Scn4a
entrez
110880
canonical
uniprot
Q9ER60
canonical
ensembl
ENSMUSG00000001027
resolver
ensp
ENSMUSP00000021056
resolver
enst
ENSMUST00000021056
resolver
genesymbol
Scn4a
resolver
uniprot
A2VDE9
resolver
uniprot
B1ARK0
resolver
uniprot
G3X8T7
resolver
uniprot_entry
G3X8T7_MOUSE
resolver
uniprot_entry
SCN4A_MOUSE
resolver
uniprot_sec
A2VDE9
resolver
uniprot_sec
B1ARK0
resolver
activity_regulation
ACTIVITY REGULATION: The channel is inhibited by tetrodotoxin. {ECO:0000269|PubMed:11834499}.
uniprot
proteins
amino_acid_sequence
MASSSLPTLVPPGPHCLRPFTPESLAAIEQRAMEEEARLQRNKQMEIEEPERKPRSDLEAGKNLPLIYGDPPPEVIGVPLEDLDPYYSDKKTFIVLNKGKAIFRFSATPALYMLSPFSIVRRVAIKVLIHALFSMFIMITILTNCVFMTMSNPPSWSKDVEYTFTGIYTFESLIKMLARGFCIDDFTFLRDPWNWLDFSVITMAYVTEFVDLGNISALRTFRVLRALKTITVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALVGLQLFMGNLRQKCVRWPPPMNDTNTTWYGNDTWYGNDTWYGNDTWYGNDTWNSQESWVSNSTFDWEAYINDEGNFYFLEGSNDALLCGNSSDAGHCPEGYECMKAGRNPNYGYTSYDTFSWAFLALFRLMTQDYWENLFQLTLRAAGKTYMIFFVVIIFLGSFYLINLILAVVAMAYAEQNEATLAEDQEKEEEFQQMLEKFKKHQEELEKAKAAQALEGGEEADGDPTHSKDCNGSLDTSGEKGPPRPSCSAESAISDAMEELEEAHQKCPPWWYKCAHKVLIWNCCAPWVKFKHIILLIVMDPFVDLGITICIVLNTLFMAMEHYPMTEHFDNVLSVGNLVFTGIFTAEMVLKLIAMDPYEYFQQGWNIFDSFIVTLSLVELGLANVQGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKIASDCSLPRWHMHDFFHSFLIVFRILCGEWIETMWDCMEVAGQAMCLTVFLMVMVIGNLVVLNLFLALLLSSFSADSLAASDEDGEMNNLQIAIGRIKWGIAFAKTFLLGLLHGKILSLKDIMLSLGEPGGAGENGESPPEDEKKEPPPEDGNKELKDNHILNHVGLTDGPRSSIEMDHLNFINNPYLTIHVPIASEESDLEMPTEEETDTFSEPEDIKKPLQPLYDGNSSVCSTADYKPPEEDPEEQAEENPEGELPEECFTEACVKRCPCLYVDISQGRGKMWWTLRRACFKIVEHNWFETFIVFMILLSSGALAFEDIYIEQRRVIRTILEYADKVFTYIFILEMLLKWVAYGFKVYFTNAWCWLDFLIVDVSIISLVANWLGYSELGPIKSLRTLRALRPLRALSRFEGMRVVVNALLGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYYCINTTTSERFDISVVNNKSECESLMYTGQVRWMNVKVNYDNVGLGYLSLLQVATFKGWMDIMYAAVDSREKEEQPDYEVNLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGKDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPQNKIQGMVYDFVTKQVFDISIMILICLNMVTMMVETDDQSQLKVDILYNINMVFIIVFTGECVLKMFALRHYYFTIGWNIFDFVVVILSIVGLALSDLIQKYFVSPTLFRVIRLARIGRVLRLIRGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMSNFAYVKKESGIDDMFNFETFGNSIICLFEITTSAGWDGLLNPILNSGPPDCDPTLENPGTNIKGDCGNPSIGICFFCSYIIISFLIVVNMYIAIILENFNVATEESSEPLCEDDFEMFYETWEKFDPDATQFIDYSRLSDFVDTLQEPLKIAKPNKIKLITLDLPMVPGDKIHCLDILFALTKEVLGDSGEMDALKQTMEEKFMAANPSKVSYEPITTTLKRKQEEVCAIKIQRAYRRHLLQRSVKQASYMYRHSQEGNGDGAPEKEGLLANTMNKMYGSEKEDNGVQSQGEKEKDSTEDAGPTTEVTAPSSSDTALTPPPPSPPPPSSPPQGQTVRPGVKESLV
uniprot
proteins
function
FUNCTION: Pore-forming subunit of Nav1.4, 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:11834499). Highly expressed in skeletal muscles, Nav1.4 generates the action potential crucial for muscle contraction (PubMed:18317596, PubMed:21881211). {ECO:0000269|PubMed:11834499, ECO:0000269|PubMed:18317596, ECO:0000269|PubMed:21881211}.
uniprot
proteins
mass_dalton
208798
uniprot
proteins
mutagenesis
MUTAGEN 663; /note="R->F: Homozygous mice are born at the expected Mendelian rate and have no visible phenotype. Hind-limb muscles show decreased excitability and decreased force when K(+) levels are low (in vivo). Isolated soleus muscle from homozygous mice has an increased susceptibility to loss of force generation at 2 mMK(+)."; /evidence="ECO:0000269|PubMed:21881211"; MUTAGEN 1586; /note="M->V: A very low percentage of homozygous mice are present at 30 days after birth, suggesting high perinatal lethality. In anesthesized heterozygous mice, electromyographs from hind-limb muscle show high background activity, indicative of myotonia. Isolated extensor digitorum longus muscle from heterozygous mice displays reduced twitch force, with a normal speed of muscle contraction, but an increased muscle relaxation half-time. Isolated skeletal muscle from heterozygous mice has strongly decreased force when the K(+) levels are increased to 10 mM. Homozygous mice display prominent hind-limb weakness and muscle atrophy."; /evidence="ECO:0000269|PubMed:18317596
uniprot
proteins
protein_family
Nav1.4/SCN4A subfamily
uniprot
proteins
protein_family
Sodium channel (TC 1.A.1.10) family
uniprot
proteins
pubmed
11834499
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18317596
uniprot
proteins
pubmed
18625851
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21881211
uniprot
proteins
pubmed
26427606
uniprot
proteins
pubmed
9412493
uniprot
proteins
sequence_length
1841
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11834499}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P35499}.
uniprot
proteins
transmembrane_region
TRANSMEM 132..150; /note="Helical; Name=S1 of repeat I"; /evidence="ECO:0000250|UniProtKB:P35499"; TRANSMEM 158..178; /note="Helical; Name=S2 of repeat I"; /evidence="ECO:0000250|UniProtKB:P35499"; TRANSMEM 193..210; /note="Helical; Name=S3 of repeat I"; /evidence="ECO:0000250|UniProtKB:P35499"; TRANSMEM 217..233; /note="Helical; Name=S4 of repeat I"; /evidence="ECO:0000250|UniProtKB:P35499"; TRANSMEM 253..272; /note="Helical; Name=S5 of repeat I"; /evidence="ECO:0000250|UniProtKB:P35499"; TRANSMEM 418..438; /note="Helical; Name=S6 of repeat I"; /evidence="ECO:0000250|UniProtKB:P35499"; TRANSMEM 573..591; /note="Helical; Name=S1 of repeat II"; /evidence="ECO:0000250|UniProtKB:P35499"; TRANSMEM 603..622; /note="Helical; Name=S2 of repeat II"; /evidence="ECO:0000250|UniProtKB:P35499"; TRANSMEM 637..656; /note="Helical; Name=S3 of repeat II"; /evidence="ECO:0000250|UniProtKB:P35499"; TRANSMEM 659..676; /note="Helical; Name=S4 of repeat II"; /evidence="ECO:0000250|UniProtKB:P35499"; TRANSMEM 693..711; /note="Helical; Name=S5 of repeat II"; /evidence="ECO:0000250|UniProtKB:P35499"; TRANSMEM 773..791; /note="Helical; Name=S6 of repeat II"; /evidence="ECO:0000250|UniProtKB:P35499"; TRANSMEM 1027..1044; /note="Helical; Name=S1 of repeat III"; /evidence="ECO:0000250|UniProtKB:P35499"; TRANSMEM 1058..1076; /note="Helical; Name=S2 of repeat III"; /evidence="ECO:0000250|UniProtKB:P35499"; TRANSMEM 1091..1109; /note="Helical; Name=S3 of repeat III"; /evidence="ECO:0000250|UniProtKB:P35499"; TRANSMEM 1118..1136; /note="Helical; Name=S4 of repeat III"; /evidence="ECO:0000250|UniProtKB:P35499"; TRANSMEM 1154..1173; /note="Helical; Name=S5 of repeat III"; /evidence="ECO:0000250|UniProtKB:P35499"; TRANSMEM 1264..1285; /note="Helical; Name=S6 of repeat III"; /evidence="ECO:0000250|UniProtKB:P35499"; TRANSMEM 1349..1366; /note="Helical; Name=S1 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P35499"; TRANSMEM 1378..1396; /note="Helical; Name=S2 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P35499"; TRANSMEM 1409..1426; /note="Helical; Name=S3 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P35499"; TRANSMEM 1440..1456; /note="Helical; Name=S4 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P35499"; TRANSMEM 1476..1493; /note="Helical; Name=S5 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P35499"; TRANSMEM 1569..1591; /note="Helical; Name=S6 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P35499
uniprot
proteins