Q9R053 (SCNBA_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 89.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Sodium channel protein type 11 subunit alpha Alternative name(s): NaN Sensory neuron sodium channel 2 Sodium channel protein type XI subunit alpha Voltage-gated sodium channel subunit alpha Nav1.9 | ||||
| Gene names |
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| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 1765 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| 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 sodium ions may pass in accordance with their electrochemical gradient. It is a tetrodotoxin-resistant sodium channel isoform. Also involved, with the contribution of the receptor tyrosine kinase NTRK2, in rapid BDNF-evoked neuronal depolarization By similarity. |
| Subunit structure | The voltage-resistant sodium channel consists of an ion conducting pore forming alpha-subunit regulated by one or more auxiliary subunits SCN1B, SCN2B and SCN3B. |
| Subcellular location | Membrane; Multi-pass membrane protein By similarity. |
| Tissue specificity | Expressed in the dorsal root ganglia (C-fiber neurons), spinal cord, trigeminal ganglia, testis, ovary, uterus and small intestine. Ref.2 |
| Developmental stage | Expressed in embryo at 15 dpc onwards. Ref.2 |
| 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. |
| Sequence similarities | Belongs to the sodium channel (TC 1.A.1.10) family. Nav1.9/SCN11A subfamily. [View classification] |
Ontologies
| Keywords | |
|---|---|
| Biological process | Ion transport Sodium transport Transport |
| Cellular component | Membrane |
| Domain | Repeat Transmembrane Transmembrane helix |
| Ligand | Sodium |
| Molecular function | Ion channel Sodium channel Voltage-gated channel |
| PTM | Glycoprotein Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Cellular_component | C-fiber Inferred from direct assay PubMed 16029194. Source: MGI plasma membraneInferred from direct assay PubMed 16029194. Source: MGI voltage-gated sodium channel complexInferred from electronic annotation. Source: InterPro |
| Molecular_function | voltage-gated sodium channel activity Inferred from direct assay PubMed 16029194. Source: MGI |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1765 | 1765 | Sodium channel protein type 11 subunit alpha | PRO_0000048511 | |||||
Regions | |||||||||
| Transmembrane | 127 – 148 | 22 | Helical; Name=S1 of repeat I; By similarity | ||||||
| Transmembrane | 160 – 179 | 20 | Helical; Name=S2 of repeat I; By similarity | ||||||
| Transmembrane | 192 – 211 | 20 | Helical; Name=S3 of repeat I; By similarity | ||||||
| Transmembrane | 220 – 239 | 20 | Helical; Voltage-sensor; Name=S4 of repeat I; By similarity | ||||||
| Transmembrane | 256 – 269 | 14 | Helical; Name=S5 of repeat I; By similarity | ||||||
| Transmembrane | 375 – 400 | 26 | Helical; Name=S6 of repeat I; By similarity | ||||||
| Transmembrane | 571 – 594 | 24 | Helical; Name=S1 of repeat II; By similarity | ||||||
| Transmembrane | 606 – 629 | 24 | Helical; Name=S2 of repeat II; By similarity | ||||||
| Transmembrane | 638 – 659 | 22 | Helical; Name=S3 of repeat II; By similarity | ||||||
| Transmembrane | 665 – 684 | 20 | Helical; Voltage-sensor; Name=S4 of repeat II; By similarity | ||||||
| Transmembrane | 700 – 722 | 23 | Helical; Name=S5 of repeat II; By similarity | ||||||
| Transmembrane | 774 – 799 | 26 | Helical; Name=S6 of repeat II; By similarity | ||||||
| Transmembrane | 1031 – 1053 | 23 | Helical; Name=S1 of repeat III; By similarity | ||||||
| Transmembrane | 1068 – 1093 | 26 | Helical; Name=S2 of repeat III; By similarity | ||||||
| Transmembrane | 1100 – 1117 | 18 | Helical; Name=S3 of repeat III; By similarity | ||||||
| Transmembrane | 1119 – 1140 | 22 | Helical; Voltage-sensor; Name=S4 of repeat III; By similarity | ||||||
| Transmembrane | 1160 – 1181 | 22 | Helical; Name=S5 of repeat III; By similarity | ||||||
| Transmembrane | 1263 – 1289 | 27 | Helical; Name=S6 of repeat III; By similarity | ||||||
| Transmembrane | 1343 – 1366 | 24 | Helical; Name=S1 of repeat IV; By similarity | ||||||
| Transmembrane | 1378 – 1401 | 24 | Helical; Name=S2 of repeat IV; By similarity | ||||||
| Transmembrane | 1408 – 1431 | 24 | Helical; Name=S3 of repeat IV; By similarity | ||||||
| Transmembrane | 1441 – 1463 | 23 | Helical; Voltage-sensor; Name=S4 of repeat IV; By similarity | ||||||
| Transmembrane | 1479 – 1501 | 23 | Helical; Name=S5 of repeat IV; By similarity | ||||||
| Transmembrane | 1560 – 1584 | 25 | Helical; Name=S6 of repeat IV; By similarity | ||||||
| Repeat | 126 – 401 | 276 | I | ||||||
| Repeat | 570 – 800 | 231 | II | ||||||
| Repeat | 1030 – 1290 | 261 | III | ||||||
| Repeat | 1342 – 1585 | 244 | IV | ||||||
Amino acid modifications | |||||||||
