O88457 (SCNBA_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 84.
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 | Rattus norvegicus (Rat) [Reference proteome] | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus![]() |
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. Ref.2 |
| 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 (at protein level) in myenteric sensory neurons. Expressed in small sensory neurons of the dorsal root ganglia (C-fiber neurons) and trigeminal ganglia. Ref.1 Ref.2 Ref.3 |
| Developmental stage | Expressed in dorsal root ganglia at 17 dpc onwards. Ref.3 |
| Induction | Down-regulated after axotomy and up-regulated following hind paw inflammation. Down-regulated in vitro by electrical stimulation and by deprivation of NGF. Ref.1 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) | |
| Biological_process | sodium ion transmembrane transport Inferred from electronic annotation. Source: GOC |
| Cellular_component | voltage-gated sodium channel complex Inferred from electronic annotation. Source: InterPro |
| Molecular_function | voltage-gated sodium channel activity Inferred from electronic annotation. Source: InterPro |
| 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_0000048512 | |||||
Regions | |||||||||
| Transmembrane | 127 – 148 | 22 | Helical; Name=S1 of repeat I; By similarity | ||||||
| Transmembrane | 158 – 177 | 20 | Helical; Name=S2 of repeat I; By similarity | ||||||
| Transmembrane | 190 – 209 | 20 | Helical; Name=S3 of repeat I; By similarity | ||||||
| Transmembrane | 217 – 236 | 20 | Helical; Voltage-sensor; Name=S4 of repeat I; By similarity | ||||||
| Transmembrane | 253 – 266 | 14 | Helical; Name=S5 of repeat I; By similarity | ||||||
| Transmembrane | 372 – 397 | 26 | Helical; Name=S6 of repeat I; By similarity | ||||||
| Transmembrane | 568 – 591 | 24 | Helical; Name=S1 of repeat II; By similarity | ||||||
| Transmembrane | 603 – 626 | 24 | Helical; Name=S2 of repeat II; By similarity | ||||||
| Transmembrane | 635 – 656 | 22 | Helical; Name=S3 of repeat II; By similarity | ||||||
| Transmembrane | 663 – 682 | 20 | Helical; Voltage-sensor; Name=S4 of repeat II; By similarity | ||||||
| Transmembrane | 698 – 720 | 23 | Helical; Name=S5 of repeat II; By similarity | ||||||
| Transmembrane | 773 – 798 | 26 | Helical; Name=S6 of repeat II; By similarity | ||||||
| Transmembrane | 1030 – 1052 | 23 | Helical; Name=S1 of repeat III; By similarity | ||||||
| Transmembrane | 1067 – 1092 | 26 | Helical; Name=S2 of repeat III; By similarity | ||||||
| Transmembrane | 1099 – 1116 | 18 | Helical; Name=S3 of repeat III; By similarity | ||||||
| Transmembrane | 1118 – 1139 | 22 | Helical; Voltage-sensor; Name=S4 of repeat III; By similarity | ||||||
| Transmembrane | 1159 – 1180 | 22 | Helical; Name=S5 of repeat III; By similarity | ||||||
| Transmembrane | 1262 – 1288 | 27 | Helical; Name=S6 of repeat III; By similarity | ||||||
| Transmembrane | 1342 – 1365 | 24 | Helical; Name=S1 of repeat IV; By similarity | ||||||
| Transmembrane | 1377 – 1400 | 24 | Helical; Name=S2 of repeat IV; By similarity | ||||||
| Transmembrane | 1407 – 1430 | 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 – 398 | 273 | I | ||||||
| Repeat | 567 – 799 | 233 | II | ||||||
| Repeat | 1029 – 1289 | 261 | III | ||||||
| Repeat | 1341 – 1585 | 245 | IV | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1249 | 1 | Phosphoserine By similarity | ||||||
| Glycosylation | 214 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 319 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 333 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 660 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 723 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1187 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1202 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1207 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1210 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1547 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| [1] | "NaN, a novel voltage-gated Na channel, is expressed preferentially in peripheral sensory neurons and down-regulated after axotomy." Dib-Hajj S.D., Tyrrell L., Black J.A., Waxman S.G. Proc. Natl. Acad. Sci. U.S.A. 95:8963-8968(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION. Strain: Sprague-Dawley. Tissue: Spinal ganglion. |
| [2] | "Two sodium channels contribute to the TTX-R sodium current in primary sensory neurons." Tate S.N., Benn S.C., Hick C.A., Trezise D., John V.H., Mannion R.J., Costigan M., Plumpton C., Grose D., Gladwell Z., Kendall G., Dale K., Bountra C., Woolf C.J. Nat. Neurosci. 1:653-655(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN VOLTAGE-EVOKED DEPOLARIZATION, TISSUE SPECIFICITY, INDUCTION. Strain: Sprague-Dawley. Tissue: Spinal ganglion. |
| [3] | "Developmental expression of the TTX-resistant voltage-gated sodium channels Nav1.8 (SNS) and Nav1.9 (SNS2) in primary sensory neurons." Benn S.C., Costigan M., Tate S., Fitzgerald M., Woolf C.J. J. Neurosci. 21:6077-6085(2001) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. |
| [4] | "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. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF059030 mRNA. Translation: AAC40199.1. AJ237852 mRNA. Translation: CAB41850.1. |
| IPI | IPI00392165. |
| PIR | T42388. |
| RefSeq | NP_062138.1. NM_019265.2. |
| UniGene | Rn.30023. |
3D structure databases | |
| ProteinModelPortal | O88457. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 10116.ENSRNOP00000033224. |
PTM databases | |
| PhosphoSite | O88457. |
Proteomic databases | |
| PaxDb | O88457. |
| PRIDE | O88457. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 29701. |
| KEGG | rno:29701. |
| UCSC | RGD:3630. rat. |
Organism-specific databases | |
| CTD | 11280. |
| RGD | 3630. Scn11a. |
Phylogenomic databases | |
| eggNOG | COG1226. |
| HOGENOM | HOG000231755. |
| HOVERGEN | HBG053100. |
| InParanoid | O88457. |
| KO | K04843. |
| OrthoDB | EOG41RPT1. |
Gene expression databases | |
| ArrayExpress | O88457. |
| Genevestigator | O88457. |
| GermOnline | ENSRNOG00000032884. Rattus norvegicus. |
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 | |
| BindingDB | O88457. |
| ChEMBL | CHEMBL2629. |
| NextBio | 610107. |
Entry information
| Entry name | SCNBA_RAT | ||||||||
| Accession | Primary (citable) accession number: O88457 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
