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Database: UniProt
Entry: SCNBA_MOUSE
LinkDB: SCNBA_MOUSE
Original site: SCNBA_MOUSE 
ID   SCNBA_MOUSE             Reviewed;        1765 AA.
AC   Q9R053; E9QM88; Q9JMD4;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   25-OCT-2017, entry version 124.
DE   RecName: Full=Sodium channel protein type 11 subunit alpha;
DE   AltName: Full=NaN;
DE   AltName: Full=Sensory neuron sodium channel 2;
DE   AltName: Full=Sodium channel protein type XI subunit alpha;
DE   AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.9;
GN   Name=Scn11a; Synonyms=Nan, Nat, Sns2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR; TISSUE=Trigeminal ganglion;
RX   PubMed=10444332; DOI=10.1006/geno.1999.5890;
RA   Dib-Hajj S.D., Tyrrell L., Escayg A., Wood P.M., Meisler M.H.,
RA   Waxman S.G.;
RT   "Coding sequence, genomic organization, and conserved chromosomal
RT   localization of the mouse gene Scn11a encoding the sodium channel
RT   NaN.";
RL   Genomics 59:309-318(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   TISSUE=Testis;
RX   PubMed=10623609; DOI=10.1006/bbrc.1999.1858;
RA   Ogata K., Jeong S.-Y., Murakami H., Hashida H., Suzuki T., Masuda N.,
RA   Hirai M., Isahara K., Uchiyama Y., Goto J., Kanazawa I.;
RT   "Cloning and expression study of the mouse tetrodotoxin-resistant
RT   voltage-gated sodium channel alpha subunit NaT/Scn11a.";
RL   Biochem. Biophys. Res. Commun. 267:271-277(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   INDUCTION.
RX   PubMed=14515348; DOI=10.1002/jnr.10768;
RA   Klein J.P., Tendi E.A., Dib-Hajj S.D., Fields R.D., Waxman S.G.;
RT   "Patterned electrical activity modulates sodium channel expression in
RT   sensory neurons.";
RL   J. Neurosci. Res. 74:192-198(2003).
RN   [5]
RP   REVIEW.
RX   PubMed=12536125; DOI=10.1016/S0166-2236(02)00030-9;
RA   Delmas P., Coste B.;
RT   "Na+ channel Nav1.9: in search of a gating mechanism.";
RL   Trends Neurosci. 26:55-57(2003).
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 sodium ions may pass in accordance with their
CC       electrochemical gradient. It is a tetrodotoxin-resistant sodium
CC       channel isoform. Also involved, with the contribution of the
CC       receptor tyrosine kinase NTRK2, in rapid BDNF-evoked neuronal
CC       depolarization (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: The voltage-resistant sodium channel consists of an ion
CC       conducting pore forming alpha-subunit regulated by one or more
CC       auxiliary subunits SCN1B, SCN2B and SCN3B.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:D0E0C2}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:D0E0C2}.
CC   -!- TISSUE SPECIFICITY: Expressed in the dorsal root ganglia (C-fiber
CC       neurons), spinal cord, trigeminal ganglia, testis, ovary, uterus
CC       and small intestine. {ECO:0000269|PubMed:10623609}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryo at 15 dpc onwards.
CC       {ECO:0000269|PubMed:10623609}.
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       Nav1.9/SCN11A subfamily. {ECO:0000305}.
DR   EMBL; AF118044; AAD53403.1; -; mRNA.
DR   EMBL; AB031389; BAA92154.1; -; mRNA.
DR   EMBL; AC124662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC162937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS40804.1; -.
DR   RefSeq; NP_036017.3; NM_011887.3.
DR   UniGene; Mm.469833; -.
DR   UniGene; Mm.89981; -.
DR   ProteinModelPortal; Q9R053; -.
DR   BioGrid; 204861; 1.
DR   STRING; 10090.ENSMUSP00000065466; -.
DR   iPTMnet; Q9R053; -.
DR   PhosphoSitePlus; Q9R053; -.
DR   PaxDb; Q9R053; -.
DR   PRIDE; Q9R053; -.
DR   Ensembl; ENSMUST00000070617; ENSMUSP00000065466; ENSMUSG00000034115.
DR   Ensembl; ENSMUST00000215718; ENSMUSP00000149420; ENSMUSG00000034115.
