Q9NY46 · SCN3A_HUMAN
- ProteinSodium channel protein type 3 subunit alpha
- GeneSCN3A
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2000 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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)
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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Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Cellular Component | sarcoplasm | |
Cellular Component | voltage-gated sodium channel complex | |
Molecular Function | voltage-gated sodium channel activity | |
Biological Process | behavioral response to pain | |
Biological Process | cardiac muscle cell action potential involved in contraction | |
Biological Process | membrane depolarization during action potential | |
Biological Process | sodium ion transmembrane transport | |
Biological Process | sodium ion transport |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
SCN3A is present in dividing cells and newbowrn neurons in the fetal human cerebral cortex. Gain-of-function mutations generate cortical malformations in individuals, leading to an overfolded cerebral cortex.
Names & Taxonomy
Protein names
- Recommended nameSodium channel protein type 3 subunit alpha
- Alternative names
Gene names
- Community suggested namesNaV1.3; SCN3A.
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9NY46
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane, intramembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-128 | Cytoplasmic | ||||
Sequence: MAQALLVPPGPESFRLFTRESLAAIEKRAAEEKAKKPKKEQDNDDENKPKPNSDLEAGKNLPFIYGDIPPEMVSEPLEDLDPYYINKKTFIVMNKGKAIFRFSATSALYILTPLNPVRKIAIKILVHS | ||||||
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: VSLGNVS | ||||||
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: MGNLRNKCLQWPPSDSAFETNTTSYFNGTMDSNGTFVNVTMSTFNWKDYIGDDSHFYVLDGQKDPLLCGNGSDAGQCPEGYICVKAGRNPNYGYTSFDTF | ||||||
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 | 425-761 | Cytoplasmic | ||||
Sequence: MAYEEQNQATLEEAEQKEAEFQQMLEQLKKQQEEAQAVAAASAASRDFSGIGGLGELLESSSEASKLSSKSAKEWRNRRKKRRQREHLEGNNKGERDSFPKSESEDSVKRSSFLFSMDGNRLTSDKKFCSPHQSLLSIRGSLFSPRRNSKTSIFSFRGRAKDVGSENDFADDEHSTFEDSESRRDSLFVPHRHGERRNSNVSQASMSSRMVPGLPANGKMHSTVDCNGVVSLVGGPSALTSPTGQLPPEGTTTETEVRKRRLSSYQISMEMLEDSSGRQRAVSIASILTNTMEELEESRQKCPPCWYRFANVFLIWDCCDAWLKVKHLVNLIVMDPF | ||||||
Transmembrane | 762-779 | Helical; Name=S1 of repeat II | ||||
Sequence: VDLAITICIVLNTLFMAM | ||||||
Topological domain | 780-787 | Extracellular | ||||
Sequence: EHYPMTEQ | ||||||
Transmembrane | 788-812 | Helical; Name=S2 of repeat II | ||||
Sequence: FSSVLTVGNLVFTGIFTAEMVLKII | ||||||
Topological domain | 813-822 | Cytoplasmic | ||||
Sequence: AMDPYYYFQE | ||||||
Transmembrane | 823-842 | Helical; Name=S3 of repeat II | ||||
Sequence: GWNIFDGIIVSLSLMELGLS | ||||||
Topological domain | 843-846 | Extracellular | ||||
Sequence: NVEG | ||||||
Transmembrane | 847-865 | Helical; Name=S4 of repeat II | ||||
Sequence: LSVLRSFRLLRVFKLAKSW | ||||||
