ASI1B_DANRE
ID ASI1B_DANRE Reviewed; 557 AA.
AC Q708S8;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Acid-sensing ion channel 1B;
DE Short=ASIC1-B;
DE AltName: Full=Acid-sensing ion channel 1.1-B;
DE AltName: Full=Amiloride-sensitive cation channel 2-A, neuronal-B;
DE AltName: Full=ZASIC1.1;
GN Name=asic1b; Synonyms=accn2a;
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,
RP FUNCTION, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
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: Proton-gated sodium channel; it is activated by a drop of the
CC extracellular pH and then becomes rapidly desensitized. Generates a
CC biphasic current with a fast inactivating and a slow sustained phase.
CC Has high selectivity for sodium ions and can also transport lithium
CC ions with high efficiency. Can also transport potassium ions, but with
CC lower efficiency. It is nearly impermeable to the larger rubidium and
CC cesium ions. {ECO:0000269|PubMed:14970195}.
CC -!- ACTIVITY REGULATION: 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:0000269|PubMed:14970195};
CC Multi-pass membrane protein {ECO:0000269|PubMed:14970195}.
CC -!- TISSUE SPECIFICITY: Expressed in central nervous system.
CC {ECO:0000269|PubMed:14970195}.
CC -!- DEVELOPMENTAL STAGE: Expression starts 30 hours post-fertilization
CC (hpf) and is restricted to the anterior and posterior lateral line
CC ganglia and the otic sensory neurons. At 48 hpf expression becomes also
CC evident in the trigeminal ganglia. At 96 hpf expressed throughout most
CC of the central nervous system. Excluded from the dorsal forebrain
CC except for the habenula nuclei. {ECO:0000269|PubMed:14970195}.
CC -!- DOMAIN: Channel opening involves a conformation change that affects
CC primarily the extracellular domain and the second transmembrane helix
CC and its orientation in the membrane. In the open state, the second
CC transmembrane helix is nearly perpendicular to the plane of the
CC membrane; in the desensitized state it is strongly tilted. Besides, the
CC second transmembrane domain is discontinuously helical in the open
CC state. The GAS motif of the selectivity filter is in an extended
CC conformation, giving rise to a distinct kink in the polypeptide chain.
CC A domain swap between subunits gives rise to a full-length
CC transmembrane helix (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC 1.A.6) family. ASIC1 subfamily. {ECO:0000305}.
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DR EMBL; AJ609615; CAE81918.1; -; mRNA.
DR RefSeq; NP_999956.1; NM_214791.1.
DR AlphaFoldDB; Q708S8; -.
DR SMR; Q708S8; -.
DR STRING; 7955.ENSDARP00000116909; -.
DR PaxDb; Q708S8; -.
DR Ensembl; ENSDART00000165549; ENSDARP00000133845; ENSDARG00000101866.
DR GeneID; 407672; -.
DR KEGG; dre:407672; -.
DR CTD; 407672; -.
DR ZFIN; ZDB-GENE-040513-1; asic1b.
DR eggNOG; KOG4294; Eukaryota.
DR GeneTree; ENSGT00940000164727; -.
DR InParanoid; Q708S8; -.
DR OMA; ERVANNM; -.
DR OrthoDB; 686369at2759; -.
DR PhylomeDB; Q708S8; -.
DR TreeFam; TF330663; -.
DR Reactome; R-DRE-2672351; Stimuli-sensing channels.
DR PRO; PR:Q708S8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 22.
DR Bgee; ENSDARG00000101866; Expressed in spleen and 13 other tissues.
DR ExpressionAtlas; Q708S8; baseline.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:ZFIN.
DR GO; GO:0044736; F:acid-sensing ion channel activity; ISS:UniProtKB.
DR GO; GO:0015280; F:ligand-gated sodium channel activity; IDA:ZFIN.
DR GO; GO:0071467; P:cellular response to pH; ISS:UniProtKB.
DR GO; GO:0070207; P:protein homotrimerization; ISS:UniProtKB.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR InterPro; IPR001873; ENaC.
DR InterPro; IPR004724; ENaC_chordates.
DR InterPro; IPR020903; ENaC_CS.
DR PANTHER; PTHR11690; PTHR11690; 1.
DR Pfam; PF00858; ASC; 1.
DR PRINTS; PR01078; AMINACHANNEL.
DR TIGRFAMs; TIGR00859; ENaC; 1.
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..557
FT /note="Acid-sensing ion channel 1B"
FT /id="PRO_0000181296"
FT TOPO_DOM 1..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 95..118
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 119..460
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 461..487
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 488..557
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 36..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 477..479
FT /note="Selectivity filter"
FT /evidence="ECO:0000305"
FT SITE 120
FT /note="Important for channel gating"
FT /evidence="ECO:0000250"
FT SITE 128
FT /note="Important for channel desensitizing"
FT /evidence="ECO:0000250"
FT SITE 322
FT /note="Important for channel gating"
FT /evidence="ECO:0000250"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 142..229
FT /evidence="ECO:0000250|UniProtKB:Q1XA76"
FT DISULFID 207..214
FT /evidence="ECO:0000250|UniProtKB:Q1XA76"
FT DISULFID 325..400
FT /evidence="ECO:0000250|UniProtKB:Q1XA76"
FT DISULFID 343..396
FT /evidence="ECO:0000250|UniProtKB:Q1XA76"
FT DISULFID 347..394
FT /evidence="ECO:0000250|UniProtKB:Q1XA76"
FT DISULFID 356..378
FT /evidence="ECO:0000250|UniProtKB:Q1XA76"
FT DISULFID 358..370
FT /evidence="ECO:0000250|UniProtKB:Q1XA76"
SQ SEQUENCE 557 AA; 63540 MW; C57C00F09D5A7F9F CRC64;
MVRITCTISF STDDEPVGRS RQGSFDDHYK RVVWSKDGEQ GKYQEEGDDP DAYDGPEDEE
APDISLATFF GGCSLHGANH VFVEDKKFSI RQGLWALVFL LAISMFLLQV VDRVIYYLQY
DYVTLLDERN AKNMTFPAIT LCNYNTFRRS QLSYSDLLFM GPLLGYEDNM APGIPLAPEP
DRQGSRFSLA EFFNRTRHRM DDMLLECNFA GKECGAEHWR EIFTRYGKCY TFNSGQDGRP
LLITTKGGMG NGLEIMLDIQ QDEYLPVWGE TDETTFEAGI KVQIHTQDEP PFIDQLGFGV
APGFQTFVSC QEQRLTYLPP PWGDCKATPI DSDFFNTYSI TACRIDCETR YLVENCNCRM
VHMPGDAPYC TPEQYKECAD PALDFLVERD NDYCVCETPC NMTRYGKELS FVRIPSKASA
KYLAKKYNKT EQYISDNIMV LDIFFEALNY ETIEQKKAYE LAGLLGDIGG QMGLFIGASI
LTILELFDYL YEVIKFKLCR CAKKKHQRSN NNERGAVLSL DDVKRHAPCD NLRTPSTYPA
NMLPHHPGQG NFEDFTC
