ASIC1_OPSTA
ID ASIC1_OPSTA Reviewed; 522 AA.
AC Q7T1N4;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 11-DEC-2019, entry version 61.
DE RecName: Full=Acid-sensing ion channel 1;
DE Short=ASIC1;
DE AltName: Full=Amiloride-sensitive cation channel 2, neuronal;
GN Name=asic1; Synonyms=accn2;
OS Opsanus tau (Oyster toadfish) (Gadus tau).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Batrachoidaria; Batrachoididae; Opsanus.
OX NCBI_TaxID=8068;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF 128-HIS--GLU-131 AND
RP 83-PRO--MET-85, AND FUNCTION.
RC TISSUE=Brain, and Spinal cord;
RX PubMed=12947112; DOI=10.1074/jbc.m304441200;
RA Coric T., Zhang P., Todorovic N., Canessa C.M.;
RT "The extracellular domain determines the kinetics of desensitization in
RT acid-sensitive ion channel 1.";
RL J. Biol. Chem. 278:45240-45247(2003).
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:12947112}.
CC -!- SUBUNIT: Homotrimer or heterotrimer with other ASIC proteins.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
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; AY278028; AAP78806.1; -; mRNA.
DR PRIDE; Q7T1N4; -.
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: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; ISS:UniProtKB.
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; Sodium; Sodium channel; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..522
FT /note="Acid-sensing ion channel 1"
FT /id="PRO_0000181299"
FT TOPO_DOM 1..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 46..69
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 70..425
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 426..452
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 453..522
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOTIF 442..444
FT /note="Selectivity filter"
FT /evidence="ECO:0000305"
FT SITE 71
FT /note="Important for channel gating"
FT /evidence="ECO:0000250"
FT SITE 79
FT /note="Important for channel desensitizing"
FT /evidence="ECO:0000250"
FT SITE 287
FT /note="Important for channel gating"
FT /evidence="ECO:0000250"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 93..194
FT /evidence="ECO:0000250|UniProtKB:Q1XA76"
FT DISULFID 172..179
FT /evidence="ECO:0000250|UniProtKB:Q1XA76"
FT DISULFID 290..365
FT /evidence="ECO:0000250|UniProtKB:Q1XA76"
FT DISULFID 308..361
FT /evidence="ECO:0000250|UniProtKB:Q1XA76"
FT DISULFID 312..359
FT /evidence="ECO:0000250|UniProtKB:Q1XA76"
FT DISULFID 321..343
FT /evidence="ECO:0000250|UniProtKB:Q1XA76"
FT DISULFID 323..335
FT /evidence="ECO:0000250|UniProtKB:Q1XA76"
FT MUTAGEN 83..85
FT /note="PLM->SQL: Reduces desensitization rates."
FT /evidence="ECO:0000269|PubMed:12947112"
FT MUTAGEN 128..131
FT /note="HLVE->QMAD: No effect on desensitization rates."
FT /evidence="ECO:0000269|PubMed:12947112"
SQ SEQUENCE 522 AA; 59729 MW; 2947C022B867A6F3 CRC64;
MDLKADSEDV DYKQPAPIED FASRSTLHGI SHMFTYERVC IKRTLWILFF LGSVGALALV
CVDRVQFYFQ YPHVTKLDEV AAPLMTFPAV TFCNLNSFRF SRVTRNDLYH AGELXALLNG
RYEIRDTHLV EENVLEILKE RANFDNYKPR PFNMREFYDR TGHDIKDMLL SCYYRGVECN
AENFKVIFTR YGKCYTFNSG KDGRPLLLTM KGGMGNGLEL MLDIQQDEYL PVWGETDETS
FEAGIKVQIH TQSEPPFIDQ LGFGVAPGFQ TFVSCQEQRL TYLPPPWGDC KAAPMDSDFF
STYSITACRI DCETRYLVEN CNCRMVHMPG DAPYCTPEQY KECADPALDF LVERDNDYCV
CKTPCNLTRF GKEMSFVKIP SKASAKYLAK KFXKTEQYIA DNILVLDIYF DALNYETIEQ
KKAYEVAGLL GDIGGQMGLF IGASILTILE LFDYLYEVLK YKLCRCVKKK HKGRGNKDRG
AVLSLDDVKR HAPCENLRTP STYPGNMLPH HPGQGNFEDF TC
