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Entry version 164 (18 Sep 2019)
Sequence version 1 (13 Aug 1987)
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Protein

Sodium channel protein type 2 subunit alpha

Gene

Scn2a

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

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. Implicated in the regulation of hippocampal replay occurring within sharp wave ripples (SPW-R) important for memory (By similarity).By similarity3 Publications

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>Sitei1489Important for channel closure1

<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 functionIon 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 2 subunit alpha
Alternative name(s):
Sodium channel protein brain II subunit alpha
Sodium channel protein type II subunit alpha
Voltage-gated sodium channel subunit alpha Nav1.2
<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:Scn2a
Synonyms:Scn2a1
<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
3632 Scn2a

<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 – 129CytoplasmicCuratedAdd BLAST129
<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>Transmembranei130 – 148Helical; Name=S1 of repeat IBy similarityAdd BLAST19
Topological domaini149 – 155ExtracellularCurated7
Transmembranei156 – 176Helical; Name=S2 of repeat IBy similarityAdd BLAST21
Topological domaini177 – 190CytoplasmicCuratedAdd BLAST14
Transmembranei191 – 208Helical; Name=S3 of repeat IBy similarityAdd BLAST18
Topological domaini209 – 214ExtracellularCurated6
Transmembranei215 – 231Helical; Name=S4 of repeat IBy similarityAdd BLAST17
Topological domaini232 – 250CytoplasmicCuratedAdd BLAST19
Transmembranei251 – 270Helical; Name=S5 of repeat IBy similarityAdd BLAST20
Topological domaini271 – 369ExtracellularCuratedAdd BLAST99
<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>Intramembranei370 – 394Pore-formingBy similarityAdd BLAST25
Topological domaini395 – 401ExtracellularCurated7
Transmembranei402 – 422Helical; Name=S6 of repeat IBy similarityAdd BLAST21
Topological domaini423 – 759CytoplasmicCuratedAdd BLAST337
Transmembranei760 – 778Helical; Name=S1 of repeat IIBy similarityAdd BLAST19
Topological domaini779 – 789ExtracellularCuratedAdd BLAST11
Transmembranei790 – 809Helical; Name=S2 of repeat IIBy similarityAdd BLAST20
Topological domaini810 – 823CytoplasmicCuratedAdd BLAST14
Transmembranei824 – 843Helical; Name=S3 of repeat IIBy similarityAdd BLAST20
Topological domaini844 – 845ExtracellularCurated2
Transmembranei846 – 863Helical; Name=S4 of repeat IIBy similarityAdd BLAST18
Topological domaini864 – 879CytoplasmicCuratedAdd BLAST16
Transmembranei880 – 898Helical; Name=S5 of repeat IIBy similarityAdd BLAST19
Topological domaini899 – 927ExtracellularCuratedAdd BLAST29
Intramembranei928 – 948Pore-formingBy similarityAdd BLAST21
Topological domaini949 – 961ExtracellularCuratedAdd BLAST13
Transmembranei962 – 982Helical; Name=S6 of repeat IIBy similarityAdd BLAST21
Topological domaini983 – 1209CytoplasmicCuratedAdd BLAST227
Transmembranei1210 – 1227Helical; Name=S1 of repeat IIIBy similarityAdd BLAST18
Topological domaini1228 – 1240ExtracellularCuratedAdd BLAST13
Transmembranei1241 – 1259Helical; Name=S2 of repeat IIIBy similarityAdd BLAST19
Topological domaini1260 – 1273CytoplasmicCuratedAdd BLAST14
Transmembranei1274 – 1292Helical; Name=S3 of repeat IIIBy similarityAdd BLAST19
Topological domaini1293 – 1300ExtracellularCurated8
Transmembranei1301 – 1319Helical; Name=S4 of repeat IIIBy similarityAdd BLAST19
Topological domaini1320 – 1336CytoplasmicCuratedAdd BLAST17
Transmembranei1337 – 1356Helical; Name=S5 of repeat IIIBy similarityAdd BLAST20
Topological domaini1357 – 1408ExtracellularCuratedAdd BLAST52
Intramembranei1409 – 1430Pore-formingBy similarityAdd BLAST22
Topological domaini1431 – 1447ExtracellularCuratedAdd BLAST17
Transmembranei1448 – 1469Helical; Name=S6 of repeat IIIBy similarityAdd BLAST22
Topological domaini1470 – 1532CytoplasmicCuratedAdd BLAST63
Transmembranei1533 – 1550Helical; Name=S1 of repeat IVBy similarityAdd BLAST18
Topological domaini1551 – 1561ExtracellularCuratedAdd BLAST11
Transmembranei1562 – 1580Helical; Name=S2 of repeat IVBy similarityAdd BLAST19
Topological domaini1581 – 1592CytoplasmicCuratedAdd BLAST12
Transmembranei1593 – 1610Helical; Name=S3 of repeat IVBy similarityAdd BLAST18
Topological domaini1611 – 1623ExtracellularCuratedAdd BLAST13
Transmembranei1624 – 1640Helical; Name=S4 of repeat IVBy similarityAdd BLAST17
Topological domaini1641 – 1659CytoplasmicCuratedAdd BLAST19
Transmembranei1660 – 1677Helical; Name=S5 of repeat IVBy similarityAdd BLAST18
Topological domaini1678 – 1699ExtracellularCuratedAdd BLAST22
Intramembranei1700 – 1722Pore-formingBy similarityAdd BLAST23
Topological domaini1723 – 1752ExtracellularCuratedAdd BLAST30
Transmembranei1753 – 1775Helical; Name=S6 of repeat IVBy similarityAdd BLAST23
Topological domaini1776 – 2005CytoplasmicCuratedAdd BLAST230