DR   GeneID; 24046; -.
DR   KEGG; mmu:24046; -.
DR   UCSC; uc009sbk.1; mouse.
DR   CTD; 11280; -.
DR   MGI; MGI:1345149; Scn11a.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128242; -.
DR   HOGENOM; HOG000231755; -.
DR   HOVERGEN; HBG053100; -.
DR   InParanoid; Q9R053; -.
DR   KO; K04843; -.
DR   OMA; CYQIVKH; -.
DR   OrthoDB; EOG091G00FK; -.
DR   TreeFam; TF323985; -.
DR   ChiTaRS; Scn11a; mouse.
DR   PRO; PR:Q9R053; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   Bgee; ENSMUSG00000034115; -.
DR   CleanEx; MM_SCN11A; -.
DR   Genevisible; Q9R053; MM.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0044299; C:C-fiber; IDA:MGI.
DR   GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:InterPro.
DR   GO; GO:0005248; F:voltage-gated sodium channel activity; IDA:MGI.
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   GO; GO:0051930; P:regulation of sensory perception of pain; IMP:UniProtKB.
DR   GO; GO:0006814; P:sodium ion transport; IDA:MGI.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR028821; Na_channel_a11su.
DR   InterPro; IPR001696; Na_channel_asu.
DR   InterPro; IPR010526; Na_trans_assoc.
DR   PANTHER; PTHR10037:SF210; PTHR10037:SF210; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   Pfam; PF06512; Na_trans_assoc; 1.
DR   PRINTS; PR00170; NACHANNEL.
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   1765       Sodium channel protein type 11 subunit
FT                                alpha.
FT                                /FTId=PRO_0000048511.
FT   TOPO_DOM      1    126       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    127    148       Helical; Name=S1 of repeat I.
FT                                {ECO:0000250}.
FT   TOPO_DOM    149    159       Extracellular. {ECO:0000305}.
FT   TRANSMEM    160    179       Helical; Name=S2 of repeat I.
FT                                {ECO:0000250}.
FT   TOPO_DOM    180    191       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    192    211       Helical; Name=S3 of repeat I.
FT                                {ECO:0000250}.
FT   TOPO_DOM    212    219       Extracellular. {ECO:0000305}.
FT   TRANSMEM    220    239       Helical; Voltage-sensor; Name=S4 of
FT                                repeat I. {ECO:0000250}.
FT   TOPO_DOM    240    255       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    256    269       Helical; Name=S5 of repeat I.
FT                                {ECO:0000250}.
FT   TOPO_DOM    270    342       Extracellular. {ECO:0000305}.
FT   INTRAMEM    343    367       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    368    374       Extracellular. {ECO:0000305}.
FT   TRANSMEM    375    400       Helical; Name=S6 of repeat I.
FT                                {ECO:0000250}.
FT   TOPO_DOM    401    570       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    571    594       Helical; Name=S1 of repeat II.
FT                                {ECO:0000250}.
FT   TOPO_DOM    595    605       Extracellular. {ECO:0000305}.
FT   TRANSMEM    606    629       Helical; Name=S2 of repeat II.
FT                                {ECO:0000250}.
FT   TOPO_DOM    630    637       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    638    659       Helical; Name=S3 of repeat II.
FT                                {ECO:0000250}.
FT   TOPO_DOM    660    664       Extracellular. {ECO:0000305}.
FT   TRANSMEM    665    684       Helical; Voltage-sensor; Name=S4 of
FT                                repeat II. {ECO:0000250}.
FT   TOPO_DOM    685    699       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    700    722       Helical; Name=S5 of repeat II.
FT                                {ECO:0000250}.
FT   TOPO_DOM    723    742       Extracellular. {ECO:0000305}.
FT   INTRAMEM    743    763       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    764    773       Extracellular. {ECO:0000305}.
FT   TRANSMEM    774    799       Helical; Name=S6 of repeat II.
FT                                {ECO:0000250}.
FT   TOPO_DOM    800   1030       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1031   1053       Helical; Name=S1 of repeat III.
FT                                {ECO:0000250}.
FT   TOPO_DOM   1054   1067       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1068   1093       Helical; Name=S2 of repeat III.
FT                                {ECO:0000250}.
FT   TOPO_DOM   1094   1099       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1100   1117       Helical; Name=S3 of repeat III.
