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ASIC4_RAT
ID   ASIC4_RAT               Reviewed;         539 AA.
AC   Q9JHS6; Q9QYV9;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Acid-sensing ion channel 4;
DE            Short=ASIC4;
DE   AltName: Full=Amiloride-sensitive cation channel 4;
DE   AltName: Full=Spinal cord ASIC;
GN   Name=Asic4; Synonyms=Accn4, Spasic;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=10852210; DOI=10.1097/00001756-200006050-00003;
RA   Gruender S., Geisler H.-S., Baessler E.-L., Ruppersberg J.P.;
RT   "A new member of acid-sensing ion channels from pituitary gland.";
RL   NeuroReport 11:1607-1611(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP   FUNCTION.
RC   TISSUE=Spinal ganglion;
RX   PubMed=10923674; DOI=10.1097/00001756-200007140-00031;
RA   Akopian A.N., Chen C.-C., Ding Y., Cesare P., Wood J.N.;
RT   "A new member of the acid-sensing ion channel family.";
RL   NeuroReport 11:2217-2222(2000).
CC   -!- FUNCTION: Probable cation channel with high affinity for sodium.
CC       {ECO:0000269|PubMed:10923674}.
CC   -!- SUBUNIT: Homotrimer or heterotrimer with other ASIC proteins.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, spinal cord and dorsal root
CC       ganglion (DRG). Expressed by a subset of sensory neurons in the DRG.
CC       Expressed by granule cells in the cerebellar cortex. In hippocampus,
CC       expression is detected in dentate gyrus granule cells, in pyramidal
CC       cells of CA1-CA3 subfields and in interneurons of the striatum oriens
CC       and radiatum of all subfields. In cerebral cortex expressed in small,
CC       medium and large pyramidal cells in layers 2, 3 and 5 respectively.
CC       Also expressed in striatum, globus pallidus, inferior and superior
CC       calliculi, amygdala, magnocellular preoptic nucleus, islands of Calleja
CC       and large neurons of olfactory tubercules.
CC       {ECO:0000269|PubMed:10923674}.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in newborn spinal cord but hardly
CC       detected in the cerebellum compared to adult. Expressed at postnatal
CC       day 1 in ependymal cells lining the central canal of spinal cord and in
CC       motor neurons. In adult, expression decreases in ependymal cells and
CC       increases in motor neurons. The number of positive interneurons
CC       decreases but the individual interneuron expression increases in adult
CC       spinal cord compared to newborn. {ECO:0000269|PubMed:10923674}.
CC   -!- MISCELLANEOUS: In vitro, has no proton-gated channel activity.
CC   -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC       1.A.6) family. ASIC4 subfamily. {ECO:0000305}.
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DR   EMBL; AJ271642; CAB93984.1; -; mRNA.
DR   EMBL; AJ242554; CAB61836.1; -; mRNA.
DR   RefSeq; NP_071570.2; NM_022234.2.
DR   AlphaFoldDB; Q9JHS6; -.
DR   SMR; Q9JHS6; -.
DR   STRING; 10116.ENSRNOP00000027135; -.
DR   GlyGen; Q9JHS6; 4 sites.
DR   PaxDb; Q9JHS6; -.
DR   GeneID; 63882; -.
DR   KEGG; rno:63882; -.
DR   UCSC; RGD:621068; rat.
DR   CTD; 55515; -.
DR   RGD; 621068; Asic4.
DR   eggNOG; KOG4294; Eukaryota.
DR   InParanoid; Q9JHS6; -.
DR   OrthoDB; 686369at2759; -.
DR   PhylomeDB; Q9JHS6; -.
DR   Reactome; R-RNO-2672351; Stimuli-sensing channels.
DR   PRO; PR:Q9JHS6; -.
DR   Proteomes; UP000002494; Unplaced.
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:0001662; P:behavioral fear response; ISO:RGD.
DR   GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR   InterPro; IPR001873; ENaC.
DR   InterPro; IPR020903; ENaC_CS.
DR   PANTHER; PTHR11690; PTHR11690; 1.
DR   Pfam; PF00858; ASC; 1.
DR   PRINTS; PR01078; AMINACHANNEL.
DR   PROSITE; PS01206; ASC; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
KW   Reference proteome; Sodium; Sodium channel; Sodium transport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..539
FT                   /note="Acid-sensing ion channel 4"
FT                   /id="PRO_0000181306"
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..438
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        439..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        460..539
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          501..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        243
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        341
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        376
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        118..202
FT                   /evidence="ECO:0000250"
FT   DISULFID        180..187
FT                   /evidence="ECO:0000250"
FT   DISULFID        296..375
FT                   /evidence="ECO:0000250"
FT   DISULFID        318..371
FT                   /evidence="ECO:0000250"
FT   DISULFID        322..369
FT                   /evidence="ECO:0000250"
FT   DISULFID        331..353
FT                   /evidence="ECO:0000250"
FT   DISULFID        333..345
FT                   /evidence="ECO:0000250"
FT   CONFLICT        283
FT                   /note="K -> E (in Ref. 2; CAB61836)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        401
FT                   /note="K -> R (in Ref. 2; CAB61836)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        536
FT                   /note="D -> N (in Ref. 2; CAB61836)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   539 AA;  59325 MW;  3D73DE0EAAFF7097 CRC64;
     MPIEIVCKIK FAEEDAKPKE KEAGDEQSLL GAAQGPAAPR DLATFASTST LHGLGRACGP
     GPHGLRRTLW VLALLTSLAA FLYQAASLAR GYLTRPHLVA MDPAAPAPVA GFPAVTLCNI
     NRFRHSALSD ADIFHLANLT GLPPKDRDGH RAAGLRYPEP DMVDILNRTG HQLADMLKSC
     NFSGHHCSAS NFSVVYTRYG KCYTFNADPQ SSLPSRAGGM GSGLEIMLDI QQEEYLPIWR
     ETNETSFEAG IRVQIHSQEE PPYIHQLGFG VSPGFQTFVS CQKQRLTYLP QPWGNCRAES
     KLREPELQGY SAYSVSACRL RCEKEAVLQR CHCRMVHMPG NETICPPNIY IECADHTLDS
     LGGGSEGPCF CPTPCNLTRY GKEISMVKIP NRGSARYLAR KYNRNETYIR ENFLVLDVFF
     EALTSEAMEQ RAAYGLSALL GDLGGQMGLF IGASILTLLE ILDYIYEVSW DRLKRVWRRP
     KTPLRTSTGG ISTLGLQELK EQSPCPNRGR AEGGGASNLL PNHHHPHGPP GSLFEDFAC
 
 
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