Asic2

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

GO - Molecular functionⁱ

ion channel activity
Source: RGD
Inferred from direct assayⁱ
- 14976185
ligand-gated sodium channel activity Source: InterPro
voltage-gated sodium channel activity
Source: RGD
Inferred from direct assayⁱ
- 9368048

GO - Biological processⁱ

cellular response to acidic pH
Source: RGD
Inferred from direct assayⁱ
- 12736332
cellular response to drug
Source: RGD
Inferred from direct assayⁱ
- 12736332
positive regulation of cation channel activity
Source: RGD
Inferred from direct assayⁱ
- 12736332
sodium ion transport
Source: RGD
Inferred from direct assayⁱ
- 9368048

Complete GO annotation...

Protein family/group databases

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

TCDBⁱ

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

Names & Taxonomyⁱ

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 homolog Short name: MDEG
Gene namesⁱ	Name:Asic2 Synonyms:Accn1, Bnac1, Mdeg
Organismⁱ	Rattus norvegicus (Rat)
Taxonomic identifierⁱ	10116 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus
Proteomesⁱ	UP000002494 Componentⁱ: Unplaced

Organism-specific databases

RGDⁱ	2017. Asic2.

Subcellular locationⁱ

Cell membrane
2 Publications
Manual assertion based on experiment inⁱ
- Ref.6
  "Functional implications of the localization and activity of acid-sensitive channels in rat peripheral nervous system."
  Alvarez de la Rosa D., Zhang P., Shao D., White F., Canessa C.M.
  Proc. Natl. Acad. Sci. U.S.A. 99:2326-2331(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
- Ref.9
  "A stomatin dimer modulates the activity of acid-sensing ion channels."
  Brand J., Smith E.S., Schwefel D., Lapatsina L., Poole K., Omerbasic D., Kozlenkov A., Behlke J., Lewin G.R., Daumke O.
  EMBO J. 31:3635-3646(2012) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, INTERACTION WITH STOM, SUBCELLULAR LOCATION.
; Multi-pass membrane protein
2 Publications
Manual assertion based on experiment inⁱ
- Ref.6
  "Functional implications of the localization and activity of acid-sensitive channels in rat peripheral nervous system."
  Alvarez de la Rosa D., Zhang P., Shao D., White F., Canessa C.M.
  Proc. Natl. Acad. Sci. U.S.A. 99:2326-2331(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
- Ref.9
  "A stomatin dimer modulates the activity of acid-sensing ion channels."
  Brand J., Smith E.S., Schwefel D., Lapatsina L., Poole K., Omerbasic D., Kozlenkov A., Behlke J., Lewin G.R., Daumke O.
  EMBO J. 31:3635-3646(2012) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, INTERACTION WITH STOM, SUBCELLULAR LOCATION.

Note:

Localized at the plasma membrane of neurons, in the soma and punctated peripheral processes.

Topology

Feature key	Position(s)	Length	Description	Actions
Topological domainⁱ	1 – 37	37	Cytoplasmic1 Publication Manual assertion based on experiment inⁱ Ref.8 "Analysis of the membrane topology of the acid-sensing ion channel 2a." Saugstad J.A., Roberts J.A., Dong J., Zeitouni S., Evans R.J. J. Biol. Chem. 279:55514-55519(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-365 AND ASN-392, MUTAGENESIS OF LYS-4; ASN-22; PRO-37; ARG-63; TYR-67; HIS-72; ALA-81; ASN-365; ASN-392; TYR-414; 423-TYR--VAL-425; 453-TYR--TYR-455; ASN-478 AND ASN-487, TOPOLOGY.	Add BLAST
Transmembraneⁱ	38 – 58	21	HelicalSequence analysis	Add BLAST
Topological domainⁱ	59 – 427	369	Extracellular1 Publication Manual assertion based on experiment inⁱ Ref.8 "Analysis of the membrane topology of the acid-sensing ion channel 2a." Saugstad J.A., Roberts J.A., Dong J., Zeitouni S., Evans R.J. J. Biol. Chem. 279:55514-55519(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-365 AND ASN-392, MUTAGENESIS OF LYS-4; ASN-22; PRO-37; ARG-63; TYR-67; HIS-72; ALA-81; ASN-365; ASN-392; TYR-414; 423-TYR--VAL-425; 453-TYR--TYR-455; ASN-478 AND ASN-487, TOPOLOGY.	Add BLAST
Transmembraneⁱ	428 – 448	21	HelicalSequence analysis	Add BLAST
Topological domainⁱ	449 – 512	64	Cytoplasmic1 Publication Manual assertion based on experiment inⁱ Ref.8 "Analysis of the membrane topology of the acid-sensing ion channel 2a." Saugstad J.A., Roberts J.A., Dong J., Zeitouni S., Evans R.J. J. Biol. Chem. 279:55514-55519(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-365 AND ASN-392, MUTAGENESIS OF LYS-4; ASN-22; PRO-37; ARG-63; TYR-67; HIS-72; ALA-81; ASN-365; ASN-392; TYR-414; 423-TYR--VAL-425; 453-TYR--TYR-455; ASN-478 AND ASN-487, TOPOLOGY.	Add BLAST

GO - Cellular componentⁱ

integral component of membrane Source: UniProtKB-KW
plasma membrane Source: UniProtKB-SubCell

Complete GO annotation...

