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Entry version 161 (16 Jan 2019)
Sequence version 1 (01 Aug 1988)
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Protein

Sodium channel protein type 3 subunit alpha

Gene

Scn3a

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, forms a sodium-selective channel through which Na+ ions may pass in accordance with their electrochemical gradient (By similarity). May contribute to the regulation of serotonin/5-hydroxytryptamine release by enterochromaffin cells (By similarity). In pancreatic endocrine cells, required for both glucagon and glucose-induced insulin secretion (By similarity).By similarity

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>Sitei1503Important residue that permits the spider RTX-VII toxin to inhibit fast inactivation of the channel1 Publication1
Sitei1506Important residue that permits the spider RTX-VII toxin to inhibit fast inactivation of the channel1 Publication1
Sitei1507Important residue that permits the spider RTX-VII toxin to inhibit fast inactivation of the channel1 Publication1
Sitei1510Key residue that permits the spider beta/delta-theraphotoxin-Pre1a to inhibit fast inactivation of the channel1 Publication1
Sitei1562Important residue that permits the spider RTX-VII toxin to inhibit fast inactivation of the channel1 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 functionIon channel, Sodium channel, Voltage-gated channel
Biological processIon transport, Sodium transport, Transport
LigandSodium

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.A.1.10.1 the voltage-gated ion channel (vic) superfamily

<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 3 subunit alpha
Alternative name(s):
Sodium channel protein brain III subunit alpha
Sodium channel protein type III subunit alpha
Voltage-gated sodium channel subtype III
Voltage-gated sodium channel subunit alpha Nav1.3
<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:Scn3a
<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
3635 Scn3a

