Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 145 (18 Sep 2019)
Sequence version 1 (01 Apr 1990)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Sodium channel protein type 5 subunit alpha

Gene

Scn5a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

This protein mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na+ ions may pass in accordance with their electrochemical gradient. It is a tetrodotoxin-resistant Na+ channel isoform. This channel is responsible for the initial upstroke of the action potential. Channel inactivation is regulated by intracellular calcium levels.By similarity

Miscellaneous

Na+ channels in mammalian cardiac membrane have functional properties quite distinct from Na+ channels in nerve and skeletal muscle.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei374Cys residue near the selectivity filter, which has a free thiol that is susceptible to reaction with methanethiosulfonate (MTSET); Sodium current is irreversibly blocked by MTSETBy similarity1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionCalmodulin-binding, Ion channel, Sodium channel, Voltage-gated channel
Biological processIon transport, Sodium transport, Transport
LigandSodium

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-5576892 Phase 0 - rapid depolarisation

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Sodium channel protein type 5 subunit alpha
Alternative name(s):
Sodium channel protein cardiac muscle subunit alpha
Sodium channel protein type V subunit alpha
Voltage-gated sodium channel subunit alpha Nav1.5
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Scn5a
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
3637 Scn5a

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 132CytoplasmicCuratedAdd BLAST132
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei133 – 151Helical; Name=S1 of repeat IBy similarityAdd BLAST19
Topological domaini152 – 158ExtracellularCurated7
Transmembranei159 – 179Helical; Name=S2 of repeat IBy similarityAdd BLAST21
Topological domaini180 – 193CytoplasmicCuratedAdd BLAST14
Transmembranei194 – 211Helical; Name=S3 of repeat IBy similarityAdd BLAST18
Topological domaini212 – 217ExtracellularCurated6
Transmembranei218 – 234Helical; Name=S4 of repeat IBy similarityAdd BLAST17
Topological domaini235 – 253CytoplasmicCuratedAdd BLAST19
Transmembranei254 – 273Helical; Name=S5 of repeat IBy similarityAdd BLAST20
Topological domaini274 – 358ExtracellularCuratedAdd BLAST85
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei359 – 383Pore-formingBy similarityAdd BLAST25
Topological domaini384 – 390ExtracellularCurated7
Transmembranei391 – 411Helical; Name=S6 of repeat IBy similarityAdd BLAST21
Topological domaini412 – 718CytoplasmicCuratedAdd BLAST307
Transmembranei719 – 737Helical; Name=S1 of repeat IIBy similarityAdd BLAST19
Topological domaini738 – 748ExtracellularCuratedAdd BLAST11
Transmembranei749 – 768Helical; Name=S2 of repeat IIBy similarityAdd BLAST20
Topological domaini769 – 782CytoplasmicCuratedAdd BLAST14
Transmembranei783 – 802Helical; Name=S3 of repeat IIBy similarityAdd BLAST20
Topological domaini803 – 804ExtracellularCurated2
Transmembranei805 – 822Helical; Name=S4 of repeat IIBy similarityAdd BLAST18
Topological domaini823 – 838CytoplasmicCuratedAdd BLAST16
Transmembranei839 – 857Helical; Name=S5 of repeat IIBy similarityAdd BLAST19
Topological domaini858 – 886ExtracellularCuratedAdd BLAST29
Intramembranei887 – 907Pore-formingBy similarityAdd BLAST21
Topological domaini908 – 920ExtracellularCuratedAdd BLAST13
Transmembranei921 – 941Helical; Name=S6 of repeat IIBy similarityAdd BLAST21
Topological domaini942 – 1208CytoplasmicCuratedAdd BLAST267
Transmembranei1209 – 1226Helical; Name=S1 of repeat IIIBy similarityAdd BLAST18
Topological domaini1227 – 1239ExtracellularCuratedAdd BLAST13
Transmembranei1240 – 1258Helical; Name=S2 of repeat IIIBy similarityAdd BLAST19
Topological domaini1259 – 1272CytoplasmicCuratedAdd BLAST14
Transmembranei1273 – 1291Helical; Name=S3 of repeat IIIBy similarityAdd BLAST19
Topological domaini1292 – 1299ExtracellularCurated8
Transmembranei1300 – 1318Helical; Name=S4 of repeat IIIBy similarityAdd BLAST19
Topological domaini1319 – 1335CytoplasmicCuratedAdd BLAST17
Transmembranei1336 – 1355Helical; Name=S5 of repeat IIIBy similarityAdd BLAST20
Topological domaini1356 – 1407ExtracellularCuratedAdd BLAST52
Intramembranei1408 – 1429Pore-formingBy similarityAdd BLAST22
Topological domaini1430 – 1446ExtracellularCuratedAdd BLAST17
Transmembranei1447 – 1468Helical; Name=S6 of repeat IIIBy similarityAdd BLAST22
Topological domaini1469 – 1531CytoplasmicCuratedAdd BLAST63
Transmembranei1532 – 1549Helical; Name=S1 of repeat IVBy similarityAdd BLAST18
Topological domaini1550 – 1560ExtracellularCuratedAdd BLAST11
Transmembranei1561 – 1579Helical; Name=S2 of repeat IVBy similarityAdd BLAST19
Topological domaini1580 – 1591CytoplasmicCuratedAdd BLAST12
Transmembranei1592 – 1609Helical; Name=S3 of repeat IVBy similarityAdd BLAST18
Topological domaini1610 – 1622ExtracellularCuratedAdd BLAST13
Transmembranei1623 – 1639Helical; Name=S4 of repeat IVBy similarityAdd BLAST17
Topological domaini1640 – 1658CytoplasmicCuratedAdd BLAST19
Transmembranei1659 – 1676Helical; Name=S5 of repeat IVBy similarityAdd BLAST18
Topological domaini1677 – 1698ExtracellularCuratedAdd BLAST22
Intramembranei1699 – 1721Pore-formingBy similarityAdd BLAST23
Topological domaini1722 – 1750ExtracellularCuratedAdd BLAST29
Transmembranei1751 – 1773Helical; Name=S6 of repeat IVBy similarityAdd BLAST23
Topological domaini1774 – 2019CytoplasmicCuratedAdd BLAST246