Topological domain | 866-883 | Cytoplasmic | ||||
Sequence: PTLNMLIKIIGNSVGALG | ||||||
Transmembrane | 884-904 | Helical; Name=S5 of repeat II | ||||
Sequence: NLTLVLAIIVFIFAVVGMQLF | ||||||
Topological domain | 905-929 | Extracellular | ||||
Sequence: GKSYKECVCKINDDCTLPRWHMNDF | ||||||
Intramembrane | 930-945 | Pore-forming | ||||
Sequence: FHSFLIVFRVLCGEWI | ||||||
Topological domain | 946-956 | Extracellular | ||||
Sequence: ETMWDCMEVAG | ||||||
Transmembrane | 957-983 | Helical; Name=S6 of repeat II | ||||
Sequence: QTMCLIVFMLVMVIGNLVVLNLFLALL | ||||||
Topological domain | 984-1205 | Cytoplasmic | ||||
Sequence: LSSFSSDNLAATDDDNEMNNLQIAVGRMQKGIDYVKNKMRECFQKAFFRKPKVIEIHEGNKIDSCMSNNTGIEISKELNYLRDGNGTTSGVGTGSSVEKYVIDENDYMSFINNPSLTVTVPIAVGESDFENLNTEEFSSESELEESKEKLNATSSSEGSTVDVVLPREGEQAETEPEEDLKPEACFTEGCIKKFPFCQVSTEEGKGKIWWNLRKTCYSIVEH | ||||||
Transmembrane | 1206-1226 | Helical; Name=S1 of repeat III | ||||
Sequence: NWFETFIVFMILLSSGALAFE | ||||||
Topological domain | 1227-1238 | Extracellular | ||||
Sequence: DIYIEQRKTIKT | ||||||
Transmembrane | 1239-1260 | Helical; Name=S2 of repeat III | ||||
Sequence: MLEYADKVFTYIFILEMLLKWV | ||||||
Topological domain | 1261-1266 | Cytoplasmic | ||||
Sequence: AYGFQT | ||||||
Transmembrane | 1267-1292 | Helical; Name=S3 of repeat III | ||||
Sequence: YFTNAWCWLDFLIVDVSLVSLVANAL | ||||||
Topological domain | 1293-1301 | Extracellular | ||||
Sequence: GYSELGAIK | ||||||
Transmembrane | 1302-1320 | Helical; Name=S4 of repeat III | ||||
Sequence: SLRTLRALRPLRALSRFEG | ||||||
Topological domain | 1321-1333 | Cytoplasmic | ||||
Sequence: MRVVVNALVGAIP | ||||||
Transmembrane | 1334-1356 | Helical; Name=S5 of repeat III | ||||
Sequence: SIMNVLLVCLIFWLIFSIMGVNL | ||||||
Topological domain | 1357-1402 | Extracellular | ||||
Sequence: FAGKFYHCVNMTTGNMFDISDVNNLSDCQALGKQARWKNVKVNFDN | ||||||
Intramembrane | 1403-1419 | Pore-forming | ||||
Sequence: VGAGYLALLQVATFKGW | ||||||
Topological domain | 1420-1442 | Extracellular | ||||
Sequence: MDIMYAAVDSRDVKLQPVYEENL | ||||||
Transmembrane | 1443-1468 | Helical; Name=S6 of repeat III | ||||
Sequence: YMYLYFVIFIIFGSFFTLNLFIGVII | ||||||
Topological domain | 1469-1526 | Cytoplasmic | ||||
Sequence: DNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPANKFQGMVFDFVTRQ | ||||||
Transmembrane | 1527-1545 | Helical; Name=S1 of repeat IV | ||||
Sequence: VFDISIMILICLNMVTMMV | ||||||
Topological domain | 1546-1553 | Extracellular | ||||
Sequence: ETDDQGKY | ||||||
Transmembrane | 1554-1577 | Helical; Name=S2 of repeat IV | ||||
Sequence: MTLVLSRINLVFIVLFTGEFVLKL | ||||||
Topological domain | 1578-1587 | Cytoplasmic | ||||
Sequence: VSLRHYYFTI | ||||||
Transmembrane | 1588-1605 | Helical; Name=S3 of repeat IV | ||||
Sequence: GWNIFDFVVVILSIVGMF | ||||||
Topological domain | 1606-1617 | Extracellular | ||||
Sequence: LAEMIEKYFVSP | ||||||
Transmembrane | 1618-1640 | Helical; Name=S4 of repeat IV | ||||
Sequence: TLFRVIRLARIGRILRLIKGAKG | ||||||