<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 – 128CytoplasmicCuratedAdd BLAST128
<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>Transmembranei129 – 147Helical; Name=S1 of repeat IBy similarityAdd BLAST19
Topological domaini148 – 154ExtracellularCurated7
Transmembranei155 – 175Helical; Name=S2 of repeat IBy similarityAdd BLAST21
Topological domaini176 – 189CytoplasmicCuratedAdd BLAST14
Transmembranei190 – 207Helical; Name=S3 of repeat IBy similarityAdd BLAST18
Topological domaini208 – 213ExtracellularCurated6
Transmembranei214 – 230Helical; Name=S4 of repeat IBy similarityAdd BLAST17
Topological domaini231 – 249CytoplasmicCuratedAdd BLAST19
Transmembranei250 – 269Helical; Name=S5 of repeat IBy similarityAdd BLAST20
Topological domaini270 – 368ExtracellularCuratedAdd 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>Intramembranei369 – 393Pore-formingBy similarityAdd BLAST25
Topological domaini394 – 400ExtracellularCurated7
Transmembranei401 – 421Helical; Name=S6 of repeat IBy similarityAdd BLAST21
Topological domaini422 – 711CytoplasmicCuratedAdd BLAST290
Transmembranei712 – 730Helical; Name=S1 of repeat IIBy similarityAdd BLAST19
Topological domaini731 – 741ExtracellularCuratedAdd BLAST11
Transmembranei742 – 761Helical; Name=S2 of repeat IIBy similarityAdd BLAST20
Topological domaini762 – 775CytoplasmicCuratedAdd BLAST14
Transmembranei776 – 795Helical; Name=S3 of repeat IIBy similarityAdd BLAST20
Topological domaini796 – 797ExtracellularCurated2
Transmembranei798 – 815Helical; Name=S4 of repeat IIBy similarityAdd BLAST18
Topological domaini816 – 831CytoplasmicCuratedAdd BLAST16
Transmembranei832 – 850Helical; Name=S5 of repeat IIBy similarityAdd BLAST19
Topological domaini851 – 879ExtracellularCuratedAdd BLAST29
Intramembranei880 – 900Pore-formingBy similarityAdd BLAST21
Topological domaini901 – 913ExtracellularCuratedAdd BLAST13
Transmembranei914 – 934Helical; Name=S6 of repeat IIBy similarityAdd BLAST21
Topological domaini935 – 1158CytoplasmicCuratedAdd BLAST224
Transmembranei1159 – 1176Helical; Name=S1 of repeat IIIBy similarityAdd BLAST18
Topological domaini1177 – 1189ExtracellularCuratedAdd BLAST13
Transmembranei1190 – 1208Helical; Name=S2 of repeat IIIBy similarityAdd BLAST19
Topological domaini1209 – 1222CytoplasmicCuratedAdd BLAST14
Transmembranei1223 – 1241Helical; Name=S3 of repeat IIIBy similarityAdd BLAST19
Topological domaini1242 – 1249ExtracellularCurated8
Transmembranei1250 – 1268Helical; Name=S4 of repeat IIIBy similarityAdd BLAST19
Topological domaini1269 – 1285CytoplasmicCuratedAdd BLAST17
Transmembranei1286 – 1305Helical; Name=S5 of repeat IIIBy similarityAdd BLAST20
Topological domaini1306 – 1354ExtracellularCuratedAdd BLAST49
Intramembranei1355 – 1376Pore-formingBy similarityAdd BLAST22
Topological domaini1377 – 1393ExtracellularCuratedAdd BLAST17
Transmembranei1394 – 1415Helical; Name=S6 of repeat IIIBy similarityAdd BLAST22
Topological domaini1416 – 1478CytoplasmicCuratedAdd BLAST63
Transmembranei1479 – 1496Helical; Name=S1 of repeat IVBy similarityAdd BLAST18
Topological domaini1497 – 1507ExtracellularCuratedAdd BLAST11
Transmembranei1508 – 1526Helical; Name=S2 of repeat IVBy similarityAdd BLAST19
Topological domaini1527 – 1538CytoplasmicCuratedAdd BLAST12
Transmembranei1539 – 1556Helical; Name=S3 of repeat IVBy similarityAdd BLAST18
Topological domaini1557 – 1569ExtracellularCuratedAdd BLAST13
Transmembranei1570 – 1586Helical; Name=S4 of repeat IVBy similarityAdd BLAST17
Topological domaini1587 – 1605CytoplasmicCuratedAdd BLAST19
Transmembranei1606 – 1623Helical; Name=S5 of repeat IVBy similarityAdd BLAST18
Topological domaini1624 – 1645ExtracellularCuratedAdd BLAST22
Intramembranei1646 – 1668Pore-formingBy similarityAdd BLAST23
Topological domaini1669 – 1698ExtracellularCuratedAdd BLAST30
Transmembranei1699 – 1721Helical; Name=S6 of repeat IVBy similarityAdd BLAST23
Topological domaini1722 – 1951CytoplasmicCuratedAdd 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>Mutagenesisi1503K → P: 6-fold decrease in activity of the spider RTX-VII toxin. 1 Publication1
Mutagenesisi1504Y → E: 2-fold decrease in activity of the spider RTX-VII toxin. 1 Publication1
Mutagenesisi1505M → K: 4.5-fold decrease in activity of the spider RTX-VII toxin. 1 Publication1
Mutagenesisi1506T → I: 10-fold decrease in activity of the spider RTX-VII toxin. 1 Publication1
Mutagenesisi1507L → N: 12-fold decrease in activity of the spider RTX-VII toxin. 1 Publication1
Mutagenesisi1562E → Q: 5.5-fold decrease in activity of the spider RTX-VII toxin. 1 Publication1
Mutagenesisi1562E → R: 20-fold decrease in activity of the spider RTX-VII toxin. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4966

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
580

<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_00000484941 – 1951Sodium channel protein type 3 subunit alphaAdd BLAST1951

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Glycosylationi211N-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 bondi277 ↔ 346By similarity
Glycosylationi290N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi296N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi302N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi307N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi339N-linked (GlcNAc...) asparagineSequence analysis1
<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 residuei484PhosphoserineCombined sources1
Modified residuei485PhosphoserineCombined sources1
Modified residuei486PhosphoserineCombined sources1
Disulfide bondi862Interchain; with SCN2B or SCN4BBy similarity
Disulfide bondi862Interchain; 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)By similarity
Disulfide bondi902 ↔ 911By similarity
Glycosylationi1317N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1331N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei1452Phosphoserine; 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

May be ubiquitinated by NEDD4L; which would promote its endocytosis.By similarity
Phosphorylation at Ser-1452 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...
PaxDbi
P08104

PRoteomics IDEntifications database

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PRIDEi
P08104

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P08104

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

More...
PhosphoSitePlusi
P08104

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P08104

<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 2-3 smaller beta subunits. Heterooligomer with SCN2B or SCN4B; disulfide-linked. Interacts with NEDD4L (By similarity). Interacts with the conotoxin GVIIJ (PubMed:24497506). Interacts with the spider beta/delta-theraphotoxin-Pre1a (PubMed:25784299, PubMed:28428547). Interacts with the spider RTX-VII toxin (AC P0DL75) (PubMed:25784299).By similarity3 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
269080, 2 interactors

