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Entry version 147 (03 Jul 2019)
Sequence version 1 (01 Nov 1997)
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Protein

Acid-sensing ion channel 2

Gene

Asic2

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

Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride. Also permeable for Li+ and K+. Activation by an extracellular pH drop is followed by a rapid pH-independent inactivation. Heteromeric channel assembly seems to modulate channel properties.3 Publications

Miscellaneous

Regulated by Zn2+. Inhibited by anti-inflammatory drugs like salicylic acid.

<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
Biological processIon transport, Sodium transport, Transport
LigandSodium

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 2
Short name:
ASIC2
Alternative name(s):
Amiloride-sensitive brain sodium channel
Amiloride-sensitive brain sodium channel 2
Amiloride-sensitive cation channel 1, neuronal
Amiloride-sensitive cation channel neuronal 1
Brain sodium channel 1
Short name:
BNC1
Short name:
BNaC1
Mammalian degenerin homolog1 Publication
Short name:
MDEG1 Publication
<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:Asic2
Synonyms:Accn1, Bnac1, Mdeg
<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
2017 Asic2

<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 – 37Cytoplasmic1 PublicationAdd BLAST37
<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>Transmembranei38 – 58HelicalSequence analysisAdd BLAST21
Topological domaini59 – 427Extracellular1 PublicationAdd BLAST369
Transmembranei428 – 448HelicalSequence analysisAdd BLAST21
Topological domaini449 – 512Cytoplasmic1 PublicationAdd BLAST64

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>Mutagenesisi4K → N: No effect on N-glycosylation. 1 Publication1
Mutagenesisi22N → S: No effect on N-glycosylation. 1 Publication1
Mutagenesisi37P → N: No effect on N-glycosylation. 1 Publication1
Mutagenesisi63R → N: No effect on N-glycosylation. 1 Publication1
Mutagenesisi67Y → N: No effect on N-glycosylation. 1 Publication1
Mutagenesisi72H → A: Inactive. Active at lower pH; when associated with V-430. 2 Publications1
Mutagenesisi72H → N: Increases N-glycosylation. 2 Publications1
Mutagenesisi81A → N: Increases N-glycosylation. 1 Publication1
Mutagenesisi109H → A: No effect on pH dependence and function. 1 Publication1
Mutagenesisi127H → A: No effect on pH dependence and function. 1 Publication1
Mutagenesisi145H → A: No effect on pH dependence and function. 1 Publication1
Mutagenesisi158H → A: No effect on pH dependence and function. 1 Publication1
Mutagenesisi162H → A: Loss of potentiation by Zn(2+). 1 Publication1
Mutagenesisi180H → A: No effect on pH dependence and function. 1 Publication1
Mutagenesisi249H → A: No effect on pH dependence and function. 1 Publication1
Mutagenesisi326H → A: No effect on pH dependence and function. 1 Publication1
Mutagenesisi339H → A: Loss of potentiation by Zn(2+). 1 Publication1
Mutagenesisi365N → S: Reduces N-glycosylation. Abolishes N-glycosylation; when associated with S-392. 1 Publication1
Mutagenesisi392N → S: Reduces N-glycosylation. Abolishes N-glycosylation; when associated with S-365. 1 Publication1
Mutagenesisi414Y → N: Increases N-glycosylation. 1 Publication1
Mutagenesisi423 – 425YEV → NES: Increases N-glycosylation. 1 Publication3
Mutagenesisi430G → C: Partial activation. 2 Publications1
Mutagenesisi430G → F: Constitutive activation causing cell death. Inactive; when associated with F-443. 2 Publications1
Mutagenesisi430G → K or T: Constitutive activation causing cell death. 2 Publications1
Mutagenesisi430G → S: No constitutive activation. 2 Publications1
Mutagenesisi430G → V: Constitutive activation causing cell death. Activated at lower pH; when associated with A-72. 2 Publications1
Mutagenesisi443S → F: Loss of function. Inactive; when associated with F-430. 1 Publication1
Mutagenesisi453 – 455YIY → NIS: No effect on N-glycosylation. 1 Publication3
Mutagenesisi478N → S: No effect on N-glycosylation. 1 Publication1
Mutagenesisi487N → S: No effect on N-glycosylation. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3562171

