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Acid-sensing ion channel 1C (ASIC1-C) (Acid-sensing ion channel 1.3-C) (Amiloride-sensitive cation channel 2-C, neuronal-C) (ZASIC1.3)

 ASI1C_DANRE             Reviewed;         529 AA.
Q708S6;
13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
05-DEC-2018, entry version 80.
RecName: Full=Acid-sensing ion channel 1C;
Short=ASIC1-C;
AltName: Full=Acid-sensing ion channel 1.3-C;
AltName: Full=Amiloride-sensitive cation channel 2-C, neuronal-C;
AltName: Full=ZASIC1.3;
Name=asic1c; Synonyms=accn2c;
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,
INTERACTION WITH ASIC1, 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 (By
similarity). Interacts with ASIC1/ACCN2B. {ECO:0000250,
ECO:0000269|PubMed:14970195}.
-!- 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: Expressed 30 hours post-fertilization (hpf)
in the anterior and posterior lateral line ganglia where it
persisted until at least 48 hpf. Also expressed between 30 and 72
hpf in the telencephalon. Expressed in the ventral thalamus,
ventral midbrain, ventral cerebellum, and ventral hindbrain from
30 hpf. By 48 hpf, expressed also in the dorsal thalamus and
hypothalamus. At 72 hpf, weak expression was apparent in the
habenulae. {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; AJ609617; CAE81920.1; -; mRNA.
RefSeq; NP_999954.1; NM_214789.1.
UniGene; Dr.120630; -.
ProteinModelPortal; Q708S6; -.
SMR; Q708S6; -.
Ensembl; ENSDART00000169227; ENSDARP00000130223; ENSDARG00000098428.
GeneID; 407670; -.
KEGG; dre:407670; -.
CTD; 407670; -.
ZFIN; ZDB-GENE-040513-3; asic1c.
GeneTree; ENSGT00940000164727; -.
HOVERGEN; HBG004150; -.
KO; K04830; -.
OMA; HTPWTLE; -.
OrthoDB; EOG091G053J; -.
PhylomeDB; Q708S6; -.
PRO; PR:Q708S6; -.
Proteomes; UP000000437; Chromosome 24.
Bgee; ENSDARG00000098428; Expressed in 10 organ(s), highest expression level in mature ovarian follicle.
ExpressionAtlas; Q708S6; 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:0005261; F:cation channel activity; IGI:ZFIN.
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.
1: Evidence at protein 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 1 529 Acid-sensing ion channel 1C.
/FTId=PRO_0000181298.
TOPO_DOM 1 47 Cytoplasmic. {ECO:0000250}.
TRANSMEM 48 71 Helical. {ECO:0000250}.
TOPO_DOM 72 427 Extracellular. {ECO:0000250}.
TRANSMEM 428 454 Discontinuously helical. {ECO:0000250}.
TOPO_DOM 455 529 Cytoplasmic. {ECO:0000250}.
MOTIF 444 446 Selectivity filter. {ECO:0000305}.
SITE 81 81 Important for channel desensitizing.
{ECO:0000250}.
SITE 289 289 Important for channel gating.
{ECO:0000250}.
CARBOHYD 86 86 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 155 155 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 161 161 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 185 185 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 368 368 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 395 395 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 95 196 {ECO:0000250|UniProtKB:Q1XA76}.
DISULFID 174 181 {ECO:0000250|UniProtKB:Q1XA76}.
DISULFID 292 367 {ECO:0000250|UniProtKB:Q1XA76}.
DISULFID 310 363 {ECO:0000250|UniProtKB:Q1XA76}.
DISULFID 314 361 {ECO:0000250|UniProtKB:Q1XA76}.
DISULFID 323 345 {ECO:0000250|UniProtKB:Q1XA76}.
DISULFID 325 337 {ECO:0000250|UniProtKB:Q1XA76}.
SEQUENCE 529 AA; 60035 MW; D657D7A7AD42E29E CRC64;
MTAMKGDSED SIESMRPSNL QVFANNSTLH GMSHIFAYGH MTFRRFLWTL SFMGSLGLLM
YVCMDRVYYY FEFPHVTKLD EVAAPNLTFP AVTFCNLNEF RFSKITKNDL YHVGELLALL
NENYQIANPH LADPEVLTLL KEKASFNGFK PKQFNMTDFY NRTGHDINEM LLQCSFRGEE
CFPLNFTTIY TRYGKCYTFN SGLDGNPLLT TLKGGTGNGL EIMLDIQQDE YLPVWGDTDE
TSYEAGIKVQ IHSQDEPPFI DQLGFGVAPG FQTFVSCQQQ LLLYLPPPWG DCRSAPMDSE
YFSTYSITAC RIDCETRYLL ENCNCRMVHM PGTSTVCTPE QYKDCADPAL DFLVEKDNDY
CVCDTPCNMT RYGKELSMVK IPSKASAKYL AKKFNKTEQY ITDNILVLDI FFEALNYEKI
EQKKAYEVAG LLGDIGGQMG LFIGASVLTI LEIFDYLYEV LKDKILGSVL RKRRPHRSAS
DNLVIVSLHD FKISSVFLLA SYMCFVCYIV LLNAACVYLP FVVGSNSGK


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