P08104 · SCN3A_RAT
- ProteinSodium channel protein type 3 subunit alpha
- GeneScn3a
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1951 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Pore-forming subunit of Nav1.3, a voltage-gated sodium (Nav) channel that directly mediates the depolarizing phase of action potentials in excitable membranes. Navs, also called VGSCs (voltage-gated sodium channels) or VDSCs (voltage-dependent sodium channels), operate by switching between closed and open conformations depending on the voltage difference across the membrane. In the open conformation they allow Na+ ions to selectively pass through the pore, along their electrochemical gradient. The influx of Na+ ions provokes membrane depolarization, initiating the propagation of electrical signals throughout cells and tissues (PubMed:25784299).
In some secretory cell types, it also participates in cell excitability through membrane depolarization and regulates cells responsiveness to stimuli triggering secretion. For instance, it controls the release of serotonin/5-hydroxytryptamine by enterochromaffin cells and is required for both glucagon- and glucose-induced insulin secretion in pancreatic endocrine cells (By similarity).
In some secretory cell types, it also participates in cell excitability through membrane depolarization and regulates cells responsiveness to stimuli triggering secretion. For instance, it controls the release of serotonin/5-hydroxytryptamine by enterochromaffin cells and is required for both glucagon- and glucose-induced insulin secretion in pancreatic endocrine cells (By similarity).
Catalytic activity
- Na+(in) = Na+(out)
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 1503 | Important residue that permits the spider RTX-VII toxin to inhibit fast inactivation of the channel | ||||
Sequence: K | ||||||
Site | 1506 | Important residue that permits the spider RTX-VII toxin to inhibit fast inactivation of the channel | ||||
Sequence: T | ||||||
Site | 1507 | Important residue that permits the spider RTX-VII toxin to inhibit fast inactivation of the channel | ||||
Sequence: L | ||||||
Site | 1510 | Key residue that permits the spider beta/delta-theraphotoxin-Pre1a to inhibit fast inactivation of the channel | ||||
Sequence: S | ||||||
Site | 1562 | Important residue that permits the spider RTX-VII toxin to inhibit fast inactivation of the channel | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | membrane | |
Cellular Component | neuronal cell body | |
Cellular Component | sarcoplasm | |
Cellular Component | voltage-gated sodium channel complex | |
Molecular Function | calmodulin binding | |
Molecular Function | sodium ion binding | |
Molecular Function | voltage-gated sodium channel activity | |
Biological Process | behavioral response to pain | |
Biological Process | cellular response to antibiotic | |
Biological Process | membrane depolarization during action potential | |
Biological Process | nervous system development | |
Biological Process | neuronal action potential | |
Biological Process | response to pyrethroid | |
Biological Process | sodium ion transmembrane transport |
Keywords
- Molecular function
- Biological process
- Ligand
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSodium channel protein type 3 subunit alpha
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP08104
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Basal cell membrane ; Multi-pass membrane protein
Note: In enterochromaffin cells, localized highly asymmetrically, almost exclusively at the basal side.