Topological domain | 1641-1653 | Cytoplasmic | ||||
Sequence: IRTLLFALMMSLP | ||||||
Transmembrane | 1654-1677 | Helical; Name=S5 of repeat IV | ||||
Sequence: ALFNIGLLLFLVMFIYAIFGMSNF | ||||||
Topological domain | 1678-1699 | Extracellular | ||||
Sequence: AYVKKEAGIDDMFNFETFGNSM | ||||||
Intramembrane | 1700-1712 | Pore-forming | ||||
Sequence: ICLFQITTSAGWD | ||||||
Topological domain | 1713-1744 | Extracellular | ||||
Sequence: GLLAPILNSAPPDCDPDTIHPGSSVKGDCGNP | ||||||
Transmembrane | 1745-1770 | Helical; Name=S6 of repeat IV | ||||
Sequence: SVGIFFFVSYIIISFLVVVNMYIAVI | ||||||
Topological domain | 1771-2000 | Cytoplasmic | ||||
Sequence: LENFSVATEESAEPLSEDDFEMFYEVWEKFDPDATQFIEFSKLSDFAAALDPPLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDALRIQMEDRFMASNPSKVSYEPITTTLKRKQEEVSAAIIQRNFRCYLLKQRLKNISSNYNKEAIKGRIDLPIKQDMIIDKLNGNSTPEKTDGSSSTTSPPSYDSVTKPDKEKFEKDKPEKESKGKEVRENQK |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Epilepsy, familial focal, with variable foci 4 (FFEVF4)
- Note
- DescriptionAn autosomal dominant form of epilepsy characterized by focal seizures arising from different cortical regions, including the temporal, frontal, parietal, and occipital lobes. Seizure types commonly include temporal lobe epilepsy, frontal lobe epilepsy, and nocturnal frontal lobe epilepsy. Some patients may have intellectual disability or autism spectrum disorders. Seizure onset usually occurs in the first or second decades, although later onset has been reported, and there is phenotypic variability within families. A subset of patients have structural brain abnormalities. Penetrance of the disorder is incomplete. FFEVF4 is characterized by onset of focal seizures in the first years of life.
- See alsoMIM:617935
Natural variants in FFEVF4
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_080503 | 247 | L>P | in FFEVF4; loss of localization at the cell surface | |
VAR_080504 | 357 | R>Q | in FFEVF4; affects voltage-dependent sodium channel activity; smaller current density and slower activation compared to wild-type channels and increased current activation in response to depolarizing voltage ramps; dbSNP:rs774195502 | |
VAR_080505 | 815 | D>N | in FFEVF4; uncertain significance; increased current activation in response to depolarizing voltage ramps; dbSNP:rs755440336 | |
VAR_080507 | 1160 | E>K | in FFEVF4; affects voltage-dependent sodium channel activity; increased level of persistent sodium current compared to wild-type channels and increased current activation in response to depolarizing voltage ramps; dbSNP:rs377632429 | |
VAR_080509 | 1372 | M>V | in FFEVF4; uncertain significance; increased current activation in response to depolarizing voltage ramps; dbSNP:rs758906955 |
Developmental and epileptic encephalopathy 62 (DEE62)
- Note
- DescriptionA form of epileptic encephalopathy, a heterogeneous group of severe early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. DEE62 is characterized by onset of seizures in the first year of life.
