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Database: UniProt
Entry: SC4AB_TAKRU
LinkDB: SC4AB_TAKRU
Original site: SC4AB_TAKRU 
ID   SC4AB_TAKRU             Reviewed;        1719 AA.
AC   Q2XVR6;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-OCT-2017, entry version 68.
DE   RecName: Full=Sodium channel protein type 4 subunit alpha B;
DE   AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.4b;
GN   Name=scn4ab; Synonyms=nav1.4b;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae;
OC   Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16303569; DOI=10.1016/j.cub.2005.10.068;
RA   Venkatesh B., Lu S.Q., Dandona N., See S.L., Brenner S., Soong T.W.;
RT   "Genetic basis of tetrodotoxin resistance in pufferfishes.";
RL   Curr. Biol. 15:2069-2072(2005).
CC   -!- FUNCTION: This protein mediates the voltage-dependent sodium ion
CC       permeability of excitable membranes. Assuming opened or closed
CC       conformations in response to the voltage difference across the
CC       membrane, the protein forms a sodium-selective channel through
CC       which Na(+) ions may pass in accordance with their electrochemical
CC       gradient. This sodium channel may be present in both denervated
CC       and innervated skeletal muscle.
CC   -!- SUBUNIT: Muscle sodium channels contain an alpha subunit and a
CC       smaller beta subunit.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:P35499}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:D0E0C2}.
CC   -!- DOMAIN: The sequence contains 4 internal repeats, each with 5
CC       hydrophobic segments (S1, S2, S3, S5, S6) and one positively
CC       charged segment (S4). Segments S4 are probably the voltage-sensors
CC       and are characterized by a series of positively charged amino
CC       acids at every third position. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC       Nav1.4/SCN4A subfamily. {ECO:0000305}.
DR   EMBL; DQ221250; ABB29442.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q2XVR6; -.
DR   HOGENOM; HOG000231755; -.
DR   InParanoid; Q2XVR6; -.
DR   Proteomes; UP000005226; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:InterPro.
DR   GO; GO:0005248; F:voltage-gated sodium channel activity; IBA:GO_Central.
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   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR028817; Na_channel_a4suB.
DR   InterPro; IPR001696; Na_channel_asu.
DR   InterPro; IPR010526; Na_trans_assoc.
DR   PANTHER; PTHR10037:SF186; PTHR10037:SF186; 2.
DR   Pfam; PF00520; Ion_trans; 4.
DR   Pfam; PF06512; Na_trans_assoc; 1.
DR   PRINTS; PR00170; NACHANNEL.
PE   3: Inferred from homology;
KW   Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
KW   Ion channel; Ion transport; Membrane; Reference proteome; Repeat;
KW   Sodium; Sodium channel; Sodium transport; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1   1719       Sodium channel protein type 4 subunit
FT                                alpha B.
FT                                /FTId=PRO_0000371320.
FT   TOPO_DOM      1    126       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    127    145       Helical; Name=S1 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    146    152       Extracellular. {ECO:0000305}.
FT   TRANSMEM    153    173       Helical; Name=S2 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    174    187       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    188    205       Helical; Name=S3 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    206    211       Extracellular. {ECO:0000305}.
FT   TRANSMEM    212    228       Helical; Name=S4 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    229    247       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    248    267       Helical; Name=S5 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    268    368       Extracellular. {ECO:0000305}.
FT   INTRAMEM    369    393       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    394    400       Extracellular. {ECO:0000305}.
FT   TRANSMEM    401    421       Helical; Name=S6 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    422    513       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    514    532       Helical; Name=S1 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    533    543       Extracellular. {ECO:0000305}.
FT   TRANSMEM    544    563       Helical; Name=S2 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    564    577       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    578    597       Helical; Name=S3 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    598    599       Extracellular. {ECO:0000305}.
FT   TRANSMEM    600    617       Helical; Name=S4 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    618    633       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    634    652       Helical; Name=S5 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    653    681       Extracellular. {ECO:0000305}.
FT   INTRAMEM    682    702       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    703    715       Extracellular. {ECO:0000305}.
FT   TRANSMEM    716    736       Helical; Name=S6 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    737    919       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    920    937       Helical; Name=S1 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    938    950       Extracellular. {ECO:0000305}.
FT   TRANSMEM    951    969       Helical; Name=S2 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    970    983       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    984   1002       Helical; Name=S3 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1003   1010       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1011   1029       Helical; Name=S4 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1030   1046       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1047   1066       Helical; Name=S5 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1067   1119       Extracellular. {ECO:0000305}.
FT   INTRAMEM   1120   1141       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1142   1158       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1159   1180       Helical; Name=S6 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1181   1243       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1244   1261       Helical; Name=S1 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1262   1272       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1273   1291       Helical; Name=S2 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1292   1303       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1304   1321       Helical; Name=S3 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1322   1334       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1335   1351       Helical; Name=S4 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1352   1370       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1371   1388       Helical; Name=S5 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1389   1410       Extracellular. {ECO:0000305}.
FT   INTRAMEM   1411   1433       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1434   1462       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1463   1485       Helical; Name=S6 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1486   1719       Cytoplasmic. {ECO:0000305}.