STRING: functional protein association networks

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STRINGi
10116.ENSRNOP00000006646

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P08104

<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

11951
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1QG9NMR-A156-176[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P08104

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

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SMRi
P08104

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P08104

<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>Repeati110 – 455ICuratedAdd BLAST346
Repeati693 – 965IICuratedAdd BLAST273
Repeati1139 – 1450IIICuratedAdd BLAST312
Repeati1459 – 1757IVCuratedAdd 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>Domaini1851 – 1880IQAdd 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 HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG053100

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P08104

KEGG Orthology (KO)

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KOi
K04836

Database of Orthologous Groups

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OrthoDBi
56920at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P08104

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
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

<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>.<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 1 potential isoform that is computationally mapped.Show allAlign All

P08104-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAQALLVPPG PESFRLFTRE SLAAIEKRAA EEKAKKPKKE QDIDDENKPK
60 70 80 90 100
PNSDLEAGKN LPFIYGDIPP EMVSEPLEDL DPYYVSKKTF VVLNKGKAIF
110 120 130 140 150
RFSATSALYI LTPLNPVRKI AIKILVHSLF SMLIMCTILT NCVFMTLSNP
160 170 180 190 200
PDWTKNVEYT FTGIYTFESL IKILARGFCL EDFTFLRDPW NWLDFSVIVM
210 220 230 240 250
AYVTEFVDLG NVSALRTFRV LRALKTISVI PGLKTIVGAL IQSVKKLSDV
260 270 280 290 300
MILTVFCLSV FALIGLQLFM GNLRNKCSQW PPSDSAFETN TTSYFNGTMD
310 320 330 340 350
SNGTFVNVTM STFNWKDYIA DDSHFYVLDG QKDPLLCGNG SDAGQCPEGY
360 370 380 390 400
ICVKAGRNPN YGYTSFDTFS WAFLSLFRLM TQDYWENLYQ LTLRAAGKTY
410 420 430 440 450
MIFFVLVIFL GSFYLVNLIL AVVAMAYEEQ NQATLEEAEQ KEAEFQQMLE
460 470 480 490 500
QLKKQQEEAQ AVAAASAASR DFSGIGGLGE LLESSSEASK LSSKSAKEWR
510 520 530 540 550
NRRKKRRQRE HLEGNHRADG DRFPKSESED SVKRRSFLLS LDGNPLTGDK
560 570 580 590 600
KLCSPHQSLL SIRGSLFSPR RNSKTSIFSF RGRAKDVGSE NDFADDEHST
610 620 630 640 650
FEDSESRRDS LFVPHRPGER RNSNGTTTET EVRKRRLSSY QISMEMLEDS
660 670 680 690 700
SGRQRSMSIA SILTNTMEEL EESRQKCPPC WYRFANVFLI WDCCDAWLKV
710 720 730 740 750
KHLVNLIVMD PFVDLAITIC IVLNTLFMAM EHYPMTQQFS SVLTVGNLVF
760 770 780 790 800
TGIFTAEMVL KIIAMDPYYY FQEGWNIFDG IIVSLSLMEL GLANVEGLSV
810 820 830 840 850
LRSFRLLRVF KLAKSWPTLN MLIKIIGNSV GALGNLTLVL AIIVFIFAVV
860 870 880 890 900
GMQLFGKSYK ECVCKINVDC KLPRWHMNDF FHSFLIVFRV LCGEWIETMW
910 920 930 940 950
DCMEVAGQTM CLIVFMLVMV IGNLVVLNLF LALLLSSFSS DNLAATDDDN
960 970 980 990 1000
EMNNLQIAVG RMQKGIDFVK NKIRECFRKA FFRKPKVIEI QEGNKIDSCM
1010 1020 1030 1040 1050
SNNTGIEISK ELNYLKDGNG TTSGVGTGSS VEKYVIDEND YMSFINNPSL
1060 1070 1080 1090 1100
TVTVPIAVGE SDFENLNTEE FSSESELEES KEKLNATSSS EGSTVDVAPP
1110 1120 1130 1140 1150
REGEQAEIEP EEDLKPEACF TEGCIKKFPF CQVSTEEGKG KIWWNLRKTC
1160 1170 1180 1190 1200
YSIVEHNWFE TFIVFMILLS SGALAFEDIY IEQRKTIKTM LEYADKVFTY
1210 1220 1230 1240 1250
IFILEMLLKW VAYGFQTYFT NAWCWLDFLI VDVSLVSLVA NALGYSELGA
1260 1270 1280 1290 1300
IKSLRTLRAL RPLRALSRFE GMRVVVNALV GAIPSIMNVL LVCLIFWLIF
1310 1320 1330 1340 1350
SIMGVNLFAG KFYHCVNTTT GNMFEIKEVN NFSDCQALGK QARWKNVKVN
1360 1370 1380 1390 1400
FDNVGAGYLA LLQVATFKGW MDIMYAAVDS RDVKLQPIYE ENLYMYLYFV
1410 1420 1430 1440 1450
IFIIFGSFFT LNLFIGVIID NFNQQKKKFG GQDIFMTEEQ KKYYNAMKKL
1460 1470 1480 1490 1500
GSKKPQKPIP RPANKFQGMV FDFVTRQVFD ISIMILICLN MVTMMVETDD
1510 1520 1530 1540 1550
QSKYMTLVLS RINLVFIVLF TGEFLLKLIS LRYYYFTIGW NIFDFVVVIL
1560 1570 1580 1590 1600
SIVGMFLAEL IEKYFVSPTL FRVIRLARIG RILRLIKGAK GIRTLLFALM
1610 1620 1630 1640 1650
MSLPALFNIG LLLFLVMFIY AIFGMSNFAY VKKEAGIDDM FNFETFGNSM
1660 1670 1680 1690 1700
ICLFQITTSA GWDGLLAPIL NSAPPDCDPD AIHPGSSVKG DCGNPSVGIF
1710 1720 1730 1740 1750
FFVSYIIISF LVVVNMYIAV ILENFSVATE ESAEPLSEDD FEMFYEVWEK
1760 1770 1780 1790 1800
FDPDATQFIE FCKLSDFAAA LDPPLLIAKP NKVQLIAMDL PMVSGDRIHC
1810 1820 1830 1840 1850
LDILFAFTKR VLGESGEMDA LRIQMEDRFM ASNPSKVSYE PITTTLKRKQ
1860 1870 1880 1890 1900
EEVSAAIIQR NYRCYLLKQR LKNISSKYDK ETIKGRIDLP IKGDMVIDKL
1910 1920 1930 1940 1950
NGNSTPEKTD GSSSTTSPPS YDSVTKPDKE KFEKDKPEKE IKGKEVRENQ