- See alsoMIM:617938
Natural variants in DEE62
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_080506 | 875 | I>T | in DEE62; prominent gain of channel function, with markedly increased amplitude of the slowly inactivating current component and a leftward shift in the voltage dependence of activation to more hyperpolarized potentials; dbSNP:rs1057518801 | |
VAR_080508 | 1333 | P>L | in DEE62; prominent gain of channel function, with markedly increased amplitude of the slowly inactivating current component and a leftward shift in the voltage dependence of activation to more hyperpolarized potentials; dbSNP:rs1057520753 | |
VAR_080510 | 1642 | R>C | in DEE62; uncertain significance; no gain of function in channel activity; channel recovery from inactivation is more rapid than that of wild-type channel; dbSNP:rs1312429782 | |
VAR_080511 | 1769 | V>A | in DEE62; prominent gain of channel function, with markedly increased amplitude of the slowly inactivating current component; dbSNP:rs1553517274 | |
VAR_080512 | 1799 | K>Q | in DEE62; uncertain significance; no gain of function in channel activity; dbSNP:rs1170839078 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_029743 | 43 | ||||
Sequence: Missing | ||||||
Natural variant | VAR_080503 | 247 | in FFEVF4; loss of localization at the cell surface | |||
Sequence: L → P | ||||||
Natural variant | VAR_080504 | 357 | in FFEVF4; affects voltage-dependent sodium channel activity; smaller current density and slower activation compared to wild-type channels and increased current activation in response to depolarizing voltage ramps; dbSNP:rs774195502 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_014275 | 606 | ||||
Sequence: S → T | ||||||
Natural variant | VAR_080505 | 815 | in FFEVF4; uncertain significance; increased current activation in response to depolarizing voltage ramps; dbSNP:rs755440336 | |||
Sequence: D → N | ||||||
Natural variant | VAR_080506 | 875 | in DEE62; prominent gain of channel function, with markedly increased amplitude of the slowly inactivating current component and a leftward shift in the voltage dependence of activation to more hyperpolarized potentials; dbSNP:rs1057518801 | |||
Sequence: I → T | ||||||
Natural variant | VAR_076435 | 1084 | in dbSNP:rs140990288 | |||
Sequence: V → I | ||||||
Natural variant | VAR_029744 | 1107 | in dbSNP:rs12474273 | |||
Sequence: V → A | ||||||
Natural variant | VAR_080507 | 1160 | in FFEVF4; affects voltage-dependent sodium channel activity; increased level of persistent sodium current compared to wild-type channels and increased current activation in response to depolarizing voltage ramps; dbSNP:rs377632429 | |||
Sequence: E → K | ||||||
Natural variant | VAR_080508 | 1333 | in DEE62; prominent gain of channel function, with markedly increased amplitude of the slowly inactivating current component and a leftward shift in the voltage dependence of activation to more hyperpolarized potentials; dbSNP:rs1057520753 | |||
Sequence: P → L | ||||||
Natural variant | VAR_080509 | 1372 | in FFEVF4; uncertain significance; increased current activation in response to depolarizing voltage ramps; dbSNP:rs758906955 | |||
Sequence: M → V | ||||||
Natural variant | VAR_080510 | 1642 | in DEE62; uncertain significance; no gain of function in channel activity; channel recovery from inactivation is more rapid than that of wild-type channel; dbSNP:rs1312429782 | |||
Sequence: R → C | ||||||