Keywords - Cellular componenti

Cell membrane, 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>Mutagenesisi38K → Q: Abolishes SUMOylation. No increase of voltage-gated sodium current upon hypoxia. 1 Publication1
Mutagenesisi385F → C: Sodium current is irreversibly blocked by methanethiosulfonate (MTSET); the mutated Cys residue has a free thiol susceptible to reaction with MTSET, and inhibition of current is due to the fact that the residue is close to the selectivity filter. By similarity1 Publication1
Mutagenesisi879 – 881GAL → QQQ: Slowed inactivation and increased persistent current. Gain of function mutation. 1 Publication3
Mutagenesisi910C → L: >1000-fold reduction of sensitivity to the conotoxin GVIIJ(SSG). 1 Publication1
Mutagenesisi1489F → Q: Strongly impairs channel inactivation. 1 Publication1
Mutagenesisi1506S → A: Blocks the reduction of Na+ current and the slowing of inactivation caused by PKC. 1 Publication1
Mutagenesisi1613E → D: Increase in sensitivity to the scorpion toxin BMK M1. 1 Publication1
Mutagenesisi1975Y → A: Abolishes interaction with NEDD4L. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3399

DrugCentral

More...
DrugCentrali
P04775

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
579

<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_00000484921 – 2005Sodium channel protein type 2 subunit alphaAdd BLAST2005

