Scn3a
entrez
497770
canonical
uniprot
P08104
canonical
ensembl
ENSRNOG00000005007
resolver
ensp
ENSRNOP00000006646
resolver
ensp
ENSRNOP00000072091
resolver
enst
ENSRNOT00000081401
resolver
genesymbol
Scn3a
resolver
uniprot
A0A0G2K237
resolver
uniprot_entry
A0A0G2K237_RAT
resolver
uniprot_entry
SCN3A_RAT
resolver
amino_acid_sequence
MAQALLVPPGPESFRLFTRESLAAIEKRAAEEKAKKPKKEQDIDDENKPKPNSDLEAGKNLPFIYGDIPPEMVSEPLEDLDPYYVSKKTFVVLNKGKAIFRFSATSALYILTPLNPVRKIAIKILVHSLFSMLIMCTILTNCVFMTLSNPPDWTKNVEYTFTGIYTFESLIKILARGFCLEDFTFLRDPWNWLDFSVIVMAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCSQWPPSDSAFETNTTSYFNGTMDSNGTFVNVTMSTFNWKDYIADDSHFYVLDGQKDPLLCGNGSDAGQCPEGYICVKAGRNPNYGYTSFDTFSWAFLSLFRLMTQDYWENLYQLTLRAAGKTYMIFFVLVIFLGSFYLVNLILAVVAMAYEEQNQATLEEAEQKEAEFQQMLEQLKKQQEEAQAVAAASAASRDFSGIGGLGELLESSSEASKLSSKSAKEWRNRRKKRRQREHLEGNHRADGDRFPKSESEDSVKRRSFLLSLDGNPLTGDKKLCSPHQSLLSIRGSLFSPRRNSKTSIFSFRGRAKDVGSENDFADDEHSTFEDSESRRDSLFVPHRPGERRNSNGTTTETEVRKRRLSSYQISMEMLEDSSGRQRSMSIASILTNTMEELEESRQKCPPCWYRFANVFLIWDCCDAWLKVKHLVNLIVMDPFVDLAITICIVLNTLFMAMEHYPMTQQFSSVLTVGNLVFTGIFTAEMVLKIIAMDPYYYFQEGWNIFDGIIVSLSLMELGLANVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKINVDCKLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQTMCLIVFMLVMVIGNLVVLNLFLALLLSSFSSDNLAATDDDNEMNNLQIAVGRMQKGIDFVKNKIRECFRKAFFRKPKVIEIQEGNKIDSCMSNNTGIEISKELNYLKDGNGTTSGVGTGSSVEKYVIDENDYMSFINNPSLTVTVPIAVGESDFENLNTEEFSSESELEESKEKLNATSSSEGSTVDVAPPREGEQAEIEPEEDLKPEACFTEGCIKKFPFCQVSTEEGKGKIWWNLRKTCYSIVEHNWFETFIVFMILLSSGALAFEDIYIEQRKTIKTMLEYADKVFTYIFILEMLLKWVAYGFQTYFTNAWCWLDFLIVDVSLVSLVANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYHCVNTTTGNMFEIKEVNNFSDCQALGKQARWKNVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRDVKLQPIYEENLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPANKFQGMVFDFVTRQVFDISIMILICLNMVTMMVETDDQSKYMTLVLSRINLVFIVLFTGEFLLKLISLRYYYFTIGWNIFDFVVVILSIVGMFLAELIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKKEAGIDDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSAPPDCDPDAIHPGSSVKGDCGNPSVGIFFFVSYIIISFLVVVNMYIAVILENFSVATEESAEPLSEDDFEMFYEVWEKFDPDATQFIEFCKLSDFAAALDPPLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDALRIQMEDRFMASNPSKVSYEPITTTLKRKQEEVSAAIIQRNYRCYLLKQRLKNISSKYDKETIKGRIDLPIKGDMVIDKLNGNSTPEKTDGSSSTTSPPSYDSVTKPDKEKFEKDKPEKEIKGKEVRENQK
uniprot
proteins
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). {ECO:0000250|UniProtKB:A2ASI5, ECO:0000269|PubMed:25784299}.
uniprot
proteins
mass_dalton
221387
uniprot
proteins
mutagenesis
MUTAGEN 1503; /note="K->P: 6-fold decrease in activity of the spider RTX-VII toxin."; /evidence="ECO:0000269|PubMed:25784299"; MUTAGEN 1504; /note="Y->E: 2-fold decrease in activity of the spider RTX-VII toxin."; /evidence="ECO:0000269|PubMed:25784299"; MUTAGEN 1505; /note="M->K: 4.5-fold decrease in activity of the spider RTX-VII toxin."; /evidence="ECO:0000269|PubMed:25784299"; MUTAGEN 1506; /note="T->I: 10-fold decrease in activity of the spider RTX-VII toxin."; /evidence="ECO:0000269|PubMed:25784299"; MUTAGEN 1507; /note="L->N: 12-fold decrease in activity of the spider RTX-VII toxin."; /evidence="ECO:0000269|PubMed:25784299"; MUTAGEN 1559; /note="E->D: Increase in sensitivity to the scorpion toxin BMKM1."; /evidence="ECO:0000269|PubMed:20678086"; MUTAGEN 1562; /note="E->Q: 5.5-fold decrease in activity of the spider RTX-VII toxin."; /evidence="ECO:0000269|PubMed:25784299"; MUTAGEN 1562; /note="E->R: 20-fold decrease in activity of the spider RTX-VII toxin."; /evidence="ECO:0000269|PubMed:25784299
uniprot
proteins
post_translational_modification
PTM: May be ubiquitinated by NEDD4L; which would promote its endocytosis. {ECO:0000250|UniProtKB:Q9NY46}.; PTM: Phosphorylation at Ser-1452 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents. {ECO:0000250|UniProtKB:Q14524}.
uniprot
proteins
protein_family
Nav1.3/SCN3A subfamily
uniprot
proteins
protein_family
Sodium channel (TC 1.A.1.10) family
uniprot
proteins
pubmed
20678086
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
2449363
uniprot
proteins
pubmed
24497506
uniprot
proteins
pubmed
25784299
uniprot
proteins
pubmed
28428547
uniprot
proteins
sequence_length
1951
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NY46}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NY46}. Basal cell membrane {ECO:0000250|UniProtKB:A2ASI5}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NY46}. Note=In enterochromaffin cells, localized highly asymmetrically, almost exclusively at the basal side. {ECO:0000250|UniProtKB:A2ASI5}.
uniprot
proteins
transmembrane_region
TRANSMEM 129..146; /note="Helical; Name=S1 of repeat I"; /evidence="ECO:0000250|UniProtKB:Q9NY46"; TRANSMEM 153..174; /note="Helical; Name=S2 of repeat I"; /evidence="ECO:0000250|UniProtKB:Q9NY46"; TRANSMEM 189..206; /note="Helical; Name=S3 of repeat I"; /evidence="ECO:0000250|UniProtKB:Q9NY46"; TRANSMEM 214..235; /note="Helical; Name=S4 of repeat I"; /evidence="ECO:0000250|UniProtKB:Q9NY46"; TRANSMEM 250..269; /note="Helical; Name=S5 of repeat I"; /evidence="ECO:0000250|UniProtKB:Q9NY46"; TRANSMEM 398..424; /note="Helical; Name=S6 of repeat I"; /evidence="ECO:0000250|UniProtKB:Q9NY46"; TRANSMEM 713..730; /note="Helical; Name=S1 of repeat II"; /evidence="ECO:0000250|UniProtKB:Q9NY46"; TRANSMEM 739..763; /note="Helical; Name=S2 of repeat II"; /evidence="ECO:0000250|UniProtKB:Q9NY46"; TRANSMEM 774..793; /note="Helical; Name=S3 of repeat II"; /evidence="ECO:0000250|UniProtKB:Q9NY46"; TRANSMEM 798..816; /note="Helical; Name=S4 of repeat II"; /evidence="ECO:0000250|UniProtKB:Q9NY46"; TRANSMEM 835..855; /note="Helical; Name=S5 of repeat II"; /evidence="ECO:0000250|UniProtKB:Q9NY46"; TRANSMEM 908..934; /note="Helical; Name=S6 of repeat II"; /evidence="ECO:0000250|UniProtKB:Q9NY46"; TRANSMEM 1157..1177; /note="Helical; Name=S1 of repeat III"; /evidence="ECO:0000250|UniProtKB:Q9NY46"; TRANSMEM 1190..1211; /note="Helical; Name=S2 of repeat III"; /evidence="ECO:0000250|UniProtKB:Q9NY46"; TRANSMEM 1218..1243; /note="Helical; Name=S3 of repeat III"; /evidence="ECO:0000250|UniProtKB:Q9NY46"; TRANSMEM 1253..1271; /note="Helical; Name=S4 of repeat III"; /evidence="ECO:0000250|UniProtKB:Q9NY46"; TRANSMEM 1285..1307; /note="Helical; Name=S5 of repeat III"; /evidence="ECO:0000250|UniProtKB:Q9NY46"; TRANSMEM 1394..1419; /note="Helical; Name=S6 of repeat III"; /evidence="ECO:0000250|UniProtKB:Q9NY46"; TRANSMEM 1478..1496; /note="Helical; Name=S1 of repeat IV"; /evidence="ECO:0000250|UniProtKB:Q9NY46"; TRANSMEM 1505..1528; /note="Helical; Name=S2 of repeat IV"; /evidence="ECO:0000250|UniProtKB:Q9NY46"; TRANSMEM 1539..1556; /note="Helical; Name=S3 of repeat IV"; /evidence="ECO:0000250|UniProtKB:Q9NY46"; TRANSMEM 1569..1591; /note="Helical; Name=S4 of repeat IV"; /evidence="ECO:0000250|UniProtKB:Q9NY46"; TRANSMEM 1605..1628; /note="Helical; Name=S5 of repeat IV"; /evidence="ECO:0000250|UniProtKB:Q9NY46"; TRANSMEM 1696..1721; /note="Helical; Name=S6 of repeat IV"; /evidence="ECO:0000250|UniProtKB:Q9NY46
uniprot
proteins