Keywords - Cellular componentⁱ

Cell membrane, Membrane

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	Length	Description
Mutagenesisⁱ	4 – 4	1	K → N: No effect on N-glycosylation. 1 Publication Manual assertion based on experiment inⁱ Ref.8 "Analysis of the membrane topology of the acid-sensing ion channel 2a." Saugstad J.A., Roberts J.A., Dong J., Zeitouni S., Evans R.J. J. Biol. Chem. 279:55514-55519(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-365 AND ASN-392, MUTAGENESIS OF LYS-4; ASN-22; PRO-37; ARG-63; TYR-67; HIS-72; ALA-81; ASN-365; ASN-392; TYR-414; 423-TYR--VAL-425; 453-TYR--TYR-455; ASN-478 AND ASN-487, TOPOLOGY.
Mutagenesisⁱ	22 – 22	1	N → S: No effect on N-glycosylation. 1 Publication Manual assertion based on experiment inⁱ Ref.8 "Analysis of the membrane topology of the acid-sensing ion channel 2a." Saugstad J.A., Roberts J.A., Dong J., Zeitouni S., Evans R.J. J. Biol. Chem. 279:55514-55519(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-365 AND ASN-392, MUTAGENESIS OF LYS-4; ASN-22; PRO-37; ARG-63; TYR-67; HIS-72; ALA-81; ASN-365; ASN-392; TYR-414; 423-TYR--VAL-425; 453-TYR--TYR-455; ASN-478 AND ASN-487, TOPOLOGY.
Mutagenesisⁱ	37 – 37	1	P → N: No effect on N-glycosylation. 1 Publication Manual assertion based on experiment inⁱ Ref.8 "Analysis of the membrane topology of the acid-sensing ion channel 2a." Saugstad J.A., Roberts J.A., Dong J., Zeitouni S., Evans R.J. J. Biol. Chem. 279:55514-55519(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-365 AND ASN-392, MUTAGENESIS OF LYS-4; ASN-22; PRO-37; ARG-63; TYR-67; HIS-72; ALA-81; ASN-365; ASN-392; TYR-414; 423-TYR--VAL-425; 453-TYR--TYR-455; ASN-478 AND ASN-487, TOPOLOGY.
Mutagenesisⁱ	63 – 63	1	R → N: No effect on N-glycosylation. 1 Publication Manual assertion based on experiment inⁱ Ref.8 "Analysis of the membrane topology of the acid-sensing ion channel 2a." Saugstad J.A., Roberts J.A., Dong J., Zeitouni S., Evans R.J. J. Biol. Chem. 279:55514-55519(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-365 AND ASN-392, MUTAGENESIS OF LYS-4; ASN-22; PRO-37; ARG-63; TYR-67; HIS-72; ALA-81; ASN-365; ASN-392; TYR-414; 423-TYR--VAL-425; 453-TYR--TYR-455; ASN-478 AND ASN-487, TOPOLOGY.
Mutagenesisⁱ	67 – 67	1	Y → N: No effect on N-glycosylation. 1 Publication Manual assertion based on experiment inⁱ Ref.8 "Analysis of the membrane topology of the acid-sensing ion channel 2a." Saugstad J.A., Roberts J.A., Dong J., Zeitouni S., Evans R.J. J. Biol. Chem. 279:55514-55519(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-365 AND ASN-392, MUTAGENESIS OF LYS-4; ASN-22; PRO-37; ARG-63; TYR-67; HIS-72; ALA-81; ASN-365; ASN-392; TYR-414; 423-TYR--VAL-425; 453-TYR--TYR-455; ASN-478 AND ASN-487, TOPOLOGY.
Mutagenesisⁱ	72 – 72	1	H → A: Inactive. Active at lower pH; when associated with V-430. 2 Publications Manual assertion based on experiment inⁱ Ref.4 "Zn2+ and H+ are coactivators of acid-sensing ion channels." Baron A., Schaefer L., Lingueglia E., Champigny G., Lazdunski M. J. Biol. Chem. 276:35361-35367(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF HIS-72; HIS-109; HIS-127; HIS-145; HIS-158; HIS-162; HIS-180; HIS-249; HIS-326; HIS-339 AND GLY-430, REGULATION BY PROTONS AND ZINC. Ref.8 "Analysis of the membrane topology of the acid-sensing ion channel 2a." Saugstad J.A., Roberts J.A., Dong J., Zeitouni S., Evans R.J. J. Biol. Chem. 279:55514-55519(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-365 AND ASN-392, MUTAGENESIS OF LYS-4; ASN-22; PRO-37; ARG-63; TYR-67; HIS-72; ALA-81; ASN-365; ASN-392; TYR-414; 423-TYR--VAL-425; 453-TYR--TYR-455; ASN-478 AND ASN-487, TOPOLOGY.
Mutagenesisⁱ	72 – 72	1	H → N: Increases N-glycosylation. 2 Publications Manual assertion based on experiment inⁱ Ref.4 "Zn2+ and H+ are coactivators of acid-sensing ion channels." Baron A., Schaefer L., Lingueglia E., Champigny G., Lazdunski M. J. Biol. Chem. 276:35361-35367(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF HIS-72; HIS-109; HIS-127; HIS-145; HIS-158; HIS-162; HIS-180; HIS-249; HIS-326; HIS-339 AND GLY-430, REGULATION BY PROTONS AND ZINC. Ref.8 "Analysis of the membrane topology of the acid-sensing ion channel 2a." Saugstad J.A., Roberts J.A., Dong J., Zeitouni S., Evans R.J. J. Biol. Chem. 279:55514-55519(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-365 AND ASN-392, MUTAGENESIS OF LYS-4; ASN-22; PRO-37; ARG-63; TYR-67; HIS-72; ALA-81; ASN-365; ASN-392; TYR-414; 423-TYR--VAL-425; 453-TYR--TYR-455; ASN-478 AND ASN-487, TOPOLOGY.
