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Protein

Acid-sensing ion channel 1

Gene

Asic1

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

Proton-gated sodium channel; it is activated by a drop of the extracellular pH and then becomes rapidly desensitized. Generates a biphasic current with a fast inactivating and a slow sustained phase. Has high selectivity for sodium ions and can also transport lithium ions with high efficiency. Can also transport potassium ions, but with lower efficiency. It is nearly impermeable to the larger rubidium and cesium ions. Isoform 3 discrimates stronger than isoform 1 between monovalent cations. Isoform 3 can flux Ca2+ while isoform 1 cannot. Heteromeric channels composed of isoform 2 and isoform 3 are active but have a lower pH-sensitivity. Mediates glutamate-independent Ca2+ entry into neurons upon acidosis. This Ca2+ overloading is toxic for cortical neurons and may be in part responsible for ischemic brain injury. Heteromeric channel assembly seems to modulate channel properties.7 Publications

Miscellaneous

Potentiated by Ca2+, Mg2+, Ba2+, multivalent cations and potentiated by FMRFamide-related neuropeptides. pH dependence may be regulated by serine proteases. Inhibited by anti-inflammatory drugs like salicylic acid. Isoform 1 homomultimeric channel is specifically and reversibly inhibited by psalmotoxin-1, a spider venom toxin, while isoform 2 and other ASICs are insensitive.

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by the diuretic amiloride.1 Publication

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>Sitei71Important for channel gatingBy similarity1
Sitei79Important for channel desensitizingBy similarity1
Sitei175Important residue in interaction with the spider venom Pi-theraphotoxin-Hm3a, which can explain functional difference between ASIC1a and ASIC1b1 Publication1
Sitei177Important residue for interaction with the spider venom Pi-theraphotoxin-Hm3a, which can explain functional difference between ASIC1a and ASIC1b1 Publication1
Sitei287Important for channel gatingBy similarity1
Sitei349Important for interaction with the snake venom mambalgin-21 Publication1
Sitei350Important for interaction with the snake venom mambalgin-1 and mambalgin-2 toxins, probably binds to its residue L-53; Important for interaction with the spider venom Pi-hexatoxin-Hi1a and psalmotoxin-15 Publications1

<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

  • acid-sensing ion channel activity Source: UniProtKB
  • ion channel activity Source: RGD

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
Biological processCalcium transport, Ion transport, Sodium transport, Transport
LigandCalcium, Sodium

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-2672351 Stimuli-sensing channels

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.A.6.1.2 the epithelial na(+) channel (enac) family

<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:
Acid-sensing ion channel 11 Publication
Short name:
ASIC11 Publication
Alternative name(s):
Amiloride-sensitive cation channel 2, neuronal
Brain sodium channel 2
Short name:
BNaC2
<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:Asic1
Synonyms:Accn2, Bnac2
<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: Chromosome 7

Organism-specific databases

Rat genome database

More...
RGDi
71062 Asic1

<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; 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 – 45CytoplasmicBy similarityAdd BLAST45
<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>Transmembranei46 – 69HelicalBy similarityAdd BLAST24
Topological domaini70 – 425ExtracellularBy similarityAdd BLAST356
Transmembranei426 – 452Discontinuously helicalBy similarityAdd BLAST27
Topological domaini453 – 526CytoplasmicBy similarityAdd BLAST74

