Scn5a
entrez
25665
canonical
uniprot
P15389
canonical
ensembl
ENSRNOG00000015049
resolver
ensp
ENSRNOP00000060180
resolver
ensp
ENSRNOP00000060586
resolver
ensp
ENSRNOP00000069875
resolver
enst
ENSRNOT00000064555
resolver
enst
ENSRNOT00000066932
resolver
enst
ENSRNOT00000082892
resolver
genesymbol
Scn5a
resolver
uniprot
A0A0G2JWG8
resolver
uniprot
F1LNF5
resolver
uniprot
F1LPK3
resolver
uniprot
Q925G6
resolver
uniprot_entry
A0A0G2JWG8_RAT
resolver
uniprot_entry
F1LNF5_RAT
resolver
uniprot_entry
F1LPK3_RAT
resolver
uniprot_entry
SCN5A_RAT
resolver
uniprot_sec
Q925G6
resolver
activity_regulation
ACTIVITY REGULATION: Channel inactivation is regulated by intracellular calcium levels (By similarity). It is a tetrodotoxin-resistant voltage-gated Na(+) channel (Nav) (PubMed:24497506). {ECO:0000250|UniProtKB:Q14524, ECO:0000269|PubMed:24497506}.
uniprot
proteins
amino_acid_sequence
MANLLLPRGTSSFRRFTRESLAAIEKRMAEKQARGGSATSQESREGLQEEEAPRPQLDLQASKKLPDLYGNPPRELIGEPLEDLDPFYSTQKTFIVLNKGKTIFRFSATNALYVLSPFHPVRRAAVKILVHSLFSMLIMCTILTNCVFMAQHDPPPWTKYVEYTFTAIYTFESLVKILARGFCLHAFTFLRDPWNWLDFSVIVMAYTTEFVDLGNVSALRTFRVLRALKTISVISGLKTIVGALIQSVKKLADVMVLTVFCLSVFALIGLQLFMGNLRHKCVRNFTELNGTNGSVEADGLVWNSLDVYLNDPANYLLKNGTTDVLLCGNSSDAGTCPEGYRCLKAGENPDHGYTSFDSFAWAFLALFRLMTQDCWERLYQQTLRSAGKIYMIFFMLVIFLGSFYLVNLILAVVAMAYEEQNQATIAETEEKEKRFQEAMEMLKKEHEALTIRGVDTVSRSSLEMSPLAPVTNHERKSKRRKRLSSGTEDGGDDRLPKSDSEDGPRALNQLSLTHGLSRTSMRPRSSRGSIFTFRRRDQGSEADFADDENSTAGESESHRTSLLVPWPLRHPSAQGQPGPGASAPGYVLNGKRNSTVDCNGVVSLLGAGDAEATSPGSYLLRPMVLDRPPDTTTPSEEPGGPQMLTPQAPCADGFEEPGARQRALSAVSVLTSALEELEESHRKCPPCWNRFAQHYLIWECCPLWMSIKQKVKFVVMDPFADLTITMCIVLNTLFMALEHYNMTAEFEEMLQVGNLVFTGIFTAEMTFKIIALDPYYYFQQGWNIFDSIIVILSLMELGLSRMGNLSVLRSFRLLRVFKLAKSWPTLNTLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKNYSELRHRISDSGLLPRWHMMDFFHAFLIIFRILCGEWIETMWDCMEVSGQSLCLLVFLLVMVIGNLVVLNLFLALLLSSFSADNLTAPDEDGEMNNLQLALARIQRGLRFVKRTTWDFCCGILRRRPKKPAALATHSQLPSCITAPRSPPPPEVEKVPPARKETRFEEDKRPGQGTPGDSEPVCVPIAVAESDTEDQEEDEENSLGTEEESSKQESQVVSGGHEPYQEPRAWSQVSETTSSEAGASTSQADWQQEQKTEPQAPGCGETPEDSYSEGSTADMTNTADLLEQIPDLGEDVKDPEDCFTEGCVRRCPCCMVDTTQSPGKVWWRLRKTCYRIVEHSWFETFIIFMILLSSGALAFEDIYLEERKTIKVLLEYADKMFTYVFVLEMLLKWVAYGFKKYFTNAWCWLDFLIVDVSLVSLVANTLGFAEMGPIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFGRCINQTEGDLPLNYTIVNNKSECESFNVTGELYWTKVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRGYEEQPQWEDNLYMYIYFVVFIIFGSFFTLNLFIGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKYQGFIFDIVTKQAFDVTIMFLICLNMVTMMVETDDQSPEKVNILAKINLLFVAIFTGECIVKMAALRHYYFTNSWNIFDFVVVILSIVGTVLSDIIQKYFFSPTLFRVIRLARIGRILRLIRGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMANFAYVKWEAGIDDMFNFQTFANSMLCLFQITTSAGWDGLLSPILNTGPPYCDPNLPNSNGSRGNCGSPAVGILFFTTYIIISFLIVVNMYIAIILENFSVATEESTEPLSEDDFDMFYEIWEKFDPEATQFIEYLALSDFADALSEPLRIAKPNQISLINMDLPMVSGDRIHCMDILFAFTKRVLGESGEMDALKIQMEEKFMAANPSKISYEPITTTLRRKHEEVSATVIQRAFRRHLLQRSVKHASFLFRQQAGGSGLSDEDAPEREGLIAYMMNGNFSRRSAPLSSSSISSTSFPPSYDSVTRATSDNLPVRASDYSRSEDLADFPPSPDRDRESIV
uniprot
proteins
function