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi869L → C: >1000-fold increase of sensitivity to the conotoxin GVIIJ(SSG). 1 Publication1
Mutagenesisi1612D → N or R: Little change in voltage-dependence of conductance and decrease in affinity to the sea anemone toxin anthopleurin-B (residue Lys-37). 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3866

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
582

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000484981 – 2019Sodium channel protein type 5 subunit alphaAdd BLAST2019

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei37PhosphoserineBy similarity1
Modified residuei39PhosphothreonineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi215N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi281 ↔ 336By similarity
Glycosylationi284N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi289N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi292N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi319N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi329N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei458PhosphoserineBy similarity1
Modified residuei461PhosphoserineBy similarity1
Modified residuei484PhosphoserineCombined sources1
Modified residuei485PhosphoserineCombined sources1
Modified residuei487PhosphothreonineCombined sources1
Modified residuei498PhosphoserineBy similarity1
Modified residuei511PhosphoserineBy similarity1
Modified residuei527Dimethylated arginine; alternateBy similarity1
Modified residuei527Omega-N-methylarginine; alternateBy similarity1
Modified residuei540PhosphoserineBy similarity1
Modified residuei572PhosphoserineBy similarity1
Modified residuei665PhosphoserineBy similarity1
Modified residuei668PhosphoserineBy similarity1
Glycosylationi741N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi804N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi865N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi909 ↔ 918By similarity
Glycosylationi1367N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1376N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1382N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1390N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei1505Phosphoserine; by PKCBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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.By similarity
Ubiquitinated by NEDD4L; which promotes its endocytosis. Does not seem to be ubiquitinated by NEDD4 or WWP2.By similarity
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-4.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P15389

PRoteomics IDEntifications database

More...
PRIDEi
P15389

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P15389

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P15389

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P15389

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Strongly expressed in the heart. Also expressed in adult and fetal brain, spinal cord, testis, and at moderate levels in kidney, adrenal gland, lung, skeletal muscle, spleen, stomach and bladder. Isoform 2 is expressed in brain.2 Publications

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with the PDZ domain of the syntrophin SNTA1, SNTB1 and SNTB2.

