ASIC1_CAEEL
ID ASIC1_CAEEL Reviewed; 823 AA.
AC O01635;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Degenerin-like protein asic-1;
DE AltName: Full=Acid-sensing/amiloride-sensitive ion channel protein 1;
GN Name=asic-1 {ECO:0000312|WormBase:ZK770.1};
GN ORFNames=ZK770.1 {ECO:0000312|WormBase:ZK770.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION.
RX PubMed=31494966; DOI=10.1002/syn.22131;
RA Formisano R., Mersha M.D., Caplan J., Singh A., Rankin C.H.,
RA Tavernarakis N., Dhillon H.S.;
RT "Synaptic vesicle fusion is modulated through feedback inhibition by
RT dopamine auto-receptors.";
RL Synapse 74:E22131-E22131(2020).
CC -!- FUNCTION: Proton-gated cation channel; it is activated by a drop of the
CC extracellular pH and then becomes rapidly desensitized (By similarity).
CC Has high selectivity for sodium ions and can also transport lithium
CC ions with high efficiency (By similarity). Can also transport potassium
CC ions, but with lower efficiency (By similarity). It is nearly
CC impermeable to the larger rubidium and cesium ions (By similarity).
CC Promotes synaptic vesicle fusion to positively regulate the release of
CC dopamine at dopaminergic neuron synapses (PubMed:31494966).
CC {ECO:0000250|UniProtKB:Q1XA76, ECO:0000269|PubMed:31494966}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q1XA76}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q1XA76};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q1XA76}.
CC -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC 1.A.6) family. {ECO:0000305}.
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DR EMBL; BX284601; CCD66427.1; -; Genomic_DNA.
DR PIR; T34468; T34468.
DR RefSeq; NP_491214.3; NM_058813.3.
DR AlphaFoldDB; O01635; -.
DR BioGRID; 55958; 2.
DR STRING; 6239.ZK770.1; -.
DR PaxDb; O01635; -.
DR PeptideAtlas; O01635; -.
DR PRIDE; O01635; -.
DR EnsemblMetazoa; ZK770.1.1; ZK770.1.1; WBGene00022815.
DR GeneID; 191422; -.
DR KEGG; cel:CELE_ZK770.1; -.
DR UCSC; ZK770.1; c. elegans.
DR CTD; 191422; -.
DR WormBase; ZK770.1; CE45595; WBGene00022815; asic-1.
DR eggNOG; KOG4294; Eukaryota.
DR HOGENOM; CLU_017673_0_0_1; -.
DR InParanoid; O01635; -.
DR OMA; AMENIIF; -.
DR OrthoDB; 686369at2759; -.
DR PhylomeDB; O01635; -.
DR PRO; PR:O01635; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00022815; Expressed in larva and 1 other tissue.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0044736; F:acid-sensing ion channel activity; ISS:UniProtKB.
DR GO; GO:0015280; F:ligand-gated sodium channel activity; IBA:GO_Central.
DR GO; GO:0071467; P:cellular response to pH; ISS:UniProtKB.
DR GO; GO:0033603; P:positive regulation of dopamine secretion; IMP:UniProtKB.
DR GO; GO:0070207; P:protein homotrimerization; ISS:UniProtKB.
DR GO; GO:0035725; P:sodium ion transmembrane transport; ISS:UniProtKB.
DR InterPro; IPR004726; Deg-1.
DR InterPro; IPR001873; ENaC.
DR InterPro; IPR020903; ENaC_CS.
DR PANTHER; PTHR11690; PTHR11690; 1.
DR Pfam; PF00858; ASC; 2.
DR PRINTS; PR01078; AMINACHANNEL.
DR TIGRFAMs; TIGR00867; deg-1; 1.
DR PROSITE; PS01206; ASC; 1.
PE 3: Inferred from homology;
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..823
FT /note="Degenerin-like protein asic-1"
FT /id="PRO_0000181315"
FT TOPO_DOM 1..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..767
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 768..788
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 789..795
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 86..518
FT /evidence="ECO:0000250|UniProtKB:Q1XA76"
FT DISULFID 494..501
FT /evidence="ECO:0000250|UniProtKB:Q1XA76"
FT DISULFID 604..687
FT /evidence="ECO:0000250|UniProtKB:Q1XA76"
FT DISULFID 625..683
FT /evidence="ECO:0000250|UniProtKB:Q1XA76"
FT DISULFID 629..681
FT /evidence="ECO:0000250|UniProtKB:Q1XA76"
FT DISULFID 638..664
FT /evidence="ECO:0000250|UniProtKB:Q1XA76"
SQ SEQUENCE 823 AA; 93584 MW; 1874E7CB7F6CF7F0 CRC64;
MGKNSLKRAL ELDVVDFAEH TSAHGIPRAY VSTGWRRYMW LLCFLFCLSC FGHQAYLIVE
RFNRNDIIVG VEIKFEEIKF PAVTICNMNP YKNSAARELG AIRNAIEAFE LAIDKSDGNA
HSKRKKRSAN SKMVPIDLLC KEEHGMFTAH DYGHVECTCV TFEDMSKVGD TDDDEIFWNC
HQRKDWTHKI CHLAEGSNQL KTCKCFEDTC VSDEVTKQLV WPLQLSKNGT KLCISPESSG
PRYCASAQKF QVSTCSNCDW LGKCEESDDM DLEEEIDSKT CICHHGNCFQ IKGNVKKRKR
RTPERKVHER LLSRYEGLLA VYSHCNCTKQ HGCVSTSVPD MDLENSNKTC LCFYNKKNEQ
IWPCYKEPEW EERKCSRCNT MGDCVYSDKP KKQTISCLCA TPIKMCVRID PPQTNDTSLD
DRVVKFWDIQ PSTTMSPIVK KKEERDKAYG YTGVKDRIAL RAKAMENMIF AVDALTEEEK
WKISYNKSDF IMKCSFNGRE CNVKHDFVEY LDPTYGACFT YGQKLGNNTN ERSGPAYGLR
LEVFVNVTEY LPTTEAAGVR LTVHATDEQP FPDTLGFSAP TGFVSSFGIK LKSMVRLPAP
YGDCVREGKT EDFIYTQKAY NTEGCQRSCI QKHLSKTCGC GDPRFPPYRE SKNCPVDDPY
KRECIKNEMH VATRDSKKLG CSCKQPCNQD VYSVSYSASR WPAIAGDLSG CPLGMAAHHC
LNYKREQGSM IEVYFEQLNY ESLLESEAYG WSNLLSDFGG QLGLWMGVSV ITIGEVACFF
FEVFISLISS NRTKRRPARK SFSSSLRCST DYNLNKDGFN LDN