Natural variant | VAR_080511 | 1769 | in DEE62; prominent gain of channel function, with markedly increased amplitude of the slowly inactivating current component; dbSNP:rs1553517274 | |||
Sequence: V → A | ||||||
Natural variant | VAR_080512 | 1799 | in DEE62; uncertain significance; no gain of function in channel activity; dbSNP:rs1170839078 | |||
Sequence: K → Q | ||||||
Natural variant | VAR_055640 | 1803 | in dbSNP:rs3731762 | |||
Sequence: D → N | ||||||
Natural variant | VAR_029745 | 1813 | ||||
Sequence: L → S | ||||||
Mutagenesis | 1970 | Abolishes interaction with NEDD4L. | ||||
Sequence: Y → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 16 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, glycosylation, modified residue, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000048493 | 1-2000 | Sodium channel protein type 3 subunit alpha | |||
Sequence: MAQALLVPPGPESFRLFTRESLAAIEKRAAEEKAKKPKKEQDNDDENKPKPNSDLEAGKNLPFIYGDIPPEMVSEPLEDLDPYYINKKTFIVMNKGKAIFRFSATSALYILTPLNPVRKIAIKILVHSLFSMLIMCTILTNCVFMTLSNPPDWTKNVEYTFTGIYTFESLIKILARGFCLEDFTFLRDPWNWLDFSVIVMAYVTEFVSLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCLQWPPSDSAFETNTTSYFNGTMDSNGTFVNVTMSTFNWKDYIGDDSHFYVLDGQKDPLLCGNGSDAGQCPEGYICVKAGRNPNYGYTSFDTFSWAFLSLFRLMTQDYWENLYQLTLRAAGKTYMIFFVLVIFLGSFYLVNLILAVVAMAYEEQNQATLEEAEQKEAEFQQMLEQLKKQQEEAQAVAAASAASRDFSGIGGLGELLESSSEASKLSSKSAKEWRNRRKKRRQREHLEGNNKGERDSFPKSESEDSVKRSSFLFSMDGNRLTSDKKFCSPHQSLLSIRGSLFSPRRNSKTSIFSFRGRAKDVGSENDFADDEHSTFEDSESRRDSLFVPHRHGERRNSNVSQASMSSRMVPGLPANGKMHSTVDCNGVVSLVGGPSALTSPTGQLPPEGTTTETEVRKRRLSSYQISMEMLEDSSGRQRAVSIASILTNTMEELEESRQKCPPCWYRFANVFLIWDCCDAWLKVKHLVNLIVMDPFVDLAITICIVLNTLFMAMEHYPMTEQFSSVLTVGNLVFTGIFTAEMVLKIIAMDPYYYFQEGWNIFDGIIVSLSLMELGLSNVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKINDDCTLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQTMCLIVFMLVMVIGNLVVLNLFLALLLSSFSSDNLAATDDDNEMNNLQIAVGRMQKGIDYVKNKMRECFQKAFFRKPKVIEIHEGNKIDSCMSNNTGIEISKELNYLRDGNGTTSGVGTGSSVEKYVIDENDYMSFINNPSLTVTVPIAVGESDFENLNTEEFSSESELEESKEKLNATSSSEGSTVDVVLPREGEQAETEPEEDLKPEACFTEGCIKKFPFCQVSTEEGKGKIWWNLRKTCYSIVEHNWFETFIVFMILLSSGALAFEDIYIEQRKTIKTMLEYADKVFTYIFILEMLLKWVAYGFQTYFTNAWCWLDFLIVDVSLVSLVANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYHCVNMTTGNMFDISDVNNLSDCQALGKQARWKNVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRDVKLQPVYEENLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPANKFQGMVFDFVTRQVFDISIMILICLNMVTMMVETDDQGKYMTLVLSRINLVFIVLFTGEFVLKLVSLRHYYFTIGWNIFDFVVVILSIVGMFLAEMIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKKEAGIDDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSAPPDCDPDTIHPGSSVKGDCGNPSVGIFFFVSYIIISFLVVVNMYIAVILENFSVATEESAEPLSEDDFEMFYEVWEKFDPDATQFIEFSKLSDFAAALDPPLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDALRIQMEDRFMASNPSKVSYEPITTTLKRKQEEVSAAIIQRNFRCYLLKQRLKNISSNYNKEAIKGRIDLPIKQDMIIDKLNGNSTPEKTDGSSSTTSPPSYDSVTKPDKEKFEKDKPEKESKGKEVRENQK | ||||||
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 | 911 | Interchain; with SCN2B or SCN4B | ||||
Sequence: C | ||||||
Disulfide bond | 911 | 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 | 913↔919 | |||||
Sequence: CKINDDC | ||||||
Disulfide bond | 951↔960 | |||||
Sequence: CMEVAGQTMC | ||||||
Disulfide bond | 1364↔1384 | |||||
Sequence: CVNMTTGNMFDISDVNNLSDC | ||||||
Glycosylation | 1366 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1380 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 1501 | Phosphoserine; by PKC | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with NEDD4L; could regulate expression of SCN3A at the plasma membrane through ubiquitination-regulated endocytosis (PubMed:15548568).