Interacts with NEDD4, NEDD4L, WWP2 and GPD1L.

Interacts with CALM.

Interacts with FGF13; the interaction is direct and may regulate SNC5A density at membranes and function. May also interact with FGF12 and FGF14.

Interacts with ANK3 (By similarity).

By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
247694, 1 interactor

Database of interacting proteins

More...
DIPi
DIP-60063N

Protein interaction database and analysis system

More...
IntActi
P15389, 2 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000060180

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P15389

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati114 – 421ICuratedAdd BLAST308
Repeati700 – 972IICuratedAdd BLAST273
Repeati1189 – 1503IIICuratedAdd BLAST315
Repeati1512 – 1809IVCuratedAdd BLAST298
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1903 – 1932IQAdd BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1841 – 1903Interaction with FGF13By similarityAdd BLAST63
Regioni1977 – 1980Interaction with NEDD4, NEDD4L and WWP2By similarity4

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The sequence contains 4 internal repeats, each with 5 hydrophobic segments (S1, S2, S3, S5, S6) and one positively charged segment (S4). Segments S4 are probably the voltage-sensors and are characterized by a series of positively charged amino acids at every third position.Curated
The IQ domain mediates association with calmodulin.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2301 Eukaryota
ENOG410XNP6 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000231755

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P15389

KEGG Orthology (KO)

More...
KOi
K04838

Database of Orthologous Groups

More...
OrthoDBi
172471at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P15389

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.120.350, 4 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR005821 Ion_trans_dom
IPR008053 Na_channel_a5su
IPR001696 Na_channel_asu
IPR010526 Na_trans_assoc
IPR024583 Na_trans_cytopl
IPR027359 Volt_channel_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00520 Ion_trans, 4 hits
PF06512 Na_trans_assoc, 1 hit
PF11933 Na_trans_cytopl, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00170 NACHANNEL
PR01666 NACHANNEL5