Features
Showing features for topological domain, transmembrane, intramembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-128 | Cytoplasmic | ||||
Sequence: MAQALLVPPGPESFRLFTRESLAAIEKRAAEEKAKKPKKEQDIDDENKPKPNSDLEAGKNLPFIYGDIPPEMVSEPLEDLDPYYVSKKTFVVLNKGKAIFRFSATSALYILTPLNPVRKIAIKILVHS | ||||||
Transmembrane | 129-146 | Helical; Name=S1 of repeat I | ||||
Sequence: LFSMLIMCTILTNCVFMT | ||||||
Topological domain | 147-152 | Extracellular | ||||
Sequence: LSNPPD | ||||||
Transmembrane | 153-174 | Helical; Name=S2 of repeat I | ||||
Sequence: WTKNVEYTFTGIYTFESLIKIL | ||||||
Topological domain | 175-188 | Cytoplasmic | ||||
Sequence: ARGFCLEDFTFLRD | ||||||
Transmembrane | 189-206 | Helical; Name=S3 of repeat I | ||||
Sequence: PWNWLDFSVIVMAYVTEF | ||||||
Topological domain | 207-213 | Extracellular | ||||
Sequence: VDLGNVS | ||||||
Transmembrane | 214-235 | Helical; Name=S4 of repeat I | ||||
Sequence: ALRTFRVLRALKTISVIPGLKT | ||||||
Topological domain | 236-249 | Cytoplasmic | ||||
Sequence: IVGALIQSVKKLSD | ||||||
Transmembrane | 250-269 | Helical; Name=S5 of repeat I | ||||
Sequence: VMILTVFCLSVFALIGLQLF | ||||||
Topological domain | 270-369 | Extracellular | ||||
Sequence: MGNLRNKCSQWPPSDSAFETNTTSYFNGTMDSNGTFVNVTMSTFNWKDYIADDSHFYVLDGQKDPLLCGNGSDAGQCPEGYICVKAGRNPNYGYTSFDTF | ||||||
Intramembrane | 370-386 | Pore-forming | ||||
Sequence: SWAFLSLFRLMTQDYWE | ||||||
Topological domain | 387-397 | Extracellular | ||||
Sequence: NLYQLTLRAAG | ||||||
Transmembrane | 398-424 | Helical; Name=S6 of repeat I | ||||
Sequence: KTYMIFFVLVIFLGSFYLVNLILAVVA | ||||||
Topological domain | 425-712 | Cytoplasmic | ||||
Sequence: MAYEEQNQATLEEAEQKEAEFQQMLEQLKKQQEEAQAVAAASAASRDFSGIGGLGELLESSSEASKLSSKSAKEWRNRRKKRRQREHLEGNHRADGDRFPKSESEDSVKRRSFLLSLDGNPLTGDKKLCSPHQSLLSIRGSLFSPRRNSKTSIFSFRGRAKDVGSENDFADDEHSTFEDSESRRDSLFVPHRPGERRNSNGTTTETEVRKRRLSSYQISMEMLEDSSGRQRSMSIASILTNTMEELEESRQKCPPCWYRFANVFLIWDCCDAWLKVKHLVNLIVMDPF | ||||||
Transmembrane | 713-730 | Helical; Name=S1 of repeat II | ||||
Sequence: VDLAITICIVLNTLFMAM | ||||||
Topological domain | 731-738 | Extracellular | ||||
Sequence: EHYPMTQQ | ||||||
Transmembrane | 739-763 | Helical; Name=S2 of repeat II | ||||
Sequence: FSSVLTVGNLVFTGIFTAEMVLKII | ||||||
Topological domain | 764-773 | Cytoplasmic | ||||
Sequence: AMDPYYYFQE | ||||||
Transmembrane | 774-793 | Helical; Name=S3 of repeat II | ||||
Sequence: GWNIFDGIIVSLSLMELGLA | ||||||
Topological domain | 794-797 | Extracellular | ||||
Sequence: NVEG | ||||||
Transmembrane | 798-816 | Helical; Name=S4 of repeat II | ||||
Sequence: LSVLRSFRLLRVFKLAKSW | ||||||
Topological domain | 817-834 | Cytoplasmic | ||||
Sequence: PTLNMLIKIIGNSVGALG | ||||||
Transmembrane | 835-855 | Helical; Name=S5 of repeat II | ||||
Sequence: NLTLVLAIIVFIFAVVGMQLF | ||||||
Topological domain | 856-880 | Extracellular | ||||
Sequence: GKSYKECVCKINVDCKLPRWHMNDF | ||||||
Intramembrane | 881-896 | Pore-forming | ||||
Sequence: FHSFLIVFRVLCGEWI | ||||||
Topological domain | 897-907 | Extracellular | ||||
Sequence: ETMWDCMEVAG | ||||||
Transmembrane | 908-934 | Helical; Name=S6 of repeat II | ||||
