEMIEKY FVSPTLFRVI RLARIGRILR LIKGAKGIRT LLFALMMSLP ALFNIGLLLF
LVMFIYAIFG MSNFAYVKRE AGIDDMFNFE TFGNSMICLF QITTSAGWDG LLAPILNSGE
PDCDPHKAHP GSSVKGDCGN PSVGIFFFVS YIIISFLVVV NMYIAVILEN FGVATEESAE
PLSEDDFEMF YEVWEKFDPD ATQFMEFEKL SDFAAALEPP LHLPKPNKVQ LIAMDLPMVS
GDRIHCLDIL FAFTKRVLGE SGEMDALRIQ MEDRFMASNP SKASYEPITT TLKRKQEEVS
AVIIQRAYRR HLLKRTVKQA SFIYNKNKTE GGAGQGMKDE ILIDKLNENS FTEKTDITPS
TAVCPPSYDR VTRPVKEKYE KEGKD
//