FUNCTION: Pore-forming subunit of Nav1.5, a voltage-gated sodium (Nav) channel that directly mediates the depolarizing phase of action potentials in excitable membranes (By similarity). 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 (By similarity). The influx of Na(+) ions provokes membrane depolarization, initiating the propagation of electrical signals throughout cells and tissues (PubMed:24497506, PubMed:31866066). Nav1.5 is the predominant sodium channel expressed in myocardial cells and it is responsible for the initial upstroke of the action potential in cardiac myocytes, thereby initiating the heartbeat (By similarity). Required for normal electrical conduction including formation of the infranodal ventricular conduction system and normal action potential configuration, as a result of its interaction with XIRP2 (By similarity). {ECO:0000250|UniProtKB:Q14524, ECO:0000250|UniProtKB:Q9JJV9, ECO:0000269|PubMed:24497506, ECO:0000269|PubMed:31866066}.
uniprot
proteins
mass_dalton
227367
uniprot
proteins
mutagenesis
MUTAGEN 869; /note="L->C: >1000-fold increase of sensitivity to the conotoxin GVIIJ(SSG)."; /evidence="ECO:0000269|PubMed:24497506"; MUTAGEN 1612; /note="D->N,R: Little change in voltage-dependence of conductance and decrease in affinity to the sea anemone toxin anthopleurin-B (residue Lys-37)."; /evidence="ECO:0000269|PubMed:9417050
uniprot
proteins
post_translational_modification
PTM: N-glycosylated at Asn-319, hinders potential interaction with regulatory subunits. {ECO:0000269|PubMed:31866066}.; PTM: Phosphorylation at Ser-1505 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents. Regulated through phosphorylation by CaMK2D. {ECO:0000250|UniProtKB:Q14524, ECO:0000250|UniProtKB:Q9JJV9}.; PTM: Ubiquitinated by NEDD4L; which promotes its endocytosis. Does not seem to be ubiquitinated by NEDD4 or WWP2. {ECO:0000250|UniProtKB:Q14524}.; PTM: Lacks the cysteine which covalently binds the conotoxin GVIIJ. This cysteine (position 869) is speculated in other sodium channel subunits alpha to be implied in covalent binding with the sodium channel subunit beta-2 or beta-4. {ECO:0000305|PubMed:24497506}.
uniprot
proteins
protein_family
Nav1.5/SCN5A subfamily
uniprot
proteins
protein_family
Sodium channel (TC 1.A.1.10) family
uniprot
proteins
pubmed
15579534
uniprot
proteins
pubmed
18386309
uniprot
proteins
pubmed
19376164
uniprot
proteins
pubmed
19661460
uniprot
proteins
pubmed
21617128
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
24497506
uniprot
proteins
pubmed
2554302
uniprot
proteins
pubmed
26039939
uniprot
proteins
pubmed
31866066
uniprot
proteins
pubmed
9417050
uniprot
proteins
sequence_length
2019
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21617128}; Multi-pass membrane protein {ECO:0000269|PubMed:31866066}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q14524}. Cell membrane, sarcolemma, T-tubule {ECO:0000269|PubMed:15579534}. Cell junction {ECO:0000269|PubMed:19661460}. Note=RANGRF promotes trafficking to the cell membrane. Colocalizes with PKP2 at intercalated disks in the heart (PubMed:19661460). {ECO:0000250|UniProtKB:Q14524, ECO:0000269|PubMed:19661460}.
