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Sodium channel protein type 4 subunit alpha A (Voltage-gated sodium channel subunit alpha Nav1.4a)

 SC4AA_DANRE             Reviewed;        1829 AA.
Q2XVR3; Q20JQ6;
05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
07-FEB-2006, sequence version 2.
23-MAY-2018, entry version 86.
RecName: Full=Sodium channel protein type 4 subunit alpha A;
AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.4a;
Name=scn4aa; Synonyms=nav1.4a;
Danio rerio (Zebrafish) (Brachydanio rerio).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Danio.
NCBI_TaxID=7955;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=16830092; DOI=10.1007/s00239-005-0287-9;
Novak A.E., Jost M.C., Lu Y., Taylor A.D., Zakon H.H., Ribera A.B.;
"Gene duplications and evolution of vertebrate voltage-gated sodium
channels.";
J. Mol. Evol. 63:208-221(2006).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=16303569; DOI=10.1016/j.cub.2005.10.068;
Venkatesh B., Lu S.Q., Dandona N., See S.L., Brenner S., Soong T.W.;
"Genetic basis of tetrodotoxin resistance in pufferfishes.";
Curr. Biol. 15:2069-2072(2005).
-!- FUNCTION: This protein mediates the voltage-dependent sodium ion
permeability of excitable membranes. Assuming opened or closed
conformations in response to the voltage difference across the
membrane, the protein forms a sodium-selective channel through
which Na(+) ions may pass in accordance with their electrochemical
gradient. This sodium channel may be present in both denervated
and innervated skeletal muscle.
-!- SUBUNIT: Muscle sodium channels contain an alpha subunit and a
smaller beta subunit.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P35499}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:D0E0C2}.
-!- TISSUE SPECIFICITY: Expressed in skeletal muscle, brain, spinal
cord, and eye. {ECO:0000269|PubMed:16830092}.
-!- DOMAIN: The sequence contains 4 internal repeats, each with 5
hydrophobic segments (S1, S2, S3, S5, S6) and one positively
charged segment (S4). Segments S4 are probably the voltage-sensors
and are characterized by a series of positively charged amino
acids at every third position. {ECO:0000305}.
-!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
Nav1.4/SCN4A subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; DQ149506; ABA54921.1; -; mRNA.
EMBL; DQ221253; ABB29445.2; -; Genomic_DNA.
RefSeq; NP_001034914.1; NM_001039825.1.
UniGene; Dr.117129; -.
ProteinModelPortal; Q2XVR3; -.
STRING; 7955.ENSDARP00000097312; -.
PaxDb; Q2XVR3; -.
PRIDE; Q2XVR3; -.
GeneID; 572442; -.
KEGG; dre:572442; -.
CTD; 572442; -.
ZFIN; ZDB-GENE-051201-2; scn4aa.
eggNOG; KOG2301; Eukaryota.
eggNOG; ENOG410XNP6; LUCA.
HOGENOM; HOG000231755; -.
InParanoid; Q2XVR3; -.
KO; K04837; -.
PhylomeDB; Q2XVR3; -.
PRO; PR:Q2XVR3; -.
Proteomes; UP000000437; Unplaced.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:InterPro.
GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
GO; GO:0005248; F:voltage-gated sodium channel activity; IBA:GO_Central.
GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
Gene3D; 1.20.120.350; -; 4.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR000048; IQ_motif_EF-hand-BS.
InterPro; IPR001696; Na_channel_asu.
InterPro; IPR010526; Na_trans_assoc.
InterPro; IPR027359; Volt_channel_dom_sf.
Pfam; PF00520; Ion_trans; 4.
Pfam; PF06512; Na_trans_assoc; 1.
PRINTS; PR00170; NACHANNEL.
PROSITE; PS50096; IQ; 1.
2: Evidence at transcript level;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
Ion channel; Ion transport; Membrane; Reference proteome; Repeat;
Sodium; Sodium channel; Sodium transport; Transmembrane;
Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1 1829 Sodium channel protein type 4 subunit
alpha A.
/FTId=PRO_0000371317.
TOPO_DOM 1 124 Cytoplasmic. {ECO:0000305}.
TRANSMEM 125 143 Helical; Name=S1 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 144 150 Extracellular. {ECO:0000305}.
TRANSMEM 151 171 Helical; Name=S2 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 172 185 Cytoplasmic. {ECO:0000305}.
