ASIC5_MOUSE
ID ASIC5_MOUSE Reviewed; 495 AA.
AC Q9R0Y1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Acid-sensing ion channel 5;
DE Short=ASIC5;
DE AltName: Full=Amiloride-sensitive cation channel 5;
DE AltName: Full=Brain-liver-intestine amiloride-sensitive Na(+) channel;
DE Short=BLINaC;
GN Name=Asic5; Synonyms=Accn5, Blinac;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain, Intestine, and Liver;
RX PubMed=10457052; DOI=10.1111/j.1469-7793.1999.0323m.x;
RA Sakai H., Lingueglia E., Champigny G., Mattei M.-G., Lazdunski M.;
RT "Cloning and functional expression of a novel degenerin-like Na+ channel
RT gene in mammals.";
RL J. Physiol. (Lond.) 519:323-333(1999).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=24663811; DOI=10.1371/journal.pone.0091326;
RA Boiko N., Kucher V., Wang B., Stockand J.D.;
RT "Restrictive expression of acid-sensing ion channel 5 (asic5) in unipolar
RT brush cells of the vestibulocerebellum.";
RL PLoS ONE 9:E91326-E91326(2014).
CC -!- FUNCTION: Cation channel that gives rise to very low constitutive
CC currents in the absence of activation. The activated channel exhibits
CC selectivity for sodium and lithium, and is inhibited by amiloride (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer or heterotrimer with other ASIC proteins.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in cerebellum, brainstem, kidney, liver,
CC hepatocytes, lung, intestine and embryo. In the cerebellum. restricted
CC to interneurons in the granular layer, specifically in GRM1-expressing
CC unipolar brush cells of the vestibulocerebellum.
CC {ECO:0000269|PubMed:10457052, ECO:0000269|PubMed:24663811}.
CC -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC 1.A.6) family. ASIC5 subfamily. {ECO:0000305}.
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DR EMBL; Y19035; CAB54040.1; -; mRNA.
DR CCDS; CCDS17428.1; -.
DR RefSeq; NP_067345.1; NM_021370.2.
DR RefSeq; XP_006501884.1; XM_006501821.1.
DR RefSeq; XP_006501886.1; XM_006501823.2.
DR AlphaFoldDB; Q9R0Y1; -.
DR SMR; Q9R0Y1; -.
DR STRING; 10090.ENSMUSP00000029641; -.
DR GlyGen; Q9R0Y1; 2 sites.
DR PhosphoSitePlus; Q9R0Y1; -.
DR PaxDb; Q9R0Y1; -.
DR PRIDE; Q9R0Y1; -.
DR Antibodypedia; 48122; 116 antibodies from 21 providers.
DR DNASU; 58170; -.
DR Ensembl; ENSMUST00000029641; ENSMUSP00000029641; ENSMUSG00000028008.
DR GeneID; 58170; -.
DR KEGG; mmu:58170; -.
DR UCSC; uc008pop.1; mouse.
DR CTD; 51802; -.
DR MGI; MGI:1929259; Asic5.
DR VEuPathDB; HostDB:ENSMUSG00000028008; -.
DR eggNOG; KOG4294; Eukaryota.
DR GeneTree; ENSGT00940000160549; -.
DR InParanoid; Q9R0Y1; -.
DR OMA; QNFSIAE; -.
DR OrthoDB; 686369at2759; -.
DR PhylomeDB; Q9R0Y1; -.
DR TreeFam; TF330663; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR BioGRID-ORCS; 58170; 4 hits in 73 CRISPR screens.
DR PRO; PR:Q9R0Y1; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9R0Y1; protein.
DR Bgee; ENSMUSG00000028008; Expressed in liver and 12 other tissues.
DR ExpressionAtlas; Q9R0Y1; baseline and differential.
DR Genevisible; Q9R0Y1; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IC:MGI.
DR GO; GO:0015280; F:ligand-gated sodium channel activity; ISO:MGI.
DR GO; GO:0015252; F:proton channel activity; IDA:MGI.
DR GO; GO:0005272; F:sodium channel activity; IDA:MGI.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IDA:MGI.
DR InterPro; IPR001873; ENaC.
DR PANTHER; PTHR11690; PTHR11690; 1.
DR Pfam; PF00858; ASC; 1.
DR PRINTS; PR01078; AMINACHANNEL.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Membrane; Reference proteome; Sodium; Sodium channel; Sodium transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..495
FT /note="Acid-sensing ion channel 5"
FT /id="PRO_0000335598"
FT TOPO_DOM 1..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..459
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 481..495
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 112..207
FT /evidence="ECO:0000250"
FT DISULFID 185..192
FT /evidence="ECO:0000250"
FT DISULFID 298..377
FT /evidence="ECO:0000250"
FT DISULFID 315..373
FT /evidence="ECO:0000250"
FT DISULFID 319..364
FT /evidence="ECO:0000250"
FT DISULFID 328..350
FT /evidence="ECO:0000250"
FT DISULFID 330..342
FT /evidence="ECO:0000250"
SQ SEQUENCE 495 AA; 56523 MW; BE710FD1B415A9F1 CRC64;
MEHTEKSQVH AEKGLLGKIK RYLSKRPLPS PTDRKKFDQD FAMSTSFHGI HNIAQNQNKV
RKVIWLAVVL GSVSLLVWQI YSRLVNYFTW PTTTSIEVQY VEKIEFPAVT LCNLNRFQTE
AVSRFGIIFF LWDIVSKVLR LQEISANNTG SPETLDFVTN HQNFSITEFV KNNGFYLNND
TLVHCEFFGK TCSPKDFKHV FTEYGNCFTF NYGENIQNKN KVSVSGRGLK LLLDVHQEEF
TDNPVPGFAD AGVIFVIHSP KKEPQFDGLG LSSPVGMHAR VTIRQLKTVH QEYPWGECNP
NIKLRNFITY STYGCLKECK ARHIQRLCGC LPFLLPGNGV ECDLLEYYNC VSPILDHIER
KGLCTMGTHN SSCPVSCEET EYPATVSYST FPSQRATRFL AKKLNQSQEY IRENLVNIEI
NYSDLNYKIT QQQKAVSVPE LLADVGGQLG LFCGASLITI IEIIEYFFTN FYWVLIFFLL
KILETIQRTS PPQAV