K
Length:1,951
Mass (Da):221,387
Last modified:August 1, 1988 - 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:i74E5E851524BD10E
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F1LX08F1LX08_RAT
Sodium channel protein
Scn3a
1,951Annotation 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

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Y00766 mRNA Translation: CAA68735.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S00320

NCBI Reference Sequences

More...
RefSeqi
NP_037251.1, NM_013119.1

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Rn.87394

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
497770

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:497770

<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
Y00766 mRNA Translation: CAA68735.1
PIRiS00320
RefSeqiNP_037251.1, NM_013119.1
UniGeneiRn.87394

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QG9NMR-A156-176[»]
ProteinModelPortaliP08104
SMRiP08104
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi269080, 2 interactors
STRINGi10116.ENSRNOP00000006646

Chemistry databases

BindingDBiP08104
ChEMBLiCHEMBL4966
GuidetoPHARMACOLOGYi580

Protein family/group databases

TCDBi1.A.1.10.1 the voltage-gated ion channel (vic) superfamily

PTM databases

iPTMnetiP08104
PhosphoSitePlusiP08104
SwissPalmiP08104

Proteomic databases

PaxDbiP08104
PRIDEiP08104

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi497770
KEGGirno:497770

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
6328
RGDi3635 Scn3a

Phylogenomic databases

eggNOGiKOG2301 Eukaryota
ENOG410XNP6 LUCA
HOVERGENiHBG053100
InParanoidiP08104
KOiK04836
OrthoDBi56920at2759
PhylomeDBiP08104

Miscellaneous databases

EvolutionaryTraceiP08104

Protein Ontology

More...
PROi
PR:P08104

Family and domain databases

Gene3Di1.20.120.350, 4 hits
InterProiView protein in InterPro
IPR005821 Ion_trans_dom
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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiSCN3A_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: P08104
<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 1, 1988
Last sequence update: August 1, 1988
Last modified: January 16, 2019
This is version 161 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. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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