FT                                {ECO:0000250}.
FT   TOPO_DOM   1118   1118       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1119   1140       Helical; Voltage-sensor; Name=S4 of
FT                                repeat III. {ECO:0000250}.
FT   TOPO_DOM   1141   1159       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1160   1181       Helical; Name=S5 of repeat III.
FT                                {ECO:0000250}.
FT   TOPO_DOM   1182   1224       Extracellular. {ECO:0000305}.
FT   INTRAMEM   1225   1246       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1247   1262       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1263   1289       Helical; Name=S6 of repeat III.
FT                                {ECO:0000250}.
FT   TOPO_DOM   1290   1342       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1343   1366       Helical; Name=S1 of repeat IV.
FT                                {ECO:0000250}.
FT   TOPO_DOM   1367   1377       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1378   1401       Helical; Name=S2 of repeat IV.
FT                                {ECO:0000250}.
FT   TOPO_DOM   1402   1407       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1408   1431       Helical; Name=S3 of repeat IV.
FT                                {ECO:0000250}.
FT   TOPO_DOM   1432   1440       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1441   1463       Helical; Voltage-sensor; Name=S4 of
FT                                repeat IV. {ECO:0000250}.
FT   TOPO_DOM   1464   1478       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1479   1501       Helical; Name=S5 of repeat IV.
FT                                {ECO:0000250}.
FT   TOPO_DOM   1502   1515       Extracellular. {ECO:0000305}.
FT   INTRAMEM   1516   1538       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1539   1559       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1560   1584       Helical; Name=S6 of repeat IV.
FT                                {ECO:0000250}.
FT   TOPO_DOM   1585   1765       Cytoplasmic. {ECO:0000305}.
FT   REPEAT      115    406       I. {ECO:0000305}.
FT   REPEAT      557    821       II. {ECO:0000305}.
FT   REPEAT     1023   1320       III. {ECO:0000305}.
FT   REPEAT     1329   1619       IV. {ECO:0000305}.
FT   CARBOHYD    149    149       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    217    217       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    303    303       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    327    327       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    336    336       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    662    662       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    725    725       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1188   1188       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1197   1197       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1203   1203       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1211   1211       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    283    320       {ECO:0000250|UniProtKB:D0E0C2}.
FT   DISULFID    765    775       {ECO:0000250|UniProtKB:D0E0C2}.
FT   CONFLICT    400    400       A -> G (in Ref. 2; BAA92154).
FT                                {ECO:0000305}.
FT   CONFLICT    427    427       R -> K (in Ref. 2; BAA92154).
FT                                {ECO:0000305}.
FT   CONFLICT    489    489       N -> K (in Ref. 2; BAA92154).
FT                                {ECO:0000305}.
FT   CONFLICT    738    738       W -> R (in Ref. 2; BAA92154).
FT                                {ECO:0000305}.
FT   CONFLICT    761    761       N -> T (in Ref. 2; BAA92154).
FT                                {ECO:0000305}.
FT   CONFLICT    764    764       E -> D (in Ref. 2; BAA92154).
FT                                {ECO:0000305}.
FT   CONFLICT    843    843       C -> R (in Ref. 2; BAA92154).
FT                                {ECO:0000305}.
FT   CONFLICT   1023   1024       NL -> IF (in Ref. 2; BAA92154).
FT                                {ECO:0000305}.
FT   CONFLICT   1054   1054       F -> L (in Ref. 2; BAA92154).
FT                                {ECO:0000305}.
FT   CONFLICT   1113   1113       G -> V (in Ref. 1; AAD53403 and 2;
FT                                BAA92154). {ECO:0000305}.
FT   CONFLICT   1212   1212       Y -> H (in Ref. 2; BAA92154).
FT                                {ECO:0000305}.
FT   CONFLICT   1376   1376       K -> Q (in Ref. 2; BAA92154).
FT                                {ECO:0000305}.
FT   CONFLICT   1496   1496       N -> S (in Ref. 2; BAA92154).
FT                                {ECO:0000305}.