Mutagenesisⁱ	81 – 81	1	A → N: Increases N-glycosylation. 1 Publication Manual assertion based on experiment inⁱ Ref.8 "Analysis of the membrane topology of the acid-sensing ion channel 2a." Saugstad J.A., Roberts J.A., Dong J., Zeitouni S., Evans R.J. J. Biol. Chem. 279:55514-55519(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-365 AND ASN-392, MUTAGENESIS OF LYS-4; ASN-22; PRO-37; ARG-63; TYR-67; HIS-72; ALA-81; ASN-365; ASN-392; TYR-414; 423-TYR--VAL-425; 453-TYR--TYR-455; ASN-478 AND ASN-487, TOPOLOGY.
Mutagenesisⁱ	109 – 109	1	H → A: No effect on pH dependence and function. 1 Publication Manual assertion based on experiment inⁱ Ref.4 "Zn2+ and H+ are coactivators of acid-sensing ion channels." Baron A., Schaefer L., Lingueglia E., Champigny G., Lazdunski M. J. Biol. Chem. 276:35361-35367(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF HIS-72; HIS-109; HIS-127; HIS-145; HIS-158; HIS-162; HIS-180; HIS-249; HIS-326; HIS-339 AND GLY-430, REGULATION BY PROTONS AND ZINC.
Mutagenesisⁱ	127 – 127	1	H → A: No effect on pH dependence and function. 1 Publication Manual assertion based on experiment inⁱ Ref.4 "Zn2+ and H+ are coactivators of acid-sensing ion channels." Baron A., Schaefer L., Lingueglia E., Champigny G., Lazdunski M. J. Biol. Chem. 276:35361-35367(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF HIS-72; HIS-109; HIS-127; HIS-145; HIS-158; HIS-162; HIS-180; HIS-249; HIS-326; HIS-339 AND GLY-430, REGULATION BY PROTONS AND ZINC.
Mutagenesisⁱ	145 – 145	1	H → A: No effect on pH dependence and function. 1 Publication Manual assertion based on experiment inⁱ Ref.4 "Zn2+ and H+ are coactivators of acid-sensing ion channels." Baron A., Schaefer L., Lingueglia E., Champigny G., Lazdunski M. J. Biol. Chem. 276:35361-35367(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF HIS-72; HIS-109; HIS-127; HIS-145; HIS-158; HIS-162; HIS-180; HIS-249; HIS-326; HIS-339 AND GLY-430, REGULATION BY PROTONS AND ZINC.
Mutagenesisⁱ	158 – 158	1	H → A: No effect on pH dependence and function. 1 Publication Manual assertion based on experiment inⁱ Ref.4 "Zn2+ and H+ are coactivators of acid-sensing ion channels." Baron A., Schaefer L., Lingueglia E., Champigny G., Lazdunski M. J. Biol. Chem. 276:35361-35367(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF HIS-72; HIS-109; HIS-127; HIS-145; HIS-158; HIS-162; HIS-180; HIS-249; HIS-326; HIS-339 AND GLY-430, REGULATION BY PROTONS AND ZINC.
Mutagenesisⁱ	162 – 162	1	H → A: Loss of potentiation by Zn(2+). 1 Publication Manual assertion based on experiment inⁱ Ref.4 "Zn2+ and H+ are coactivators of acid-sensing ion channels." Baron A., Schaefer L., Lingueglia E., Champigny G., Lazdunski M. J. Biol. Chem. 276:35361-35367(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF HIS-72; HIS-109; HIS-127; HIS-145; HIS-158; HIS-162; HIS-180; HIS-249; HIS-326; HIS-339 AND GLY-430, REGULATION BY PROTONS AND ZINC.
Mutagenesisⁱ	180 – 180	1	H → A: No effect on pH dependence and function. 1 Publication Manual assertion based on experiment inⁱ Ref.4 "Zn2+ and H+ are coactivators of acid-sensing ion channels." Baron A., Schaefer L., Lingueglia E., Champigny G., Lazdunski M. J. Biol. Chem. 276:35361-35367(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF HIS-72; HIS-109; HIS-127; HIS-145; HIS-158; HIS-162; HIS-180; HIS-249; HIS-326; HIS-339 AND GLY-430, REGULATION BY PROTONS AND ZINC.
Mutagenesisⁱ	249 – 249	1	H → A: No effect on pH dependence and function. 1 Publication Manual assertion based on experiment inⁱ Ref.4 "Zn2+ and H+ are coactivators of acid-sensing ion channels." Baron A., Schaefer L., Lingueglia E., Champigny G., Lazdunski M. J. Biol. Chem. 276:35361-35367(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF HIS-72; HIS-109; HIS-127; HIS-145; HIS-158; HIS-162; HIS-180; HIS-249; HIS-326; HIS-339 AND GLY-430, REGULATION BY PROTONS AND ZINC.
Mutagenesisⁱ	326 – 326	1	H → A: No effect on pH dependence and function. 1 Publication Manual assertion based on experiment inⁱ Ref.4 "Zn2+ and H+ are coactivators of acid-sensing ion channels." Baron A., Schaefer L., Lingueglia E., Champigny G., Lazdunski M. J. Biol. Chem. 276:35361-35367(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF HIS-72; HIS-109; HIS-127; HIS-145; HIS-158; HIS-162; HIS-180; HIS-249; HIS-326; HIS-339 AND GLY-430, REGULATION BY PROTONS AND ZINC.