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P15389-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MANLLLPRGT SSFRRFTRES LAAIEKRMAE KQARGGSATS QESREGLQEE
60 70 80 90 100
EAPRPQLDLQ ASKKLPDLYG NPPRELIGEP LEDLDPFYST QKTFIVLNKG
110 120 130 140 150
KTIFRFSATN ALYVLSPFHP VRRAAVKILV HSLFSMLIMC TILTNCVFMA
160 170 180 190 200
QHDPPPWTKY VEYTFTAIYT FESLVKILAR GFCLHAFTFL RDPWNWLDFS
210 220 230 240 250
VIVMAYTTEF VDLGNVSALR TFRVLRALKT ISVISGLKTI VGALIQSVKK
260 270 280 290 300
LADVMVLTVF CLSVFALIGL QLFMGNLRHK CVRNFTELNG TNGSVEADGL
310 320 330 340 350
VWNSLDVYLN DPANYLLKNG TTDVLLCGNS SDAGTCPEGY RCLKAGENPD
360 370 380 390 400
HGYTSFDSFA WAFLALFRLM TQDCWERLYQ QTLRSAGKIY MIFFMLVIFL
410 420 430 440 450
GSFYLVNLIL AVVAMAYEEQ NQATIAETEE KEKRFQEAME MLKKEHEALT
460 470 480 490 500
IRGVDTVSRS SLEMSPLAPV TNHERKSKRR KRLSSGTEDG GDDRLPKSDS
510 520 530 540 550
EDGPRALNQL SLTHGLSRTS MRPRSSRGSI FTFRRRDQGS EADFADDENS
560 570 580 590 600
TAGESESHRT SLLVPWPLRH PSAQGQPGPG ASAPGYVLNG KRNSTVDCNG
610 620 630 640 650
VVSLLGAGDA EATSPGSYLL RPMVLDRPPD TTTPSEEPGG PQMLTPQAPC
660 670 680 690 700
ADGFEEPGAR QRALSAVSVL TSALEELEES HRKCPPCWNR FAQHYLIWEC
710 720 730 740 750
CPLWMSIKQK VKFVVMDPFA DLTITMCIVL NTLFMALEHY NMTAEFEEML
760 770 780 790 800
QVGNLVFTGI FTAEMTFKII ALDPYYYFQQ GWNIFDSIIV ILSLMELGLS
810 820 830 840 850
RMGNLSVLRS FRLLRVFKLA KSWPTLNTLI KIIGNSVGAL GNLTLVLAII
860 870 880 890 900
VFIFAVVGMQ LFGKNYSELR HRISDSGLLP RWHMMDFFHA FLIIFRILCG
910 920 930 940 950
EWIETMWDCM EVSGQSLCLL VFLLVMVIGN LVVLNLFLAL LLSSFSADNL
960 970 980 990 1000
TAPDEDGEMN NLQLALARIQ RGLRFVKRTT WDFCCGILRR RPKKPAALAT
1010 1020 1030 1040 1050
HSQLPSCITA PRSPPPPEVE KVPPARKETR FEEDKRPGQG TPGDSEPVCV
1060 1070 1080 1090 1100
PIAVAESDTE DQEEDEENSL GTEEESSKQE SQVVSGGHEP YQEPRAWSQV
1110 1120 1130 1140 1150
SETTSSEAGA STSQADWQQE QKTEPQAPGC GETPEDSYSE GSTADMTNTA
1160 1170 1180 1190 1200
DLLEQIPDLG EDVKDPEDCF TEGCVRRCPC CMVDTTQSPG KVWWRLRKTC
1210 1220 1230 1240 1250
YRIVEHSWFE TFIIFMILLS SGALAFEDIY LEERKTIKVL LEYADKMFTY
1260 1270 1280 1290 1300
VFVLEMLLKW VAYGFKKYFT NAWCWLDFLI VDVSLVSLVA NTLGFAEMGP
1310 1320 1330 1340 1350
IKSLRTLRAL RPLRALSRFE GMRVVVNALV GAIPSIMNVL LVCLIFWLIF
1360 1370 1380 1390 1400
SIMGVNLFAG KFGRCINQTE GDLPLNYTIV NNKSECESFN VTGELYWTKV
1410 1420 1430 1440 1450
KVNFDNVGAG YLALLQVATF KGWMDIMYAA VDSRGYEEQP QWEDNLYMYI
1460 1470 1480 1490 1500
YFVVFIIFGS FFTLNLFIGV IIDNFNQQKK KLGGQDIFMT EEQKKYYNAM
1510 1520 1530 1540 1550
KKLGSKKPQK PIPRPLNKYQ GFIFDIVTKQ AFDVTIMFLI CLNMVTMMVE
1560 1570 1580 1590 1600
TDDQSPEKVN ILAKINLLFV AIFTGECIVK MAALRHYYFT NSWNIFDFVV
1610 1620 1630 1640 1650
VILSIVGTVL SDIIQKYFFS PTLFRVIRLA RIGRILRLIR GAKGIRTLLF
1660 1670 1680 1690 1700
ALMMSLPALF NIGLLLFLVM FIYSIFGMAN FAYVKWEAGI DDMFNFQTFA
1710 1720 1730 1740 1750
NSMLCLFQIT TSAGWDGLLS PILNTGPPYC DPNLPNSNGS RGNCGSPAVG
1760 1770 1780 1790 1800
ILFFTTYIII SFLIVVNMYI AIILENFSVA TEESTEPLSE DDFDMFYEIW
1810 1820 1830 1840 1850
EKFDPEATQF IEYLALSDFA DALSEPLRIA KPNQISLINM DLPMVSGDRI
1860 1870 1880 1890 1900
HCMDILFAFT KRVLGESGEM DALKIQMEEK FMAANPSKIS YEPITTTLRR
1910 1920 1930 1940 1950
KHEEVSATVI QRAFRRHLLQ RSVKHASFLF RQQAGGSGLS DEDAPEREGL
1960 1970 1980 1990 2000
IAYMMNGNFS RRSAPLSSSS ISSTSFPPSY DSVTRATSDN LPVRASDYSR
2010
SEDLADFPPS PDRDRESIV
Length:2,019
Mass (Da):227,367
Last modified:April 1, 1990 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iCFC3B03CEAE708AD
GO
Isoform 2 (identifier: P15389-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1080-1132: Missing.

