P15390 (SCN4A_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 110.
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 4 subunit alpha Alternative name(s): Mu-1 SkM1 Sodium channel protein skeletal muscle subunit alpha Sodium channel protein type IV subunit alpha Voltage-gated sodium channel subunit alpha Nav1.4 | ||
| 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 | 1840 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript 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 Na+ ions may pass in accordance with their electrochemical gradient. This sodium channel may be present in both denervated and innervated skeletal muscle. |
| Subunit structure | Muscle sodium channels contain an alpha subunit and a smaller beta subunit. Interacts with the PDZ domain of the syntrophin SNTA1, SNTB1 and SNTB2 By similarity. |
| Subcellular location | |
| 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. Nav1.4/SCN4A subfamily. [View classification] Contains 1 IQ domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Ion transport Sodium transport Transport |
| Cellular component | Membrane |
| Coding sequence diversity | Polymorphism |
| 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 | voltage-gated sodium channel complex Inferred from electronic annotation. Source: InterPro |
| Molecular_function | voltage-gated sodium channel activity Traceable author statement Ref.2. Source: RGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1840 | 1840 | Sodium channel protein type 4 subunit alpha | PRO_0000048496 | |||||
Regions | |||||||||
| Transmembrane | 130 – 152 | 23 | Helical; Name=S1 of repeat I | ||||||
| Transmembrane | 156 – 179 | 24 | Helical; Name=S2 of repeat I | ||||||
| Transmembrane | 192 – 212 | 21 | Helical; Name=S3 of repeat I | ||||||
| Transmembrane | 214 – 233 | 20 | Helical; Voltage-sensor; Name=S4 of repeat I | ||||||
| Transmembrane | 252 – 274 | 23 | Helical; Name=S5 of repeat I | ||||||
| Transmembrane | 417 – 444 | 28 | Helical; Name=S6 of repeat I | ||||||
| Transmembrane | 571 – 593 | 23 | Helical; Name=S1 of repeat II | ||||||
| Transmembrane | 602 – 626 | 25 | Helical; Name=S2 of repeat II | ||||||
| Transmembrane | 634 – 654 | 21 | Helical; Name=S3 of repeat II | ||||||
| Transmembrane | 661 – 680 | 20 | Helical; Voltage-sensor; Name=S4 of repeat II | ||||||
| Transmembrane | 697 – 717 | 21 | Helical; Name=S5 of repeat II | ||||||
| Transmembrane | 771 – 796 | 26 | Helical; Name=S6 of repeat II | ||||||
| Transmembrane | 1020 – 1043 | 24 | Helical; Name=S1 of repeat III | ||||||
| Transmembrane | 1057 – 1082 | 26 | Helical; Name=S2 of repeat III | ||||||
| Transmembrane | 1088 – 1110 | 23 | Helical; Name=S3 of repeat III | ||||||
| Transmembrane | 1115 – 1136 | 22 | Helical; Voltage-sensor; Name=S4 of repeat III | ||||||
| Transmembrane | 1156 – 1177 | 22 | Helical; Name=S5 of repeat III | ||||||
| Transmembrane | 1262 – 1288 | 27 | Helical; Name=S6 of repeat III | ||||||
| Transmembrane | 1342 – 1365 | 24 | Helical; Name=S1 of repeat IV | ||||||
| Transmembrane | 1377 – 1400 | 24 | Helical; Name=S2 of repeat IV | ||||||
| Transmembrane | 1407 – 1430 | 24 | Helical; Name=S3 of repeat IV | ||||||
| Transmembrane | 1441 – 1462 | 22 | Helical; Voltage-sensor; Name=S4 of repeat IV | ||||||
| Transmembrane | 1478 – 1500 | 23 | Helical; Name=S5 of repeat IV | ||||||
| Transmembrane | 1567 – 1591 | 25 | Helical; Name=S6 of repeat IV | ||||||
| Repeat | 128 – 444 | 317 | I | ||||||
| Repeat | 565 – 790 | 226 | II | ||||||
| Repeat | 1017 – 1274 | 258 | III | ||||||
| Repeat | 1342 – 1588 | 247 | IV | ||||||
| Domain | 1720 – 1749 | 30 | IQ | ||||||
Amino acid modifications | |||||||||
| Modified residue | 56 | 1 | Phosphoserine; by PKA Potential | ||||||