Sequence: QTMCLIVFMLVMVIGNLVVLNLFLALL | ||||||
Topological domain | 935-1156 | Cytoplasmic | ||||
Sequence: LSSFSSDNLAATDDDNEMNNLQIAVGRMQKGIDFVKNKIRECFRKAFFRKPKVIEIQEGNKIDSCMSNNTGIEISKELNYLKDGNGTTSGVGTGSSVEKYVIDENDYMSFINNPSLTVTVPIAVGESDFENLNTEEFSSESELEESKEKLNATSSSEGSTVDVAPPREGEQAEIEPEEDLKPEACFTEGCIKKFPFCQVSTEEGKGKIWWNLRKTCYSIVEH | ||||||
Transmembrane | 1157-1177 | Helical; Name=S1 of repeat III | ||||
Sequence: NWFETFIVFMILLSSGALAFE | ||||||
Topological domain | 1178-1189 | Extracellular | ||||
Sequence: DIYIEQRKTIKT | ||||||
Transmembrane | 1190-1211 | Helical; Name=S2 of repeat III | ||||
Sequence: MLEYADKVFTYIFILEMLLKWV | ||||||
Topological domain | 1212-1217 | Cytoplasmic | ||||
Sequence: AYGFQT | ||||||
Transmembrane | 1218-1243 | Helical; Name=S3 of repeat III | ||||
Sequence: YFTNAWCWLDFLIVDVSLVSLVANAL | ||||||
Topological domain | 1244-1252 | Extracellular | ||||
Sequence: GYSELGAIK | ||||||
Transmembrane | 1253-1271 | Helical; Name=S4 of repeat III | ||||
Sequence: SLRTLRALRPLRALSRFEG | ||||||
Topological domain | 1272-1284 | Cytoplasmic | ||||
Sequence: MRVVVNALVGAIP | ||||||
Transmembrane | 1285-1307 | Helical; Name=S5 of repeat III | ||||
Sequence: SIMNVLLVCLIFWLIFSIMGVNL | ||||||
Topological domain | 1308-1353 | Extracellular | ||||
Sequence: FAGKFYHCVNTTTGNMFEIKEVNNFSDCQALGKQARWKNVKVNFDN | ||||||
Intramembrane | 1354-1370 | Pore-forming | ||||
Sequence: VGAGYLALLQVATFKGW | ||||||
Topological domain | 1371-1393 | Extracellular | ||||
Sequence: MDIMYAAVDSRDVKLQPIYEENL | ||||||
Transmembrane | 1394-1419 | Helical; Name=S6 of repeat III | ||||
Sequence: YMYLYFVIFIIFGSFFTLNLFIGVII | ||||||
Topological domain | 1420-1477 | Cytoplasmic | ||||
Sequence: DNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPANKFQGMVFDFVTRQ | ||||||
Transmembrane | 1478-1496 | Helical; Name=S1 of repeat IV | ||||
Sequence: VFDISIMILICLNMVTMMV | ||||||
Topological domain | 1497-1504 | Extracellular | ||||
Sequence: ETDDQSKY | ||||||
Transmembrane | 1505-1528 | Helical; Name=S2 of repeat IV | ||||
Sequence: MTLVLSRINLVFIVLFTGEFLLKL | ||||||
Topological domain | 1529-1538 | Cytoplasmic | ||||
Sequence: ISLRYYYFTI | ||||||
Transmembrane | 1539-1556 | Helical; Name=S3 of repeat IV | ||||
Sequence: GWNIFDFVVVILSIVGMF | ||||||
Topological domain | 1557-1568 | Extracellular | ||||
Sequence: LAELIEKYFVSP | ||||||
Transmembrane | 1569-1591 | Helical; Name=S4 of repeat IV | ||||
Sequence: TLFRVIRLARIGRILRLIKGAKG | ||||||
Topological domain | 1592-1604 | Cytoplasmic | ||||
Sequence: IRTLLFALMMSLP | ||||||
Transmembrane | 1605-1628 | Helical; Name=S5 of repeat IV | ||||
Sequence: ALFNIGLLLFLVMFIYAIFGMSNF | ||||||
Topological domain | 1629-1650 | Extracellular | ||||
Sequence: AYVKKEAGIDDMFNFETFGNSM | ||||||
Intramembrane | 1651-1663 | Pore-forming | ||||
Sequence: ICLFQITTSAGWD | ||||||
Topological domain | 1664-1695 | Extracellular | ||||
Sequence: GLLAPILNSAPPDCDPDAIHPGSSVKGDCGNP | ||||||
Transmembrane | 1696-1721 | Helical; Name=S6 of repeat IV | ||||
Sequence: SVGIFFFVSYIIISFLVVVNMYIAVI | ||||||
Topological domain | 1722-1951 | Cytoplasmic | ||||