uniprot
proteins
transmembrane_region
TRANSMEM 131..150; /note="Helical; Name=S1 of repeat I"; /evidence="ECO:0000305|PubMed:31866066, ECO:0007744|PDB:6UZ0"; TRANSMEM 159..180; /note="Helical; Name=S2 of repeat I"; /evidence="ECO:0000305|PubMed:31866066, ECO:0007744|PDB:6UZ0"; TRANSMEM 190..210; /note="Helical; Name=S3 of repeat I"; /evidence="ECO:0000305|PubMed:31866066, ECO:0007744|PDB:6UZ0"; TRANSMEM 218..237; /note="Helical; Name=S4 of repeat I"; /evidence="ECO:0000305|PubMed:31866066, ECO:0007744|PDB:6UZ0"; TRANSMEM 251..273; /note="Helical; Name=S5 of repeat I"; /evidence="ECO:0000305|PubMed:31866066, ECO:0007744|PDB:6UZ0"; TRANSMEM 388..414; /note="Helical; Name=S6 of repeat I"; /evidence="ECO:0000305|PubMed:31866066, ECO:0007744|PDB:6UZ0"; TRANSMEM 721..738; /note="Helical; Name=S1 of repeat II"; /evidence="ECO:0000305|PubMed:31866066, ECO:0007744|PDB:6UZ0"; TRANSMEM 748..770; /note="Helical; Name=S2 of repeat II"; /evidence="ECO:0000250|UniProtKB:Q14524"; TRANSMEM 777..797; /note="Helical; Name=S3 of repeat II"; /evidence="ECO:0000250|UniProtKB:Q14524"; TRANSMEM 808..822; /note="Helical; Name=S4 of repeat II"; /evidence="ECO:0000305|PubMed:31866066, ECO:0007744|PDB:6UZ0"; TRANSMEM 840..861; /note="Helical; Name=S5 of repeat II"; /evidence="ECO:0000250|UniProtKB:Q14524"; TRANSMEM 916..944; /note="Helical; Name=S6 of repeat II"; /evidence="ECO:0000250|UniProtKB:D0E0C2"; TRANSMEM 1206..1227; /note="Helical; Name=S1 of repeat III"; /evidence="ECO:0000250|UniProtKB:D0E0C2"; TRANSMEM 1239..1261; /note="Helical; Name=S2 of repeat III"; /evidence="ECO:0000250|UniProtKB:D0E0C2"; TRANSMEM 1271..1293; /note="Helical; Name=S3 of repeat III"; /evidence="ECO:0000250|UniProtKB:D0E0C2"; TRANSMEM 1300..1319; /note="Helical; Name=S4 of repeat III"; /evidence="ECO:0000250|UniProtKB:D0E0C2"; TRANSMEM 1333..1357; /note="Helical; Name=S5 of repeat III"; /evidence="ECO:0000250|UniProtKB:D0E0C2"; TRANSMEM 1448..1472; /note="Helical; Name=S6 of repeat III"; /evidence="ECO:0000250|UniProtKB:Q14524"; TRANSMEM 1531..1549; /note="Helical; Name=S1 of repeat IV"; /evidence="ECO:0000250|UniProtKB:Q14524"; TRANSMEM 1561..1582; /note="Helical; Name=S2 of repeat IV"; /evidence="ECO:0000250|UniProtKB:Q14524"; TRANSMEM 1592..1614; /note="Helical; Name=S3 of repeat IV"; /evidence="ECO:0000250|UniProtKB:Q14524"; TRANSMEM 1622..1642; /note="Helical; Name=S4 of repeat IV"; /evidence="ECO:0000305|PubMed:31866066, ECO:0007744|PDB:6UZ0"; TRANSMEM 1653..1681; /note="Helical; Name=S5 of repeat IV"; /evidence="ECO:0000305|PubMed:31866066, ECO:0007744|PDB:6UZ0"; TRANSMEM 1748..1773; /note="Helical; Name=S6 of repeat IV"; /evidence="ECO:0000305|PubMed:31866066, ECO:0007744|PDB:6UZ0
uniprot
proteins