ASIC5_RAT
ID ASIC5_RAT Reviewed; 495 AA.
AC Q9R0W5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 113.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF ALA-443, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; 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).
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.
CC {ECO:0000269|PubMed:10457052}.
CC -!- SUBUNIT: Homotrimer or heterotrimer with other ASIC proteins.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10457052};
CC Multi-pass membrane protein {ECO:0000269|PubMed:10457052}.
CC -!- TISSUE SPECIFICITY: Detected in brain, liver, duodenum, jejunum, ileum
CC and testis. {ECO:0000269|PubMed:10457052}.
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; Y19034; CAB54072.1; -; mRNA.
DR RefSeq; NP_071563.1; NM_022227.1.
DR AlphaFoldDB; Q9R0W5; -.
DR SMR; Q9R0W5; -.
DR STRING; 10116.ENSRNOP00000016039; -.
DR BindingDB; Q9R0W5; -.
DR ChEMBL; CHEMBL3621030; -.
DR TCDB; 1.A.6.1.3; the epithelial na(+) channel (enac) family.
DR GlyGen; Q9R0W5; 2 sites.
DR PaxDb; Q9R0W5; -.
DR Ensembl; ENSRNOT00000016039; ENSRNOP00000016039; ENSRNOG00000011842.
DR GeneID; 63866; -.
DR KEGG; rno:63866; -.
DR UCSC; RGD:69295; rat.
DR CTD; 51802; -.
DR RGD; 69295; Asic5.
DR eggNOG; KOG4294; Eukaryota.
DR GeneTree; ENSGT00940000160549; -.
DR HOGENOM; CLU_020415_4_0_1; -.
DR InParanoid; Q9R0W5; -.
DR OMA; QNFSIAE; -.
DR OrthoDB; 686369at2759; -.
DR PhylomeDB; Q9R0W5; -.
DR TreeFam; TF330663; -.
DR Reactome; R-RNO-2672351; Stimuli-sensing channels.
DR PRO; PR:Q9R0W5; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000011842; Expressed in liver and 1 other tissue.
DR Genevisible; Q9R0W5; RN.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015280; F:ligand-gated sodium channel activity; IDA:RGD.
DR GO; GO:0015252; F:proton channel activity; ISO:RGD.
DR GO; GO:0005272; F:sodium channel activity; ISO:RGD.
DR GO; GO:0035725; P:sodium ion transmembrane transport; ISO:RGD.
DR InterPro; IPR001873; ENaC.
DR PANTHER; PTHR11690; PTHR11690; 1.
DR Pfam; PF00858; ASC; 1.
DR PRINTS; PR01078; AMINACHANNEL.
PE 1: Evidence at protein 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_0000335599"
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"
FT MUTAGEN 443
FT /note="A->C,S: Minimal channel activation."
FT /evidence="ECO:0000269|PubMed:10457052"
FT MUTAGEN 443
FT /note="A->F,T,V: Activates the channel."
FT /evidence="ECO:0000269|PubMed:10457052"
FT MUTAGEN 443
FT /note="A->K: Partial channel activation."
FT /evidence="ECO:0000269|PubMed:10457052"
SQ SEQUENCE 495 AA; 56464 MW; FAB265F495EA02AE CRC64;
MEHTEKSKGP AEKGLLGKIR RYLSKRPLPS PTDRKKFDHD FAISTSFHGI HNIAQNQNKV
RKVIWLSVVL GSVSLLVWQI YSRLVNYFMW PTTTSIEVQY VEKIEFPAVT FCNLNRFQTE
AVSRFGIIFF LWDIVSKVLR LQEISGNNTG SPEALDFVAS HRNFSITEFV KNNGFYLNHD
TLVHCEFFGK TCDPKDFKHV FTEYGNCFTF NYGENVQSKN KVSVSGRGLK LLLDVHQEEF
TDNPVPGFAD AGVIFVIHSP KKEPQFDGLG LSSPVGMHAR VTIRQLKTIH QEYPWGECNP
DIKLRNFTTY STYGCLKECK AKHIQRLCGC LPFLLPGNGV ECDLLKYYNC VSPILDHIER
KGLCTMGTHN SSCPVPCEET EYPATIAYST FPSQRATKFL AKKLNQSQEY IRENLVNIEI
NYSDLNYKIT QQQKAVSVPE LLADVGGQLG LFCGASLITI IEIIEYLFTS FYWVFIFFLL
KILEMIQRTS PPQTV