<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_00001812921 – 512Acid-sensing ion channel 2Add BLAST512

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 residuei8PhosphoserineCombined sources1
Modified residuei11PhosphoserineCombined sources1
<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 bondi92 ↔ 193By similarity
Disulfide bondi171 ↔ 178By similarity
Disulfide bondi289 ↔ 364By similarity
Disulfide bondi307 ↔ 360By similarity
Disulfide bondi311 ↔ 358By similarity
Disulfide bondi320 ↔ 342By similarity
Disulfide bondi322 ↔ 334By 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>Glycosylationi365N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi392N-linked (GlcNAc...) asparagine1 Publication1

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>Sitei478Not glycosylated1
Sitei487Not glycosylated1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q62962

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q62962

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

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PhosphoSitePlusi
Q62962

<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 sciatic nerve and dorsal root ganglion (DRG) (at protein level). Both isoforms display the same expression pattern except in DRG where isoform 2 is more abundantly expressed. Widely distributed throughout the brain. Highly expressed in the main olfactory bulb, neo- and allo-cortical regions, hippocampal formation, habenula, basolateral amygdaloid nuclei, and cerebellum. In the olfactory system, expressed in the glomerular cell layer, the internal granular layer, and the mitral and internal plexiform cell layers. Within the glomerular layer, restricted to the periglomerular cells. In the neocortex, strongly expressed in the large pyramidal neurons in all cortical layers as well as in the oligo-, astro-, or micro-glia cells. In the hippocampal formation, expressed in dentate granule cells and hilar neurons, as well as in pyramidal cells of CA1-CA3 subfields. Expressed in stratum oriens and radiatum of all subfields. Within the thalamus, expressed moderately in the medial and lateral habenula. In the cerebellar cortex expressed in Purkinje cells and granule cells. Expressed at low levels in choroid plexus.4 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Appears just before birth, reaches maximum levels after birth, then declines slightly until adulthood.

<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

<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 PRKCABP (By similarity).

Interacts with STOM; this regulates channel activity.

Interacts with ASIC1. Isoform 2 interacts with ASIC3. Heterotrimer of Asic1a-Asic2a interacts with the snake venom mambalgin-1, mambalgin-2 and mambalgin-3 (PubMed:23034652, PubMed:23624383). Heterotrimer of Asic1a-Asic2b interacts with the snake venom mambalgin-1 and mambalgin-2 (PubMed:23034652).

By similarity4 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

WithEntry#Exp.IntActNotes
Stoml3D4A1002EBI-15615798,EBI-15615743

Protein-protein interaction databases

Database of interacting proteins

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DIPi
DIP-41193N

Protein interaction database and analysis system

More...
IntActi
Q62962, 1 interactor

Molecular INTeraction database

More...
MINTi
Q62962

<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

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

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SMRi
Q62962

Database of comparative protein structure models

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ModBasei
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

<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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000247010

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q62962

KEGG Orthology (KO)

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KOi
K04828

Database of Orthologous Groups

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OrthoDBi
686369at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q62962

TreeFam database of animal gene trees

More...
TreeFami
TF330663

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
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

More...
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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

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

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

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: Q62962-1) [UniParc]FASTAAdd to basket
Also known as: Mdeg11 Publication, Asic2a

