Scn5a
entrez
20271
canonical
uniprot
Q9JJV9
canonical
ensembl
ENSMUSG00000032511
resolver
ensp
ENSMUSP00000066228
resolver
ensp
ENSMUSP00000112838
resolver
ensp
ENSMUSP00000113272
resolver
enst
ENSMUST00000065196
resolver
enst
ENSMUST00000117911
resolver
genesymbol
Scn5a
resolver
uniprot
A0A0R4J1M7
resolver
uniprot
E9Q1D2
resolver
uniprot
K3W4N7
resolver
uniprot
Q3UH91
resolver
uniprot
Q8C3I3
resolver
uniprot_entry
A0A0R4J1M7_MOUSE
resolver
uniprot_entry
K3W4N7_MOUSE
resolver
uniprot_entry
Q8C3I3_MOUSE
resolver
uniprot_entry
SCN5A_MOUSE
resolver
uniprot_sec
E9Q1D2
resolver
uniprot_sec
Q3UH91
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) (By similarity). {ECO:0000250|UniProtKB:Q14524}.
uniprot
proteins
amino_acid_sequence
MANFLLPRGTSSFRRFTRESLAAIEKRMAEKQARGSATSQESREGLPEEEAPRPQLDLQASKKLPDLYGNPPRELIGEPLEDLDPFYSTQKTFIVLNKGKTIFRFSATNALYVLSPFHPVRRAAVKILVHSLFSMLIMCTILTNCVFMAQHDPPPWTKYVEYTFTAIYTFESLVKILARGFCLHAFTFLRDPWNWLDFSVIVMAYTTEFVDLGNVSALRTFRVLRALKTISVISGLKTIVGALIQSVKKLADVMVLTVFCLSVFALIGLQLFMGNLRHKCVRNFTELNGTNGSVEADGIVWNSLDVYLNDPANYLLKNGTTDVLLCGNSSDAGTCPEGYRCLKAGENPDHGYTSFDSFAWAFLALFRLMTQDCWERLYQQTLRSAGKIYMIFFMLVIFLGSFYLVNLILAVVAMAYEEQNQATIAETEEKEKRFQEAMEMLKKEHEALTIRGVDTVSRSSLEMSPLAPVTNHERRSKRRKRLSSGTEDGGDDRLPKSDSEDGPRALNQLSLTHGLSRTSMRPRSSRGSIFTFRRRDQGSEADFADDENSTAGESESHRTSLLVPWPLRRPSTQGQPGFGTSAPGHVLNGKRNSTVDCNGVVSLLGAGDAEATSPGSHLLRPIVLDRPPDTTTPSEEPGGPQMLTPQAPCADGFEEPGARQRALSAVSVLTSALEELEESHRKCPPCWNRFAQHYLIWECCPLWMSIKQKVKFVVMDPFADLTITMCIVLNTLFMALEHYNMTAEFEEMLQVGNLVFTGIFTAEMTFKIIALDPYYYFQQGWNIFDSIIVILSLMELGLSRMGNLSVLRSFRLLRVFKLAKSWPTLNTLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKNYSELRHRISDSGLLPRWHMMDFFHAFLIIFRILCGEWIETMWDCMEVSGQSLCLLVFLLVMVIGNLVVLNLFLALLLSSFSADNLTAPDEDGEMNNLQLALARIQRGLRFVKRTTWDFCCGLLRRRPKKPAALATHSQLPSCIAAPRSPPPPEVEKAPPARKETRFEEDKRPGQGTPGDTEPVCVPIAVAESDTDDQEEDEENSLGTEEEESSKQESQVVSGGHEPPQEPRAWSQVSETTSSEAEASTSQADWQQEREAEPRAPGCGETPEDSYSEGSTADMTNTADLLEQIPDLGEDVKDPEDCFTEGCVRRCPCCMVDTTQAPGKVWWRLRKTCYRIVEHSWFETFIIFMILLSSGALAFEDIYLEERKTIKVLLEYADKMFTYVFVLEMLLKWVAYGFKKYFTNAWCWLDFLIVDVSLVSLVANTLGFAEMGPIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFGRCINQTEGDLPLNYTIVNNKSECESFNVTGELYWTKVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRGYEEQPQWEDNLYMYIYFVVFIIFGSFFTLNLFIGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKYQGFIFDIVTKQAFDVTIMFLICLNMVTMMVETDDQSPEKVNILAKINLLFVAIFTGECIVKMAALRHYYFTNSWNIFDFVVVILSIVGTVLSDIIQKYFFSPTLFRVIRLARIGRILRLIRGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMANFAYVKWEAGIDDMFNFQTFANSMLCLFQITTSAGWDGLLSPILNTGPPYCDPNLPNSNGSRGNCGSPAVGILFFTTYIIISFLIVVNMYIAIILENFSVATEESTEPLSEDDFDMFYEIWEKFDPEATQFIEYLALSDFADALSEPLRIAKPNQISLINMDLPMVSGDRIHCMDILFAFTKRVLGESGEMDALKIQMEEKFMAANPSKISYEPITTTLRRKHEEVSATVIQRAFRRHLLQRSVKHASFLFRQQAGSSGLSDEDAPEREGLIAYMMNENFSRRSGPLSSSSISSTSFPPSYDSVTRATSDNLPVRASDYSRSEDLADFPPSPDRDRESIV
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:11834499, PubMed:23420830). 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 (PubMed:11834499, PubMed:23420830, PubMed:29306897). 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 (PubMed:29306897). {ECO:0000250|UniProtKB:Q14524, ECO:0000269|PubMed:11834499, ECO:0000269|PubMed:23420830, ECO:0000269|PubMed:29306897}.