Mutagenesisⁱ	339 – 339	1	H → A: Loss of potentiation by Zn(2+). 1 Publication Manual assertion based on experiment inⁱ Ref.4 "Zn2+ and H+ are coactivators of acid-sensing ion channels." Baron A., Schaefer L., Lingueglia E., Champigny G., Lazdunski M. J. Biol. Chem. 276:35361-35367(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF HIS-72; HIS-109; HIS-127; HIS-145; HIS-158; HIS-162; HIS-180; HIS-249; HIS-326; HIS-339 AND GLY-430, REGULATION BY PROTONS AND ZINC.
Mutagenesisⁱ	365 – 365	1	N → S: Reduces N-glycosylation. Abolishes N-glycosylation; when associated with S-392. 1 Publication Manual assertion based on experiment inⁱ Ref.8 "Analysis of the membrane topology of the acid-sensing ion channel 2a." Saugstad J.A., Roberts J.A., Dong J., Zeitouni S., Evans R.J. J. Biol. Chem. 279:55514-55519(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-365 AND ASN-392, MUTAGENESIS OF LYS-4; ASN-22; PRO-37; ARG-63; TYR-67; HIS-72; ALA-81; ASN-365; ASN-392; TYR-414; 423-TYR--VAL-425; 453-TYR--TYR-455; ASN-478 AND ASN-487, TOPOLOGY.
Mutagenesisⁱ	392 – 392	1	N → S: Reduces N-glycosylation. Abolishes N-glycosylation; when associated with S-365. 1 Publication Manual assertion based on experiment inⁱ Ref.8 "Analysis of the membrane topology of the acid-sensing ion channel 2a." Saugstad J.A., Roberts J.A., Dong J., Zeitouni S., Evans R.J. J. Biol. Chem. 279:55514-55519(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-365 AND ASN-392, MUTAGENESIS OF LYS-4; ASN-22; PRO-37; ARG-63; TYR-67; HIS-72; ALA-81; ASN-365; ASN-392; TYR-414; 423-TYR--VAL-425; 453-TYR--TYR-455; ASN-478 AND ASN-487, TOPOLOGY.
Mutagenesisⁱ	414 – 414	1	Y → N: Increases N-glycosylation. 1 Publication Manual assertion based on experiment inⁱ Ref.8 "Analysis of the membrane topology of the acid-sensing ion channel 2a." Saugstad J.A., Roberts J.A., Dong J., Zeitouni S., Evans R.J. J. Biol. Chem. 279:55514-55519(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-365 AND ASN-392, MUTAGENESIS OF LYS-4; ASN-22; PRO-37; ARG-63; TYR-67; HIS-72; ALA-81; ASN-365; ASN-392; TYR-414; 423-TYR--VAL-425; 453-TYR--TYR-455; ASN-478 AND ASN-487, TOPOLOGY.
Mutagenesisⁱ	423 – 425	3	YEV → NES: Increases N-glycosylation. 1 Publication Manual assertion based on experiment inⁱ Ref.8 "Analysis of the membrane topology of the acid-sensing ion channel 2a." Saugstad J.A., Roberts J.A., Dong J., Zeitouni S., Evans R.J. J. Biol. Chem. 279:55514-55519(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-365 AND ASN-392, MUTAGENESIS OF LYS-4; ASN-22; PRO-37; ARG-63; TYR-67; HIS-72; ALA-81; ASN-365; ASN-392; TYR-414; 423-TYR--VAL-425; 453-TYR--TYR-455; ASN-478 AND ASN-487, TOPOLOGY.
Mutagenesisⁱ	430 – 430	1	G → C: Partial activation. 2 Publications Manual assertion based on experiment inⁱ Ref.1 "The mammalian degenerin MDEG, an amiloride-sensitive cation channel activated by mutations causing neurodegeneration in Caenorhabditis elegans." Waldmann R., Champigny G., Voilley N., Lauritzen I., Lazdunski M. J. Biol. Chem. 271:10433-10436(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, MUTAGENESIS OF GLY-430 AND SER-443, FUNCTION. Ref.4 "Zn2+ and H+ are coactivators of acid-sensing ion channels." Baron A., Schaefer L., Lingueglia E., Champigny G., Lazdunski M. J. Biol. Chem. 276:35361-35367(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF HIS-72; HIS-109; HIS-127; HIS-145; HIS-158; HIS-162; HIS-180; HIS-249; HIS-326; HIS-339 AND GLY-430, REGULATION BY PROTONS AND ZINC.
Mutagenesisⁱ	430 – 430	1	G → F: Constitutive activation causing cell death. Inactive; when associated with F-443. 2 Publications Manual assertion based on experiment inⁱ Ref.1 "The mammalian degenerin MDEG, an amiloride-sensitive cation channel activated by mutations causing neurodegeneration in Caenorhabditis elegans." Waldmann R., Champigny G., Voilley N., Lauritzen I., Lazdunski M. J. Biol. Chem. 271:10433-10436(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, MUTAGENESIS OF GLY-430 AND SER-443, FUNCTION. Ref.4 "Zn2+ and H+ are coactivators of acid-sensing ion channels." Baron A., Schaefer L., Lingueglia E., Champigny G., Lazdunski M. J. Biol. Chem. 276:35361-35367(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF HIS-72; HIS-109; HIS-127; HIS-145; HIS-158; HIS-162; HIS-180; HIS-249; HIS-326; HIS-339 AND GLY-430, REGULATION BY PROTONS AND ZINC.
