O88420 · SCN8A_RAT
- ProteinSodium channel protein type 8 subunit alpha
- GeneScn8a
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1978 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Pore-forming subunit of a voltage-gated sodium channel complex assuming opened or closed conformations in response to the voltage difference across membranes and through which sodium ions selectively pass along their electrochemical gradient. Contributes to neuronal excitability by regulating action potential threshold and propagation.
Catalytic activity
- Na+(in) = Na+(out)
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameSodium channel protein type 8 subunit alpha
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionO88420
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Note: Mainly localizes to the axon initial segment.
Features
Showing features for topological domain, transmembrane, intramembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-132 | Cytoplasmic | ||||
Sequence: MAARLLAPPGPDSFKPFTPESLANIERRIAESKLKKPPKADGSHREDDEDSKPKPNSDLEAGKSLPFIYGDIPQGLVAVPLEDFDPYYLTQKTFVVLNRGKTLFRFSATPALYILSPFNLIRRIAIKILIHS | ||||||
Transmembrane | 133-151 | Helical; Name=S1 of repeat I | ||||
Sequence: VFSMIIMCTILTNCVFMTF | ||||||
Topological domain | 152-158 | Extracellular | ||||
Sequence: SNPPEWS | ||||||
Transmembrane | 159-179 | Helical; Name=S2 of repeat I | ||||
Sequence: KNVEYTFTGIYTFESLVKIIA | ||||||
Topological domain | 180-193 | Cytoplasmic | ||||
Sequence: RGFCIDGFTFLRDP | ||||||
Transmembrane | 194-211 | Helical; Name=S3 of repeat I | ||||
Sequence: WNWLDFSVIMMAYVTEFV | ||||||
Topological domain | 212-217 | Extracellular | ||||
Sequence: DLGNVS | ||||||
Transmembrane | 218-234 | Helical; Name=S4 of repeat I | ||||
Sequence: ALRTFRVLRALKTISVI | ||||||
Topological domain | 235-253 | Cytoplasmic | ||||
Sequence: PGLKTIVGALIQSVKKLSD | ||||||
Transmembrane | 254-273 | Helical; Name=S5 of repeat I | ||||
Sequence: VMILTVFCLSVFALIGLQLF | ||||||
Topological domain | 274-355 | Extracellular | ||||
Sequence: MGNLRNKCVVWPINFNESYLENGTRGFDWEEYINNKTNFYMVPGMLEPLLCGNSSDAGQCPEGFQCMKAGRNPNYGYTSFDT | ||||||
Intramembrane | 356-380 | Pore-forming | ||||
Sequence: FSWAFLALFRLMTQDYWENLYQLTL | ||||||
Topological domain | 381-387 | Extracellular | ||||
Sequence: RAAGKTY | ||||||
Transmembrane | 388-408 | Helical; Name=S6 of repeat I | ||||
Sequence: MIFFVLVIFVGSFYLVNLILA | ||||||
Topological domain | 409-751 | Cytoplasmic | ||||
Sequence: VVAMAYEEQNQATLEEAEQKEAEFKAMLEQLKKQQEEAQAAAMATSAGTVSEDAIEEEGEDGVGSPRSSSELSKLSSKSAKERRNRRKKRKQKELSEGEEKGDPEKVFKSESEDGMRRKAFRLPDNRIGRKFSIMNQSLLSIPGSPFLSRHNSKSSIFSFRGPGRFRDPGSENEFADDEHSTVEESEGRRDSLFIPIRARERRSSYSGYSGYSQCSRSSRIFPSLRRSVKRNSTVDCNGVVSLIGPGSHIGRLLPEATTEVEIKKKGPGSLLVSMDQLASYGRKDRINSIMSVVTNTLVEELEESQRKCPPCWYKFANTFLIWECHPYWIKLKEIVNLIVMDP | ||||||
Transmembrane | 752-770 | Helical; Name=S1 of repeat II | ||||
Sequence: FVDLAITICIVLNTLFMAM | ||||||
Topological domain | 771-781 | Extracellular | ||||
Sequence: EHHPMTPQFEH | ||||||
Transmembrane | 782-801 | Helical; Name=S2 of repeat II | ||||
Sequence: VLAVGNLVFTGIFTAEMFLK | ||||||
Topological domain | 802-815 | Cytoplasmic | ||||
Sequence: LIAMDPYYYFQEGW | ||||||
Transmembrane | 816-835 | Helical; Name=S3 of repeat II | ||||
Sequence: NIFDGFIVSLSLMELSLADV | ||||||
Topological domain | 836-837 | Extracellular | ||||
Sequence: EG | ||||||
Transmembrane | 838-855 | Helical; Name=S4 of repeat II | ||||
Sequence: LSVLRSFRLLRVFKLAKS | ||||||
Topological domain | 856-871 | Cytoplasmic | ||||
Sequence: WPTLNMLIKIIGNSVG | ||||||
Transmembrane | 872-890 | Helical; Name=S5 of repeat II | ||||
Sequence: ALGNLTLVLAIIVFIFAVV | ||||||
Topological domain | 891-919 | Extracellular | ||||
Sequence: GMQLFGKSYKECVCKINQECKLPRWHMND | ||||||
Intramembrane | 920-940 | Pore-forming | ||||
Sequence: FFHSFLIVFRVLCGEWIETMW | ||||||
Topological domain | 941-953 | Extracellular | ||||
Sequence: DCMEVAGQAMCLI | ||||||
Transmembrane | 954-974 | Helical; Name=S6 of repeat II | ||||
Sequence: VFMMVMVIGNLVVLNLFLALL | ||||||
Topological domain | 975-1197 | Cytoplasmic | ||||
Sequence: LSSFSADNLAATDDDGEMNNLQISVIRIKKGVAWTKVKVHAFMQAHFKQREADEVKPLDELYEKKANCIANHTGVDIHRNGDFQKNGNGTTSGIGSSVEKYIIDEDHMSFINNPNLTVRVPIAVGESDFENLNTEDVSSESDPEGSKDKLDDTSSSEGSTIDIKPEVEEVPVEQPEEYLDPDACFTEGCVQRFKCCQVNIEEGLGKSWWILRKTCFLIVEHNW | ||||||
Transmembrane | 1198-1215 | Helical; Name=S1 of repeat III | ||||
Sequence: FETFIIFMILLSSGALAF | ||||||
Topological domain | 1216-1228 | Extracellular | ||||
Sequence: EDIYIEQRKTIRT | ||||||
Transmembrane | 1229-1247 | Helical; Name=S2 of repeat III | ||||
Sequence: ILEYADKVFTYIFILEMLL | ||||||
Topological domain | 1248-1261 | Cytoplasmic | ||||
Sequence: KWTAYGFVKFFTNA | ||||||
Transmembrane | 1262-1280 | Helical; Name=S3 of repeat III | ||||
Sequence: WCWLDFLIVAVSLVSLIAN | ||||||
Topological domain | 1281-1288 | Extracellular | ||||
Sequence: ALGYSELG | ||||||
Transmembrane | 1289-1307 | Helical; Name=S4 of repeat III | ||||
Sequence: AIKSLRTLRALRPLRALSR | ||||||
Topological domain | 1308-1324 | Cytoplasmic | ||||
Sequence: FEGMRVVVNALVGAIPS | ||||||
Transmembrane | 1325-1344 | Helical; Name=S5 of repeat III | ||||
Sequence: IMNVLLVCLIFWLIFSIMGV | ||||||
Topological domain | 1345-1397 | Extracellular | ||||
Sequence: NLFAGKYHYCFNETSEIRFEIDIVNNKTDCEKLMEGNSTEIRWKNVKINFDNV | ||||||
Intramembrane | 1398-1419 | Pore-forming | ||||
Sequence: GAGYLALLQVATFKGWMDIMYA | ||||||
