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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)DescriptionActionsGraphical viewLength
Sitei72Important for channel gating1
Sitei80Important for channel desensitizing1
Sitei288Important for channel gating1

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)DescriptionActionsGraphical viewLength
Topological domaini1 – 46CytoplasmicAdd BLAST46
Transmembranei47 – 70HelicalAdd BLAST24
Topological domaini71 – 426ExtracellularAdd BLAST356
Transmembranei427 – 453Discontinuously helicalAdd BLAST27
Topological domaini454 – 527CytoplasmicAdd BLAST74

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)DescriptionActionsGraphical viewLength
Mutagenesisi1 – 25Missing : Impairs channel activity; when associated with missing 464-L--C-527. 2 PublicationsAdd BLAST25
Mutagenesisi1 – 13Missing : No effect on channel activity; when associated with missing 464-L--C-527. 1 PublicationAdd BLAST13
Mutagenesisi80E → A: Strongly increases speed of desensitation. 1 Publication1
Mutagenesisi464 – 527Missing : 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 BLAST64

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003084171 – 527Acid-sensing ion channel 1Add BLAST527

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Glycosylationi367N-linked (GlcNAc...)3 Publications1
Glycosylationi394N-linked (GlcNAc...)3 Publications1

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Gene expression databases

BgeeiENSGALG00000006240.

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

1527
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi45 – 69Combined sources25
Beta strandi74 – 81Combined sources8
Beta strandi84 – 87Combined sources4
Beta strandi90 – 96Combined sources7
Helixi101 – 103Combined sources3
Helixi106 – 112Combined sources7
Turni113 – 117Combined sources5
Beta strandi121 – 124Combined sources4
Helixi134 – 142Combined sources9
Helixi155 – 162Combined sources8
Helixi166 – 169Combined sources4
Beta strandi170 – 175Combined sources6
Helixi182 – 184Combined sources3
Beta strandi185 – 190Combined sources6
Beta strandi193 – 198Combined sources6
Beta strandi203 – 206Combined sources4
Beta strandi212 – 214Combined sources3
Helixi215 – 217Combined sources3
Beta strandi218 – 224Combined sources7
Helixi227 – 229Combined sources3
Beta strandi244 – 251Combined sources8
Helixi259 – 262Combined sources4
Beta strandi264 – 266Combined sources3
Beta strandi270 – 282Combined sources13
Turni286 – 288Combined sources3
Beta strandi301 – 303Combined sources3
Helixi306 – 322Combined sources17
Beta strandi323 – 325Combined sources3
Beta strandi331 – 333Combined sources3
Helixi338 – 343Combined sources6
Helixi345 – 354Combined sources10
Beta strandi357 – 360Combined sources4
Beta strandi365 – 381Combined sources17
Turni383 – 385Combined sources3
Helixi386 – 393Combined sources8
Helixi397 – 403Combined sources7
Beta strandi404 – 425Combined sources22
Helixi427 – 457Combined sources31

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ1XA76.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi443 – 445Selectivity filterCurated3

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.
OMAiPCHGHGV.
OrthoDBiEOG091G053J.
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

EnsembliENSGALT00000055224; ENSGALP00000057289; ENSGALG00000034025.
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
PDB 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.
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

EnsembliENSGALT00000055224; ENSGALP00000057289; ENSGALG00000034025.
GeneIDi426883.
KEGGigga:426883.

Organism-specific databases

CTDi426883.

Phylogenomic databases

GeneTreeiENSGT00760000119120.
HOGENOMiHOG000247010.
HOVERGENiHBG004150.
InParanoidiQ1XA76.
KOiK04829.
OMAiPCHGHGV.
OrthoDBiEOG091G053J.
PhylomeDBiQ1XA76.

Enzyme and pathway databases

ReactomeiR-GGA-2672351. Stimuli-sensing channels.

Miscellaneous databases

EvolutionaryTraceiQ1XA76.
PROiQ1XA76.

Gene expression databases

BgeeiENSGALG00000006240.

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...

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: November 30, 2016
This is version 85 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.