Interacts with the conotoxin GVIIJ (PubMed:15548568, PubMed:24497506).
Protein-protein interaction databases
Chemistry
Miscellaneous
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: RAAEEKAKKPKKEQDNDDENKPKPNS | ||||||
Region | 28-60 | Disordered | ||||
Sequence: RAAEEKAKKPKKEQDNDDENKPKPNSDLEAGKN | ||||||
Repeat | 110-455 | I | ||||
Sequence: ILTPLNPVRKIAIKILVHSLFSMLIMCTILTNCVFMTLSNPPDWTKNVEYTFTGIYTFESLIKILARGFCLEDFTFLRDPWNWLDFSVIVMAYVTEFVSLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCLQWPPSDSAFETNTTSYFNGTMDSNGTFVNVTMSTFNWKDYIGDDSHFYVLDGQKDPLLCGNGSDAGQCPEGYICVKAGRNPNYGYTSFDTFSWAFLSLFRLMTQDYWENLYQLTLRAAGKTYMIFFVLVIFLGSFYLVNLILAVVAMAYEEQNQATLEEAEQKEAEFQQMLEQLKKQ | ||||||
Region | 493-528 | Disordered | ||||
Sequence: SKSAKEWRNRRKKRRQREHLEGNNKGERDSFPKSES | ||||||
Compositional bias | 511-528 | Basic and acidic residues | ||||
Sequence: HLEGNNKGERDSFPKSES | ||||||
Compositional bias | 587-622 | Basic and acidic residues | ||||
Sequence: VGSENDFADDEHSTFEDSESRRDSLFVPHRHGERRN | ||||||
Region | 587-631 | Disordered | ||||
Sequence: VGSENDFADDEHSTFEDSESRRDSLFVPHRHGERRNSNVSQASMS | ||||||
Compositional bias | 662-676 | Polar residues | ||||
Sequence: ALTSPTGQLPPEGTT | ||||||
Region | 662-681 | Disordered | ||||
Sequence: ALTSPTGQLPPEGTTTETEV | ||||||
Repeat | 742-1014 | II | ||||
Sequence: CCDAWLKVKHLVNLIVMDPFVDLAITICIVLNTLFMAMEHYPMTEQFSSVLTVGNLVFTGIFTAEMVLKIIAMDPYYYFQEGWNIFDGIIVSLSLMELGLSNVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKINDDCTLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQTMCLIVFMLVMVIGNLVVLNLFLALLLSSFSSDNLAATDDDNEMNNLQIAVGRMQKG | ||||||
Region | 1118-1162 | Disordered | ||||
Sequence: EEFSSESELEESKEKLNATSSSEGSTVDVVLPREGEQAETEPEED | ||||||
Repeat | 1188-1499 | III | ||||
Sequence: KGKIWWNLRKTCYSIVEHNWFETFIVFMILLSSGALAFEDIYIEQRKTIKTMLEYADKVFTYIFILEMLLKWVAYGFQTYFTNAWCWLDFLIVDVSLVSLVANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYHCVNMTTGNMFDISDVNNLSDCQALGKQARWKNVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRDVKLQPVYEENLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKL | ||||||
Repeat | 1508-1806 | IV | ||||
Sequence: IPRPANKFQGMVFDFVTRQVFDISIMILICLNMVTMMVETDDQGKYMTLVLSRINLVFIVLFTGEFVLKLVSLRHYYFTIGWNIFDFVVVILSIVGMFLAEMIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKKEAGIDDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSAPPDCDPDTIHPGSSVKGDCGNPSVGIFFFVSYIIISFLVVVNMYIAVILENFSVATEESAEPLSEDDFEMFYEVWEKFDPDATQ | ||||||
Domain | 1900-1929 | IQ | ||||
Sequence: EEVSAAIIQRNFRCYLLKQRLKNISSNYNK | ||||||
Compositional bias | 1949-1972 | Polar residues | ||||
Sequence: LNGNSTPEKTDGSSSTTSPPSYDS | ||||||
Region | 1949-2000 | Disordered | ||||
Sequence: LNGNSTPEKTDGSSSTTSPPSYDSVTKPDKEKFEKDKPEKESKGKEVRENQK | ||||||
Compositional bias | 1973-2000 | Basic and acidic residues | ||||
Sequence: VTKPDKEKFEKDKPEKESKGKEVRENQK |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing. Exons 6A and 6N only differ by a single residue.
