ID A0A093SWE2_9PASS Unreviewed; 2013 AA.
AC A0A093SWE2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
GN ORFNames=N305_06577 {ECO:0000313|EMBL:KFW86849.1};
OS Manacus vitellinus (golden-collared manakin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW86849.1, ECO:0000313|Proteomes:UP000053258};
RN [1] {ECO:0000313|EMBL:KFW86849.1, ECO:0000313|Proteomes:UP000053258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW86849.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-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; KL672766; KFW86849.1; -; Genomic_DNA.
DR STRING; 328815.ENSMVIP00005024196; -.
DR Proteomes; UP000053258; 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; 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:SF237; SODIUM CHANNEL PROTEIN TYPE 3 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.
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|ARBA:ARBA00023303, 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:UP000053258};
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 130..151
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 231..248
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 404..431
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 768..786
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 798..821
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 878..906
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 968..991
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1219..1237
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1258..1280
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1286..1306
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1335..1361
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1459..1483
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1541..1559
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1571..1589
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1601..1621
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1658..1686
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1762..1785
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 136..438
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 565..717
FT /note="Voltage-gated Na+ ion channel cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF11933"
FT DOMAIN 767..998
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1005..1212
FT /note="Sodium ion transport-associated"
FT /evidence="ECO:0000259|Pfam:PF06512"
FT DOMAIN 1217..1492
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1540..1795
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 28..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1130..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1964..2013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 428..473
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 28..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1969..1985
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1986..2013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2013 AA; 228399 MW; AC2B5322361475B4 CRC64;
MAQALLAPPG PESFRYFTRD SLAAIEKRCA EEKAKKPKQE HTDDDDENGP KPNSDLEAGK
TLPFIYGDIP PGMVSEPLED LDPYYINKKT FIVLNKGKAI FRFSATSALY ILTPFNPIRK
IAIKILVHSY PFFLIMLIMC TILTNCVFMT MSNPPDWTKN VEYTFTGIYT FESLIKILAR
GFCLEGFTFL RDPWNWLDFS VILMAYVTEF VDLGNVSALR TFRVLRALKT ISVIPGLKTI
VGALIQSVKK LSDVMILTVF CLSVFALIGL QLFMGNLRNK CLQWPPDNST FEISIISYFN
STMNENGTLV NMTVSTFNWK DYIEDETHFY ILEGQRDALL CGNSSDAGQC PEGYICVKAG
RNPNYGYTSF DTFSWAFLSL FRLMTQDFWE NLYQLTLRAA GKTYMIFFVL VIFLGSFYLI
NLILAVVAMA YEEQNQATME EAEQKEAEFQ QMLEQLKKQQ EEAQTTAAVA AASVASRDFS
GVGGLGELLE SSSEASKLSS KSAKERRNRR KKRRQREMSE AEDKGDSDKF PKSESEDSIR
RKSFRFSTEG SQLTYEKRLT SPHQSLLSIR GSLFSPRRNS KTSIFSFRGH AKDVGSENDF
ADDEHSTLED NESRRDSLFV PNRHGERRNS NVSQASVSSR MIPALPVNGK MHSTVDCNGV
VSLVGGPSTL TSPTGQLIPE GTTTETEIRK RRLSSYQISM EMLEESAARQ RAMSIASILT
NTMEELEESR QKCPPCWYRF ANTFLIWDCW SPWLKVKHIV NLVVMDPFVD LAITICIVLN
TLFMAMEHYP MTEQFSSVLS VGNLVFTGIF TAEMVLKIIA MDPYYYFQEG WNIFDGIIVS
LSLMELGLAN VEGLSVLRSF RLLRVFKLAK SWPTLNMLIK IIGNSVGALG NLTLVLAIIV
FIFAVVGMQL FGKSYKECVC KISSDCELPR WHMHDFFPSF LIVFRVLCGE WIETMWDCME
VAGQTMCLIV FMLVMVIGNL VVLNLFLALL LSSFSSDNLA ATDDDNEMNN LQIAVARIQK
GIDYVKKKIQ EFIQKAFVRK QKSLEEIKAL EELNNKKDSC ISNHTAVEIS KDLNYLKDGN
GTTSGVGTGS SVEKYVIDEN DYMSFINNPG LTVTVPIAVG ESDFENLNTE EFSSESDMEE
SKQKLNASSS SEGSTVDIAP PGEGEQAEIE SEEALEPEAC FTEGCVQKFP CCQVSIEDGK
GKTWWNLRKT CYSIVEHNWF ETFIVFMILL SSGALAFEDI YIEQRKTIKT MLEYADKVFT
YIFILEMLLK WVAYGFQIYF TNAWCWLDFL IVDVSLVSLI ANALGYSELG AIKSLRTLRA
LRPLRALSRF EGMRVVVNAL VGAIPSIMNV LLVCLIFWLI FSIMGVNLFA GKFYHCVNTT
TGEMFDISDV NNYTQCQELI KNNQSARWKN VKVNFDNVGA GYLALLQVAT FKGWMDIMYA
AVDSRDVEDQ PKYEDNLYMY LYFVIFIIFG SFFTLNLFIG VIIDNFNQQK KKISQDIFMT
EEQKKYYNAM KKLGSKKPQK PIPRPVNKFQ GMIFDFVTKQ VFDISIMILI CLNMVTMMVE
TDDQSKEMET ILSRINLVFI ILFTGEFVLK LISLRHYYFT IGWNIFDFVV VILSIVGMFL
AEMIEKYFVS PTLFRVIRLA RIGRILRLIK GAKGIRTLLF ALMMSLPALF NIGLLLFLVM
FIYAIFGMSN FAYVKREVGI DDMFNFETFG NSMICLFQIT TSAGWDGLLA PILNSGEPDC
DPHKDHPGSS VKGDCGNPSV GIFFFVSYII ISFLVVVNMY IAVILENFSV ATEESAEPLS
EDDFEMFYEV WEKFDPDATQ FIEYSKLSDF AASLDPPLLI AKPNKVQLIA MDLPMVSGDR
IHCLDILFAF TKRVLGESGE MDALRIQMED RFMAANPSKV SYEPITTTLK RKQEEVSAVI
IQRAYRCYLL RQKVKQVSSM YNRNKNKEGD GQVIKEIIID KLKGNSTPEK TDESSSTTSP
PSYDSVTKPD KEKYEKDKAE KNYKGKDIRE NKK
//