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>Mutagenesisi83S → P: No effect. Increases desensitization rates; when associated with L-84 and M-85. 1 Publication1
Mutagenesisi84Q → L: No effect. Increases desensitization rates; when associated with P-83 and M-85. 1 Publication1
Mutagenesisi85L → M: No effect. Increases desensitization rates; when associated with P-83 and L-84. 1 Publication1
Mutagenesisi100F → L: No effect on channel activation and inactivation. 1 Publication1
Mutagenesisi103V → L: No effect on channel activation and inactivation. 1 Publication1
Mutagenesisi105K → Y: Activated and inactivated at lower pH. 1 Publication1
Mutagenesisi106N → P: Activated and inactivated at lower pH. 1 Publication1
Mutagenesisi128 – 131QMAD → HLVE: No effect on desensitization rates. 1 Publication4
Mutagenesisi173H → S: No significant decrease in inhibition by the spider pi-theraphotoxin-Hm3a. 1 Publication1
Mutagenesisi174F → Y: No significant decrease in inhibition by the spider pi-theraphotoxin-Hm3a. 1 Publication1
Mutagenesisi175R → C: 18-fold decrease in inhibition by the spider pi-theraphotoxin-Hm3a. 1 Publication1
Mutagenesisi177E → G: 10-fold decrease in inhibition by the spider pi-theraphotoxin-Hm3a. 1 Publication1
Mutagenesisi178A → P: No significant decrease in inhibition by the spider pi-theraphotoxin-Hm3a. 1 Publication1
Mutagenesisi178A → V: No significant decrease in inhibition by the spider pi-theraphotoxin-Hm3a. 1 Publication1
Mutagenesisi190R → K: Small decrease in inhibition by the snake mambalgin-2 toxin; RDQ-KQE mutant. 1 Publication1
Mutagenesisi235E → A: No change in the shift of pH for both activation and desensitization by the spider venom psalmotoxin-1. 1 Publication1
Mutagenesisi259 – 260DQ → QE: Small decrease in inhibition by the snake mambalgin-2 toxin; RDQ-KQE mutant. 1 Publication2
Mutagenesisi316Y → A: No change in the shift of pH for both activation and desensitization by the spider venom psalmotoxin-1. 1 Publication1
Mutagenesisi349 – 350DF → GL: Complete loss in inhibition by 200 nM of the snake mambalgin-2 toxin. 1 Publication2
Mutagenesisi349D → G: High decrease in inhibition by the snake mambalgin-2 toxin. 1 Publication1
Mutagenesisi350F → A: Complete loss of inhibition by the spider Pi-hexatoxin-Hi1a, and by the snake mambalgin-2 toxin. Potentiated by the spider pi-theraphotoxin-Hm3a (at both pH 7.35 and 7.45) and inhibited at higher toxin concentration at pH 7.35. Complete loss in the shift of pH for both activation and desensitization by the spider venom psalmotoxin-1. 4 Publications1
Mutagenesisi350F → L: 37-fold decrease in inbibition by the snake mambalgin-1 toxin. Very high decrease in inhibition by the snake mambalgin-2 toxin. 2 Publications1
Mutagenesisi352V → A: Moderate decrease in inhibition by the snake mambalgin-2 toxin. 1 Publication1
Mutagenesisi354K → A: No change in the shift of pH for both activation and desensitization by the spider venom psalmotoxin-1. 1 Publication1
Mutagenesisi356Q → S: Moderate decrease in inhibition by the snake mambalgin-2 toxin. 1 Publication1
Mutagenesisi357E → N: Moderate decrease in inhibition by the snake mambalgin-2 toxin. 1 Publication1
Mutagenesisi425E → G: Reduction of Ca(2+) block. Loss of Ca(2+) block; when associated with C-432. 1 Publication1
Mutagenesisi431G → V or F: Constitutive channel activity. 1 Publication1
Mutagenesisi432D → A: Reduction of Ca(2+) block. 1 Publication1
Mutagenesisi432D → C: Reduction of Ca(2+) block. Loss of Ca(2+) block; when associated with G-425. 1 Publication1
Mutagenesisi436Q → N: No effect on Ca(2+) block. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3562170

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
684

<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_00001813001 – 526Acid-sensing ion channel 1Add BLAST526