Mutagenesisⁱ	430 – 430	1	G → K or T: Constitutive activation causing cell death. 2 Publications Manual assertion based on experiment inⁱ Ref.1 "The mammalian degenerin MDEG, an amiloride-sensitive cation channel activated by mutations causing neurodegeneration in Caenorhabditis elegans." Waldmann R., Champigny G., Voilley N., Lauritzen I., Lazdunski M. J. Biol. Chem. 271:10433-10436(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, MUTAGENESIS OF GLY-430 AND SER-443, FUNCTION. Ref.4 "Zn2+ and H+ are coactivators of acid-sensing ion channels." Baron A., Schaefer L., Lingueglia E., Champigny G., Lazdunski M. J. Biol. Chem. 276:35361-35367(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF HIS-72; HIS-109; HIS-127; HIS-145; HIS-158; HIS-162; HIS-180; HIS-249; HIS-326; HIS-339 AND GLY-430, REGULATION BY PROTONS AND ZINC.
Mutagenesisⁱ	430 – 430	1	G → S: No constitutive activation. 2 Publications Manual assertion based on experiment inⁱ Ref.1 "The mammalian degenerin MDEG, an amiloride-sensitive cation channel activated by mutations causing neurodegeneration in Caenorhabditis elegans." Waldmann R., Champigny G., Voilley N., Lauritzen I., Lazdunski M. J. Biol. Chem. 271:10433-10436(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, MUTAGENESIS OF GLY-430 AND SER-443, FUNCTION. Ref.4 "Zn2+ and H+ are coactivators of acid-sensing ion channels." Baron A., Schaefer L., Lingueglia E., Champigny G., Lazdunski M. J. Biol. Chem. 276:35361-35367(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF HIS-72; HIS-109; HIS-127; HIS-145; HIS-158; HIS-162; HIS-180; HIS-249; HIS-326; HIS-339 AND GLY-430, REGULATION BY PROTONS AND ZINC.
Mutagenesisⁱ	430 – 430	1	G → V: Constitutive activation causing cell death. Activated at lower pH; when associated with A-72. 2 Publications Manual assertion based on experiment inⁱ Ref.1 "The mammalian degenerin MDEG, an amiloride-sensitive cation channel activated by mutations causing neurodegeneration in Caenorhabditis elegans." Waldmann R., Champigny G., Voilley N., Lauritzen I., Lazdunski M. J. Biol. Chem. 271:10433-10436(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, MUTAGENESIS OF GLY-430 AND SER-443, FUNCTION. Ref.4 "Zn2+ and H+ are coactivators of acid-sensing ion channels." Baron A., Schaefer L., Lingueglia E., Champigny G., Lazdunski M. J. Biol. Chem. 276:35361-35367(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF HIS-72; HIS-109; HIS-127; HIS-145; HIS-158; HIS-162; HIS-180; HIS-249; HIS-326; HIS-339 AND GLY-430, REGULATION BY PROTONS AND ZINC.
Mutagenesisⁱ	443 – 443	1	S → F: Loss of function. Inactive; when associated with F-430. 1 Publication Manual assertion based on experiment inⁱ Ref.1 "The mammalian degenerin MDEG, an amiloride-sensitive cation channel activated by mutations causing neurodegeneration in Caenorhabditis elegans." Waldmann R., Champigny G., Voilley N., Lauritzen I., Lazdunski M. J. Biol. Chem. 271:10433-10436(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, MUTAGENESIS OF GLY-430 AND SER-443, FUNCTION.
Mutagenesisⁱ	453 – 455	3	YIY → NIS: No effect on N-glycosylation. 1 Publication Manual assertion based on experiment inⁱ Ref.8 "Analysis of the membrane topology of the acid-sensing ion channel 2a." Saugstad J.A., Roberts J.A., Dong J., Zeitouni S., Evans R.J. J. Biol. Chem. 279:55514-55519(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-365 AND ASN-392, MUTAGENESIS OF LYS-4; ASN-22; PRO-37; ARG-63; TYR-67; HIS-72; ALA-81; ASN-365; ASN-392; TYR-414; 423-TYR--VAL-425; 453-TYR--TYR-455; ASN-478 AND ASN-487, TOPOLOGY.
Mutagenesisⁱ	478 – 478	1	N → S: No effect on N-glycosylation. 1 Publication Manual assertion based on experiment inⁱ Ref.8 "Analysis of the membrane topology of the acid-sensing ion channel 2a." Saugstad J.A., Roberts J.A., Dong J., Zeitouni S., Evans R.J. J. Biol. Chem. 279:55514-55519(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-365 AND ASN-392, MUTAGENESIS OF LYS-4; ASN-22; PRO-37; ARG-63; TYR-67; HIS-72; ALA-81; ASN-365; ASN-392; TYR-414; 423-TYR--VAL-425; 453-TYR--TYR-455; ASN-478 AND ASN-487, TOPOLOGY.
Mutagenesisⁱ	487 – 487	1	N → S: No effect on N-glycosylation. 1 Publication Manual assertion based on experiment inⁱ Ref.8 "Analysis of the membrane topology of the acid-sensing ion channel 2a." Saugstad J.A., Roberts J.A., Dong J., Zeitouni S., Evans R.J. J. Biol. Chem. 279:55514-55519(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-365 AND ASN-392, MUTAGENESIS OF LYS-4; ASN-22; PRO-37; ARG-63; TYR-67; HIS-72; ALA-81; ASN-365; ASN-392; TYR-414; 423-TYR--VAL-425; 453-TYR--TYR-455; ASN-478 AND ASN-487, TOPOLOGY.

