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Database: UniProt
Entry: SC4AB_DANRE
LinkDB: SC4AB_DANRE
Original site: SC4AB_DANRE 
ID   SC4AB_DANRE             Reviewed;        1784 AA.
AC   Q20JQ7; Q2XVR2;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   10-MAY-2017, entry version 81.
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   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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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, heart, brain,
CC       spinal 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   -!- PTM: Lacks the cysteine which covalently binds the conotoxin
CC       GVIIJ. This cysteine (position 719) is speculated in other sodium
CC       channel subunits alpha to be implied in covalent binding with the
CC       sodium channel subunit beta-2 or beta-4.
CC       {ECO:0000250|UniProtKB:P15389}.
CC   -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC       Nav1.4/SCN4A subfamily. {ECO:0000305}.
DR   EMBL; DQ149505; ABA54920.1; -; mRNA.
DR   EMBL; DQ221254; ABB29446.2; -; Genomic_DNA.
DR   EMBL; BC163558; AAI63558.1; -; mRNA.
DR   RefSeq; NP_001038530.1; NM_001045065.1.
DR   UniGene; Dr.67010; -.
DR   ProteinModelPortal; Q20JQ7; -.
DR   STRING; 7955.ENSDARP00000044156; -.
DR   PaxDb; Q20JQ7; -.
DR   Ensembl; ENSDART00000104004; ENSDARP00000094779; ENSDARG00000034588.
DR   GeneID; 564977; -.
DR   KEGG; dre:564977; -.
DR   CTD; 564977; -.
DR   ZFIN; ZDB-GENE-051201-1; scn4ab.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128242; -.
DR   HOGENOM; HOG000231755; -.
DR   InParanoid; Q20JQ7; -.
DR   KO; K04837; -.
DR   PhylomeDB; Q20JQ7; -.
DR   TreeFam; TF323985; -.
DR   PRO; PR:Q20JQ7; -.
DR   Proteomes; UP000000437; Chromosome 3.
DR   Bgee; ENSDARG00000034588; -.
DR   ExpressionAtlas; Q20JQ7; baseline.
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; IPR028817; Na_channel_a4suB.
DR   InterPro; IPR001696; Na_channel_asu.
DR   InterPro; IPR010526; Na_trans_assoc.
DR   PANTHER; PTHR10037:SF244; PTHR10037:SF244; 1.
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   1784       Sodium channel protein type 4 subunit
FT                                alpha B.
FT                                /FTId=PRO_0000371318.
FT   TOPO_DOM      1    130       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    131    149       Helical; Name=S1 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    150    156       Extracellular. {ECO:0000305}.
FT   TRANSMEM    157    177       Helical; Name=S2 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    178    191       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    192    209       Helical; Name=S3 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    210    215       Extracellular. {ECO:0000305}.
FT   TRANSMEM    216    232       Helical; Name=S4 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    233    251       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    252    271       Helical; Name=S5 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    272    366       Extracellular. {ECO:0000305}.
FT   INTRAMEM    367    391       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    392    398       Extracellular. {ECO:0000305}.
FT   TRANSMEM    399    419       Helical; Name=S6 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    420    568       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    569    587       Helical; Name=S1 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    588    598       Extracellular. {ECO:0000305}.
FT   TRANSMEM    599    618       Helical; Name=S2 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    619    632       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    633    652       Helical; Name=S3 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    653    654       Extracellular. {ECO:0000305}.
FT   TRANSMEM    655    672       Helical; Name=S4 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    673    688       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    689    707       Helical; Name=S5 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    708    736       Extracellular. {ECO:0000305}.
FT   INTRAMEM    737    757       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    758    770       Extracellular. {ECO:0000305}.
FT   TRANSMEM    771    791       Helical; Name=S6 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    792    973       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    974    991       Helical; Name=S1 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    992   1004       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1005   1023       Helical; Name=S2 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1024   1037       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1038   1056       Helical; Name=S3 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1057   1064       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1065   1083       Helical; Name=S4 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1084   1101       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1102   1121       Helical; Name=S5 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1122   1173       Extracellular. {ECO:0000305}.
FT   INTRAMEM   1174   1195       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1196   1212       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1213   1234       Helical; Name=S6 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1235   1297       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1298   1315       Helical; Name=S1 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1316   1326       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1327   1345       Helical; Name=S2 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1346   1357       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1358   1375       Helical; Name=S3 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1376   1388       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1389   1405       Helical; Name=S4 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1406   1424       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1425   1442       Helical; Name=S5 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1443   1464       Extracellular. {ECO:0000305}.
FT   INTRAMEM   1465   1487       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1488   1516       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1517   1539       Helical; Name=S6 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1540   1784       Cytoplasmic. {ECO:0000305}.
FT   REPEAT      112    429       I. {ECO:0000305}.
FT   REPEAT      550    821       II. {ECO:0000305}.
FT   REPEAT      954   1269       III. {ECO:0000305}.
FT   REPEAT     1278   1575       IV. {ECO:0000305}.
