UniProtKB - Q62962 (ASIC2_RAT)
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Protein
Acid-sensing ion channel 2
Gene
Asic2
Organism
Rattus norvegicus (Rat)
Status
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.
GO - Molecular functioni
- cation channel activity Source: RGD
- ion channel activity Source: RGD
- ion gated channel activity Source: RGD
- ligand-gated sodium channel activity Source: RGD
- voltage-gated sodium channel activity Source: RGD
GO - Biological processi
- cation transport Source: RGD
- cellular response to acidic pH Source: RGD
- cellular response to drug Source: RGD
- detection of mechanical stimulus involved in sensory perception Source: RGD
- ion transmembrane transport Source: RGD
- negative regulation of apoptotic process Source: RGD
- phototransduction Source: RGD
- positive regulation of cation channel activity Source: RGD
- positive regulation of synapse assembly Source: RGD
- protein localization to synapse Source: RGD
- regulation of blood coagulation Source: RGD
- regulation of gene expression Source: RGD
- regulation of ion transmembrane transport Source: RGD
- regulation of membrane potential Source: RGD
- regulation of systemic arterial blood pressure by aortic arch baroreceptor feedback Source: RGD
- regulation of vasoconstriction Source: RGD
- response to acidic pH Source: RGD
- response to mechanical stimulus Source: RGD
- sensory perception of sound Source: RGD
- sensory perception of sour taste Source: RGD
- sodium ion transport Source: RGD
Keywordsi
Molecular function | Ion channel, Sodium channel |
Biological process | Ion transport, Sodium transport, Transport |
Ligand | Sodium |
Protein family/group databases
TCDBi | 1.A.6.1.2. the epithelial na(+) channel (enac) family. |
Names & Taxonomyi
Protein namesi | Recommended name: Acid-sensing ion channel 2Short 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 |
Gene namesi | Name:Asic2 Synonyms:Accn1, Bnac1, Mdeg |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 2017. Asic2. |
Subcellular locationi
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 37 | Cytoplasmic1 PublicationAdd BLAST | 37 | |
Transmembranei | 38 – 58 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 59 – 427 | Extracellular1 PublicationAdd BLAST | 369 | |
Transmembranei | 428 – 448 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 449 – 512 | Cytoplasmic1 PublicationAdd BLAST | 64 |
Keywords - Cellular componenti
Cell membrane, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 4 | K → N: No effect on N-glycosylation. 1 Publication | 1 | |
Mutagenesisi | 22 | N → S: No effect on N-glycosylation. 1 Publication | 1 | |
Mutagenesisi | 37 | P → N: No effect on N-glycosylation. 1 Publication | 1 | |
Mutagenesisi | 63 | R → N: No effect on N-glycosylation. 1 Publication | 1 | |
Mutagenesisi | 67 | Y → N: No effect on N-glycosylation. 1 Publication | 1 | |
Mutagenesisi | 72 | H → A: Inactive. Active at lower pH; when associated with V-430. 2 Publications | 1 | |
Mutagenesisi | 72 | H → N: Increases N-glycosylation. 2 Publications | 1 | |
Mutagenesisi | 81 | A → N: Increases N-glycosylation. 1 Publication | 1 | |
Mutagenesisi | 109 | H → A: No effect on pH dependence and function. 1 Publication | 1 | |
Mutagenesisi | 127 | H → A: No effect on pH dependence and function. 1 Publication | 1 | |
Mutagenesisi | 145 | H → A: No effect on pH dependence and function. 1 Publication | 1 | |
Mutagenesisi | 158 | H → A: No effect on pH dependence and function. 1 Publication | 1 | |
Mutagenesisi | 162 | H → A: Loss of potentiation by Zn(2+). 1 Publication | 1 | |
Mutagenesisi | 180 | H → A: No effect on pH dependence and function. 1 Publication | 1 | |
Mutagenesisi | 249 | H → A: No effect on pH dependence and function. 1 Publication | 1 | |
Mutagenesisi | 326 | H → A: No effect on pH dependence and function. 1 Publication | 1 | |
Mutagenesisi | 339 | H → A: Loss of potentiation by Zn(2+). 1 Publication | 1 | |
Mutagenesisi | 365 | N → S: Reduces N-glycosylation. Abolishes N-glycosylation; when associated with S-392. 1 Publication | 1 | |
Mutagenesisi | 392 | N → S: Reduces N-glycosylation. Abolishes N-glycosylation; when associated with S-365. 1 Publication | 1 | |
Mutagenesisi | 414 | Y → N: Increases N-glycosylation. 1 Publication | 1 | |
Mutagenesisi | 423 – 425 | YEV → NES: Increases N-glycosylation. 1 Publication | 3 | |
Mutagenesisi | 430 | G → C: Partial activation. 2 Publications | 1 | |
Mutagenesisi | 430 | G → F: Constitutive activation causing cell death. Inactive; when associated with F-443. 2 Publications | 1 | |
Mutagenesisi | 430 | G → K or T: Constitutive activation causing cell death. 2 Publications | 1 | |