Topological domain | 1420-1436 | Extracellular | ||||
Sequence: AVDSRKPDEQPDYEGNI | ||||||
Transmembrane | 1437-1458 | Helical; Name=S6 of repeat III | ||||
Sequence: YMYIYFVIFIIFGSFFTLNLFI | ||||||
Topological domain | 1459-1521 | Cytoplasmic | ||||
Sequence: GVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKIQGIVFDFVTQQA | ||||||
Transmembrane | 1522-1539 | Helical; Name=S1 of repeat IV | ||||
Sequence: FDIVIMMLICLNMVTMMV | ||||||
Topological domain | 1540-1550 | Extracellular | ||||
Sequence: ETDTQSKQMEN | ||||||
Transmembrane | 1551-1569 | Helical; Name=S2 of repeat IV | ||||
Sequence: ILYWINLVFVIFFTCECVL | ||||||
Topological domain | 1570-1581 | Cytoplasmic | ||||
Sequence: KMFALRHYYFTI | ||||||
Transmembrane | 1582-1599 | Helical; Name=S3 of repeat IV | ||||
Sequence: GWNIFDFVVVILSIVGMF | ||||||
Topological domain | 1600-1612 | Extracellular | ||||
Sequence: LADIIEKYFVSPT | ||||||
Transmembrane | 1613-1629 | Helical; Name=S4 of repeat IV | ||||
Sequence: LFRVIRLARIGRILRLI | ||||||
Topological domain | 1630-1648 | Cytoplasmic | ||||
Sequence: KGAKGIRTLLFALMMSLPA | ||||||
Transmembrane | 1649-1666 | Helical; Name=S5 of repeat IV | ||||
Sequence: LFNIGLLLFLVMFIFSIF | ||||||
Topological domain | 1667-1688 | Extracellular | ||||
Sequence: GMSNFAYVKHEAGIDDMFNFET | ||||||
Intramembrane | 1689-1711 | Pore-forming | ||||
Sequence: FGNSMICLFQITTSAGWDGLLLP | ||||||
Topological domain | 1712-1740 | Extracellular | ||||
Sequence: ILNRPPDCSLDKEHPGSGFKGDCGNPSVG | ||||||
Transmembrane | 1741-1763 | Helical; Name=S6 of repeat IV | ||||
Sequence: IFFFVSYIIISFLIVVNMYIAII | ||||||
Topological domain | 1764-1978 | Cytoplasmic | ||||
Sequence: LENFSVATEESADPLSEDDFETFYEIWEKFDPDATQFIEYCKLADFADALEHPLRVPKPNTIELIAMDLPMVSGDRIHCLDILFAFTKRVLGDSGELDILRQQMEERFVASNPSKVSYEPITTTLRRKQEEVSAVVLQRAYRGHLARRGFICRKMASNKLENGGTHRDKKESTPSTASLPSYDSVTKPDKEKQQRAEEGRRERAKRQKEVRESKC |
Keywords
- Cellular component
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000390890 | 1-1978 | Sodium channel protein type 8 subunit alpha | |||
Sequence: MAARLLAPPGPDSFKPFTPESLANIERRIAESKLKKPPKADGSHREDDEDSKPKPNSDLEAGKSLPFIYGDIPQGLVAVPLEDFDPYYLTQKTFVVLNRGKTLFRFSATPALYILSPFNLIRRIAIKILIHSVFSMIIMCTILTNCVFMTFSNPPEWSKNVEYTFTGIYTFESLVKIIARGFCIDGFTFLRDPWNWLDFSVIMMAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCVVWPINFNESYLENGTRGFDWEEYINNKTNFYMVPGMLEPLLCGNSSDAGQCPEGFQCMKAGRNPNYGYTSFDTFSWAFLALFRLMTQDYWENLYQLTLRAAGKTYMIFFVLVIFVGSFYLVNLILAVVAMAYEEQNQATLEEAEQKEAEFKAMLEQLKKQQEEAQAAAMATSAGTVSEDAIEEEGEDGVGSPRSSSELSKLSSKSAKERRNRRKKRKQKELSEGEEKGDPEKVFKSESEDGMRRKAFRLPDNRIGRKFSIMNQSLLSIPGSPFLSRHNSKSSIFSFRGPGRFRDPGSENEFADDEHSTVEESEGRRDSLFIPIRARERRSSYSGYSGYSQCSRSSRIFPSLRRSVKRNSTVDCNGVVSLIGPGSHIGRLLPEATTEVEIKKKGPGSLLVSMDQLASYGRKDRINSIMSVVTNTLVEELEESQRKCPPCWYKFANTFLIWECHPYWIKLKEIVNLIVMDPFVDLAITICIVLNTLFMAMEHHPMTPQFEHVLAVGNLVFTGIFTAEMFLKLIAMDPYYYFQEGWNIFDGFIVSLSLMELSLADVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKINQECKLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQAMCLIVFMMVMVIGNLVVLNLFLALLLSSFSADNLAATDDDGEMNNLQISVIRIKKGVAWTKVKVHAFMQAHFKQREADEVKPLDELYEKKANCIANHTGVDIHRNGDFQKNGNGTTSGIGSSVEKYIIDEDHMSFINNPNLTVRVPIAVGESDFENLNTEDVSSESDPEGSKDKLDDTSSSEGSTIDIKPEVEEVPVEQPEEYLDPDACFTEGCVQRFKCCQVNIEEGLGKSWWILRKTCFLIVEHNWFETFIIFMILLSSGALAFEDIYIEQRKTIRTILEYADKVFTYIFILEMLLKWTAYGFVKFFTNAWCWLDFLIVAVSLVSLIANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKYHYCFNETSEIRFEIDIVNNKTDCEKLMEGNSTEIRWKNVKINFDNVGAGYLALLQVATFKGWMDIMYAAVDSRKPDEQPDYEGNIYMYIYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKIQGIVFDFVTQQAFDIVIMMLICLNMVTMMVETDTQSKQMENILYWINLVFVIFFTCECVLKMFALRHYYFTIGWNIFDFVVVILSIVGMFLADIIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIFSIFGMSNFAYVKHEAGIDDMFNFETFGNSMICLFQITTSAGWDGLLLPILNRPPDCSLDKEHPGSGFKGDCGNPSVGIFFFVSYIIISFLIVVNMYIAIILENFSVATEESADPLSEDDFETFYEIWEKFDPDATQFIEYCKLADFADALEHPLRVPKPNTIELIAMDLPMVSGDRIHCLDILFAFTKRVLGDSGELDILRQQMEERFVASNPSKVSYEPITTTLRRKQEEVSAVVLQRAYRGHLARRGFICRKMASNKLENGGTHRDKKESTPSTASLPSYDSVTKPDKEKQQRAEEGRRERAKRQKEVRESKC | ||||||
Glycosylation | 215 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 281↔333 | |||||
Sequence: CVVWPINFNESYLENGTRGFDWEEYINNKTNFYMVPGMLEPLLCGNSSDAGQC | ||||||
Glycosylation | 289 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 295 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 308 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 326 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 518 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 520 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 902 | Interchain; with SCN2B or SCN4B | ||||
Sequence: C | ||||||
Disulfide bond | 902 | Interchain; with the conotoxin GVIIJ (when the channel is not linked to SCN2B or SCN4B; the bond to SCN2B or SCN4B protects the channel from the inhibition by toxin) | ||||
Sequence: C | ||||||
Disulfide bond | 904↔910 | |||||
Sequence: CKINQEC | ||||||
Disulfide bond | 942↔951 | |||||
Sequence: CMEVAGQAMC | ||||||
Disulfide bond | 1354↔1374 | |||||
Sequence: CFNETSEIRFEIDIVNNKTDC | ||||||
Glycosylation | 1356 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1370 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1381 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 1495 | Phosphoserine; by PKC | ||||
Sequence: S | ||||||
Disulfide bond | 1719↔1734 | |||||
Sequence: CSLDKEHPGSGFKGDC |
Post-translational modification
May be ubiquitinated by NEDD4L; which would promote its endocytosis.