| Modified residue | 251 | 1 | Phosphoserine; by PKA Potential | ||||||
| Modified residue | 1321 | 1 | Phosphoserine; by PKA Potential | ||||||
| Modified residue | 1504 | 1 | Phosphoserine; by PKA Potential | ||||||
| Glycosylation | 288 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 291 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 297 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 303 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 309 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 315 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 327 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 356 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 502 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 954 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1198 | 1 | N-linked (GlcNAc...) Potential | ||||||
Natural variations | |||||||||
| Natural variant | 120 | 1 | V → I in strain: COP; prostatic cancer cell lines. Ref.2 | ||||||
| Natural variant | 916 | 1 | Q → H in strain: COP; prostatic cancer cell lines. Ref.2 | ||||||
| Natural variant | 1202 | 1 | S → C in strain: COP; prostatic cancer cell lines. Ref.2 | ||||||
| Natural variant | 1257 | 1 | H → D in strain: COP; prostatic cancer cell lines. Ref.2 | ||||||
| Natural variant | 1755 | 1 | D → G in strain: COP; prostatic cancer cell lines. Ref.2 | ||||||
| Natural variant | 1803 | 1 | E → K in strain: COP; prostatic cancer cell lines. Ref.2 | ||||||
Sequences
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References
| [1] | "Primary structure and functional expression of a mammalian skeletal muscle sodium channel." Trimmer J.S., Cooperman S.S., Tomiko S.A., Zhou J., Crean S.M., Boyle M.B., Kallen R.G., Sheng Z., Barchi R.L., Sigworth F.J., Goodman R.H., Agnew W.S., Mandel G. Neuron 3:33-49(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Expression of skeletal muscle-type voltage-gated Na+ channel in rat and human prostate cancer cell lines." Diss J.K.J., Stewart D., Fraser S.P., Black J.A., Dibb-Hajj S., Waxman S.G., Archer S.N., Djamgoz M.B.A. FEBS Lett. 427:5-10(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ILE-120; HIS-916; CYS-1202; ASP-1257; GLY-1755 AND LYS-1803. Strain: COP. Tissue: Prostate. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M26643 mRNA. Translation: AAA41682.1. Y17153 mRNA. Translation: CAA76659.1. |
| IPI | IPI00339065. |
| PIR | CHRTM1. JN0007. |
| RefSeq | NP_037310.1. NM_013178.1. |
| UniGene | Rn.9700. |
3D structure databases | |
| ProteinModelPortal | P15390. |
| ModBase | Search... |
Proteomic databases | |
| PaxDb | P15390. |
| PRIDE | P15390. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 25722. |
| KEGG | rno:25722. |
| UCSC | RGD:3636. rat. |
Organism-specific databases | |
| CTD | 6329. |
| RGD | 3636. Scn4a. |
Phylogenomic databases | |
| eggNOG | COG1226. |
| HOGENOM | HOG000231755. |
| HOVERGEN | HBG053100. |
| InParanoid | O70611. |
| KO | K04837. |
| OrthoDB | EOG4B2SW8. |
Gene expression databases | |
| ArrayExpress | P15390. |
| Genevestigator | P15390. |
| GermOnline | ENSRNOG00000012134. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR005821. Ion_trans_dom. IPR000048. IQ_motif_EF-hand-BS. IPR008052. Na_channel_a4su. 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. PR01665. NACHANNEL4. |
| SMART | SM00015. IQ. 1 hit. [Graphical view] |
| PROSITE | PS50096. IQ. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| BindingDB | P15390. |
| ChEMBL | CHEMBL3509. |
| NextBio | 607821. |
Entry information
| Entry name | SCN4A_RAT | ||||||||
| Accession | Primary (citable) accession number: P15390 Secondary accession number(s): O70611 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