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bondi93 ↔ 194By similarity
Disulfide bondi172 ↔ 179By similarity
Disulfide bondi290 ↔ 365By similarity
Disulfide bondi308 ↔ 361By similarity
Disulfide bondi312 ↔ 359By similarity
Disulfide bondi321 ↔ 343By similarity
Disulfide bondi323 ↔ 335By similarity
<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>Glycosylationi366N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi393N-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 residuei477PhosphoserineBy similarity1
Modified residuei497PhosphoserineBy 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 by PKA regulates interaction with PRKCABP and subcellular location. Phosphorylation by PKC may regulate the channel (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

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PRIDEi
P55926

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P55926

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

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PhosphoSitePlusi
P55926

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P55926

<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 dorsal root ganglia and sciatic nerve (at protein level). Widely distributed throughout the brain. Expressed in olfactory bulb, neo and allocortical regions, dentate granule cells, pyramidal cells of CA1-CA3 subfields of the hippocampal formation, habenula, basolateral amygdaloid nuclei, and in the Purkinje and granule cells of the cerebellum. Diffusely detected over most other regions of the basal ganglia, including thalamic nuclei, substantia nigra, striatum and globus pallidus, hypothalamus, midbrain, pons, medulla and choroid plexus. Isoform 3 is expressed only in dorsal root ganglion (DRG) while isoform 1 is expressed in DRG, spinal chord, trigeminal ganglia and the trigeminal mesencephalic nucleus.4 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulation upon tissues inflammation is abolished by anti-inflammatory drugs.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSRNOG00000059765 Expressed in 10 organ(s), highest expression level in brain

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P55926 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P55926 RN

<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

Homotrimer or heterotrimer with other ASIC proteins (By similarity). Interacts with STOM and PRKCABP (By similarity). Interacts with ASIC2. Interacts with the spider venom Pi-hexatoxin-Hi1a (PubMed:28320941). Homotrimer of Asic1a interacts with the spider venom psalmotoxin-1 (PubMed:10829030, PubMed:26248594). Homotrimer of Asic1a and Asic1b and heterotrimer of Asic1a/Asic1b interact with the spider venom Pi-theraphotoxin-Hm3a (PubMed:28327374). Homotrimer of Asic1a interacts with the snake venom mambalgin-1, mambalgin-2 and mambalgin-3 (PubMed:23034652, PubMed:23624383, PubMed:24323786, PubMed:24695733, PubMed:26680001). Homotrimer of Asic1b interacts with the snake venom mambalgin-1, mambalgin-2 and mambalgin-3 (PubMed:23034652, PubMed:23624383, PubMed:24323786, PubMed:26680001). Heterotrimer of Asic1a-Asic1b interacts with the snake venom mambalgin-1 and mambalgin-2 (PubMed:23034652). Heterotrimer of Asic1a-Asic2a interacts with the snake venom mambalgin-1, mambalgin-2 and mambalgin-3 (PubMed:23034652, PubMed:23624383, PubMed:26680001). Heterotrimer of Asic1a-Asic2b interacts with the snake venom mambalgin-1 and mambalgin-2 (PubMed:23034652).By similarity10 Publications

Protein-protein interaction databases

Molecular INTeraction database

More...
MINTi
P55926

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P55926

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

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SMRi
P55926

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...

<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

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>Regioni20 – 25Involved in divalent cations permeability6

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi442 – 444Selectivity filterCurated3

<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

Channel opening involves a conformation change that affects primarily the extracellular domain and the second transmembrane helix and its orientation in the membrane. In the open state, the second transmembrane helix is nearly perpendicular to the plane of the membrane; in the desensitized state it is strongly tilted. Besides, the second transmembrane domain is discontinuously helical in the open state. The GAS motif of the selectivity filter is in an extended conformation, giving rise to a distinct kink in the polypeptide chain. A domain swap between subunits gives rise to a full-length transmembrane helix (By similarity).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

Transmembrane, Transmembrane helix

Phylogenomic databases

Ensembl GeneTree

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GeneTreei
ENSGT00940000158414

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000247010

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG004150

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P55926

KEGG Orthology (KO)