Q9NY46-1
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
- Synonyms6A-12+12b
- Length2,000
- Mass (Da)226,294
- Last updated2002-11-08 v2
- ChecksumF754A1C7D49ECB58
Q9NY46-2
- Name2
- Synonyms6A-12
- Differences from canonical
- 625-673: Missing
Q9NY46-3
- Name3
- Synonyms6N-12+12b
- Differences from canonical
- 208-208: S → D
Q9NY46-4
- Name4
- Synonyms6N-12
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E7EUE6 | E7EUE6_HUMAN | SCN3A | 1364 | ||
A0A1W2PQ58 | A0A1W2PQ58_HUMAN | SCN3A | 674 | ||
C9JBM7 | C9JBM7_HUMAN | SCN3A | 200 | ||
A0A1W2PSB2 | A0A1W2PSB2_HUMAN | SCN3A | 1115 | ||
A0A1W2PRD1 | A0A1W2PRD1_HUMAN | SCN3A | 1979 | ||
A0A590UJW3 | A0A590UJW3_HUMAN | SCN3A | 498 | ||
A0A590UJH3 | A0A590UJH3_HUMAN | SCN3A | 1086 | ||
A0A994J5P2 | A0A994J5P2_HUMAN | SCN3A | 1983 |
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 28-53 | Basic and acidic residues | ||||
Sequence: RAAEEKAKKPKKEQDNDDENKPKPNS | ||||||
Sequence conflict | 175 | in Ref. 4; AAC29514/AAC29515 | ||||
Sequence: A → V | ||||||
Alternative sequence | VSP_001033 | 208 | in isoform 3 and isoform 4 | |||
Sequence: S → D | ||||||
Sequence conflict | 318 | in Ref. 4; AAC29514/AAC29515 | ||||
Sequence: Y → N | ||||||
Sequence conflict | 401 | in Ref. 4; AAC29514/AAC29515 | ||||
Sequence: M → T | ||||||
Sequence conflict | 475 | in Ref. 2; AAK00219 | ||||
Sequence: I → V | ||||||
Sequence conflict | 495 | in Ref. 2; AAK00219 | ||||
Sequence: S → G | ||||||
Compositional bias | 511-528 | Basic and acidic residues | ||||
Sequence: HLEGNNKGERDSFPKSES | ||||||
Compositional bias | 587-622 | Basic and acidic residues | ||||
Sequence: VGSENDFADDEHSTFEDSESRRDSLFVPHRHGERRN | ||||||
Sequence conflict | 604 | in Ref. 2; AAK00219 | ||||
Sequence: S → G | ||||||
Sequence conflict | 613 | in Ref. 4; AAC29514/AAC29515 | ||||
Sequence: V → E | ||||||
Alternative sequence | VSP_001034 | 625-673 | in isoform 2 and isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 662-676 | Polar residues | ||||
Sequence: ALTSPTGQLPPEGTT | ||||||
Sequence conflict | 1060 | in Ref. 4; AAC29514/AAC29515 | ||||
Sequence: E → A | ||||||
Sequence conflict | 1163 | in Ref. 2; AAK00219 | ||||
Sequence: L → F | ||||||
Sequence conflict | 1274 | in Ref. 4; AAC29514/AAC29515 | ||||
Sequence: W → R | ||||||
Sequence conflict | 1329 | in Ref. 6; AAB30530 | ||||
Sequence: V → L | ||||||
Sequence conflict | 1414-1415 | in Ref. 4; AAC29514/AAC29515 | ||||
Sequence: AT → VS | ||||||
Sequence conflict | 1614 | in Ref. 2; AAK00219 | ||||
Sequence: F → S | ||||||
Sequence conflict | 1741-1743 | in Ref. 2; AAK00219 | ||||
Sequence: CGN → RGD | ||||||
Sequence conflict | 1862 | in Ref. 2; AAK00219 | ||||
Sequence: G → C | ||||||
Compositional bias | 1949-1972 | Polar residues | ||||
Sequence: LNGNSTPEKTDGSSSTTSPPSYDS | ||||||
Sequence conflict | 1966 | in Ref. 2; AAK00219 | ||||
Sequence: S → P | ||||||
Compositional bias | 1973-2000 | Basic and acidic residues | ||||
Sequence: VTKPDKEKFEKDKPEKESKGKEVRENQK |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ251507 EMBL· GenBank· DDBJ | CAB85895.1 EMBL· GenBank· DDBJ | mRNA | ||
AF225987 EMBL· GenBank· DDBJ | AAK00219.1 EMBL· GenBank· DDBJ | mRNA | ||