Phosphorylation at Ser-1495 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Isoform 1 is highly expressed in brain, moderately in spinal cord, and at low levels in dorsal root ganglia, nodose ganglia and superior cervical ganglia. Not detected in sciatic nerve and non-neuronal tissues. Isoform 2 is hardly detectable, if at all, in brain, expressed at low levels in spinal cord and at highest levels in dorsal root ganglia.
Interaction
Subunit
The voltage-sensitive sodium channel consists of an ion-conducting pore-forming alpha subunit regulated by one or more beta-1 (SCN1B), beta-2 (SCN2B), beta-3 (SCN3B) and/or beta-4 (SCN4B) subunits. Beta-1 (SCN1B) and beta-3 (SCN3B) are non-covalently associated with alpha, while beta-2 (SCN2B) and beta-4 (SCN4B) are covalently linked by disulfide bonds. Interacts with NEDD4 and NEDD4L (By similarity).
Interacts with FGF13 (PubMed:15282281).
Interacts with FGF14, GBG3, GBB2 and SCN1B (By similarity).
Interacts with TMEM233 (By similarity).
Interacts with the conotoxin GVIIJ (PubMed:24497506).
Interacts with CALM1; the interaction modulates the inactivation rate of SCN8A (By similarity).
Interacts with FGF13 (PubMed:15282281).
Interacts with FGF14, GBG3, GBB2 and SCN1B (By similarity).
Interacts with TMEM233 (By similarity).
Interacts with the conotoxin GVIIJ (PubMed:24497506).
Interacts with CALM1; the interaction modulates the inactivation rate of SCN8A (By similarity).
Protein-protein interaction databases
Chemistry
Structure
Family & Domains
Features
Showing features for region, compositional bias, repeat, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-20 | Disordered | ||||
Sequence: MAARLLAPPGPDSFKPFTPE | ||||||
Compositional bias | 28-57 | Basic and acidic residues | ||||
Sequence: RIAESKLKKPPKADGSHREDDEDSKPKPNS | ||||||
Region | 28-62 | Disordered | ||||
Sequence: RIAESKLKKPPKADGSHREDDEDSKPKPNSDLEAG | ||||||
Repeat | 114-442 | I | ||||
Sequence: ILSPFNLIRRIAIKILIHSVFSMIIMCTILTNCVFMTFSNPPEWSKNVEYTFTGIYTFESLVKIIARGFCIDGFTFLRDPWNWLDFSVIMMAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCVVWPINFNESYLENGTRGFDWEEYINNKTNFYMVPGMLEPLLCGNSSDAGQCPEGFQCMKAGRNPNYGYTSFDTFSWAFLALFRLMTQDYWENLYQLTLRAAGKTYMIFFVLVIFVGSFYLVNLILAVVAMAYEEQNQATLEEAEQKEAEFKAMLEQLKKQ | ||||||
Region | 446-530 | Disordered | ||||
Sequence: AQAAAMATSAGTVSEDAIEEEGEDGVGSPRSSSELSKLSSKSAKERRNRRKKRKQKELSEGEEKGDPEKVFKSESEDGMRRKAFR | ||||||
Compositional bias | 500-530 | Basic and acidic residues | ||||
Sequence: QKELSEGEEKGDPEKVFKSESEDGMRRKAFR | ||||||
Region | 576-597 | Disordered | ||||
Sequence: DPGSENEFADDEHSTVEESEGR | ||||||
Repeat | 733-1005 | II | ||||