Show »
Length:1,966
Mass (Da):221,706
Checksum:iE4AC1FB7CF825647
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F1LPK3F1LPK3_RAT
Sodium channel protein
Scn5a
2,019Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0G2JWG8A0A0G2JWG8_RAT
Sodium channel protein
Scn5a
2,019Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F1LNF5F1LNF5_RAT
Sodium channel protein
Scn5a
1,966Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0374821080 – 1132Missing in isoform 2. 1 PublicationAdd BLAST53

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M27902 mRNA Translation: AAA42114.1
AF353637 mRNA Translation: AAK38884.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A33996

NCBI Reference Sequences

More...
RefSeqi
NP_001153634.1, NM_001160162.1 [P15389-2]
NP_037257.1, NM_013125.2 [P15389-1]

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
25665

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:25665

UCSC genome browser

More...
UCSCi
RGD:3637 rat [P15389-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27902 mRNA Translation: AAA42114.1
AF353637 mRNA Translation: AAK38884.1
PIRiA33996
RefSeqiNP_001153634.1, NM_001160162.1 [P15389-2]
NP_037257.1, NM_013125.2 [P15389-1]

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

BioGridi247694, 1 interactor
DIPiDIP-60063N
IntActiP15389, 2 interactors
STRINGi10116.ENSRNOP00000060180

Chemistry databases

BindingDBiP15389
ChEMBLiCHEMBL3866

DrugCentral

More...
DrugCentrali
P15389
GuidetoPHARMACOLOGYi582

PTM databases

iPTMnetiP15389
PhosphoSitePlusiP15389
SwissPalmiP15389

Proteomic databases

PaxDbiP15389
PRIDEiP15389

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25665
KEGGirno:25665
UCSCiRGD:3637 rat [P15389-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
6331
RGDi3637 Scn5a

Phylogenomic databases

eggNOGiKOG2301 Eukaryota
ENOG410XNP6 LUCA
HOGENOMiHOG000231755
InParanoidiP15389
KOiK04838
OrthoDBi172471at2759
PhylomeDBiP15389

Enzyme and pathway databases

ReactomeiR-RNO-5576892 Phase 0 - rapid depolarisation

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P15389

Family and domain databases

Gene3Di1.20.120.350, 4 hits
InterProiView protein in InterPro
IPR005821 Ion_trans_dom
IPR008053 Na_channel_a5su
IPR001696 Na_channel_asu
IPR010526 Na_trans_assoc
IPR024583 Na_trans_cytopl
IPR027359 Volt_channel_dom_sf
PfamiView protein in Pfam
PF00520 Ion_trans, 4 hits
PF06512 Na_trans_assoc, 1 hit
PF11933 Na_trans_cytopl, 1 hit
PRINTSiPR00170 NACHANNEL
PR01666 NACHANNEL5

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSCN5A_RAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P15389
Secondary accession number(s): Q925G6
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: September 18, 2019
This is version 145 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again