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Protein

Acid-sensing ion channel 1

Gene

ASIC1

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.5 Publications

Enzyme regulationi

Inhibited by the diuretic amiloride. Inhibited by Cs1+ ions. Inhibited by spider venom psalmotoxin 1; this locks the channel into its desensitized conformation. Channel activity is increased by the heterodimeric snake venom neurotoxin composed of MitTx-alpha and MitTx-beta. This slows channel closure and increases the magnitude of the steady-state current that is triggered by low pH.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei72 – 721Important for channel gating
Sitei80 – 801Important for channel desensitizing
Sitei288 – 2881Important for channel gating

GO - Molecular functioni

  • acid-sensing ion channel activity Source: UniProtKB
  • ion gated channel activity Source: Ensembl

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Sodium channel

Keywords - Biological processi

Ion transport, Sodium transport, Transport

Keywords - Ligandi

Sodium

Enzyme and pathway databases

ReactomeiR-GGA-2672351. Stimuli-sensing channels.

Protein family/group databases

TCDBi1.A.6.1.5. the epithelial na(+) channel (enac) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Acid-sensing ion channel 1
Short name:
ASIC1
Alternative name(s):
Amiloride-sensitive cation channel 2, neuronal
Gene namesi
Name:ASIC1
Synonyms:ACCN2
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4646CytoplasmicAdd
BLAST
Transmembranei47 – 7024HelicalAdd
BLAST
Topological domaini71 – 426356ExtracellularAdd
BLAST
Transmembranei427 – 45327Discontinuously helicalAdd
BLAST
Topological domaini454 – 52774CytoplasmicAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: UniProtKB
  • synapse Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1 – 2525Missing : Impairs channel activity; when associated with missing 464-L--C-527. 2 PublicationsAdd
BLAST
Mutagenesisi1 – 1313Missing : No effect on channel activity; when associated with missing 464-L--C-527. 1 PublicationAdd
BLAST
Mutagenesisi80 – 801E → A: Strongly increases speed of desensitation. 1 Publication
Mutagenesisi464 – 52764Missing : No effect on channel activity; when associated with missing 1-M--S-13. Impairs channel activity; when associated with missing 1-M--S-25. 3 PublicationsAdd
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 527527Acid-sensing ion channel 1PRO_0000308417Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi94 ↔ 195Combined sources5 Publications
Disulfide bondi173 ↔ 180Combined sources5 Publications
Disulfide bondi291 ↔ 366Combined sources5 Publications
Disulfide bondi309 ↔ 362Combined sources5 Publications
Disulfide bondi313 ↔ 360Combined sources5 Publications
Disulfide bondi322 ↔ 344Combined sources5 Publications
Disulfide bondi324 ↔ 336Combined sources5 Publications
Glycosylationi367 – 3671N-linked (GlcNAc...)3 Publications
Glycosylationi394 – 3941N-linked (GlcNAc...)3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotrimer. Interacts with spider venom psalmotoxin 1 with a one to one stoichiometry. Interacts with the heterodimeric snake venom neurotoxin composed of MitTx-alpha and MitTx-beta.4 Publications

Protein-protein interaction databases

DIPiDIP-59283N.

Structurei

Secondary structure

1
527
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi45 – 6925Combined sources
Beta strandi74 – 818Combined sources
Beta strandi84 – 874Combined sources
Beta strandi90 – 967Combined sources
Helixi101 – 1033Combined sources
Helixi106 – 1127Combined sources
Turni113 – 1175Combined sources
Beta strandi121 – 1244Combined sources
Helixi134 – 1429Combined sources
Helixi155 – 1628Combined sources
Helixi166 – 1694Combined sources
Beta strandi170 – 1756Combined sources
Helixi182 – 1843Combined sources
Beta strandi185 – 1906Combined sources
Beta strandi193 – 1986Combined sources
Beta strandi203 – 2064Combined sources
Beta strandi212 – 2143Combined sources
Helixi215 – 2173Combined sources
Beta strandi218 – 2247Combined sources
Helixi227 – 2293Combined sources
Beta strandi244 – 2518Combined sources
Helixi259 – 2624Combined sources
Beta strandi264 – 2663Combined sources
Beta strandi270 – 28213Combined sources
Turni286 – 2883Combined sources
Beta strandi301 – 3033Combined sources
Helixi306 – 32217Combined sources
Beta strandi323 – 3253Combined sources
Beta strandi331 – 3333Combined sources
Helixi338 – 3436Combined sources
Helixi345 – 35410Combined sources
Beta strandi357 – 3604Combined sources
Beta strandi365 – 38117Combined sources
Turni383 – 3853Combined sources
Helixi386 – 3938Combined sources
Helixi397 – 4037Combined sources
Beta strandi404 – 42522Combined sources
Helixi427 – 45731Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QTSX-ray1.90A/B/C/D/E/F26-463[»]
3IJ4X-ray3.00A2-466[»]
3S3WX-ray2.60A/B/C26-463[»]
3S3XX-ray2.99A/B/C26-463[»]
4FZ0X-ray2.80A/B/C14-463[»]
4FZ1X-ray3.36A14-463[»]
4NTWX-ray2.07A14-463[»]
4NTXX-ray2.27A14-463[»]
4NTYX-ray2.65A14-463[»]
4NYKX-ray3.00A2-466[»]
ProteinModelPortaliQ1XA76.
SMRiQ1XA76. Positions 41-461.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ1XA76.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi443 – 4453Selectivity filterCurated