TRANSMEM 186 203 Helical; Name=S3 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 204 209 Extracellular. {ECO:0000305}.
TRANSMEM 210 226 Helical; Name=S4 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 227 245 Cytoplasmic. {ECO:0000305}.
TRANSMEM 246 265 Helical; Name=S5 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 266 358 Extracellular. {ECO:0000305}.
INTRAMEM 359 383 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 384 390 Extracellular. {ECO:0000305}.
TRANSMEM 391 411 Helical; Name=S6 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 412 582 Cytoplasmic. {ECO:0000305}.
TRANSMEM 583 601 Helical; Name=S1 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 602 612 Extracellular. {ECO:0000305}.
TRANSMEM 613 632 Helical; Name=S2 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 633 646 Cytoplasmic. {ECO:0000305}.
TRANSMEM 647 666 Helical; Name=S3 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 667 668 Extracellular. {ECO:0000305}.
TRANSMEM 669 686 Helical; Name=S4 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 687 702 Cytoplasmic. {ECO:0000305}.
TRANSMEM 703 721 Helical; Name=S5 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 722 750 Extracellular. {ECO:0000305}.
INTRAMEM 751 771 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 772 784 Extracellular. {ECO:0000305}.
TRANSMEM 785 805 Helical; Name=S6 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 806 998 Cytoplasmic. {ECO:0000305}.
TRANSMEM 999 1016 Helical; Name=S1 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1017 1029 Extracellular. {ECO:0000305}.
TRANSMEM 1030 1048 Helical; Name=S2 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1049 1062 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1063 1081 Helical; Name=S3 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1082 1089 Extracellular. {ECO:0000305}.
TRANSMEM 1090 1108 Helical; Name=S4 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1109 1125 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1126 1145 Helical; Name=S5 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1146 1196 Extracellular. {ECO:0000305}.
INTRAMEM 1197 1218 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1219 1235 Extracellular. {ECO:0000305}.
TRANSMEM 1236 1257 Helical; Name=S6 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1258 1320 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1321 1338 Helical; Name=S1 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1339 1349 Extracellular. {ECO:0000305}.
TRANSMEM 1350 1368 Helical; Name=S2 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1369 1380 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1381 1398 Helical; Name=S3 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1399 1411 Extracellular. {ECO:0000305}.
TRANSMEM 1412 1428 Helical; Name=S4 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1429 1447 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1448 1465 Helical; Name=S5 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1466 1487 Extracellular. {ECO:0000305}.
INTRAMEM 1488 1510 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1511 1540 Extracellular. {ECO:0000305}.
TRANSMEM 1541 1563 Helical; Name=S6 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1564 1829 Cytoplasmic. {ECO:0000305}.
REPEAT 106 421 I. {ECO:0000305}.
REPEAT 564 836 II. {ECO:0000305}.
REPEAT 979 1292 III. {ECO:0000305}.
REPEAT 1301 1599 IV. {ECO:0000305}.
DOMAIN 1693 1722 IQ. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
CARBOHYD 207 207 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 280 280 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 293 293 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 329 329 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1157 1157 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1171 1171 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 273 336 {ECO:0000250|UniProtKB:D0E0C2}.
DISULFID 733 733 Interchain; with SCN2B or SCN4B.
{ECO:0000250|UniProtKB:P04775}.
DISULFID 773 782 {ECO:0000250|UniProtKB:D0E0C2}.
CONFLICT 310 310 N -> S (in Ref. 1; ABA54921).
{ECO:0000305}.
CONFLICT 1054 1054 Missing (in Ref. 1; ABA54921).
{ECO:0000305}.
CONFLICT 1305 1305 Missing (in Ref. 1; ABA54921).
{ECO:0000305}.
CONFLICT 1721 1721 R -> Q (in Ref. 1; ABA54921).
{ECO:0000305}.
CONFLICT 1811 1811 I -> T (in Ref. 1; ABA54921).
{ECO:0000305}.
CONFLICT 1815 1815 L -> F (in Ref. 1; ABA54921).
{ECO:0000305}.
