SC4AA_TETNG
ID SC4AA_TETNG Reviewed; 1863 AA.
AC Q2XVR5;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 2.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Sodium channel protein type 4 subunit alpha A;
DE AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.4a;
GN Name=scn4aa; Synonyms=nav1.4a;
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; DQ221251; ABB29443.2; -; Genomic_DNA.
DR AlphaFoldDB; Q2XVR5; -.
DR SMR; Q2XVR5; -.
DR STRING; 99883.ENSTNIP00000000434; -.
DR PRIDE; Q2XVR5; -.
DR InParanoid; Q2XVR5; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; 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; IPR002048; EF_hand_dom.
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.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037; PTHR10037; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR Pfam; PF06512; Na_trans_assoc; 1.
DR PRINTS; PR00170; NACHANNEL.
DR PROSITE; PS50096; IQ; 1.
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..1863
FT /note="Sodium channel protein type 4 subunit alpha A"
FT /id="PRO_0000371321"
FT TOPO_DOM 1..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 126..140
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 141..147
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 148..168
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 169..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 183..200
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 201..206
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 207..223
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 224..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 243..262
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 263..361
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 362..386
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 387..393
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 394..414
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 415..592
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 593..611
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 612..622
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 623..642
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 643..656
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 657..676
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 677..678
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 679..696
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 697..712
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 713..731
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 732..760
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 761..781
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 782..792
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 793..811
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 812..1051
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1052..1069
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1070..1082
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1083..1101
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1102..1115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1116..1134
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1135..1142
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1143..1161
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1162..1178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1179..1198
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1199..1250
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1251..1272
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1273..1289
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1290..1311
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1312..1374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1375..1392
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1393..1403
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1404..1422
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1423..1434
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1435..1452
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1453..1465
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1466..1482
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1483..1501
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1502..1519
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1520..1541
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1542..1564
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1565..1594
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1595..1617
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1618..1863
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 107..424
FT /note="I"
FT /evidence="ECO:0000305"
FT REPEAT 574..846
FT /note="II"
FT /evidence="ECO:0000305"
FT REPEAT 1032..1346
FT /note="III"
FT /evidence="ECO:0000305"
FT REPEAT 1355..1653
FT /note="IV"
FT /evidence="ECO:0000305"
FT DOMAIN 1747..1776
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 28..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 982..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1330..1332
FT /note="Important for rapid channel inactivation"
FT /evidence="ECO:0000250|UniProtKB:P15390"
FT REGION 1771..1834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..949
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1776..1793
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1802..1816
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 270..330
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT DISULFID 339..345
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT DISULFID 745..751
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT DISULFID 783..792
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT DISULFID 1208..1228
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT DISULFID 1573..1588
FT /evidence="ECO:0000250|UniProtKB:P35499"
SQ SEQUENCE 1863 AA; 210434 MW; 26A0EF6467ABE847 CRC64;
MATILPPPGT AMFRHFTPQS LAKIERLKEE TKKAAEVGPR EEEEPPTPNP DLEAGKGLPR
IYGEPPAELL STPLEDLDPF YKAQKTFVVI TKGNTIYRFN AEPACYILSP FSRVRRGAIK
ILIHSLIMIT ILSNCVFMTM SNPPAWSKTV EYVFTGIYTF EATVKVLSRG FCVGPFTFLR
DPWNWLDFMV ISMAYITEFV DLGNVSALRT FRVLRALKTI TVIPGLKTIV AALIQSVKKM
VDVMILTVFA LSVFALVGLQ LFMGNLRHKC IRWPVAANQS AFEPFNSTVG NDTTGLNDTL
FSNITFDFTE YIENAENQYF LPGSADALLC GNSSDAGRCP EGYECMKAGR NPNYGYTSFD
SFGWAFLALF RLMTQDCWEN LFQQTLRAAG KTYMLFFVVV IFLGSFYLIN LILAVVAMAY
EEQNQASQQE AREKEEEFQW LLEQLKNQEQ AQVLGSRASP TSEKSVSLTT SDAPDEDQSL
ENDEALKDCN GRFIPRLIVR APTMKESAAD YESGEKVEGS THSRLHVEDA GLKQRSASAV
TVLTAAAVEE LEEAQRPCPP IWYKFANMFL KWNCCQPWAV FKEWVHFVVM DPFVDLAITI
CIVLNTLFMA MEHYPMTQEF DYMLSVGNLV FTGIFAAEMF FKLIAMDPYY YFQVGWNIFD
SIIVTLSLVE LGLANVQGLS VLRSFRLLRV FKLAKSWPTL NMLIKIIGSS VGALGNLTLV
LAIIVFIFAV VGMQLFGKSY KDCVCKISTE CELPRWHMND FFHSFLIVFR ILCGEWIENM
WACMEVAGAG MCLVVFMMVM VIGNLVVLNL FLALLLSSFS GDNLSIGEDD GEMNNLQIAI
GRITRGGNWL KTLVIRTVLQ LLGREQGKPA EEDPAEEGEQ KPERIEMNHL DQLKTADGIA
NCLVGRQPSG TAADGESVIN VPIALGESDS EHQSEGDDYQ EDDVDSESTC EENEHGSNSM
EDGFGVLQHV KLMGALTDGE SSVCSTADYR PPEPETLEEE EEEPEPLEPE ACFTDNCVKH
WPCLNVDVTQ GQGKKWWNLR KTCFTIVEHD WFETFIIFMI LLSSGALAFE DIYIERRRTV
KIILEFADKV FTFIFVLEMV LKWVAYGFKT YFTNAWCWLD FFIVDISLIS LSANLMGLSD
LGPIKSLRTL RALRPLRALS RFEGMRVVVN ALIGAIPSIF NVLLVCLIFW LIFSIMGVNL
FAGKFYHCIN TTTQELFPIS VVNNKSDCMA VQEATQEARW VNVKVNYDNV GKGYLSLLQI
ATFKGWTAIM YAAVDSREVE EQPSYEINLY MYIYFVIFII FGAFFTLNLF IGVIIDNFNQ
QKRKLGDKDI FMTEEQKKYY EAMKKLGSKK PQKPIPRPTN LIQGMVFDFI SQQFFDIFIM
VLICLNMVTM MVETDDQSPE KEDFLFKVNV AFIVVFTGEC MLKLIALRQY FFTNGWNIFD
FVVVILSIAG TMLSDLIEKY FVSPTLFRVI RLARIGRILR LIKGARGIRT LLFALMMSLP
ALFNIGLLLF LIMFIFSIFG MSNFAYVKKE AGIDDMFNFE TFGSSIICLF QITTSGGWDQ
ILLPILNKEP PDCDPTLENP GTDVKGNCGN PMVGMMFFCS YIIISFLVVV NMYIAIILEN
FNVAQEESGD ALCEEDFEMF NETWEKFDTG GTQFIEYSQL SDFCDTLQEP LRVAKPNRLR
LIEMDLPLVI GDRIHCVDVL LAVTQEVLGD TIEMVAMRES IEAKFNLNNP TSVSYAPITT
TVRQKEEEMA AVVIQRAYRN HLHKRGIHHA AYIQRSKTGR KADSEDAPEK EGLLAEKMGA
LYGREAEGRE RAPDPETPPR CSGARCGPEP PEPNVIVVPV EITNEFLLHS APPTHTSYPR
RQT