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KOi
K04829

Identification of Orthologs from Complete Genome Data

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OMAi
CSDKKHK

Database of Orthologous Groups

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OrthoDBi
686369at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P55926

TreeFam database of animal gene trees

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TreeFami
TF330663

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR001873 ENaC
IPR004724 ENaC_chordates
IPR020903 ENaC_CS

The PANTHER Classification System

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PANTHERi
PTHR11690 PTHR11690, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00858 ASC, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR01078 AMINACHANNEL

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR00859 ENaC, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS01206 ASC, 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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)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 3 <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 3 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: P55926-1) [UniParc]FASTAAdd to basket
Also known as: ASIC-alpha, asic1alpha

This isoform has been chosen as the 'canonical' 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
MELKTEEEEV GGVQPVSIQA FASSSTLHGL AHIFSYERLS LKRALWALCF
60 70 80 90 100
LGSLAVLLCV CTERVQYYFC YHHVTKLDEV AASQLTFPAV TLCNLNEFRF
110 120 130 140 150
SQVSKNDLYH AGELLALLNN RYEIPDTQMA DEKQLEILQD KANFRSFKPK
160 170 180 190 200
PFNMREFYDR AGHDIRDMLL SCHFRGEACS AEDFKVVFTR YGKCYTFNSG
210 220 230 240 250
QDGRPRLKTM KGGTGNGLEI MLDIQQDEYL PVWGETDETS FEAGIKVQIH
260 270 280 290 300
SQDEPPFIDQ LGFGVAPGFQ TFVSCQEQRL IYLPSPWGTC NAVTMDSDFF
310 320 330 340 350
DSYSITACRI DCETRYLVEN CNCRMVHMPG DAPYCTPEQY KECADPALDF
360 370 380 390 400
LVEKDQEYCV CEMPCNLTRY GKELSMVKIP SKASAKYLAK KFNKSEQYIG
410 420 430 440 450
ENILVLDIFF EVLNYETIEQ KKAYEIAGLL GDIGGQMGLF IGASILTVLE
460 470 480 490 500
LFDYAYEVIK HRLCRRGKCQ KEAKRSSADK GVALSLDDVK RHNPCESLRG
510 520
HPAGMTYAAN ILPHHPARGT FEDFTC
Length:526
Mass (Da):59,641
Last modified:November 1, 1997 - 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:i5462A7786E2A1726
GO
Isoform 2 (identifier: P55926-2) [UniParc]FASTAAdd to basket
Also known as: ASIC-beta2

The sequence of this isoform differs from the canonical sequence as follows:
     1-185: Missing.
     186-186: V → MADIWGPHHH...VIALGAFLCQ

Note: Inactive.
Show »
Length:425
Mass (Da):47,563
Checksum:i8B4A9EDFCE348B89
GO
Isoform 3 (identifier: P55926-3) [UniParc]FASTAAdd to basket
Also known as: ASIC-beta, ASIC1b

The sequence of this isoform differs from the canonical sequence as follows:
     1-185: Missing.
     186-186: V → MPIQIFCSVS...GPCGPHNFSV

Note: Blocked by Ca2+. Mutagenesis of Asp-465 to Asn reduces Ca2+ block.Curated
Show »
Length:559
Mass (Da):62,217
Checksum:i0F438117B95C18E5
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
A0A0G2JX02A0A0G2JX02_RAT
Acid-sensing ion channel 1
Asic1
456Annotation score:

Annotation score:1 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CAA07080 differs from that shown. Reason: Frameshift at positions 119, 122 and 142.Curated
Isoform 3 : The sequence CAA07080 differs from that shown. Reason: Frameshift at positions 7 and 14.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Isoform 3 (identifier: P55926-3)
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti128T → S in CAA07080 (PubMed:9707631).Curated1