SEQUENCE 1829 AA; 207737 MW; D68901979E1D5842 CRC64;
MARLLPPTGT SVFRRFTPES LVEIERLIQE KSTREELEGA EEEPQAPSSD LEAGKCLPMI
YGDPPGDLLN TPLEDIDPFY KTQKTFIVIS KGNTIFRFSS EPAMFCISPF SIVRRGAIKI
LIHSLFSMFI MITILSNCVF MTMSNPPAWS KTVEYVFTGI YTFEATVKVL SRGFCIGPFT
FLRDPWNWLD FMVISMAYVT EFVDLGNVSA LRTFRVLRAL KTITVIPGLK TIVGALIQSV
KKMIDVMILT IFALAVFALI GLQLFMGNLR QKCIRWPILN STIFDVYNSN MVNDTTLNVT
DTFDFKAYIN NEENQYFLEG SLDALLCGNS SDAGRCPEGY TCMKAGRNPN YGYTSYDNFG
WAFLALFRLM TQDFWENLFQ LTLRAAGKTY MIFFVVVIFL GSFYLINLIL AVVAMAYDEQ
NEATLAEARD KEEEFQRLLE QLKNQETGSK ASLASQKTQS RGSNRTGSLH DLADEDVIKD
CNGRIVPRLI VNRVSSNKEL SAEEDQKSLS SKHSMQYLDQ PKLSKRTASA LSVLTATMEG
LEDAQRPCPP GWYKFADMFL KWDCCAPWIL FKKWVHFVVM DPFVDLGITI CIVLNTLFMA
MEHYPMSPHF EHVLSVGNLV FTGIFTAEMV FKLIAMDPYY YFQVGWNIFD SIIVTLSLVE
LGLANVQGLS VLRSFRLLRV FKLAKSWPTL NMLIKIIGNS VGALGNLTLV LAIIVFIFAV
VGMQLFGKSY KDCVCKISED CELPRWHMND FFHSFLIVFR ILCGEWIETM WDCMEVAGAS
MCLIVFMMVM VIGNLVVLNL FLALLLSSFS GDNLSGGDDD GEMNNLQIAI GRITRGIDWV
KALVASMVQR ILGKKPDNTK EEGEGDIELY ALNHLDEGKM ADGLTNCLSP TLTVPIARCE
SDVEEDEDSE SSDEEDAKAT LNDGDSSVCS TVDYQPPEPE PEPEEVEEEE PEPEEPEACF
TEGCIRRCAC LSVDITEGWG KKWWNLRRTC FTIVEHDYFE TFIIFMILLS SGALAFEDIN
IERRRVIKTI LEYADKVFTY IFIVEMLLKW VAYGFKTYFT NAWCWLDFLI VDVSLVSLTA
NLMGYSELGA IKSLRTLRAL RPLRALSRFE GMRVVVNALV GAIPSIFNVL LVCLIFWLIF
SIMGVNLFAG KFYHCINTTT EERIPMDVVN NKSDCMALMY TNEVRWVNVK VNYDNVGLGY
LSLLQIATFK GWMDIMYAAV DSREVDEQPS YEINLYMYLY FVIFIIFGSF FTLNLFIGVI
IDNFNQQKSK FGGKDIFMTE EQKKYYNAMK KLGAKKRPKP IPRPSNIIQG LVFDFISKQF
FDIFIMVLIC LNMVTMMIET DDQSAEKEYV LYQINLVFIV VFTSECVLKL FALRQYFFTI
GWNVFDFVVV ILSIAGLMLS DIIEKYFVSP TLFRVIRLAR IGRVLRLIRG AKGIRTLLFA
LMMSLPALFN IGLLLFLIMF IFSIFGMSNF AYVKKQAGID DIFNFETFGG SIICLFEITT
SAGWDGLLLP ILNSGPPDCD PDFENPGTDV RGNCGNPGMG IMFFCSYIIM SFLVVVNMYI
AIILENFNNA QEESGDPLCE DDFDMFDETW EKFDVDATQF IEYDRLFDFV DALQEPLRIA
KPNRLKLISM DIPIVNGDKI HSQDILLAVT REVLGDTIEM DAMKESIEAK FIMNNPTSAS
FEPIITTLRR KEEERAAIAV QRIYRRHLLK RAIRYACFMR RSKRKVRNPN DNEPPETEGL
IARKMNTLYG SNPELAMALE LETRPMRPNS QPPKPSQVTQ TRASVTFPRP QGQLILPVEL
TSEVILRSAP ITHSLNSSEN ATTIKESIV


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