FT   DOMAIN     1669   1698       IQ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00116}.
FT   CARBOHYD    213    213       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    291    291       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    304    304       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    337    337       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1133   1133       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1147   1147       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    279    344       {ECO:0000250|UniProtKB:D0E0C2}.
FT   DISULFID    759    768       {ECO:0000250|UniProtKB:D0E0C2}.
FT   CONFLICT   1089   1089       Missing (in Ref. 2; ABB29446 and 3;
FT                                AAI63558). {ECO:0000305}.
SQ   SEQUENCE   1784 AA;  201663 MW;  63B260ED94E3BBFF CRC64;
     MARLLPPTGT DVFRPLTLES LAEIDRRMAE EAAEQERMKE QNVKVAEEDL PKPTSDLEAG
     KVLPFIYGDP PPNLLNVPIE ELDPYYKAQK TFIVIDKKNT IYRFNTEPAC YCLSPFNPVR
     RAAIRILIHS LFSLVIMLTI LTNCVFMAMS DPPGWSKILE YVFTGIYTFE AMVKVLSRGF
     CIGDFTFLRD PWNWLDFMVI SMAYLTEFVD LGNISALRTF RVLRALKTIT VIPGLKTIVG
     ALIQSVKKLA DVMILTVFCL SVFALIGLQL FMGNLRQKCV LWPPVGWYSD NLTVLSNYTD
     INGNGTANST FDYQKYINSE ENYYYVPGQM DPLVCGNSSD AGLCPEGYIC LKAGRNPNYG
     YTSYDNFGWA FLALFRLMTQ DFWENLFQLT LRAAGKTYMI FFVVIIFLGS FYLINLILAV
     VAMAYAEQNE ATAAEAKEKE EEYAKIMEQL KKQAEQKNGM VNGSKTSLSS KKKGDNDQMQ
     SDYDGIALKP LSKSNGSKGN INYLEVPDSQ IRKPSVVSAV ESALDAQEDI ERPCPPGWYK
     FADIFLKWDC CIPWVKFKRI VYLFVMDPFV DLGITLCIVL NTVFMAMEHY PMSVHVEEVL
     AIGNLVFTGI FAAEMVLKLI ALDPYYYFQV GWNIFDSIIV TMSLVELMLA DVEGLSVLRS
     FRLMRVFKLA KSWPTLNMLI KIIGNSVGAL GNLTLVLAII VFIFAVVGMQ LFGKSYTDSV
     CKISSDCELP RWHMADFFHA FLIIFRVLCG EWIETMWDCM EVAGQGMCII VFMMVMVIGN
     LVVLNLFLAL LLSSFSGDNL SASDDDGENN LQIAISRITR GIDWIKAFVN KHVRQCLNLK
     PKEEGAKVNG EGDAKMNAIM NSSSSMVKVP IANGESDDDD GNGSSEDEDD EGRDINMKKK
     NGDESSTCST VDKPPEVEDL VEEEEEDLTS PEDCYTENCI RRCPCLDLDV SQGKGKAWWN
     FRKTCFAIVE HSYFETFIIF MILLSSGALA FEDIYIEQRR MIKIILEYAD QVFTYVFVVE
     MLLKWVAYGF KVYFTNAWCW LDFLIVDVSL ISLTANILGY SELGAIKSLR TLRALRPLRA
     LSRFEGMRVV VVNALVGAIP SIFNVLLVCL IFWLIFSIMG VNLFAGKFYY CFNETSEEVF
     DHNVVNNKTD CYELMEFHPE VRWMNGKINF DNVGMGYLAL LQVATFKGWM DIMYSAVDSR
     AIESQPVYEA NLYMYIYFVI FIIFGSFFTL NLFIGVIIDN FNQQKAKLGG TDIFMTEEQK
     KYYNAMKKLG SKKPQKPIPR PTNCCQGLVF DFVTQQFFDI FIMVMICLNM VTMMVETDDQ
     SAEIEEILFY INFAFIILFT GECVLKITAL RYHYFSIGWN IFDFVVVILS ILGIGLADLI
     EKYFVSPTLF RVIRLARIGR VLRLIRGAKG IRTLLFALMM SLPALFNIGL LLFLIMFIFS
     IFGMSNFAYV KKEVGIDDMM NFETFGNSII CMFMITTSAG WDGLLAPILN SPPDCDPDVD
     NPGSTTRGNC GNAAVGIVFF CSYIVMSFLV VVNMYIAIIL ENFNVATEES SDPLCEDDFE
     MFYETWEKFD PTASQFIDYN RLSEFCDTLK DPLRIPKPNT LKLITMDIPM VTGDKIHCLD
     LLLALTGEVL GGSDQMDGMK ATMEEKFMAN NPSKASYEPI TSTLKRKQEE VAASTIQRAY
     RSHILKRCVK QASYMYRDKT GSKKPTGEAP EKVGMIAENM RSLYGDQAVE DDHPVGCSFS
     QHGKTQFGAK RPPVKVQSDV VLHSAPFPVP ESSTAADNLR ESIV
//
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