Sequence: LENFSVATEESAEPLSEDDFEMFYEVWEKFDPDATQFIEFCKLSDFAAALDPPLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDALRIQMEDRFMASNPSKVSYEPITTTLKRKQEEVSAAIIQRNYRCYLLKQRLKNISSKYDKETIKGRIDLPIKGDMVIDKLNGNSTPEKTDGSSSTTSPPSYDSVTKPDKEKFEKDKPEKEIKGKEVRENQK |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 1503 | 6-fold decrease in activity of the spider RTX-VII toxin. | ||||
Sequence: K → P | ||||||
Mutagenesis | 1504 | 2-fold decrease in activity of the spider RTX-VII toxin. | ||||
Sequence: Y → E | ||||||
Mutagenesis | 1505 | 4.5-fold decrease in activity of the spider RTX-VII toxin. | ||||
Sequence: M → K | ||||||
Mutagenesis | 1506 | 10-fold decrease in activity of the spider RTX-VII toxin. | ||||
Sequence: T → I | ||||||
Mutagenesis | 1507 | 12-fold decrease in activity of the spider RTX-VII toxin. | ||||
Sequence: L → N | ||||||
Mutagenesis | 1559 | Increase in sensitivity to the scorpion toxin BMKM1. | ||||
Sequence: E → D | ||||||
Mutagenesis | 1562 | 5.5-fold decrease in activity of the spider RTX-VII toxin. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 1562 | 20-fold decrease in activity of the spider RTX-VII toxin. | ||||
Sequence: E → R |
Chemistry
PTM/Processing
Features
Showing features for chain, glycosylation, modified residue, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000048494 | 1-1951 | Sodium channel protein type 3 subunit alpha | |||
Sequence: MAQALLVPPGPESFRLFTRESLAAIEKRAAEEKAKKPKKEQDIDDENKPKPNSDLEAGKNLPFIYGDIPPEMVSEPLEDLDPYYVSKKTFVVLNKGKAIFRFSATSALYILTPLNPVRKIAIKILVHSLFSMLIMCTILTNCVFMTLSNPPDWTKNVEYTFTGIYTFESLIKILARGFCLEDFTFLRDPWNWLDFSVIVMAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCSQWPPSDSAFETNTTSYFNGTMDSNGTFVNVTMSTFNWKDYIADDSHFYVLDGQKDPLLCGNGSDAGQCPEGYICVKAGRNPNYGYTSFDTFSWAFLSLFRLMTQDYWENLYQLTLRAAGKTYMIFFVLVIFLGSFYLVNLILAVVAMAYEEQNQATLEEAEQKEAEFQQMLEQLKKQQEEAQAVAAASAASRDFSGIGGLGELLESSSEASKLSSKSAKEWRNRRKKRRQREHLEGNHRADGDRFPKSESEDSVKRRSFLLSLDGNPLTGDKKLCSPHQSLLSIRGSLFSPRRNSKTSIFSFRGRAKDVGSENDFADDEHSTFEDSESRRDSLFVPHRPGERRNSNGTTTETEVRKRRLSSYQISMEMLEDSSGRQRSMSIASILTNTMEELEESRQKCPPCWYRFANVFLIWDCCDAWLKVKHLVNLIVMDPFVDLAITICIVLNTLFMAMEHYPMTQQFSSVLTVGNLVFTGIFTAEMVLKIIAMDPYYYFQEGWNIFDGIIVSLSLMELGLANVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKINVDCKLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQTMCLIVFMLVMVIGNLVVLNLFLALLLSSFSSDNLAATDDDNEMNNLQIAVGRMQKGIDFVKNKIRECFRKAFFRKPKVIEIQEGNKIDSCMSNNTGIEISKELNYLKDGNGTTSGVGTGSSVEKYVIDENDYMSFINNPSLTVTVPIAVGESDFENLNTEEFSSESELEESKEKLNATSSSEGSTVDVAPPREGEQAEIEPEEDLKPEACFTEGCIKKFPFCQVSTEEGKGKIWWNLRKTCYSIVEHNWFETFIVFMILLSSGALAFEDIYIEQRKTIKTMLEYADKVFTYIFILEMLLKWVAYGFQTYFTNAWCWLDFLIVDVSLVSLVANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYHCVNTTTGNMFEIKEVNNFSDCQALGKQARWKNVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRDVKLQPIYEENLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPANKFQGMVFDFVTRQVFDISIMILICLNMVTMMVETDDQSKYMTLVLSRINLVFIVLFTGEFLLKLISLRYYYFTIGWNIFDFVVVILSIVGMFLAELIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKKEAGIDDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSAPPDCDPDAIHPGSSVKGDCGNPSVGIFFFVSYIIISFLVVVNMYIAVILENFSVATEESAEPLSEDDFEMFYEVWEKFDPDATQFIEFCKLSDFAAALDPPLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDALRIQMEDRFMASNPSKVSYEPITTTLKRKQEEVSAAIIQRNYRCYLLKQRLKNISSKYDKETIKGRIDLPIKGDMVIDKLNGNSTPEKTDGSSSTTSPPSYDSVTKPDKEKFEKDKPEKEIKGKEVRENQK | ||||||