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 residuei4Phosphoserine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki38Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication
<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>Glycosylationi212N-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 bondi278 ↔ 347By similarity
Glycosylationi285N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi291N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi297N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi303N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi308N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi340N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei468Phosphoserine1 Publication1
Modified residuei471Phosphoserine1 Publication1
Modified residuei484PhosphoserineCombined sources1 Publication1
Modified residuei526PhosphoserineCombined sources1
Modified residuei528PhosphoserineCombined sources1 Publication1
Modified residuei531PhosphoserineCombined sources1
Modified residuei553PhosphoserineCombined sources1
Modified residuei554PhosphoserineCombined sources2 Publications1
Modified residuei554Phosphoserine; by PKC; in vitroCombined sources2 Publications1
Modified residuei558PhosphoserineCombined sources1
Modified residuei573Phosphoserine; by PKC; in vitro1 Publication1
Modified residuei576Phosphoserine; by PKC; in vitro1 Publication1
Modified residuei589PhosphoserineCombined sources1
Modified residuei610Phosphoserine1 Publication1
Modified residuei623Phosphoserine1 Publication1
Modified residuei687Phosphoserine1 Publication1
Modified residuei688Phosphoserine1 Publication1
Modified residuei721PhosphoserineCombined sources1 Publication1
Disulfide bondi910Interchain; with SCN2B or SCN4B1 Publication
Disulfide bondi910Interchain; with the conotoxin GVIIJ (when the channel is not linked to SCN2B or SCN4B; the bond to SCN2B or SCN4B protects the channel from the inhibition by toxin)1 Publication
Disulfide bondi950 ↔ 959By similarity
Glycosylationi1368N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1382N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1393N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei1506Phosphoserine; by PKC2 Publications1
Modified residuei1930Phosphoserine1 Publication1
Modified residuei1943PhosphothreonineCombined sources1
Modified residuei1963PhosphothreonineCombined sources1
Modified residuei1966Phosphothreonine1 Publication1
Modified residuei1971Phosphoserine1 Publication1

<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

May be ubiquitinated by NEDD4L; which would promote its endocytosis.
Phosphorylation at Ser-1506 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents.3 Publications
Sumoylated at Lys-38. Sumoylation is induced by hypoxia, increases voltage-gated sodium current and mediates the early response to acute hypoxia in neurons (PubMed:28029095). Sumoylated SCN2A is located at the cell membrane (PubMed:28029095).1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...
PaxDbi
P04775

PRoteomics IDEntifications database

More...
PRIDEi
P04775

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P04775

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

More...
PhosphoSitePlusi
P04775

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P04775

<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

Expressed in brain (at protein level) (PubMed:10827969). Expressed in cerebellar granule neurons (at protein level) (PubMed:28029095).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

Heterooligomer of a large alpha subunit and a smaller beta subunit. Heterooligomer with SCN2B or SCN4B; disulfide-linked.

Interacts with NEDD4L.

Interacts with CALM.

Interacts with the conotoxin GVIIJ (PubMed:24497506).

Interacts with the scorpion toxin BMK M1 (PubMed:20678086).

4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
246890, 4 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P04775

Database of interacting proteins

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DIPi
DIP-57088N

Protein interaction database and analysis system

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IntActi
P04775, 2 interactors

STRING: functional protein association networks

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STRINGi
10116.ENSRNOP00000007069

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P04775

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

12005
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P04775

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P04775

<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>Repeati111 – 456ICuratedAdd BLAST346
Repeati741 – 1013IICuratedAdd BLAST273
Repeati1190 – 1504IIICuratedAdd BLAST315
Repeati1513 – 1811IVCuratedAdd BLAST299
<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>Domaini1905 – 1934IQPROSITE-ProRule annotationAdd BLAST30

<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

<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

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eggNOGi
KOG2301 Eukaryota
ENOG410XNP6 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000231755

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P04775

KEGG Orthology (KO)

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KOi
K04834

Database of Orthologous Groups

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OrthoDBi
56920at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P04775

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.20.120.350, 4 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR005821 Ion_trans_dom
IPR000048 IQ_motif_EF-hand-BS
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

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PRINTSi
PR00170 NACHANNEL

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00015 IQ, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50096 IQ, 1 hit

