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-MAY-2022, entry version 85.
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; 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: Pore-forming subunit of a voltage-gated sodium channel
CC complex through which Na(+) ions pass in accordance with their
CC electrochemical gradient. Alternates between resting, activated and
CC inactivated states. Required for normal muscle fiber excitability,
CC normal muscle contraction and relaxation cycles.
CC {ECO:0000250|UniProtKB:P35499}.
CC -!- ACTIVITY REGULATION: Channel activity is regulated by ancillary beta
CC subunits. Interaction with a beta subunit is required for rapid channel
CC inactivation and rapid recovery after inactivation, and prevents
CC decrease of channel activity in response to repetitive, high-frequency
CC depolarizations. {ECO:0000250|UniProtKB:P15390}.
CC -!- SUBUNIT: Component of a voltage-sensitive sodium channel complex that
CC consists of a pore-forming alpha subunit and one or more regulatory
CC beta subunits. {ECO:0000250|UniProtKB:P15390}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15390};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P35499}.
CC -!- DOMAIN: The sequence contains 4 internal repeats, each with 5
CC hydrophobic segments (S1, S2, S3, S5, S6) and one positively charged
CC segment (S4). Segments S4 are probably the voltage-sensors and are
CC characterized by a series of positively charged amino acids at every
CC third position. {ECO:0000250|UniProtKB:P35499}.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC Nav1.4/SCN4A subfamily. {ECO:0000305}.
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DR EMBL; DQ221250; ABB29442.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2XVR6; -.
DR SMR; Q2XVR6; -.
DR eggNOG; KOG2301; Eukaryota.
DR InParanoid; Q2XVR6; -.
DR Proteomes; UP000005226; Unplaced.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:InterPro.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR CDD; cd13433; Na_channel_gate; 1.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR001696; Na_channel_asu.
DR InterPro; IPR044564; Na_chnl_inactivation_gate.
DR InterPro; IPR010526; Na_trans_assoc.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037; PTHR10037; 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; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Membrane; Reference proteome; Repeat; Sodium; Sodium channel;
KW Sodium transport; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..1719
FT /note="Sodium channel protein type 4 subunit alpha B"
FT /id="PRO_0000371320"
FT TOPO_DOM 1..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 127..145
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 146..152
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 153..173
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 174..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 188..205
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 206..211
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 212..228
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 229..247
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 248..267
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 268..368
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 369..393
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 394..400
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 401..421
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 422..513
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 514..532
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 533..543
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 544..563
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 564..577
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 578..597
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 598..599
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 600..617
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 618..633
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 634..652
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 653..681
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 682..702
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 703..713
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 714..732
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 733..919
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 920..937
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 938..950
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 951..969
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 970..983
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 984..1002
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1003..1010
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1011..1029
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1030..1046
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1047..1066
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1067..1119
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1120..1141
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1142..1158
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1159..1180
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1181..1243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1244..1261
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1262..1272
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1273..1291
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1292..1303
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1304..1321
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1322..1334
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1335..1351
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1352..1370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1371..1388
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1389..1410
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1411..1433
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1434..1462
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1463..1485
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1486..1719
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 108..431
FT /note="I"
FT /evidence="ECO:0000305"
FT REPEAT 495..766
FT /note="II"
FT /evidence="ECO:0000305"
FT REPEAT 900..1215
FT /note="III"
FT /evidence="ECO:0000305"
FT REPEAT 1224..1521
FT /note="IV"
FT /evidence="ECO:0000305"
FT DOMAIN 1615..1644
FT /note="IQ"
FT REGION 28..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1199..1201
FT /note="Important for rapid channel inactivation"
FT /evidence="ECO:0000250|UniProtKB:P15390"
FT COMPBIAS 28..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1078
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1092
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 275..337
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT DISULFID 346..352
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT DISULFID 666..672
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT DISULFID 704..713
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT DISULFID 1076..1096
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT DISULFID 1441..1456
FT /evidence="ECO:0000250|UniProtKB:P35499"
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