Sequence: CHPYWIKLKEIVNLIVMDPFVDLAITICIVLNTLFMAMEHHPMTPQFEHVLAVGNLVFTGIFTAEMFLKLIAMDPYYYFQEGWNIFDGFIVSLSLMELSLADVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKINQECKLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQAMCLIVFMMVMVIGNLVVLNLFLALLLSSFSADNLAATDDDGEMNNLQISVIRIKKG | ||||||
Region | 1105-1146 | Disordered | ||||
Sequence: NLNTEDVSSESDPEGSKDKLDDTSSSEGSTIDIKPEVEEVPV | ||||||
Compositional bias | 1114-1129 | Basic and acidic residues | ||||
Sequence: ESDPEGSKDKLDDTSS | ||||||
Repeat | 1178-1493 | III | ||||
Sequence: LGKSWWILRKTCFLIVEHNWFETFIIFMILLSSGALAFEDIYIEQRKTIRTILEYADKVFTYIFILEMLLKWTAYGFVKFFTNAWCWLDFLIVAVSLVSLIANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKYHYCFNETSEIRFEIDIVNNKTDCEKLMEGNSTEIRWKNVKINFDNVGAGYLALLQVATFKGWMDIMYAAVDSRKPDEQPDYEGNIYMYIYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKL | ||||||
Repeat | 1502-1799 | IV | ||||
Sequence: IPRPLNKIQGIVFDFVTQQAFDIVIMMLICLNMVTMMVETDTQSKQMENILYWINLVFVIFFTCECVLKMFALRHYYFTIGWNIFDFVVVILSIVGMFLADIIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIFSIFGMSNFAYVKHEAGIDDMFNFETFGNSMICLFQITTSAGWDGLLLPILNRPPDCSLDKEHPGSGFKGDCGNPSVGIFFFVSYIIISFLIVVNMYIAIILENFSVATEESADPLSEDDFETFYEIWEKFDPDATQ | ||||||
Domain | 1893-1922 | IQ | ||||
Sequence: EEVSAVVLQRAYRGHLARRGFICRKMASNK | ||||||
Region | 1923-1978 | Disordered | ||||
Sequence: LENGGTHRDKKESTPSTASLPSYDSVTKPDKEKQQRAEEGRRERAKRQKEVRESKC | ||||||
Compositional bias | 1948-1978 | Basic and acidic residues | ||||
Sequence: VTKPDKEKQQRAEEGRRERAKRQKEVRESKC |
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. Nav1.6/SCN8A subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
O88420-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsPN4
- Length1,978
- Mass (Da)225,159
- Last updated1998-11-01 v1
- Checksum9160843C5935B88B
O88420-2
- Name2
- SynonymsPN4a
- NoteMay be due to competing donor splice site.
- Differences from canonical
- 664-664: E → EVKIDKAATDS
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F1LMH2 | F1LMH2_RAT | Scn8a | 1978 | ||
A0A0G2KB93 | A0A0G2KB93_RAT | Scn8a | 1977 | ||
A0A8I5ZX68 | A0A8I5ZX68_RAT | Scn8a | 1937 |
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 28-57 | Basic and acidic residues | ||||
Sequence: RIAESKLKKPPKADGSHREDDEDSKPKPNS | ||||||
Compositional bias | 500-530 | Basic and acidic residues | ||||
Sequence: QKELSEGEEKGDPEKVFKSESEDGMRRKAFR | ||||||
Alternative sequence | VSP_038652 | 664 | in isoform 2 | |||
Sequence: E → EVKIDKAATDS | ||||||
Compositional bias | 1114-1129 | Basic and acidic residues | ||||
Sequence: ESDPEGSKDKLDDTSS | ||||||
Compositional bias | 1948-1978 | Basic and acidic residues | ||||
Sequence: VTKPDKEKQQRAEEGRRERAKRQKEVRESKC |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF049239 EMBL· GenBank· DDBJ | AAC26014.1 EMBL· GenBank· DDBJ | mRNA | ||
AF049240 EMBL· GenBank· DDBJ | AAC26015.1 EMBL· GenBank· DDBJ | mRNA |