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Chainⁱ	1 – 512	512	Acid-sensing ion channel 2		PRO_0000181292	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description
Modified residueⁱ	8 – 8	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.10 "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues." Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V. Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-11, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	11 – 11	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.10 "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues." Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V. Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-11, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 – 365	1	N-linked (GlcNAc...)1 Publication Manual assertion based on experiment inⁱ Ref.8 "Analysis of the membrane topology of the acid-sensing ion channel 2a." Saugstad J.A., Roberts J.A., Dong J., Zeitouni S., Evans R.J. J. Biol. Chem. 279:55514-55519(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-365 AND ASN-392, MUTAGENESIS OF LYS-4; ASN-22; PRO-37; ARG-63; TYR-67; HIS-72; ALA-81; ASN-365; ASN-392; TYR-414; 423-TYR--VAL-425; 453-TYR--TYR-455; ASN-478 AND ASN-487, TOPOLOGY.
Glycosylationⁱ	392 – 392	1	N-linked (GlcNAc...)1 Publication Manual assertion based on experiment inⁱ Ref.8 "Analysis of the membrane topology of the acid-sensing ion channel 2a." Saugstad J.A., Roberts J.A., Dong J., Zeitouni S., Evans R.J. J. Biol. Chem. 279:55514-55519(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-365 AND ASN-392, MUTAGENESIS OF LYS-4; ASN-22; PRO-37; ARG-63; TYR-67; HIS-72; ALA-81; ASN-365; ASN-392; TYR-414; 423-TYR--VAL-425; 453-TYR--TYR-455; ASN-478 AND ASN-487, TOPOLOGY.

