ASI1C_DANRE
ID ASI1C_DANRE Reviewed; 529 AA.
AC Q708S6;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Acid-sensing ion channel 1C;
DE Short=ASIC1-C;
DE AltName: Full=Acid-sensing ion channel 1.3-C;
DE AltName: Full=Amiloride-sensitive cation channel 2-C, neuronal-C;
DE AltName: Full=ZASIC1.3;
GN Name=asic1c; Synonyms=accn2c;
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 INTERACTION WITH ASIC1, FUNCTION, SUBCELLULAR LOCATION, AND ACTIVITY
RP 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 (By
CC similarity). Interacts with ASIC1/ACCN2B. {ECO:0000250,
CC ECO:0000269|PubMed:14970195}.
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: Expressed 30 hours post-fertilization (hpf) in the
CC anterior and posterior lateral line ganglia where it persisted until at
CC least 48 hpf. Also expressed between 30 and 72 hpf in the
CC telencephalon. Expressed in the ventral thalamus, ventral midbrain,
CC ventral cerebellum, and ventral hindbrain from 30 hpf. By 48 hpf,
CC expressed also in the dorsal thalamus and hypothalamus. At 72 hpf, weak
CC expression was apparent in the habenulae.
CC {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; AJ609617; CAE81920.1; -; mRNA.
DR RefSeq; NP_999954.1; NM_214789.1.
DR AlphaFoldDB; Q708S6; -.
DR SMR; Q708S6; -.
DR Ensembl; ENSDART00000169227; ENSDARP00000130223; ENSDARG00000098428.
DR GeneID; 407670; -.
DR KEGG; dre:407670; -.
DR CTD; 407670; -.
DR ZFIN; ZDB-GENE-040513-3; asic1c.
DR GeneTree; ENSGT00940000164727; -.
DR HOGENOM; CLU_020415_1_2_1; -.
DR OMA; VSFYMPR; -.
DR OrthoDB; 686369at2759; -.
DR PhylomeDB; Q708S6; -.
DR Reactome; R-DRE-2672351; Stimuli-sensing channels.
DR PRO; PR:Q708S6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 24.
DR Bgee; ENSDARG00000098428; Expressed in ovary and 6 other tissues.
DR ExpressionAtlas; Q708S6; 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:0005261; F:cation channel activity; IGI:ZFIN.
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 1: Evidence at protein 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..529
FT /note="Acid-sensing ion channel 1C"
FT /id="PRO_0000181298"
FT TOPO_DOM 1..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 48..71
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 72..427
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 428..454
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 455..529
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOTIF 444..446
FT /note="Selectivity filter"
FT /evidence="ECO:0000305"
FT SITE 81
FT /note="Important for channel desensitizing"
FT /evidence="ECO:0000250"
FT SITE 289
FT /note="Important for channel gating"
FT /evidence="ECO:0000250"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..196
FT /evidence="ECO:0000250|UniProtKB:Q1XA76"
FT DISULFID 174..181
FT /evidence="ECO:0000250|UniProtKB:Q1XA76"
FT DISULFID 292..367
FT /evidence="ECO:0000250|UniProtKB:Q1XA76"
FT DISULFID 310..363
FT /evidence="ECO:0000250|UniProtKB:Q1XA76"
FT DISULFID 314..361
FT /evidence="ECO:0000250|UniProtKB:Q1XA76"
FT DISULFID 323..345
FT /evidence="ECO:0000250|UniProtKB:Q1XA76"
FT DISULFID 325..337
FT /evidence="ECO:0000250|UniProtKB:Q1XA76"
SQ 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