Glycosylation | 211 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 290 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 296 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 302 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 307 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 339 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 484 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 485 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 486 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 862 | Interchain; with SCN2B or SCN4B | ||||
Sequence: C | ||||||
Disulfide bond | 862 | 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 | 864↔870 | |||||
Sequence: CKINVDC | ||||||
Disulfide bond | 902↔911 | |||||
Sequence: CMEVAGQTMC | ||||||
Disulfide bond | 1315↔1335 | |||||
Sequence: CVNTTTGNMFEIKEVNNFSDC | ||||||
Glycosylation | 1317 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1331 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 1452 | Phosphoserine; by PKC | ||||
Sequence: S |
Post-translational modification
May be ubiquitinated by NEDD4L; which would promote its endocytosis.
Phosphorylation at Ser-1452 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
Interaction
Subunit
Heterooligomer of an alpha subunit, SCN3A, and 1 to 3 regulatory beta subunits including SCN1B and SCN2B; disulfide-linked with some beta subunits like SCN2B. Interacts with NEDD4L; could regulate expression of SCN3A at the plasma membrane through ubiquitination-regulated endocytosis (By similarity).
Interacts with the conotoxin GVIIJ (PubMed:24497506).
Interacts with the spider beta/delta-theraphotoxin-Pre1a (PubMed:25784299, PubMed:28428547).
Interacts with the spider RTX-VII toxin (AC P0DL75) (PubMed:25784299).
Interacts with the conotoxin GVIIJ (PubMed:24497506).
Interacts with the spider beta/delta-theraphotoxin-Pre1a (PubMed:25784299, PubMed:28428547).
Interacts with the spider RTX-VII toxin (AC P0DL75) (PubMed:25784299).
Protein-protein interaction databases
Chemistry
Structure
Family & Domains
Features
Showing features for compositional bias, region, repeat, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 28-53 | Basic and acidic residues | ||||
Sequence: RAAEEKAKKPKKEQDIDDENKPKPNS | ||||||
Region | 28-60 | Disordered | ||||
Sequence: RAAEEKAKKPKKEQDIDDENKPKPNSDLEAGKN | ||||||
Repeat | 110-455 | I | ||||
Sequence: ILTPLNPVRKIAIKILVHSLFSMLIMCTILTNCVFMTLSNPPDWTKNVEYTFTGIYTFESLIKILARGFCLEDFTFLRDPWNWLDFSVIVMAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCSQWPPSDSAFETNTTSYFNGTMDSNGTFVNVTMSTFNWKDYIADDSHFYVLDGQKDPLLCGNGSDAGQCPEGYICVKAGRNPNYGYTSFDTFSWAFLSLFRLMTQDYWENLYQLTLRAAGKTYMIFFVLVIFLGSFYLVNLILAVVAMAYEEQNQATLEEAEQKEAEFQQMLEQLKKQ | ||||||
Region | 493-529 | Disordered | ||||
Sequence: SKSAKEWRNRRKKRRQREHLEGNHRADGDRFPKSESE | ||||||
Compositional bias | 497-511 | Basic residues | ||||