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

« Hide
        10         20         30         40         50
MDLKESPSEG SLQPSSIQIF ANTSTLHGIR HIFVYGPLTI RRVLWAVAFV
60 70 80 90 100
GSLGLLLVES SERVSYYFSY QHVTKVDEVV AQSLVFPAVT LCNLNGFRFS
110 120 130 140 150
RLTTNDLYHA GELLALLDVN LQIPDPHLAD PTVLEALRQK ANFKHYKPKQ
160 170 180 190 200
FSMLEFLHRV GHDLKDMMLY CKFKGQECGH QDFTTVFTKY GKCYMFNSGE
210 220 230 240 250
DGKPLLTTVK GGTGNGLEIM LDIQQDEYLP IWGETEETTF EAGVKVQIHS
260 270 280 290 300
QSEPPFIQEL GFGVAPGFQT FVATQEQRLT YLPPPWGECR SSEMGLDFFP
310 320 330 340 350
VYSITACRID CETRYIVENC NCRMVHMPGD APFCTPEQHK ECAEPALGLL
360 370 380 390 400
AEKDSNYCLC RTPCNLTRYN KELSMVKIPS KTSAKYLEKK FNKSEKYISE
410 420 430 440 450
NILVLDIFFE ALNYETIEQK KAYEVAALLG DIGGQMGLFI GASLLTILEL
460 470 480 490 500
FDYIYELIKE KLLDLLGKEE EEGSHDENMS TCDTMPNHSE TISHTVNVPL
510
QTALGTLEEI AC
Length:512
Mass (Da):57,739
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:i38D0A77C3C430B03
GO
Isoform 2 (identifier: Q62962-2) [UniParc]FASTAAdd to basket
Also known as: Mdeg21 Publication, Asic2b

The sequence of this isoform differs from the canonical sequence as follows:
     1-184: Missing.
     185-185: T → MSRSGGARLP...ELCGPHNFSS

Note: Seems to be inactive as monomer or in a monomeric assembly and is not activated by mutagenesis of Gly-430. Mutagenesis of Ser-60 into Gly reduces activation by PKC through PRKCABP/PICK-1 of a ASIC3/ACCN3-ASIC2/ASIC2b channel.
Show »
Length:563
Mass (Da):63,115
Checksum:iDCE1B4A0A45F21E2
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
A0A0G2JTM0A0A0G2JTM0_RAT
Acid-sensing ion channel 2
Asic2
563Annotation 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>

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0155941 – 184Missing in isoform 2. 1 PublicationAdd BLAST184
Alternative sequenceiVSP_015595185T → MSRSGGARLPATALSGPGRF RMAREQPAPVAVAAARQPGG DRSGDPALQGPGVARRGRPS LSRTKLHGLRHMCAGRTAAG GSFQRRALWVLAFCTSLGLL LSWSSNRLLYWLSFPSHTRV HREWSRQLPFPAVTVCNNNP LRFPRLSKGDLYYAGHWLGL LLPNRTARPLVSELLRGDEP RRQWFRKLADFRLFLPPRHF EGISAAFMDRLGHQLEDMLL SCKYRGELCGPHNFSS in isoform 2. 1 Publication1

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
U53211 mRNA Translation: AAC52588.1
Y14635 mRNA Translation: CAA74979.1

NCBI Reference Sequences

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RefSeqi
NP_001029186.1, NM_001034014.1 [Q62962-1]
NP_037024.2, NM_012892.2 [Q62962-2]

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
25364

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:25364

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
U53211 mRNA Translation: AAC52588.1
Y14635 mRNA Translation: CAA74979.1
RefSeqiNP_001029186.1, NM_001034014.1 [Q62962-1]
NP_037024.2, NM_012892.2 [Q62962-2]

3D structure databases

SMRiQ62962
ModBaseiSearch...

Protein-protein interaction databases

DIPiDIP-41193N
IntActiQ62962, 1 interactor
MINTiQ62962

Chemistry databases

ChEMBLiCHEMBL3562171

Protein family/group databases

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

PTM databases

iPTMnetiQ62962
PhosphoSitePlusiQ62962

Proteomic databases

PRIDEiQ62962

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25364
KEGGirno:25364

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
40
RGDi2017 Asic2

Phylogenomic databases

HOGENOMiHOG000247010
InParanoidiQ62962
KOiK04828
OrthoDBi686369at2759
PhylomeDBiQ62962
TreeFamiTF330663

Enzyme and pathway databases

ReactomeiR-RNO-2672351 Stimuli-sensing channels

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q62962

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...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiASIC2_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: Q62962
Secondary accession number(s): O55163
<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: July 3, 2019
This is version 147 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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