ASI4A_DANRE
ID ASI4A_DANRE Reviewed; 539 AA.
AC Q708S4;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Acid-sensing ion channel 4-A {ECO:0000305};
DE Short=ASIC4-A {ECO:0000305};
DE AltName: Full=Acid-sensing ion channel 4.1 {ECO:0000303|PubMed:14970195};
DE AltName: Full=Amiloride-sensitive cation channel 4-A;
DE AltName: Full=ZASIC4.1 {ECO:0000303|PubMed:14970195};
GN Name=asic4a {ECO:0000305}; Synonyms=accn4a {ECO:0000305};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP FUNCTION.
RX PubMed=14970195; DOI=10.1074/jbc.m401477200;
RA Paukert M., Sidi S., Russell C., Siba M., Wilson S.W., Nicolson T.,
RA Gruender S.;
RT "A family of acid-sensing ion channels (ASICs) from the zebrafish:
RT widespread e xpression in the central nervous system suggests a conserved
RT role in neuronal communication.";
RL J. Biol. Chem. 279:18783-18791(2004).
CC -!- FUNCTION: Cation channel with high affinity for sodium, which is gated
CC by extracellular protons and inhibited by the diuretic amiloride.
CC {ECO:0000269|PubMed:14970195}.
CC -!- SUBUNIT: Homotrimer or heterotrimer with other ASIC proteins.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in central nervous system.
CC {ECO:0000269|PubMed:14970195}.
CC -!- DEVELOPMENTAL STAGE: First expressed at 48 hours post-fertilization
CC (hpf). Expressed in dorsal midbrain and in retinal ganglion cells.
CC {ECO:0000269|PubMed:14970195}.
CC -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC 1.A.6) family. ASIC4 subfamily. {ECO:0000305}.
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DR EMBL; AJ609619; CAE81922.1; -; mRNA.
DR RefSeq; NP_999952.1; NM_214787.2.
DR AlphaFoldDB; Q708S4; -.
DR SMR; Q708S4; -.
DR STRING; 7955.ENSDARP00000035525; -.
DR TCDB; 1.A.6.1.6; the epithelial na(+) channel (enac) family.
DR PaxDb; Q708S4; -.
DR GeneID; 407668; -.
DR KEGG; dre:407668; -.
DR CTD; 407668; -.
DR ZFIN; ZDB-GENE-040513-5; asic4a.
DR eggNOG; KOG4294; Eukaryota.
DR OrthoDB; 686369at2759; -.
DR PhylomeDB; Q708S4; -.
DR Reactome; R-DRE-2672351; Stimuli-sensing channels.
DR PRO; PR:Q708S4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0045177; C:apical part of cell; ISS:AgBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:ZFIN.
DR GO; GO:0005261; F:cation channel activity; IPI:ZFIN.
DR GO; GO:0015280; F:ligand-gated sodium channel activity; IDA:ZFIN.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; ISS:AgBase.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR InterPro; IPR001873; ENaC.
DR InterPro; IPR020903; ENaC_CS.
DR PANTHER; PTHR11690; PTHR11690; 1.
DR Pfam; PF00858; ASC; 1.
DR PRINTS; PR01078; AMINACHANNEL.
DR PROSITE; PS01206; ASC; 1.
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..539
FT /note="Acid-sensing ion channel 4-A"
FT /id="PRO_0000181307"
FT TOPO_DOM 1..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..432
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..539
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 474..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 116..200
FT /evidence="ECO:0000250"
FT DISULFID 178..185
FT /evidence="ECO:0000250"
FT DISULFID 294..369
FT /evidence="ECO:0000250"
FT DISULFID 313..365
FT /evidence="ECO:0000250"
FT DISULFID 317..363
FT /evidence="ECO:0000250"
FT DISULFID 326..347
FT /evidence="ECO:0000250"
FT DISULFID 328..340
FT /evidence="ECO:0000250"
SQ SEQUENCE 539 AA; 60814 MW; 7F0B1AFAFE18002F CRC64;
MPIEFVCKIK FAEEDEKQKG NQDGDKESLI EESCSPPTKD LAGFASASSL HGINHIFVSG
RLGVRQTLWA LAFLVSLALF LYQAAKCAIS YLEHPHVTAL NEEATPEMVF PAVTICNINR
FRFSALTDAD IYHLANLTGL PPKNKDGHKP TDLEYPAPDM QDIFNRTGHQ LEEMLKSCNF
SGQNCSAEDF TVVYTRYGKC YTFNGNKTTS RKTKQGGMGN GLEIMLDIQQ DDYLPIWKET
NETSLEAGIR VQIHSQDEPP YIHQLGFGVS PGFQTFVSCQ EQRLTYLPQP WGNCRSTSEQ
MIPGYDTYSI SACRLRCETL EVLRECKCRM VHMPGDANIC TPSDIKCVDK ALALLQKSSG
DTCFCETPCN LTRYGKELSM VKIPSKGSAR YLSRKYDKSE DYIRDNFLVL DIFFEALNYE
TIEQKKAYDV AGLLGDIGGQ MGLFIGASVL TILEILDYVY EVIKHRLERL LRPQRDDKKQ
TQQQQQASTV ATVNLEEMKA KDSSEMSRSH SEGAYANTIL PNHHHHHRTH HRVSEDFAC