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.1 Publication

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00760000119120.
HOGENOMiHOG000247010.
HOVERGENiHBG004150.
InParanoidiQ1XA76.
KOiK04829.
OMAiCESIRGH.
PhylomeDBiQ1XA76.

Family and domain databases

InterProiIPR004724. ENaC.
IPR001873. Na+channel_ASC.
IPR020903. Na+channel_ASC_CS.
[Graphical view]
PANTHERiPTHR11690. PTHR11690. 1 hit.
PfamiPF00858. ASC. 1 hit.
[Graphical view]
PRINTSiPR01078. AMINACHANNEL.
TIGRFAMsiTIGR00859. ENaC. 1 hit.
PROSITEiPS01206. ASC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q1XA76-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMDLKVDEEE VDSGQPVSIQ AFASSSTLHG ISHIFSYERL SLKRVVWALC
60 70 80 90 100
FMGSLALLAL VCTNRIQYYF LYPHVTKLDE VAATRLTFPA VTFCNLNEFR
110 120 130 140 150
FSRVTKNDLY HAGELLALLN NRYEIPDTQT ADEKQLEILQ DKANFRNFKP
160 170 180 190 200
KPFNMLEFYD RAGHDIREML LSCFFRGEQC SPEDFKVVFT RYGKCYTFNA
210 220 230 240 250
GQDGKPRLIT MKGGTGNGLE IMLDIQQDEY LPVWGETDET SFEAGIKVQI
260 270 280 290 300
HSQDEPPLID QLGFGVAPGF QTFVSCQEQR LIYLPPPWGD CKATTGDSEF
310 320 330 340 350
YDTYSITACR IDCETRYLVE NCNCRMVHMP GDAPYCTPEQ YKECADPALD
360 370 380 390 400
FLVEKDNEYC VCEMPCNVTR YGKELSMVKI PSKASAKYLA KKYNKSEQYI
410 420 430 440 450
GENILVLDIF FEALNYETIE QKKAYEVAGL LGDIGGQMGL FIGASILTVL
460 470 480 490 500
ELFDYAYEVI KHRLCRRGKC RKNHKRNNTD KGVALSMDDV KRHNPCESLR
510 520
GHPAGMTYAA NILPHHPARG TFEDFTC
Length:527
Mass (Da):60,010
Last modified:May 2, 2006 - v1
Checksum:i05BF363097F5A63E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY956393 mRNA. Translation: AAY28986.1.
RefSeqiNP_001035557.1. NM_001040467.1.
XP_015155720.1. XM_015300234.1.
XP_015155721.1. XM_015300235.1.
UniGeneiGga.17954.

Genome annotation databases

EnsembliENSGALT00000010093; ENSGALP00000010079; ENSGALG00000006240.
GeneIDi426883.
KEGGigga:426883.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY956393 mRNA. Translation: AAY28986.1.
RefSeqiNP_001035557.1. NM_001040467.1.
XP_015155720.1. XM_015300234.1.
XP_015155721.1. XM_015300235.1.
UniGeneiGga.17954.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QTSX-ray1.90A/B/C/D/E/F26-463[»]
3IJ4X-ray3.00A2-466[»]
3S3WX-ray2.60A/B/C26-463[»]
3S3XX-ray2.99A/B/C26-463[»]
4FZ0X-ray2.80A/B/C14-463[»]
4FZ1X-ray3.36A14-463[»]
4NTWX-ray2.07A14-463[»]
4NTXX-ray2.27A14-463[»]
4NTYX-ray2.65A14-463[»]
4NYKX-ray3.00A2-466[»]
ProteinModelPortaliQ1XA76.
SMRiQ1XA76. Positions 41-461.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59283N.

