SC4AB_TETNG
ID SC4AB_TETNG Reviewed; 1715 AA.
AC Q2XVR4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 72.
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 Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883;
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; DQ221252; ABB29444.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2XVR4; -.
DR SMR; Q2XVR4; -.
DR STRING; 99883.ENSTNIP00000001759; -.
DR InParanoid; Q2XVR4; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
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..1715
FT /note="Sodium channel protein type 4 subunit alpha B"
FT /id="PRO_0000371322"
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..515
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 516..534
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 535..545
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 546..565
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 566..579
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 580..599
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 600..601
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 602..619
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 620..635
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 636..654
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 655..683
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 684..704
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 705..715
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 716..734
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 735..915
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 916..933
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 934..946
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 947..965
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 966..979
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 980..998
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 999..1006
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1007..1025
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1026..1042
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1043..1062
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1063..1115
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1116..1137
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1138..1154
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1155..1176
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1177..1239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1240..1257
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1258..1268
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1269..1287
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1288..1299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1300..1317
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1318..1330
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1331..1347
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1348..1366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1367..1384
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1385..1406
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1407..1429
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1430..1458
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1459..1481
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1482..1715
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 108..431
FT /note="I"
FT /evidence="ECO:0000305"
FT REPEAT 497..768
FT /note="II"
FT /evidence="ECO:0000305"
FT REPEAT 896..1211
FT /note="III"
FT /evidence="ECO:0000305"
FT REPEAT 1220..1517
FT /note="IV"
FT /evidence="ECO:0000305"
FT DOMAIN 1611..1640
FT /note="IQ"
FT REGION 824..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1195..1197
FT /note="Important for rapid channel inactivation"
FT /evidence="ECO:0000250|UniProtKB:P15390"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
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 1074
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1088
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 668..674
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT DISULFID 706..715
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT DISULFID 1072..1092
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT DISULFID 1437..1452
FT /evidence="ECO:0000250|UniProtKB:P35499"
SQ SEQUENCE 1715 AA; 195825 MW; 31F8A2378353FF6C CRC64;
MGTLLPPVGS EVFRRFTPSS LNEIQQRQQI KEERKRANAE VSEELFSEPA SDLEAGKPLP
FIYGEPPHEL LNVPLEDMDP FYQSQKTFIV LSKGNVIHRF NAESSLYLLS PFNSMRIFAI
KILVHSLFSL FIMATILTNC VFMTLSDPPA WSKTVEYVFT FIYTFEATIK VVSRGFCVGQ
FTFLKDPWNW LDFMVISMAY LTELVDLGNV SVLRTFRVLR ALKTITVIPG LKTIVGALIQ
SVKKLADAMV LTVFCLSVFA LIGLQLFMGN LRQKCVLIPP VVSNLTFEVT NSSHGYFGND
TRGNDTENKD LMFEFEEHIN NPDNYYYLAG QRDPLLCGNS SDAGVCPESY ICLKVGRNPN
YGYTSYDSFG WAFLALFRLM TQDFWENLFQ LTLRAAGKTY MIFFVVVIFL GSFYLINLIL
AVVAMAYAEQ NQATMAEAKQ KEEEYLHILE ALKKREEEQA AWKEALKVQE PHNFEDDHKL
CPPCWYAFAN VFLKWDCCSC WRHLKRCLSA IVMDPFVDLG ITICIILNTI FMAMEHYPMS
ADFEELLSVG NLVFTGIFTC EMVLKILAMD PYFYFQVGWN IFDSIIVTMS LVELGLANVQ
GLSVLRSFRL MRVFKLAKSW PTLNMLIKII GNSVGALGNL TLVLAIIVFI FAVVGMQLFG
KNYKDCVCRI SEDCKLPRWH MNDFFHAFLI IFRVLCGEWI DTMWDCMEVS GQTMCLIVYM
MVLVIGNLVV LNLFLALLLS SFSGDNLAAQ DDEGENNLQI AVNRIKRAVA WAKTWILLHL
CILTESNHNQ HDAVSDEEEN RITKNILALT SVTSDQFFKV PIAEAESDSE DSDDDDVDED
KHSRCDESSF CSTVQDPEVK ENEADEDNVS KMPMDCWSEN CYSRCPSLDI DTSQGKGKVW
CNIRRACFII VENNYFESFI VFMILLSSGA LAFEDIYLEK HQLIKTILEY ADKVFTYVFV
VEMVLKWFAY GFKSYFSNAW CWLDFLIVDV SLVSLTANIL GYSELGAIKS LRTLRALRPL
RALSRFEGMR VVVNALVGAV PSIFNVLLVC LIFWLIFSIM GVNLFAGKFS YCFNETSQEQ
FDKKIVNNKT ECIALIEANF TEVRWKNLKV NYDNVGIGYL SLLQVATFKG WMEIMYAAVD
SRDVESQPIY EVNIYMYLYF VIFIIFGSFF TLNLFIGVII DNFNQQKAKL GGQDIFMTEE
QKKYYNAMKK LGSKKPQKPV PRPENALQGL VFDLVTKQIF DVFIMVLICL NMVTMMVETD
EQTKEKEDIL YWINVIFIVI FTTECILKTI ALRRHYFSIG WNVFDFVVVI LSILGLLLAD
IIEKYFVSPT LFRVIRLARI GRVLRLIRGA KGIRTLLFAL MMSLPALFNI GLLLFLIMFI
FSIFGMSNFA YVKKEAMIDD MFNFETFGNS MICLFMITTS AGWDGLLSPI MNKPPDCDPD
LENPGTTVRG NCGSPAIGIV FFSTYIIMSF LVVVNMYIAI ILENFNVATE ESSDPLCEDD
FDMFYETWEK FDPDATQFIQ YSKLSDFCDT LKEPLRIPKP NTIKLISLDL PLVPGDKIHC
MDILLALTAE VLGDSDEMDT LKATMEEKFM ANNPSKVSYE PISSTLRRKE EEVAARVIQR
AYRKYLLQRT VRLASFTYRE KTEGWGTKKA PETEGLLCKQ FNQLFGNKRE TEEPLMSKND
ELGQVELQSE VLLHAAPPLN TLELLLGTSE RESLV