Sites

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Siteⁱ	478 – 478	1	Not glycosylated
Siteⁱ	487 – 487	1	Not glycosylated

Keywords - PTMⁱ

Disulfide bond, Glycoprotein, Phosphoprotein

PTM databases

iPTMnetⁱ	Q62962.
PhosphoSiteⁱ	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

Gene expression databases

Bgeeⁱ	ENSRNOG00000007019.

Bgeeⁱ

ENSRNOG00000007019.

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.By similarity4 Publications

Protein-protein interaction databases

DIPⁱ	DIP-41193N.
MINTⁱ	MINT-223656.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q62962.
SMRⁱ	Q62962. Positions 40-453.
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 helix

Phylogenomic databases

HOGENOMⁱ	HOG000247010.
HOVERGENⁱ	HBG004150.
InParanoidⁱ	Q62962.
KOⁱ	K04828.
PhylomeDBⁱ	Q62962.
TreeFamⁱ	TF330663.

Family and domain databases

InterProⁱ	IPR004724. ENaC. IPR001873. Na+channel_ASC. IPR020903. Na+channel_ASC_CS. [Graphical view]
PANTHERⁱ	PTHR11690. PTHR11690. 1 hit.
Pfamⁱ	PF00858. ASC. 1 hit. [Graphical view]
PRINTSⁱ	PR01078. AMINACHANNEL.
TIGRFAMsⁱ	TIGR00859. ENaC. 1 hit.
PROSITEⁱ	PS01206. ASC. 1 hit. [Graphical view]

Sequences (2)ⁱ

Sequence statusⁱ: Complete.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket Added to basket

Isoform 1 (identifier: Q62962-1) [UniParc]FASTA Add to basket

Also known as: Mdeg1, 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.

« 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

Checksum:ⁱ38D0A77C3C430B03

GO

Isoform 2 (identifier: Q62962-2) [UniParc]FASTA Add to basket

Also known as: Mdeg2, Asic2b

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

« Hide

        10         20         30         40         50
MSRSGGARLP ATALSGPGRF RMAREQPAPV AVAAARQPGG DRSGDPALQG 
        60         70         80         90        100
PGVARRGRPS LSRTKLHGLR HMCAGRTAAG GSFQRRALWV LAFCTSLGLL 
       110        120        130        140        150
LSWSSNRLLY WLSFPSHTRV HREWSRQLPF PAVTVCNNNP LRFPRLSKGD 
       160        170        180        190        200
LYYAGHWLGL LLPNRTARPL VSELLRGDEP RRQWFRKLAD FRLFLPPRHF 
       210        220        230        240        250
EGISAAFMDR LGHQLEDMLL SCKYRGELCG PHNFSSVFTK YGKCYMFNSG 
       260        270        280        290        300
EDGKPLLTTV KGGTGNGLEI MLDIQQDEYL PIWGETEETT FEAGVKVQIH 
       310        320        330        340        350
SQSEPPFIQE LGFGVAPGFQ TFVATQEQRL TYLPPPWGEC RSSEMGLDFF 
       360        370        380        390        400
PVYSITACRI DCETRYIVEN CNCRMVHMPG DAPFCTPEQH KECAEPALGL 
       410        420        430        440        450
LAEKDSNYCL CRTPCNLTRY NKELSMVKIP SKTSAKYLEK KFNKSEKYIS 
       460        470        480        490        500
ENILVLDIFF EALNYETIEQ KKAYEVAALL GDIGGQMGLF IGASLLTILE 
       510        520        530        540        550
LFDYIYELIK EKLLDLLGKE EEEGSHDENM STCDTMPNHS ETISHTVNVP 
       560 
LQTALGTLEE IAC