<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>Sequence (1+)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 has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P04775-1 [UniParc]FASTAAdd to basket
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        10         20         30         40         50
MARSVLVPPG PDSFRFFTRE SLAAIEQRIA EEKAKRPKQE RKDEDDENGP
60 70 80 90 100
KPNSDLEAGK SLPFIYGDIP PEMVSEPLED LDPYYINKKT FIVLNKGKAI
110 120 130 140 150
SRFSATSALY ILTPFNPIRK LAIKILVHSL FNVLIMCTIL TNCVFMTMSN
160 170 180 190 200
PPDWTKNVEY TFTGIYTFES LIKILARGFC LEDFTFLRNP WNWLDFTVIT
210 220 230 240 250
FAYVTEFVNL GNVSALRTFR VLRALKTISV IPGLKTIVGA LIQSVKKLSD
260 270 280 290 300
VMILTVFCLS VFALIGLQLF MGNLRNKCLQ WPPDNSTFEI NITSFFNNSL
310 320 330 340 350
DWNGTAFNRT VNMFNWDEYI EDKSHFYFLE GQNDALLCGN SSDAGQCPEG
360 370 380 390 400
YICVKAGRNP NYGYTSFDTF SWAFLSLFRL MTQDFWENLY QLTLRAAGKT
410 420 430 440 450
YMIFFVLVIF LGSFYLINLI LAVVAMAYEE QNQATLEEAE QKEAEFQQML
460 470 480 490 500
EQLKKQQEEA QAAAAAASAE SRDFSGAGGI GVFSESSSVA SKLSSKSEKE
510 520 530 540 550
LKNRRKKKKQ KEQAGEEEKE DAVRKSASED SIRKKGFQFS LEGSRLTYEK
560 570 580 590 600
RFSSPHQSLL SIRGSLFSPR RNSRASLFNF KGRVKDIGSE NDFADDEHST
610 620 630 640 650
FEDNDSRRDS LFVPHRHGER RPSNVSQASR ASRGIPTLPM NGKMHSAVDC
660 670 680 690 700
NGVVSLVGGP SALTSPVGQL LPEGTTTETE IRKRRSSSYH VSMDLLEDPS
710 720 730 740 750
RQRAMSMASI LTNTMEELEE SRQKCPPCWY KFANMCLIWD CCKPWLKVKH
760 770 780 790 800
VVNLVVMDPF VDLAITICIV LNTLFMAMEH YPMTEQFSSV LSVGNLVFTG
810 820 830 840 850
IFTAEMFLKI IAMDPYYYFQ EGWNIFDGFI VSLSLMELGL ANVEGLSVLR
860 870 880 890 900
SFRLLRVFKL AKSWPTLNML IKIIGNSVGA LGNLTLVLAI IVFIFAVVGM
910 920 930 940 950
QLFGKSYKEC VCKISNDCEL PRWHMHHFFH SFLIVFRVLC GEWIETMWDC
960 970 980 990 1000
MEVAGQTMCL TVFMMVMVIG NLVVLNLFLA LLLSSFSSDN LAATDDDNEM
1010 1020 1030 1040 1050
NNLQIAVGRM QKGIDFVKRK IREFIQKAFV RKQKALDEIK PLEDLNNKKD
1060 1070 1080 1090 1100
SCISNHTTIE IGKDLNYLKD GNGTTSGIGS SVEKYVVDES DYMSFINNPS
1110 1120 1130 1140 1150
LTVTVPIALG ESDFENLNTE EFSSESDMEE SKEKLNATSS SEGSTVDIGA
1160 1170 1180 1190 1200
PAEGEQPEAE PEESLEPEAC FTEDCVRKFK CCQISIEEGK GKLWWNLRKT
1210 1220 1230 1240 1250
CYKIVEHNWF ETFIVFMILL SSGALAFEDI YIEQRKTIKT MLEYADKVFT
1260 1270 1280 1290 1300
YIFILEMLLK WVAYGFQMYF TNAWCWLDFL IVDVSLVSLT ANALGYSELG
1310 1320 1330 1340 1350
AIKSLRTLRA LRPLRALSRF EGMRVVVNAL LGAIPSIMNV LLVCLIFWLI
1360 1370 1380 1390 1400
FSIMGVNLFA GKFYHCINYT TGEMFDVSVV NNYSECQALI ESNQTARWKN
1410 1420 1430 1440 1450
VKVNFDNVGL GYLSLLQVAT FKGWMDIMYA AVDSRNVELQ PKYEDNLYMY
1460 1470 1480 1490 1500
LYFVIFIIFG SFFTLNLFIG VIIDNFNQQK KKFGGQDIFM TEEQKKYYNA
1510 1520 1530 1540 1550
MKKLGSKKPQ KPIPRPANKF QGMVFDFVTK QVFDISIMIL ICLNMVTMMV
1560 1570 1580 1590 1600
ETDDQSQEMT NILYWINLVF IVLFTGECVL KLISLRHYYF TIGWNIFDFV
1610 1620 1630 1640 1650
VVILSIVGMF LAELIEKYFV SPTLFRVIRL ARIGRILRLI KGAKGIRTLL
1660 1670 1680 1690 1700
FALMMSLPAL FNIGLLLFLV MFIYAIFGMS NFAYVKREVG IDDMFNFETF
1710 1720 1730 1740 1750
GNSMICLFQI TTSAGWDGLL APILNSGPPD CDPEKDHPGS SVKGDCGNPS
1760 1770 1780 1790 1800
VGIFFFVSYI IISFLVVVNM YIAVILENFS VATEESAEPL SEDDFEMFYE
1810 1820 1830 1840 1850
VWEKFDPDAT QFIEFCKLSD FAAALDPPLL IAKPNKVQLI AMDLPMVSGD
1860 1870 1880 1890 1900
RIHCLDILFA FTKRVLGESG EMDALRIQME ERFMASNPSK VSYEPITTTL
1910 1920 1930 1940 1950
KRKQEEVSAI VIQRAYRRYL LKQKVKKVSS IYKKDKGKED EGTPIKEDII
1960 1970 1980 1990 2000
TDKLNENSTP EKTDVTPSTT SPPSYDSVTK PEKEKFEKDK SEKEDKGKDI