FT   CONFLICT   1572   1572       F -> L (in Ref. 2; BAA92154).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1765 AA;  201385 MW;  0A17EA3B9D86FB9C CRC64;
     MEERYYPVIF PDERNFRPFT FDSLAAIEKR ITIQKEKKKS KDKAATEPQP RPQLDLKASR
     KLPKLYGDVP PDLIAKPLED LDPFYKDHKT FMVLNKKRTI YRFSAKRALF ILGPFNPIRS
     FMIRISVHSV FSMFIICTVI INCMFMANNS SVDSRPSSNI PEYVFIGIYV LEAVIKILAR
     GFIVDEFSYL RDPWNWLDFI VIGTAIAPCF LGNKVNNLST LRTFRVLRAL KAISVISGLK
     VIVGALLRSV KKLVDVMVLT LFCLSIFALV GQQLFMGILS QKCIKDDCGP NAFSNKDCFV
     KENDSEDFIM CGNWLGRRSC PDGSTCNKTT FNPDYNYTNF DSFGWSFLAM FRVMTQDSWE
     KLYRQILRTS GIYFVFFFVV VIFLGSFYLL NLTLAVVTMA YEEQNRNVAA ETEAKEKMFQ
     EAQQLLREEK EALVAMGIDR TSLNSLQASS FSPKKRKFFG SKTRKSFFMR GSKTARASAS
     DSEDDASKNP QLLEQTKRLS QNLPVELFDE HVDPLHRQRA LSAVSILTIT MQEQEKSQEP
     CFPCGKNLAS KYLVWECSPP WLCIKKVLQT IMTDPFTELA ITICIIVNTV FLAMEHHNMD
     NSLKDILKIG NWVFTGIFIA EMCLKIIALD PYHYFRHGWN IFDSIVALVS LADVLFHKLS
     KNLSFLASLR VLRVFKLAKS WPTLNTLIKI IGHSVGALGN LTVVLTIVVF IFSVVGMRLF
     GAKFNKTCST SPESLRRWHM GDFYHSFLVV FRILCGEWIE NMWECMQEME GSPLCVIVFV
     LIMVVGKLVV LNLFIALLLN SFSNEEKDGN PEGETRKTKV QLALDRFSRA FYFMARALQN
     FCCKRCRRQN SPKPNEATES FAGESRDTAT LDTRSWKEYD SEMTLYTGQA GAPLAPLAKE
     EDDMECCGEC DASPTSQPSE EAQACDLPLK TKRLPSPDDH GVEMEVFSEE DPNLTIQSAR
     KKSDAASMLS ECSTIDLNDI FRNLQKTVSP QKQPDRCFPK GLSCIFLCCK TIKKKSPWVL
     WWNLRKTCYQ IVKHSWFESF IIFVILLSSG ALIFEDVNLP SRPQVEKLLK CTDNIFTFIF
     LLEMILKWVA FGFRKYFTSA WCWLDFLIVV VSGLSLTNLP NLKSFRNLRA LRPLRALSQF
     EGMKVVVNAL MSAIPAILNV LLVCLIFWLI FCILGVNFFS GKFGRCINGT DINKYFNASN
     VPNQSQCLVS NYTWKVPNVN FDNVGNAYLA LLQVATYKGW LDIMNAAVDS RGKDEQPAFE
     ANLYAYLYFV VFIIFGSFFT LNLFIGVIID NFNQQQKKLG GQDIFMTEEQ KKYYNAMKKL
     GTKKPQKPIP RPLNKCQAFV FDLVTSQVFD VIILGLIVTN MIIMMAESEG QPNEVKKIFD
     ILNIVFVVIF TVECLIKVFA LRQHYFTNGW NLFDCVVVVL SIISTLVSGL ENSNVFPPTL
     FRIVRLARIG RILRLVRAAR GIRTLLFALM MSLPSLFNIG LLLFLVMFIY AIFGMNWFSK
     VKRGSGIDDI FNFDTFSGSM LCLFQITTSA GWDALLNPML ESKASCNSSS QESCQQPQIA
     IVYFVSYIII SFLIVVNMYI AVILENFNTA TEESEDPLGE DDFEIFYEIW EKFDPEATQF
     IQYSSLSDFA DALPEPLRVA KPNRFQFLMM DLPMVMGDRL HCMDVLFAFT TRVLGNSSGL
     DTMKAMMEEK FMEANPFKKL YEPIVTTTKR KEEEECAAVI QRAYRRHMEK MIKLKLKGRS
     SSSLQVFCNG DLSSLDVPKI KVHCD
//
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