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Acid-sensing ion channel 1B (ASIC1-B) (Acid-sensing ion channel 1.1-B) (Amiloride-sensitive cation channel 2-A, neuronal-B) (ZASIC1.1)

 ASI1B_DANRE             Reviewed;         557 AA.
Q708S8;
13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
12-SEP-2018, entry version 90.
RecName: Full=Acid-sensing ion channel 1B;
Short=ASIC1-B;
AltName: Full=Acid-sensing ion channel 1.1-B;
AltName: Full=Amiloride-sensitive cation channel 2-A, neuronal-B;
AltName: Full=ZASIC1.1;
Name=asic1b; Synonyms=accn2a;
Danio rerio (Zebrafish) (Brachydanio rerio).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Danio.
NCBI_TaxID=7955;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
FUNCTION, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
PubMed=14970195; DOI=10.1074/jbc.M401477200;
Paukert M., Sidi S., Russell C., Siba M., Wilson S.W., Nicolson T.,
Gruender S.;
"A family of acid-sensing ion channels (ASICs) from the zebrafish:
widespread e xpression in the central nervous system suggests a
conserved role in neuronal communication.";
J. Biol. Chem. 279:18783-18791(2004).
-!- FUNCTION: Proton-gated sodium channel; it is activated by a drop
of the extracellular pH and then becomes rapidly desensitized.
Generates a biphasic current with a fast inactivating and a slow
sustained phase. Has high selectivity for sodium ions and can also
transport lithium ions with high efficiency. Can also transport
potassium ions, but with lower efficiency. It is nearly
impermeable to the larger rubidium and cesium ions.
{ECO:0000269|PubMed:14970195}.
-!- ACTIVITY REGULATION: Inhibited by the diuretic amiloride.
{ECO:0000269|PubMed:14970195}.
-!- SUBUNIT: Homotrimer or heterotrimer with other ASIC proteins.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14970195};
Multi-pass membrane protein {ECO:0000269|PubMed:14970195}.
-!- TISSUE SPECIFICITY: Expressed in central nervous system.
{ECO:0000269|PubMed:14970195}.
-!- DEVELOPMENTAL STAGE: Expression starts 30 hours post-fertilization
(hpf) and is restricted to the anterior and posterior lateral line
ganglia and the otic sensory neurons. At 48 hpf expression becomes
also evident in the trigeminal ganglia. At 96 hpf expressed
throughout most of the central nervous system. Excluded from the
dorsal forebrain except for the habenula nuclei.
{ECO:0000269|PubMed:14970195}.
-!- DOMAIN: Channel opening involves a conformation change that
affects primarily the extracellular domain and the second
transmembrane helix and its orientation in the membrane. In the
open state, the second transmembrane helix is nearly perpendicular
to the plane of the membrane; in the desensitized state it is
strongly tilted. Besides, the second transmembrane domain is
discontinuously helical in the open state. The GAS motif of the
selectivity filter is in an extended conformation, giving rise to
a distinct kink in the polypeptide chain. A domain swap between
subunits gives rise to a full-length transmembrane helix (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
1.A.6) family. ASIC1 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ609615; CAE81918.1; -; mRNA.
RefSeq; NP_999956.1; NM_214791.1.
UniGene; Dr.91509; -.
ProteinModelPortal; Q708S8; -.
SMR; Q708S8; -.
STRING; 7955.ENSDARP00000032201; -.
PaxDb; Q708S8; -.
PRIDE; Q708S8; -.
Ensembl; ENSDART00000165549; ENSDARP00000133845; ENSDARG00000101866.
GeneID; 407672; -.
KEGG; dre:407672; -.
CTD; 407672; -.
ZFIN; ZDB-GENE-040513-1; asic1b.
eggNOG; KOG4294; Eukaryota.
eggNOG; ENOG410ZNFK; LUCA.
GeneTree; ENSGT00760000119120; -.
HOGENOM; HOG000247010; -.
HOVERGEN; HBG004150; -.
InParanoid; Q708S8; -.
KO; K04829; -.
OMA; CRCMKKK; -.
OrthoDB; EOG091G053J; -.
PhylomeDB; Q708S8; -.
TreeFam; TF330663; -.
PRO; PR:Q708S8; -.
Proteomes; UP000000437; Chromosome 22.
Bgee; ENSDARG00000101866; Expressed in 14 organ(s), highest expression level in spleen.
ExpressionAtlas; Q708S8; baseline.
GO; GO:0005887; C:integral component of plasma membrane; IDA:ZFIN.
GO; GO:0044736; F:acid-sensing ion channel activity; ISS:UniProtKB.
GO; GO:0015280; F:ligand-gated sodium channel activity; IDA:ZFIN.
GO; GO:0071467; P:cellular response to pH; ISS:UniProtKB.
GO; GO:0070207; P:protein homotrimerization; ISS:UniProtKB.
InterPro; IPR001873; ENaC.
InterPro; IPR004724; ENaC_chordates.
InterPro; IPR020903; ENaC_CS.
PANTHER; PTHR11690; PTHR11690; 1.
Pfam; PF00858; ASC; 1.
PRINTS; PR01078; AMINACHANNEL.
TIGRFAMs; TIGR00859; ENaC; 1.
PROSITE; PS01206; ASC; 1.
2: Evidence at transcript level;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
Ion channel; Ion transport; Membrane; Reference proteome; Sodium;
Sodium channel; Sodium transport; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 557 Acid-sensing ion channel 1B.
/FTId=PRO_0000181296.
TOPO_DOM 1 94 Cytoplasmic. {ECO:0000250}.
TRANSMEM 95 118 Helical. {ECO:0000250}.
TOPO_DOM 119 460 Extracellular. {ECO:0000250}.
TRANSMEM 461 487 Discontinuously helical. {ECO:0000250}.
TOPO_DOM 488 557 Cytoplasmic. {ECO:0000250}.
MOTIF 477 479 Selectivity filter. {ECO:0000305}.
SITE 120 120 Important for channel gating.
{ECO:0000250}.
SITE 128 128 Important for channel desensitizing.
{ECO:0000250}.
SITE 322 322 Important for channel gating.
{ECO:0000250}.
CARBOHYD 133 133 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 194 194 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 401 401 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 428 428 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 142 229 {ECO:0000250|UniProtKB:Q1XA76}.
DISULFID 207 214 {ECO:0000250|UniProtKB:Q1XA76}.
DISULFID 325 400 {ECO:0000250|UniProtKB:Q1XA76}.
DISULFID 343 396 {ECO:0000250|UniProtKB:Q1XA76}.
DISULFID 347 394 {ECO:0000250|UniProtKB:Q1XA76}.
DISULFID 356 378 {ECO:0000250|UniProtKB:Q1XA76}.
DISULFID 358 370 {ECO:0000250|UniProtKB:Q1XA76}.
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


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