Sequence: KEWRNRRKKRRQREH | ||||||
Compositional bias | 512-529 | Basic and acidic residues | ||||
Sequence: LEGNHRADGDRFPKSESE | ||||||
Compositional bias | 587-616 | Basic and acidic residues | ||||
Sequence: VGSENDFADDEHSTFEDSESRRDSLFVPHR | ||||||
Region | 587-633 | Disordered | ||||
Sequence: VGSENDFADDEHSTFEDSESRRDSLFVPHRPGERRNSNGTTTETEVR | ||||||
Repeat | 693-965 | II | ||||
Sequence: CCDAWLKVKHLVNLIVMDPFVDLAITICIVLNTLFMAMEHYPMTQQFSSVLTVGNLVFTGIFTAEMVLKIIAMDPYYYFQEGWNIFDGIIVSLSLMELGLANVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKINVDCKLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQTMCLIVFMLVMVIGNLVVLNLFLALLLSSFSSDNLAATDDDNEMNNLQIAVGRMQKG | ||||||
Region | 1068-1112 | Disordered | ||||
Sequence: TEEFSSESELEESKEKLNATSSSEGSTVDVAPPREGEQAEIEPEE | ||||||
Repeat | 1139-1450 | III | ||||
Sequence: KGKIWWNLRKTCYSIVEHNWFETFIVFMILLSSGALAFEDIYIEQRKTIKTMLEYADKVFTYIFILEMLLKWVAYGFQTYFTNAWCWLDFLIVDVSLVSLVANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYHCVNTTTGNMFEIKEVNNFSDCQALGKQARWKNVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRDVKLQPIYEENLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKL | ||||||
Repeat | 1459-1757 | IV | ||||
Sequence: IPRPANKFQGMVFDFVTRQVFDISIMILICLNMVTMMVETDDQSKYMTLVLSRINLVFIVLFTGEFLLKLISLRYYYFTIGWNIFDFVVVILSIVGMFLAELIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKKEAGIDDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSAPPDCDPDAIHPGSSVKGDCGNPSVGIFFFVSYIIISFLVVVNMYIAVILENFSVATEESAEPLSEDDFEMFYEVWEKFDPDATQ | ||||||
Domain | 1851-1880 | IQ | ||||
Sequence: EEVSAAIIQRNYRCYLLKQRLKNISSKYDK | ||||||
Region | 1898-1951 | Disordered | ||||
Sequence: DKLNGNSTPEKTDGSSSTTSPPSYDSVTKPDKEKFEKDKPEKEIKGKEVRENQK | ||||||
Compositional bias | 1902-1923 | Polar residues | ||||
Sequence: GNSTPEKTDGSSSTTSPPSYDS | ||||||
Compositional bias | 1924-1951 | Basic and acidic residues | ||||
Sequence: VTKPDKEKFEKDKPEKEIKGKEVRENQK |
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. Nav1.3/SCN3A subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,951
- Mass (Da)221,387
- Last updated1988-08-01 v1
- Checksum74E5E851524BD10E
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6AHR7 | A0A8I6AHR7_RAT | Scn3a | 1921 | ||
A0A0G2K237 | A0A0G2K237_RAT | Scn3a | 1983 | ||
A0A8I5ZKG7 | A0A8I5ZKG7_RAT | Scn3a | 1871 | ||
F1LX08 | F1LX08_RAT | Scn3a | 2016 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 28-53 | Basic and acidic residues | ||||
Sequence: RAAEEKAKKPKKEQDIDDENKPKPNS | ||||||
Compositional bias | 497-511 | Basic residues | ||||
Sequence: KEWRNRRKKRRQREH | ||||||
Compositional bias | 512-529 | Basic and acidic residues | ||||
Sequence: LEGNHRADGDRFPKSESE | ||||||
Compositional bias | 587-616 | Basic and acidic residues | ||||
Sequence: VGSENDFADDEHSTFEDSESRRDSLFVPHR | ||||||
Compositional bias | 1902-1923 | Polar residues | ||||
Sequence: GNSTPEKTDGSSSTTSPPSYDS | ||||||
Compositional bias | 1924-1951 | Basic and acidic residues | ||||
Sequence: VTKPDKEKFEKDKPEKEIKGKEVRENQK |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y00766 EMBL· GenBank· DDBJ | CAA68735.1 EMBL· GenBank· DDBJ | mRNA |