Q9ER60 (SCN4A_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 80.
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): Sodium channel protein skeletal muscle subunit alpha Sodium channel protein type IV subunit alpha Voltage-gated sodium channel subunit alpha Nav1.4 | ||
| Gene names |
| ||
| 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 | 1841 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 | |
| Tissue specificity | Expressed in the myocardium. Ref.1 |
| 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 |
| Domain | Repeat Transmembrane Transmembrane helix |
| Ligand | Sodium |
| Molecular function | Ion channel Sodium channel Voltage-gated channel |
| PTM | Glycoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Cellular_component | voltage-gated sodium channel complex Inferred by curator Ref.1. Source: MGI |
| Molecular_function | voltage-gated sodium channel activity Inferred from direct assay Ref.1. Source: MGI |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1841 | 1841 | Sodium channel protein type 4 subunit alpha | PRO_0000371316 | |||||
Regions | |||||||||
| Transmembrane | 129 – 150 | 22 | Helical; Name=S1 of repeat I; Potential | ||||||
| Transmembrane | 159 – 178 | 20 | Helical; Name=S2 of repeat I; Potential | ||||||
| Transmembrane | 191 – 210 | 20 | Helical; Name=S3 of repeat I; Potential | ||||||
| Transmembrane | 217 – 236 | 20 | Helical; Voltage-sensor; Name=S4 of repeat I; Potential | ||||||
| Transmembrane | 253 – 266 | 14 | Helical; Name=S5 of repeat I; Potential | ||||||
| Transmembrane | 418 – 443 | 26 | Helical; Name=S6 of repeat I; Potential | ||||||
| Transmembrane | 568 – 591 | 24 | Helical; Name=S1 of repeat II; Potential | ||||||
| Transmembrane | 603 – 626 | 24 | Helical; Name=S2 of repeat II; Potential | ||||||
| Transmembrane | 635 – 654 | 20 | Helical; Name=S3 of repeat II; Potential | ||||||
| Transmembrane | 661 – 680 | 20 | Helical; Voltage-sensor; Name=S4 of repeat II; Potential | ||||||
| Transmembrane | 696 – 718 | 23 | Helical; Name=S5 of repeat II; Potential | ||||||
| Transmembrane | 771 – 796 | 26 | Helical; Name=S6 of repeat II; Potential | ||||||
| Transmembrane | 1021 – 1043 | 23 | Helical; Name=S1 of repeat III; Potential | ||||||
| Transmembrane | 1058 – 1083 | 26 | Helical; Name=S2 of repeat III; Potential | ||||||
| Transmembrane | 1090 – 1110 | 21 | Helical; Name=S3 of repeat III; Potential | ||||||
| Transmembrane | 1116 – 1137 | 22 | Helical; Voltage-sensor; Name=S4 of repeat III; Potential | ||||||
| Transmembrane | 1157 – 1178 | 22 | Helical; Name=S5 of repeat III; Potential | ||||||
| Transmembrane | 1263 – 1289 | 27 | Helical; Name=S6 of repeat III; Potential | ||||||
| Transmembrane | 1343 – 1366 | 24 | Helical; Name=S1 of repeat IV; Potential | ||||||
| Transmembrane | 1378 – 1401 | 24 | Helical; Name=S2 of repeat IV; Potential | ||||||
| Transmembrane | 1408 – 1431 | 24 | Helical; Name=S3 of repeat IV; Potential | ||||||
| Transmembrane | 1441 – 1463 | 23 | Helical; Voltage-sensor; Name=S4 of repeat IV; Potential | ||||||
| Transmembrane | 1479 – 1501 | 23 | Helical; Name=S5 of repeat IV; Potential | ||||||
| Transmembrane | 1568 – 1592 | 25 | Helical; Name=S6 of repeat IV; Potential | ||||||
| Repeat | 128 – 444 | 317 | I | ||||||
| Repeat | 565 – 790 | 226 | II | ||||||
| Repeat | 1018 – 1275 | 258 | III | ||||||
| Repeat | 1343 – 1589 | 247 | IV | ||||||
| Domain | 1721 – 1750 | 30 | IQ | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 214 | 1 | N-linked (GlcNAc...) 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 | 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 | 955 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1185 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1199 | 1 | N-linked (GlcNAc...) Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 131 | 1 | A → T in CAM23795. Ref.2 | ||||||
| Sequence conflict | 1056 | 1 | R → Q in CAM23795. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Mouse heart Na+ channels: primary structure and function of two isoforms and alternatively spliced variants." Zimmer T., Bollensdorff C., Haufe V., Birch-Hirschfeld E., Benndorf K. Am. J. Physiol. 282:H1007-H1017(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: BALB/c. Tissue: Heart. |
| [2] | "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. |
| [3] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1841. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AJ278787 mRNA. Translation: CAC17146.1. AL604045 Genomic DNA. Translation: CAM23795.1. BC129805 mRNA. Translation: AAI29806.1. |
| IPI | IPI00318790. |
| RefSeq | NP_573462.2. NM_133199.2. |
| UniGene | Mm.432528. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1BYY based on UniProtKB P04775. |
| ProteinModelPortal | Q9ER60. |
| SMR | Q9ER60. Positions 131-272, 582-796, 1021-1290, 1340-1593, 1596-1748. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 10090.ENSMUSP00000102431. |
PTM databases | |
| PhosphoSite | Q9ER60. |
Proteomic databases | |
| PaxDb | Q9ER60. |
| PRIDE | Q9ER60. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 110880. |
| KEGG | mmu:110880. |
| UCSC | uc007lyu.1. mouse. |
Organism-specific databases | |
| CTD | 6329. |
| MGI | MGI:98250. Scn4a. |
Phylogenomic databases | |
| eggNOG | COG1226. |
| HOGENOM | HOG000231755. |
| InParanoid | B1ARK0. |
| KO | K04837. |
Gene expression databases | |
| Genevestigator | Q9ER60. |
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 | |
| NextBio | 364857. |
| SOURCE | Search... |
Entry information
| Entry name | SCN4A_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q9ER60 Secondary accession number(s): A2VDE9, B1ARK0 | ||||||||
| Entry history |
| ||||||||
| 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