Mutagenesisi | 430 | G → S: No constitutive activation. 2 Publications | 1 | |
Mutagenesisi | 430 | G → V: Constitutive activation causing cell death. Activated at lower pH; when associated with A-72. 2 Publications | 1 | |
Mutagenesisi | 443 | S → F: Loss of function. Inactive; when associated with F-430. 1 Publication | 1 | |
Mutagenesisi | 453 – 455 | YIY → NIS: No effect on N-glycosylation. 1 Publication | 3 | |
Mutagenesisi | 478 | N → S: No effect on N-glycosylation. 1 Publication | 1 | |
Mutagenesisi | 487 | N → S: No effect on N-glycosylation. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL3562171. |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000181292 | 1 – 512 | Acid-sensing ion channel 2Add BLAST | 512 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 8 | PhosphoserineCombined sources | 1 | |
Modified residuei | 11 | PhosphoserineCombined sources | 1 | |
Disulfide bondi | 92 ↔ 193 | By similarity | ||
Disulfide bondi | 171 ↔ 178 | By similarity | ||
Disulfide bondi | 289 ↔ 364 | By similarity | ||
Disulfide bondi | 307 ↔ 360 | By similarity | ||
Disulfide bondi | 311 ↔ 358 | By similarity | ||
Disulfide bondi | 320 ↔ 342 | By similarity | ||
Disulfide bondi | 322 ↔ 334 | By similarity | ||
Glycosylationi | 365 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 392 | N-linked (GlcNAc...) asparagine1 Publication | 1 |
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 478 | Not glycosylated | 1 | |
Sitei | 487 | Not glycosylated | 1 |
Keywords - PTMi
Disulfide bond, Glycoprotein, PhosphoproteinProteomic databases
PRIDEi | Q62962. |
PTM databases
iPTMneti | Q62962. |
PhosphoSitePlusi | Q62962. |
Expressioni
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
Developmental stagei
Appears just before birth, reaches maximum levels after birth, then declines slightly until adulthood.
Inductioni
Up-regulation upon tissues inflammation is abolished by anti-inflammatory drugs.1 Publication
Interactioni
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
Binary interactionsi
With | Entry | #Exp. | IntAct | Notes |
---|---|---|---|---|
Stoml3 | D4A100 | 2 | EBI-15615759,EBI-15615743 |
Protein-protein interaction databases
DIPi | DIP-41193N. |
IntActi | Q62962. 2 interactors. |
MINTi | Q62962. |
Structurei
3D structure databases
ProteinModelPortali | Q62962. |
SMRi | Q62962. |
ModBasei | Search... |
MobiDBi | Search... |
Family & Domainsi
Sequence similaritiesi
Belongs to the amiloride-sensitive sodium channel (TC 1.A.6) family. ASIC2 subfamily. [View classification]Curated
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
HOGENOMi | HOG000247010. |
HOVERGENi | HBG004150. |
InParanoidi | Q62962. |
KOi | K04828. |
PhylomeDBi | Q62962. |
TreeFami | TF330663. |
Family and domain databases
InterProi | View protein in InterPro IPR001873. ENaC. IPR004724. ENaC_chordates. IPR020903. ENaC_CS. |
PANTHERi | PTHR11690. PTHR11690. 1 hit. |
Pfami | View protein in Pfam PF00858. ASC. 1 hit. |
PRINTSi | PR01078. AMINACHANNEL. |
TIGRFAMsi | TIGR00859. ENaC. 1 hit. |
PROSITEi | View protein in PROSITE PS01206. ASC. 1 hit. |
s (2)i Sequence
Sequence statusi: Complete.
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basket
Isoform 1 (identifier: Q62962-1) [UniParc]FASTAAdd to basket
Also known as: Mdeg11 Publication, Asic2a
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.
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
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 »Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_015594 | 1 – 184 | Missing in isoform 2. 1 PublicationAdd BLAST | 184 | |
Alternative sequenceiVSP_015595 | 185 | T → MSRSGGARLPATALSGPGRF RMAREQPAPVAVAAARQPGG DRSGDPALQGPGVARRGRPS LSRTKLHGLRHMCAGRTAAG GSFQRRALWVLAFCTSLGLL LSWSSNRLLYWLSFPSHTRV HREWSRQLPFPAVTVCNNNP LRFPRLSKGDLYYAGHWLGL LLPNRTARPLVSELLRGDEP RRQWFRKLADFRLFLPPRHF EGISAAFMDRLGHQLEDMLL SCKYRGELCGPHNFSS in isoform 2. 1 Publication | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U53211 mRNA. Translation: AAC52588.1. Y14635 mRNA. Translation: CAA74979.1. |
RefSeqi | NP_001029186.1. NM_001034014.1. [Q62962-1] NP_037024.2. NM_012892.2. [Q62962-2] |
UniGenei | Rn.37523. |
Genome annotation databases
GeneIDi | 25364. |
KEGGi | rno:25364. |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Entry informationi
Entry namei | ASIC2_RAT | |
Accessioni | Q62962Primary (citable) accession number: Q62962 Secondary accession number(s): O55163 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1997 |
Last sequence update: | November 1, 1997 | |
Last modified: | March 28, 2018 | |
This is version 139 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |