ASI4B_DANRE
ID ASI4B_DANRE Reviewed; 558 AA.
AC Q708S3;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Acid-sensing ion channel 4-B {ECO:0000305};
DE Short=ASIC4-B {ECO:0000305};
DE AltName: Full=Acid-sensing ion channel 4.2 {ECO:0000303|PubMed:14970195};
DE AltName: Full=Amiloride-sensitive cation channel 4-B;
DE AltName: Full=ZASIC4.2 {ECO:0000303|PubMed:14970195};
GN Name=asic4b {ECO:0000305}; Synonyms=accn4b;
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, AND 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: Probable cation channel with high affinity for sodium.
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: Expressed along the tract of the anterior
CC commissure between 24 and 30 hours post-fertilization (hpf). At 30 hpf,
CC expressed in cells along the tract of the postoptic commissure.
CC Expressed in preoptic area from 48 hpf until 96 hpf. Expressed in
CC posterior hypothalamus, ventral midbrain, hindbrain and retinal
CC ganglion cells by 48 hpf. These domains of expression persisted and
CC strengthened in older embryos.
CC -!- MISCELLANEOUS: In vitro, has no proton-gated channel activity.
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; AJ609620; CAE81923.1; -; mRNA.
DR RefSeq; NP_999951.1; NM_214786.1.
DR AlphaFoldDB; Q708S3; -.
DR SMR; Q708S3; -.
DR STRING; 7955.ENSDARP00000095487; -.
DR TCDB; 1.A.6.1.7; the epithelial na(+) channel (enac) family.
DR PaxDb; Q708S3; -.
DR Ensembl; ENSDART00000104716; ENSDARP00000095487; ENSDARG00000004243.
DR GeneID; 407667; -.
DR KEGG; dre:407667; -.
DR CTD; 407667; -.
DR ZFIN; ZDB-GENE-040513-6; asic4b.
DR eggNOG; KOG4294; Eukaryota.
DR GeneTree; ENSGT00940000159052; -.
DR HOGENOM; CLU_020415_1_2_1; -.
DR InParanoid; Q708S3; -.
DR OMA; IHEYCDY; -.
DR OrthoDB; 686369at2759; -.
DR PhylomeDB; Q708S3; -.
DR TreeFam; TF330663; -.
DR PRO; PR:Q708S3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 6.
DR Bgee; ENSDARG00000004243; Expressed in retina and 5 other tissues.
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; IBA:GO_Central.
DR GO; GO:0048545; P:response to steroid hormone; IEP:ZFIN.
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..558
FT /note="Acid-sensing ion channel 4-B"
FT /id="PRO_0000181308"
FT TOPO_DOM 1..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..433
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 455..558
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 120..204
FT /evidence="ECO:0000250"
FT DISULFID 182..189
FT /evidence="ECO:0000250"
FT DISULFID 298..373
FT /evidence="ECO:0000250"
FT DISULFID 317..369
FT /evidence="ECO:0000250"
FT DISULFID 321..367
FT /evidence="ECO:0000250"
FT DISULFID 330..351
FT /evidence="ECO:0000250"
FT DISULFID 332..344
FT /evidence="ECO:0000250"
SQ SEQUENCE 558 AA; 62448 MW; 0D74B2474592D7DF CRC64;
MPIEFVCKIK FAEGEEAKGA STEGGGTGML DEGLRRQKEG MADLASFASS SSLHGLARAL
GTSERLGFRQ TLWGLALLVS LGLFLYQATW SAATYLERPH LAALREETRR ELTFPAITLC
NVNRFRFSAL TDADIYHLAN LTGLPPKSRK GHRPSELQYP PPNMLDIFQR TGHQLEDMLK
SCNFSGQNCS SEDFSVVYTR YGKCYTFNGN KTSPKRVRQG GTGNGLEMML DIQQDEYLPI
WRETNETTLE AGIRVQIHSQ NEPPYIHQLG FGVSPGFQTF VSCQEQRLTY LPQPWGNCRA
SSEPVIPGYD TYSVSACRLH CESTQVQREC NCRMVHMPGD ADICAPSKIK CVDKALASLQ
KSTGDSCPCE TPCNLTRYGK ELSMVKIPSR GSARYLSRKY QKSEEYIRDN FLILDIFFEA
LNYETIEQKK AYDIAGLLGD IGGQMGLFIG ASILTILEIL DYIYEVAKNK IKQLLKPKKS
QKQTNQRNLI QEQIQRTKNL REQNLKAQLT AGAIATVRFE EVKVKAANDV AQPHSAHPTS
VLPNHHNAQQ AVQQDFAC