FT   REPEAT      108    431       I. {ECO:0000305}.
FT   REPEAT      495    766       II. {ECO:0000305}.
FT   REPEAT      900   1215       III. {ECO:0000305}.
FT   REPEAT     1224   1521       IV. {ECO:0000305}.
FT   DOMAIN     1615   1644       IQ.
FT   CARBOHYD    209    209       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    285    285       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    339    339       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1078   1078       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1092   1092       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    275    346       {ECO:0000250|UniProtKB:D0E0C2}.
FT   DISULFID    664    664       Interchain; with SCN2B or SCN4B.
FT                                {ECO:0000250|UniProtKB:P04775}.
FT   DISULFID    704    713       {ECO:0000250|UniProtKB:D0E0C2}.
SQ   SEQUENCE   1719 AA;  196480 MW;  49822B75EAEECE41 CRC64;
     MRTLLPPVGS EVFRRFTQSS LNEIQQKQQI REEERKRTNA QVSEELPEPA SDLEAGKPLP
     FIYGEPPHEL LNVPLEDIDP FYQSQKTFIV LSKGNIIYRF NAESSLYLLS PFNALRIVAI
     KILIHSLFSL FIMATILTNC AFMTLSDPPA WSKTMEYVFT FIYTFEATIK ILSRGFCVGK
     FTFLKDPWNW LDFMVISMAY LTELVDLGNV SVLRTFRVLR ALKTITVIPG LKTIVGALIQ
     SVRKLADAMV LTVFCLSVFA LIGLQLFMGN LRQKCVLIPQ WLYGNLTFDI NSTNGYYGND
     THDNGTKSKH LEFEFERHIN NPDNYYYLTG QGDPLLCGNS SDAGVCPESY VCLKVGANPN
     YGYTSYDSFG WAFLALFRLM TQDFWENLFQ LTLRTAGKTY MIFFVVVIFL GSFYLINLIL
     AVVAMAYAEQ NEATLAEAKE KEEEYIHILE ALKKREEEQA ARKEPHSTVE GFEDDHRLCP
     PCWYAFANIF LKWDCCGCWR HLKECLYAIV MDPFVDLGIT ICIILNTVFM AMEHYPMSAD
     FEELLSVGNL VFTGIFTGEM VFKILAMDPY FYFQVGWNIF DSIIVTISLV ELGLANVQGL
     SVLRSFRLMR VFKLAKSWPT LNMLIKIIGN SVGALGNLTL VLAIIVFIFA VVGMQLFGKN
     YKDCVCRISE DCVLPRWHMN DFFHAFLIIF RVLCGEWIES MWDCMEVSGQ TMCLIVFMMV
     LVIGNLVVLN LFLALLLSSF SGDNLTTQDD EGENNLQIAI NRINRAMSWT KTYILLYVYT
     LTESNLNQHF AVSDDEEQRR VKDILALTSV SSDKLVSHHC GNDFFRVPIA EAESDSDDSD
     YDEDKDSQCD ESSVCSSVQK PEVQEEEMDE NCVAKTPTDC WTKKCYSRCP FLDIDTSQGR
     GKIWCNIRRT CFSIVENNYF ESFIVFMILL SSGALAFEDI YLEKHQLIKS ILEYADKVFT
     YVFVMEMVLK WFAYGFKSYF SNAWCWLDFL IVDVSLVSLT ANILGYSELG AIKSLRTLRA
     LRPLRALSRF EGMRVVVNAL VGAVPSIFNV LLVCLIFWLI FSIMGVNLFA GKFSYCFNET
     SQEIIDTKVV DNKTECIALI KANFTEVRWK NVKVNYDNVG IGYLSLLQVA TFKGWTDIMY
     AAVDSRDVES QPIYEVNLYM YLYFVIFIIF GSFFTLNLFI GVIIDNFNQQ KAKLGGQDIF
     MTEEQKKYYN AMKKLGSKKP QKPVPRPENP FQGLVFDLVT KQIFDVFIMV LICLNMVTMM
     VETDEQSDKK EEVLYWINVV FILIFTTECT LKIIALRRHY FSIGWNIFDF VVVILSILGL
     LLADIIEKYF VSPTLFRVIR LARIGRVLRL IRGAKGIRTL LFALMMSLPA LFNIGLLLFL
     IMFIFSIFGM SNFAYVKKEA LIDDMFNFET FGNSMICLFM ITTSAGWDGL LSPIMNTPPD
     CDPNVENPGT TVRGNCGSPA IGIAFFSTYI IMSFLVVVNM FIAIILENFN VATEESSDPL
     CEDDFEMFYE TWEKFDPDAS QFIQYSKLSD FCDTLKEPLR IPQPNTIKLI SMDLPLVPGD
     RIHCMDILLA LTAEVLGDSD EMDTLKATME EKFMANNPSK VSYEPISSTL LRKEEEVAAT
     VIQRAYRKYL LLRTVRLASF MYREKTEGRG KEKAPETTGL LCKQFSQLYG FNKETDEPLQ
     SKANRLGQVE LQSEVLLHAV PPLRSSEFLQ ERDQRETSV
//
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