AF330135 EMBL· GenBank· DDBJ | AAG53414.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330118 EMBL· GenBank· DDBJ | AAG53414.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330119 EMBL· GenBank· DDBJ | AAG53414.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330120 EMBL· GenBank· DDBJ | AAG53414.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330121 EMBL· GenBank· DDBJ | AAG53414.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330122 EMBL· GenBank· DDBJ | AAG53414.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330123 EMBL· GenBank· DDBJ | AAG53414.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330124 EMBL· GenBank· DDBJ | AAG53414.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330125 EMBL· GenBank· DDBJ | AAG53414.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330126 EMBL· GenBank· DDBJ | AAG53414.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330127 EMBL· GenBank· DDBJ | AAG53414.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330128 EMBL· GenBank· DDBJ | AAG53414.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330129 EMBL· GenBank· DDBJ | AAG53414.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330130 EMBL· GenBank· DDBJ | AAG53414.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330131 EMBL· GenBank· DDBJ | AAG53414.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330132 EMBL· GenBank· DDBJ | AAG53414.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330133 EMBL· GenBank· DDBJ | AAG53414.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330134 EMBL· GenBank· DDBJ | AAG53414.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330135 EMBL· GenBank· DDBJ | AAG53415.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330118 EMBL· GenBank· DDBJ | AAG53415.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330119 EMBL· GenBank· DDBJ | AAG53415.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330120 EMBL· GenBank· DDBJ | AAG53415.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330121 EMBL· GenBank· DDBJ | AAG53415.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330122 EMBL· GenBank· DDBJ | AAG53415.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330123 EMBL· GenBank· DDBJ | AAG53415.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330124 EMBL· GenBank· DDBJ | AAG53415.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330125 EMBL· GenBank· DDBJ | AAG53415.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330126 EMBL· GenBank· DDBJ | AAG53415.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330127 EMBL· GenBank· DDBJ | AAG53415.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330128 EMBL· GenBank· DDBJ | AAG53415.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330129 EMBL· GenBank· DDBJ | AAG53415.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330130 EMBL· GenBank· DDBJ | AAG53415.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330131 EMBL· GenBank· DDBJ | AAG53415.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330132 EMBL· GenBank· DDBJ | AAG53415.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330133 EMBL· GenBank· DDBJ | AAG53415.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330134 EMBL· GenBank· DDBJ | AAG53415.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC013463 EMBL· GenBank· DDBJ | AAY15072.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF035685 EMBL· GenBank· DDBJ | AAC29514.1 EMBL· GenBank· DDBJ | mRNA | ||
AF035686 EMBL· GenBank· DDBJ | AAC29515.1 EMBL· GenBank· DDBJ | mRNA | ||
S69887 EMBL· GenBank· DDBJ | AAB30530.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB037777 EMBL· GenBank· DDBJ | BAA92594.1 EMBL· GenBank· DDBJ | mRNA | ||
AF239921 EMBL· GenBank· DDBJ | AAF44690.1 EMBL· GenBank· DDBJ | mRNA |