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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0155971 – 185Missing in isoform 2 and isoform 3. 3 PublicationsAdd BLAST185
Alternative sequenceiVSP_015598186V → MADIWGPHHHRQQQDSSESE EEEEKEMEAGSELDEGDDSP RDLVAFANSCTLHGASHVFV EGGPGPRQALWAVAFVIALG AFLCQ in isoform 2. 1 Publication1
Alternative sequenceiVSP_015599186V → MPIQIFCSVSFSSGEEAPGS MADIWGPHHHRQQQDSSESE EEEEKEMEAGSELDEGDDSP RDLVAFANSCTLHGASHVFV EGGPGPRQALWAVAFVIALG AFLCQVGDRVAYYLSYPHVT LLDEVATTELVFPAVTFCNT NAVRLSQLSYPDLLYLAPML GLDESDDPGVPLAPPGPEAF SGEPFNLHRFYNRSCHRLED MLLYCSYCGGPCGPHNFSV in isoform 3. 2 Publications1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U94403 mRNA Translation: AAB53002.1
AJ006519 mRNA Translation: CAA07080.1 Frameshift.
AJ309926 mRNA Translation: CAC44267.1
AB049451 mRNA Translation: BAB39864.1

NCBI Reference Sequences

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RefSeqi
NP_077068.1, NM_024154.2 [P55926-1]
XP_006257440.1, XM_006257378.3 [P55926-3]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Rn.37385

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000077175; ENSRNOP00000072206; ENSRNOG00000059765 [P55926-2]
ENSRNOT00000088191; ENSRNOP00000068902; ENSRNOG00000059765 [P55926-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
79123

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:79123

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
U94403 mRNA Translation: AAB53002.1
AJ006519 mRNA Translation: CAA07080.1 Frameshift.
AJ309926 mRNA Translation: CAC44267.1
AB049451 mRNA Translation: BAB39864.1
RefSeqiNP_077068.1, NM_024154.2 [P55926-1]
XP_006257440.1, XM_006257378.3 [P55926-3]
UniGeneiRn.37385

3D structure databases

ProteinModelPortaliP55926
SMRiP55926
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiP55926

Chemistry databases

ChEMBLiCHEMBL3562170
GuidetoPHARMACOLOGYi684

Protein family/group databases

TCDBi1.A.6.1.2 the epithelial na(+) channel (enac) family

PTM databases

iPTMnetiP55926
PhosphoSitePlusiP55926
SwissPalmiP55926

Proteomic databases

PRIDEiP55926

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000077175; ENSRNOP00000072206; ENSRNOG00000059765 [P55926-2]
ENSRNOT00000088191; ENSRNOP00000068902; ENSRNOG00000059765 [P55926-1]
GeneIDi79123
KEGGirno:79123

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
41
RGDi71062 Asic1

Phylogenomic databases

GeneTreeiENSGT00940000158414
HOGENOMiHOG000247010
HOVERGENiHBG004150
InParanoidiP55926
KOiK04829
OMAiCSDKKHK
OrthoDBi686369at2759
PhylomeDBiP55926
TreeFamiTF330663

Enzyme and pathway databases

ReactomeiR-RNO-2672351 Stimuli-sensing channels

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P55926

Gene expression databases

BgeeiENSRNOG00000059765 Expressed in 10 organ(s), highest expression level in brain
ExpressionAtlasiP55926 baseline and differential
GenevisibleiP55926 RN

Family and domain databases

InterProiView protein in InterPro
IPR001873 ENaC
IPR004724 ENaC_chordates
IPR020903 ENaC_CS
PANTHERiPTHR11690 PTHR11690, 1 hit
PfamiView protein in Pfam
PF00858 ASC, 1 hit
PRINTSiPR01078 AMINACHANNEL
TIGRFAMsiTIGR00859 ENaC, 1 hit
PROSITEiView protein in PROSITE
PS01206 ASC, 1 hit

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 nameiASIC1_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: P55926
Secondary accession number(s): O88762, Q91YB8, Q99NA1
<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: November 1, 1997
Last sequence update: November 1, 1997
Last modified: January 16, 2019
This is version 151 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
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