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

Alternative sequence

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Alternative sequenceⁱ	1 – 184	184	Missing in isoform 2. 1 Publication Manual assertion based on opinion inⁱ Ref.2 "A modulatory subunit of acid sensing ion channels in brain and dorsal root ganglion cells." Lingueglia E., de Weille J.R., Bassilana F., Heurteaux C., Sakai H., Waldmann R., Lazdunski M. J. Biol. Chem. 272:29778-29783(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, OLIGOMERIZATION, INTERACTION WITH ASIC3.		VSP_015594	Add BLAST
Alternative sequenceⁱ	185 – 185	1	T → MSRSGGARLPATALSGPGRF RMAREQPAPVAVAAARQPGG DRSGDPALQGPGVARRGRPS LSRTKLHGLRHMCAGRTAAG GSFQRRALWVLAFCTSLGLL LSWSSNRLLYWLSFPSHTRV HREWSRQLPFPAVTVCNNNP LRFPRLSKGDLYYAGHWLGL LLPNRTARPLVSELLRGDEP RRQWFRKLADFRLFLPPRHF EGISAAFMDRLGHQLEDMLL SCKYRGELCGPHNFSS in isoform 2. 1 Publication Manual assertion based on opinion inⁱ Ref.2 "A modulatory subunit of acid sensing ion channels in brain and dorsal root ganglion cells." Lingueglia E., de Weille J.R., Bassilana F., Heurteaux C., Sakai H., Waldmann R., Lazdunski M. J. Biol. Chem. 272:29778-29783(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, OLIGOMERIZATION, INTERACTION WITH ASIC3.		VSP_015595

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 splicing

Cross-referencesⁱ

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.

3D structure databases

ProteinModelPortalⁱ	Q62962.
SMRⁱ	Q62962. Positions 40-453.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

DIPⁱ	DIP-41193N.
MINTⁱ	MINT-223656.

Protein family/group databases

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

TCDBⁱ

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

PTM databases

iPTMnetⁱ	Q62962.
PhosphoSiteⁱ	Q62962.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

GeneIDⁱ	25364.
KEGGⁱ	rno:25364.

Organism-specific databases

CTDⁱ	40.
RGDⁱ	2017. Asic2.

Phylogenomic databases

HOGENOMⁱ	HOG000247010.
HOVERGENⁱ	HBG004150.
InParanoidⁱ	Q62962.
KOⁱ	K04828.
PhylomeDBⁱ	Q62962.
TreeFamⁱ	TF330663.

Miscellaneous databases

PROⁱ	Q62962.

PROⁱ

Q62962.

Gene expression databases

Bgeeⁱ	ENSRNOG00000007019.

Bgeeⁱ

ENSRNOG00000007019.

Family and domain databases

InterProⁱ	IPR004724. ENaC. IPR001873. Na+channel_ASC. IPR020903. Na+channel_ASC_CS. [Graphical view]
PANTHERⁱ	PTHR11690. PTHR11690. 1 hit.
Pfamⁱ	PF00858. ASC. 1 hit. [Graphical view]
PRINTSⁱ	PR01078. AMINACHANNEL.
TIGRFAMsⁱ	TIGR00859. ENaC. 1 hit.
PROSITEⁱ	PS01206. ASC. 1 hit. [Graphical view]
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ

ASIC2_RAT

Accessionⁱ

Primary (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:	September 7, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]

Entry statusⁱ

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Miscellaneousⁱ

Miscellaneous

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

Keywords - Technical termⁱ

Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families

Similar proteinsⁱ

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:

100%	UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%	UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%	UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q62962 (ASIC2_RAT)

UniProt

Q62962 - ASIC2_RAT

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Acid-sensing ion channel 2

Select a section on the left to see content.

<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functioni

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Protein family/group databases

<p>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><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>Provides information on the location and the topology of the mature protein in the cell.</p><p><a href='../manual/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>Provides information on the disease(s) and phenotype(s) associated with a protein.</p><p><a href='../manual/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>Describes post-translational modifications (PTMs) and/or processing events.</p><p><a href='../manual/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Sites

PTM databases

<p>Provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.</p><p><a href='../manual/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>Provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.</p><p><a href='../manual/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>Provides information on the tertiary and secondary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>Provides information on sequence similarities with other proteins and the domain(s) present in a protein.</p><p><a href='../manual/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>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 length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequences (2)i

Alternative sequence

Sequence databases

Genome annotation databases

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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Documents

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequences (2)ⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