Na+ channel protein type 1 subunit alpha; Na+ channel protein type I subunit alpha; voltage-gated Na+ channel subunit alpha Nav1.1; Na+ channel protein, brain I subunit alpha (SCN1A, NAC1, SCN1)

Function: - mediates voltage-dependent Na⁺ permeability of excitable membranes - assumes opened or closed conformation in response to voltage difference across membrane - forms a Na⁺-selective channel through which Na⁺ ions may pass in accordance with their electrochemical gradient - the Na⁺ channel consists of a large polypeptide & 2-3 smaller ones Structure: - large polypeptide contains 4 internal repeats, each with 5 hydrophobic segments (S1,S2,S3,S5,S6) & one positively charged segment (S4) - segments S4 are probably the voltage-sensors & are characterized by a series of positively charged amino acids at every third position - belongs to the Na⁺ channel family - contains 1 IQ domain Compartment: membrane Alternative splicing: named isoforms=2 Pathology: - defects in SCN1A are the cause of a) generalized epilepsy with febrile seizures plus type 2 b) severe myoclonic epilepsy in infancy (Dravet syndrome) c) intractable childhood epilepsy with generalized tonic-clonic seizures (ICEGTC) d) familial hemiplegic migraine type 3 e) familial febrile convulsions type 3

General

glycoprotein voltage-dependent Na+ channel protein alpha subunit transmembrane 24 protein

Properties

SIZE: MW = 229 kD entity length = 2009 aa COMPARTMENT: cellular membrane MOTIF: cytoplasmic domain {1-123} transmembrane domain {124-147} exoplasmic loop {148-155} transmembrane domain {156-175} cytoplasmic loop {176-188} transmembrane domain {189-207} exoplasmic loop {208-213} MOTIF: N-glycosylation site {N211} transmembrane domain {214-233} cytoplasmic loop {234-249} transmembrane domain {250-273} exoplasmic loop {274-399} MOTIF: N-glycosylation site {N284} N-glycosylation site {N295} N-glycosylation site {N301} N-glycosylation site {N306} N-glycosylation site {N338} transmembrane domain {400-425} cytoplasmic loop {426-762} MOTIF: N-glycosylation site {N601} N-glycosylation site {N621} N-glycosylation site {N681} transmembrane domain {763-787} exoplasmic loop {788-798} transmembrane domain {799-822} cytoplasmic loop {823-830} transmembrane domain {831-850} exoplasmic loop {851-856} transmembrane domain {857-876} cytoplasmic loop {877-892} MOTIF: N-glycosylation site {N892} transmembrane domain {893-913} exoplasmic loop {914-966} transmembrane domain {967-992} cytoplasmic loop {993-1213} MOTIF: N-glycosylation site {N1064} N-glycosylation site {N1080} N-glycosylation site {N1146} transmembrane domain {1214-1237} exoplasmic loop {1238-1250} transmembrane domain {1251-1276} cytoplasmic loop {1277-1282} transmembrane domain {1283-1304} exoplasmic loop {1305-1308} transmembrane domain {1309-1330} cytoplasmic loop {1331-1349} transmembrane domain {1350-1377} exoplasmic loop {1378-1456} MOTIF: N-glycosylation site {N1378} N-glycosylation site {N1392} N-glycosylation site {N1403} transmembrane domain {1457-1483} cytoplasmic loop {1484-1536} transmembrane domain {1537-1560} exoplasmic loop {1561-1571} transmembrane domain {1572-1595} cytoplasmic loop {1596-1601} transmembrane domain {1602-1625} exoplasmic loop {1626-1635} transmembrane domain {1636-1657} cytoplasmic loop {1658-1672} transmembrane domain {1673-1695} exoplasmic loop {1696-1761} transmembrane domain {1762-1786} cytoplasmic domain {1787-2009} MOTIF: N-glycosylation site {N1788}

Database Correlations

OMIM correlations MORBIDMAP 182389 UniProt P35498 PFAM correlations Entrez Gene 6323 Kegg hsa:6323