Protein family/group databases

TCDBi1.A.6.1.5. the epithelial na(+) channel (enac) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000010093; ENSGALP00000010079; ENSGALG00000006240.
GeneIDi426883.
KEGGigga:426883.

Organism-specific databases

CTDi426883.

Phylogenomic databases

GeneTreeiENSGT00760000119120.
HOGENOMiHOG000247010.
HOVERGENiHBG004150.
InParanoidiQ1XA76.
KOiK04829.
OMAiCESIRGH.
PhylomeDBiQ1XA76.

Enzyme and pathway databases

ReactomeiR-GGA-2672351. Stimuli-sensing channels.

Miscellaneous databases

EvolutionaryTraceiQ1XA76.
PROiQ1XA76.

Family and domain databases

InterProiIPR004724. ENaC.
IPR001873. Na+channel_ASC.
IPR020903. Na+channel_ASC_CS.
[Graphical view]
PANTHERiPTHR11690. PTHR11690. 1 hit.
PfamiPF00858. ASC. 1 hit.
[Graphical view]
PRINTSiPR01078. AMINACHANNEL.
TIGRFAMsiTIGR00859. ENaC. 1 hit.
PROSITEiPS01206. ASC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Proton sensitivity of ASIC1 appeared with the rise of fishes by changes of residues in the region that follows TM1 in the ectodomain of the channel."
    Coric T., Zheng D., Gerstein M., Canessa C.M.
    J. Physiol. (Lond.) 568:725-735(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  2. "Structure of acid-sensing ion channel 1 at 1.9 A resolution and low pH."
    Jasti J., Furukawa H., Gonzales E.B., Gouaux E.
    Nature 449:316-323(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 26-463, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-367 AND ASN-394, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF 1-MET--SER-25 AND 464-LEU--CYS-527.
  3. "Pore architecture and ion sites in acid-sensing ion channels and P2X receptors."
    Gonzales E.B., Kawate T., Gouaux E.
    Nature 460:599-604(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-466, DISULFIDE BONDS, FUNCTION, TOPOLOGY, SUBCELLULAR LOCATION, SUBUNIT.
  4. "Structure of the acid-sensing ion channel 1 in complex with the gating modifier Psalmotoxin 1."
    Dawson R.J., Benz J., Stohler P., Tetaz T., Joseph C., Huber S., Schmid G., Hugin D., Pflimlin P., Trube G., Rudolph M.G., Hennig M., Ruf A.
    Nat. Commun. 3:936-936(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 26-463 IN COMPLEX WITH SPIDER VENOM PSALMOTOXIN 1, INTERACTION WITH SPIDER VENOM PSALMOTOXIN, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-367 AND ASN-394, MUTAGENESIS OF 1-MET--SER-25 AND 464-LEU--CYS-527.
  5. "Structural plasticity and dynamic selectivity of acid-sensing ion channel-spider toxin complexes."
    Baconguis I., Gouaux E.
    Nature 489:400-405(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 14-463, GLYCOSYLATION AT ASN-367 AND ASN-394, FUNCTION, ENZYME REGULATION, MUTAGENESIS OF 1-MET--SER-13; GLU-80 AND 464-LEU--CYS-527, DISULFIDE BOND.
  6. "X-Ray structure of acid-sensing ion channel 1-snake toxin complex reveals open state of a Na(+)-selective channel."
    Baconguis I., Bohlen C.J., Goehring A., Julius D., Gouaux E.
    Cell 156:717-729(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 14-463 IN COMPLEXES WITH SODIUM IONS; AMILORIDE AND THE HETERODIMERIC SNAKE VENOM NEUROTOXIN COMPOSED OF MITTX-ALPHA AND MITTX-BETA, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, ENZYME REGULATION, TOPOLOGY, DOMAIN, DISULFIDE BOND.

Entry informationi

Entry nameiASIC1_CHICK
AccessioniPrimary (citable) accession number: Q1XA76
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: May 2, 2006
Last modified: June 8, 2016
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.