uniprot
proteins
mass_dalton
227576
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-1505 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents (By similarity). Regulated through phosphorylation by CaMK2D (PubMed:17124532). {ECO:0000250|UniProtKB:Q14524, ECO:0000269|PubMed:17124532}.; 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 868) 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:0000250|UniProtKB:P15389}.; PTM: N-glycosylated at Asn-318, probably hinders potential interaction with regulatory subunits. {ECO:0000250|UniProtKB:P15389}.
uniprot
proteins
protein_family
Nav1.5/SCN5A subfamily
uniprot
proteins
protein_family
Sodium channel (TC 1.A.1.10) family
uniprot
proteins
pubmed
11834499
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17124532
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21817159
uniprot
proteins
pubmed
23420830
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
29306897
uniprot
proteins
pubmed
9412493
uniprot
proteins
sequence_length
2019
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11834499, ECO:0000269|PubMed:23420830}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P15389}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q14524}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:P15389}. Cell junction {ECO:0000250|UniProtKB:P15389}. Note=RANGRF promotes trafficking to the cell membrane. Colocalizes with PKP2 at intercalated disks in the heart (By similarity). {ECO:0000250|UniProtKB:P15389, ECO:0000269|PubMed:23420830}.
uniprot
proteins
transmembrane_region
TRANSMEM 130..149; /note="Helical; Name=S1 of repeat I"; /evidence="ECO:0000250|UniProtKB:Q14524"; TRANSMEM 158..179; /note="Helical; Name=S2 of repeat I"; /evidence="ECO:0000250|UniProtKB:Q14524"; TRANSMEM 189..209; /note="Helical; Name=S3 of repeat I"; /evidence="ECO:0000250|UniProtKB:Q14524"; TRANSMEM 217..236; /note="Helical; Name=S4 of repeat I"; /evidence="ECO:0000250|UniProtKB:Q14524"; TRANSMEM 250..272; /note="Helical; Name=S5 of repeat I"; /evidence="ECO:0000250|UniProtKB:Q14524"; TRANSMEM 387..413; /note="Helical; Name=S6 of repeat I"; /evidence="ECO:0000250|UniProtKB:Q14524"; TRANSMEM 720..737; /note="Helical; Name=S1 of repeat II"; /evidence="ECO:0000250|UniProtKB:Q14524"; TRANSMEM 747..769; /note="Helical; Name=S2 of repeat II"; /evidence="ECO:0000250|UniProtKB:Q14524"; TRANSMEM 776..796; /note="Helical; Name=S3 of repeat II"; /evidence="ECO:0000250|UniProtKB:Q14524"; TRANSMEM 807..821; /note="Helical; Name=S4 of repeat II"; /evidence="ECO:0000250|UniProtKB:Q14524"; TRANSMEM 839..860; /note="Helical; Name=S5 of repeat II"; /evidence="ECO:0000250|UniProtKB:Q14524"; TRANSMEM 915..943; /note="Helical; Name=S6 of repeat II"; /evidence="ECO:0000250|UniProtKB:Q14524"; TRANSMEM 1206..1227; /note="Helical; Name=S1 of repeat III"; /evidence="ECO:0000250|UniProtKB:Q14524"; TRANSMEM 1239..1261; /note="Helical; Name=S2 of repeat III"; /evidence="ECO:0000250|UniProtKB:Q14524"; TRANSMEM 1271..1293; /note="Helical; Name=S3 of repeat III"; /evidence="ECO:0000250|UniProtKB:Q14524"; TRANSMEM 1300..1319; /note="Helical; Name=S4 of repeat III"; /evidence="ECO:0000250|UniProtKB:Q14524"; TRANSMEM 1333..1357; /note="Helical; Name=S5 of repeat III"; /evidence="ECO:0000250|UniProtKB:Q14524"; 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:0000250|UniProtKB:Q14524"; TRANSMEM 1653..1681; /note="Helical; Name=S5 of repeat IV"; /evidence="ECO:0000250|UniProtKB:Q14524"; TRANSMEM 1748..1773; /note="Helical; Name=S6 of repeat IV"; /evidence="ECO:0000250|UniProtKB:Q14524
uniprot
proteins