ASIC2_DANRE
ID ASIC2_DANRE Reviewed; 533 AA.
AC Q708S5;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Acid-sensing ion channel 2;
DE Short=ASIC2;
DE AltName: Full=Amiloride-sensitive cation channel 1, neuronal;
DE AltName: Full=ZASIC2;
GN Name=asic2; Synonyms=accn1;
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, AND
RP 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. In
CC vitro, has no proton-gated channel activity.
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: First expressed by 30 hours post-fertilization
CC (hpf) along the tract of the anterior commissure, where it persisted
CC until 48 hpf. Detected at 48 hpf in the preoptic area, ventral
CC thalamus, and ventral midbrain and weakly in the ventral hindbrain. At
CC 72 and 96 hpf, expressed throughout most of the brain except the dorsal
CC forebrain. Expressed in the retinal ganglion cells.
CC {ECO:0000269|PubMed:14970195}.
CC -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC 1.A.6) family. ASIC2 subfamily. {ECO:0000305}.
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DR EMBL; AJ609618; CAE81921.1; -; mRNA.
DR RefSeq; NP_999953.1; NM_214788.1.
DR AlphaFoldDB; Q708S5; -.
DR SMR; Q708S5; -.
DR Ensembl; ENSDART00000039517; ENSDARP00000039516; ENSDARG00000006849.
DR Ensembl; ENSDART00000137038; ENSDARP00000122509; ENSDARG00000006849.
DR GeneID; 407669; -.
DR KEGG; dre:407669; -.
DR CTD; 40; -.
DR ZFIN; ZDB-GENE-040513-4; asic2.
DR GeneTree; ENSGT00940000154991; -.
DR HOGENOM; CLU_020415_1_2_1; -.
DR InParanoid; Q708S5; -.
DR OMA; FPSHTQV; -.
DR OrthoDB; 686369at2759; -.
DR PhylomeDB; Q708S5; -.
DR Reactome; R-DRE-2672351; Stimuli-sensing channels.
DR PRO; PR:Q708S5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 3.
DR Bgee; ENSDARG00000006849; Expressed in brain and 15 other tissues.
DR ExpressionAtlas; Q708S5; baseline.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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; 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..533
FT /note="Acid-sensing ion channel 2"
FT /id="PRO_0000181293"
FT TOPO_DOM 1..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..445
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 467..533
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 113..214
FT /evidence="ECO:0000250"
FT DISULFID 192..199
FT /evidence="ECO:0000250"
FT DISULFID 310..385
FT /evidence="ECO:0000250"
FT DISULFID 328..381
FT /evidence="ECO:0000250"
FT DISULFID 332..379
FT /evidence="ECO:0000250"
FT DISULFID 341..363
FT /evidence="ECO:0000250"
FT DISULFID 343..355
FT /evidence="ECO:0000250"
SQ SEQUENCE 533 AA; 59737 MW; CB4BF754E27F2BC4 CRC64;
MDLKEACGSE ASRETESGGM GSLGGHSSWQ SFAHRSTLHG LRFIFPYSSS SSSSSSYRST
SRRLLWSAAL LASLVLLVLE STERLAYFLS YPHVTSVDAV VSGSLVFPAV TVCNLNAYRF
TRLTQNDLYH AGELLALLDV HLQIPEPHLA EPHVLAFLTE KSNFTNYRPK PFSMREFTER
VGHDLKEMML YCRFQGQECS HQDFKTVFTR YGKCYMFNAA EEGKTLRTTM KGGTGNGLEI
MLDIQQDEYL PVWGETEETA FEAGVRVQIH SQAEPPFVHE LGFGVAPGFQ TFVATQEQRL
TYLPPPWGEC VSRALDSGLF QVYSVSACRI ECETRYIVEN CNCRMVYMPG DSPYCTPEQY
KDCAEPALAA LSAVEGTNCI CRSPCNMTRY NKELSMVKIP SKTSARYLEK KFNRSEKYIT
DNILVLDVFF EALNYETIEQ KKAYEVAGLL GDIGGQMGLF IGASILTLLE LFDYAYEVVK
ERLLDLLNRE EEEESHGEDV STCDPVVNHS ESISHTVSVP LQTTLGTLEE IAC
