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Database: UniProt
Entry: SC4AA_DANRE
LinkDB: SC4AA_DANRE
Original site: SC4AA_DANRE 
ID   SC4AA_DANRE             Reviewed;        1829 AA.
AC   Q2XVR3; Q20JQ6;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 2.
DT   10-MAY-2017, entry version 83.
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   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=16830092; DOI=10.1007/s00239-005-0287-9;
RA   Novak A.E., Jost M.C., Lu Y., Taylor A.D., Zakon H.H., Ribera A.B.;
RT   "Gene duplications and evolution of vertebrate voltage-gated sodium
RT   channels.";
RL   J. Mol. Evol. 63:208-221(2006).
RN   [2]
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   -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, brain, spinal
CC       cord, and eye. {ECO:0000269|PubMed:16830092}.
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; DQ149506; ABA54921.1; -; mRNA.
DR   EMBL; DQ221253; ABB29445.2; -; Genomic_DNA.
DR   RefSeq; NP_001034914.1; NM_001039825.1.
DR   UniGene; Dr.117129; -.
DR   ProteinModelPortal; Q2XVR3; -.
DR   STRING; 7955.ENSDARP00000097312; -.
DR   PaxDb; Q2XVR3; -.
DR   GeneID; 572442; -.
DR   KEGG; dre:572442; -.
DR   CTD; 572442; -.
DR   ZFIN; ZDB-GENE-051201-2; scn4aa.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   HOGENOM; HOG000231755; -.
DR   InParanoid; Q2XVR3; -.
DR   KO; K04837; -.
DR   PhylomeDB; Q2XVR3; -.
DR   PRO; PR:Q2XVR3; -.
DR   Proteomes; UP000000437; 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; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR001696; Na_channel_asu.
DR   InterPro; IPR010526; Na_trans_assoc.
DR   Pfam; PF00520; Ion_trans; 4.
DR   Pfam; PF06512; Na_trans_assoc; 1.
DR   PRINTS; PR00170; NACHANNEL.
DR   PROSITE; PS50096; IQ; 1.
PE   2: Evidence at transcript level;
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   1829       Sodium channel protein type 4 subunit
FT                                alpha A.
FT                                /FTId=PRO_0000371317.
FT   TOPO_DOM      1    124       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    125    143       Helical; Name=S1 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    144    150       Extracellular. {ECO:0000305}.
FT   TRANSMEM    151    171       Helical; Name=S2 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    172    185       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    186    203       Helical; Name=S3 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    204    209       Extracellular. {ECO:0000305}.
FT   TRANSMEM    210    226       Helical; Name=S4 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    227    245       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    246    265       Helical; Name=S5 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    266    358       Extracellular. {ECO:0000305}.
FT   INTRAMEM    359    383       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    384    390       Extracellular. {ECO:0000305}.
FT   TRANSMEM    391    411       Helical; Name=S6 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    412    582       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    583    601       Helical; Name=S1 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    602    612       Extracellular. {ECO:0000305}.
FT   TRANSMEM    613    632       Helical; Name=S2 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    633    646       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    647    666       Helical; Name=S3 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    667    668       Extracellular. {ECO:0000305}.
FT   TRANSMEM    669    686       Helical; Name=S4 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    687    702       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    703    721       Helical; Name=S5 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    722    750       Extracellular. {ECO:0000305}.
FT   INTRAMEM    751    771       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    772    784       Extracellular. {ECO:0000305}.
FT   TRANSMEM    785    805       Helical; Name=S6 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    806    998       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    999   1016       Helical; Name=S1 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1017   1029       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1030   1048       Helical; Name=S2 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1049   1062       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1063   1081       Helical; Name=S3 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1082   1089       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1090   1108       Helical; Name=S4 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1109   1125       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1126   1145       Helical; Name=S5 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1146   1196       Extracellular. {ECO:0000305}.
FT   INTRAMEM   1197   1218       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1219   1235       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1236   1257       Helical; Name=S6 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1258   1320       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1321   1338       Helical; Name=S1 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1339   1349       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1350   1368       Helical; Name=S2 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1369   1380       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1381   1398       Helical; Name=S3 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1399   1411       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1412   1428       Helical; Name=S4 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1429   1447       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1448   1465       Helical; Name=S5 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1466   1487       Extracellular. {ECO:0000305}.
FT   INTRAMEM   1488   1510       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1511   1540       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1541   1563       Helical; Name=S6 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1564   1829       Cytoplasmic. {ECO:0000305}.
FT   REPEAT      106    421       I. {ECO:0000305}.
FT   REPEAT      564    836       II. {ECO:0000305}.
FT   REPEAT      979   1292       III. {ECO:0000305}.
FT   REPEAT     1301   1599       IV. {ECO:0000305}.
FT   DOMAIN     1693   1722       IQ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00116}.
FT   CARBOHYD    207    207       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    280    280       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    293    293       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    329    329       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1157   1157       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1171   1171       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    273    336       {ECO:0000250|UniProtKB:D0E0C2}.
FT   DISULFID    733    733       Interchain; with SCN2B or SCN4B.
FT                                {ECO:0000250|UniProtKB:P04775}.
FT   DISULFID    773    782       {ECO:0000250|UniProtKB:D0E0C2}.
FT   CONFLICT    310    310       N -> S (in Ref. 1; ABA54921).
FT                                {ECO:0000305}.
FT   CONFLICT   1054   1054       Missing (in Ref. 1; ABA54921).
FT                                {ECO:0000305}.
FT   CONFLICT   1305   1305       Missing (in Ref. 1; ABA54921).
FT                                {ECO:0000305}.
FT   CONFLICT   1721   1721       R -> Q (in Ref. 1; ABA54921).
FT                                {ECO:0000305}.
FT   CONFLICT   1811   1811       I -> T (in Ref. 1; ABA54921).
FT                                {ECO:0000305}.
FT   CONFLICT   1815   1815       L -> F (in Ref. 1; ABA54921).
FT                                {ECO:0000305}.
SQ   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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