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Protein

Acid-sensing ion channel 1A

Gene

asic1a

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: -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.1 Publication

Enzyme regulationi

Inhibited by the diuretic amiloride.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei76Important for channel gatingBy similarity1
Sitei84Important for channel desensitizingBy similarity1
Sitei291Important for channel gatingBy similarity1

GO - Molecular functioni

  • acid-sensing ion channel activity Source: UniProtKB
  • cation channel activity Source: ZFIN
  • ligand-gated sodium channel activity Source: ZFIN

GO - Biological processi

Keywordsi

Molecular functionIon channel, Sodium channel
Biological processIon transport, Sodium transport, Transport
LigandSodium

Enzyme and pathway databases

ReactomeiR-DRE-2672351 Stimuli-sensing channels

Names & Taxonomyi

Protein namesi
Recommended name:
Acid-sensing ion channel 1A
Short name:
ASIC1-A
Alternative name(s):
Acid-sensing ion channel 1.2-A
Amiloride-sensitive cation channel 2-B, neuronal-A
ZASIC1.2
Gene namesi
Name:asic1a
Synonyms:accn2b
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
Proteomesi
  • UP000000437 Componenti: Chromosome 8

Organism-specific databases

ZFINiZDB-GENE-040513-2 asic1a

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; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 50CytoplasmicBy similarityAdd BLAST50
Transmembranei51 – 74HelicalBy similarityAdd BLAST24
Topological domaini75 – 429ExtracellularBy similarityAdd BLAST355
Transmembranei430 – 456Discontinuously helicalBy similarityAdd BLAST27
Topological domaini457 – 501CytoplasmicBy similarityAdd BLAST45

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001812971 – 501Acid-sensing ion channel 1AAdd BLAST501

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi98 ↔ 199By similarity
Glycosylationi164N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi177 ↔ 184By similarity
Disulfide bondi294 ↔ 369By similarity
Disulfide bondi312 ↔ 365By similarity
Disulfide bondi316 ↔ 363By similarity
Disulfide bondi325 ↔ 347By similarity
Disulfide bondi327 ↔ 339By similarity
Glycosylationi370N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ708S7
PRIDEiQ708S7

Expressioni

Tissue specificityi

Expressed in central nervous system. Faintly expressed in the trunk, presumably in dorsal root ganglia.1 Publication

Developmental stagei

First detected 48 hours post-fertilization (hpf) in the ventral thalamus, ventral midbrain, ventral cerebellum, ventral hindbrain, dorsal thalamus, hypothalamus, telencephalon, along the tract of the anterior commissure. Weakly expressed in the dorsal midbrain and olfactory bulb. Expression increases by 96 hpf and is detected in the tectum and trunk.1 Publication

Gene expression databases

BgeeiENSDARG00000008329
ExpressionAtlasiQ708S7 baseline

Interactioni

Subunit structurei

Homotrimer or heterotrimer with other ASIC proteins (By similarity). Interacts with asic1/accn2c.By similarity1 Publication

Protein-protein interaction databases

STRINGi7955.ENSDARP00000011782

Structurei

3D structure databases

ProteinModelPortaliQ708S7
SMRiQ708S7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi446 – 448Selectivity 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 (By similarity).By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4294 Eukaryota
ENOG410ZNFK LUCA
GeneTreeiENSGT00760000119120
HOGENOMiHOG000247010
HOVERGENiHBG004150
KOiK04829
OMAiHTPWTLE
OrthoDBiEOG091G053J
PhylomeDBiQ708S7
TreeFamiTF330663

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

Sequencei

Sequence statusi: Complete.

Q708S7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTSVMDLKV EPMDIDFDQP PPLQVFAHTS TLHGISHIFS YEKITAKCCL
60 70 80 90 100
WVVFFLSSLT FLMYVCIDRI QFYLEYPHVT KLDEITTPVM VFPAVTICNL
110 120 130 140 150
NSIRFSRITR NDLYHAGELL ALLNSRHEVR EAHLVEESVM EVLKSKTDFR
160 170 180 190 200
SFKPRHFNMW EFYNRTGHDI KDMLLSCQFR GSPCRPEDFS VVFTRYGKCY
210 220 230 240 250
TFNSGETGPP RVSVKGGMGN GLEIMLDIQQ DEYLPVWGES DESSFEAGIK
260 270 280 290 300
VQIHSQDEPP FIDQLGFGVA PGFQTFVSCQ EQRLVYLPAP WGSCKSTPPS
310 320 330 340 350
SDYFRAYSIS ACRTDCETRY LVENCNCRMV HMPGDAPYCT PVLYKECAHP
360 370 380 390 400
ALDFLVETDS DYCSCETPCN ITRYSKELSF VKIPSKASVK YLAKKYSKSE
410 420 430 440 450
KYITENVMVL DVFFEALNYE TIEQRKAYEV AGLLGDIGGQ MGLFIGASIL
460 470 480 490 500
TILELFDYLY EVMKYRLCRC SNKKHHNNNN NTDHNAVFSL DDVNCHVSKF

H
Length:501
Mass (Da):57,419
Last modified:July 5, 2004 - v1
Checksum:i5CF87EC031A87CF3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ609616 mRNA Translation: CAE81919.1
RefSeqiNP_999955.1, NM_214790.2
XP_009302015.1, XM_009303740.2
UniGeneiDr.98481

Genome annotation databases

EnsembliENSDART00000004588; ENSDARP00000011782; ENSDARG00000008329
GeneIDi791696
KEGGidre:791696

Similar proteinsi

Entry informationi

Entry nameiASI1A_DANRE
AccessioniPrimary (citable) accession number: Q708S7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: July 5, 2004
Last modified: March 28, 2018
This is version 98 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health