RESKK
Length:2,005
Mass (Da):227,874
Last modified:August 13, 1987 - 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:i861BE583D79F8324
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F1M9G9F1M9G9_RAT
Sodium channel protein
Scn2a Scn2a1
1,944Annotation score:

Annotation score:3 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>
A0A0G2K207A0A0G2K207_RAT
Sodium channel protein
Scn2a
1,860Annotation 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>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X03639 mRNA Translation: CAA27287.1

NCBI Reference Sequences

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RefSeqi
NP_036779.1, NM_012647.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
24766

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:24766

UCSC genome browser

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UCSCi
RGD:3632 rat

<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
X03639 mRNA Translation: CAA27287.1
RefSeqiNP_036779.1, NM_012647.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BYYNMR-A1474-1526[»]
2KXWNMR-B1901-1927[»]
2M5ENMR-B1901-1927[»]
SMRiP04775
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi246890, 4 interactors
CORUMiP04775
DIPiDIP-57088N
IntActiP04775, 2 interactors
STRINGi10116.ENSRNOP00000007069

Chemistry databases

BindingDBiP04775
ChEMBLiCHEMBL3399
DrugCentraliP04775
GuidetoPHARMACOLOGYi579

PTM databases

iPTMnetiP04775
PhosphoSitePlusiP04775
SwissPalmiP04775

Proteomic databases

PaxDbiP04775
PRIDEiP04775

Genome annotation databases

GeneIDi24766
KEGGirno:24766
UCSCiRGD:3632 rat

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
6326
RGDi3632 Scn2a

Phylogenomic databases

eggNOGiKOG2301 Eukaryota
ENOG410XNP6 LUCA
HOGENOMiHOG000231755
InParanoidiP04775
KOiK04834
OrthoDBi56920at2759
PhylomeDBiP04775

Enzyme and pathway databases

ReactomeiR-RNO-5576892 Phase 0 - rapid depolarisation

Miscellaneous databases

EvolutionaryTraceiP04775

Protein Ontology

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PROi
PR:P04775

Family and domain databases

Gene3Di1.20.120.350, 4 hits
InterProiView protein in InterPro
IPR005821 Ion_trans_dom
IPR000048 IQ_motif_EF-hand-BS
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
SMARTiView protein in SMART
SM00015 IQ, 1 hit
PROSITEiView protein in PROSITE
PS50096 IQ, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiSCN2A_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: P04775
<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: August 13, 1987
Last sequence update: August 13, 1987
Last modified: September 18, 2019
This is version 164 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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