| Modified residue | 734 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 1250 | 1 | Phosphoserine Ref.6 | ||||||
| Glycosylation | 149 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 217 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 303 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 327 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 336 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 662 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 725 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1188 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1197 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1203 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1211 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1676 | 1 | N-linked (GlcNAc...) Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 400 | 1 | A → G in BAA92154. Ref.2 | ||||||
| Sequence conflict | 427 | 1 | R → K in BAA92154. Ref.2 | ||||||
| Sequence conflict | 489 | 1 | N → K in BAA92154. Ref.2 | ||||||
| Sequence conflict | 738 | 1 | W → R in BAA92154. Ref.2 | ||||||
| Sequence conflict | 761 | 1 | N → T in BAA92154. Ref.2 | ||||||
| Sequence conflict | 764 | 1 | E → D in BAA92154. Ref.2 | ||||||
| Sequence conflict | 843 | 1 | C → R in BAA92154. Ref.2 | ||||||
| Sequence conflict | 1023 – 1024 | 2 | NL → IF in BAA92154. Ref.2 | ||||||
| Sequence conflict | 1054 | 1 | F → L in BAA92154. Ref.2 | ||||||
| Sequence conflict | 1113 | 1 | G → V in AAD53403. Ref.1 | ||||||
| Sequence conflict | 1113 | 1 | G → V in BAA92154. Ref.2 | ||||||
| Sequence conflict | 1212 | 1 | Y → H in BAA92154. Ref.2 | ||||||
| Sequence conflict | 1376 | 1 | K → Q in BAA92154. Ref.2 | ||||||
| Sequence conflict | 1496 | 1 | N → S in BAA92154. Ref.2 | ||||||
| Sequence conflict | 1572 | 1 | F → L in BAA92154. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Coding sequence, genomic organization, and conserved chromosomal localization of the mouse gene Scn11a encoding the sodium channel NaN." Dib-Hajj S.D., Tyrrell L., Escayg A., Wood P.M., Meisler M.H., Waxman S.G. Genomics 59:309-318(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ICR. Tissue: Trigeminal ganglion. |
| [2] | "Cloning and expression study of the mouse tetrodotoxin-resistant voltage-gated sodium channel alpha subunit NaT/Scn11a." Ogata K., Jeong S.-Y., Murakami H., Hashida H., Suzuki T., Masuda N., Hirai M., Isahara K., Uchiyama Y., Goto J., Kanazawa I. Biochem. Biophys. Res. Commun. 267:271-277(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Tissue: Testis. |
| [3] | "Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J. |
| [4] | "Patterned electrical activity modulates sodium channel expression in sensory neurons." Klein J.P., Tendi E.A., Dib-Hajj S.D., Fields R.D., Waxman S.G. J. Neurosci. Res. 74:192-198(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION. |
| [5] | "Na+ channel Nav1.9: in search of a gating mechanism." Delmas P., Coste B. Trends Neurosci. 26:55-57(2003) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW. |
| [6] | "Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-734 AND SER-1250, MASS SPECTROMETRY. Tissue: Liver. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF118044 mRNA. Translation: AAD53403.1. AB031389 mRNA. Translation: BAA92154.1. AC124662 Genomic DNA. No translation available. AC162937 Genomic DNA. No translation available. |
| IPI | IPI00126898. |
| RefSeq | NP_036017.3. NM_011887.3. |
| UniGene | Mm.89981. |
3D structure databases | |
| ProteinModelPortal | Q9R053. |
| SMR | Q9R053. Positions 1585-1728. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | Q9R053. |
Proteomic databases | |
| PaxDb | Q9R053. |
| PRIDE | Q9R053. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000070617; ENSMUSP00000065466; ENSMUSG00000034115. |
| GeneID | 24046. |
| KEGG | mmu:24046. |
| UCSC | uc009sbk.1. mouse. |
Organism-specific databases | |
| CTD | 11280. |
| MGI | MGI:1345149. Scn11a. |
Phylogenomic databases | |
| eggNOG | COG1226. |
| GeneTree | ENSGT00650000092939. |
| HOGENOM | HOG000231755. |
| HOVERGEN | HBG053100. |
| InParanoid | Q9R053. |
| KO | K04843. |
| OMA | ERCLPKG. |
| OrthoDB | EOG41RPT1. |
Gene expression databases | |
| Bgee | Q9R053. |
| CleanEx | MM_SCN11A. |
| Genevestigator | Q9R053. |
| GermOnline | ENSMUSG00000034115. Mus musculus. |
Family and domain databases | |
| InterPro | IPR005821. Ion_trans_dom. IPR001696. Na_channel_asu. IPR010526. Na_trans_assoc. [Graphical view] |
| Pfam | PF00520. Ion_trans. 4 hits. PF06512. Na_trans_assoc. 1 hit. [Graphical view] |
| PRINTS | PR00170. NACHANNEL. |
| ProtoNet | Search... |
Other | |
| ChiTaRS | SCN11A. mouse. |
| NextBio | 303975. |
| SOURCE | Search... |
Entry information
| Entry name | SCNBA_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q9R053 Secondary accession number(s): E9QM88, Q9JMD4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
