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GBRE_RAT
ID   GBRE_RAT                Reviewed;         506 AA.
AC   Q9ES14; O55209;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Gamma-aminobutyric acid receptor subunit epsilon;
DE   AltName: Full=GABA(A) receptor subunit epsilon;
DE   Flags: Precursor;
GN   Name=Gabre;
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.
RX   PubMed=11122342; DOI=10.1111/j.1460-9568.2000.01343.x;
RA   Moragues N., Ciofi P., Lafon P., Odessa M.F., Tramu G., Garret M.;
RT   "cDNA cloning and expression of a gamma-aminobutyric acid A receptor
RT   epsilon-subunit in rat brain.";
RL   Eur. J. Neurosci. 12:4318-4330(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 123-506.
RA   Hanna M.C., Hales T.G., Kirkness E.F.;
RT   "Alternative transcripts of a gene encoding the GABA-A receptor epsilon
RT   subunit on chromosome Xq28.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate
CC       brain, mediates neuronal inhibition by binding to the
CC       GABA/benzodiazepine receptor and opening an integral chloride channel.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Generally pentameric. Associates with alpha and beta subunits
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. GABRE sub-
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF255612; AAG17631.1; -; mRNA.
DR   EMBL; U92284; AAB93879.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9ES14; -.
DR   SMR; Q9ES14; -.
DR   STRING; 10116.ENSRNOP00000022431; -.
DR   ChEMBL; CHEMBL1907607; -.
DR   DrugCentral; Q9ES14; -.
DR   GlyGen; Q9ES14; 2 sites.
DR   PaxDb; Q9ES14; -.
DR   ABCD; Q9ES14; 1 sequenced antibody.
DR   RGD; 68320; Gabre.
DR   eggNOG; KOG3642; Eukaryota.
DR   InParanoid; Q9ES14; -.
DR   PRO; PR:Q9ES14; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0032590; C:dendrite membrane; IBA:GO_Central.
DR   GO; GO:1902711; C:GABA-A receptor complex; ISO:RGD.
DR   GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0098794; C:postsynapse; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR   GO; GO:0004890; F:GABA-A receptor activity; IDA:RGD.
DR   GO; GO:0022851; F:GABA-gated chloride ion channel activity; ISO:RGD.
DR   GO; GO:0005237; F:inhibitory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR   GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR   GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006821; P:chloride transport; TAS:RGD.
DR   GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IDA:RGD.
DR   GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:2001226; P:negative regulation of chloride transport; ISO:RGD.
DR   GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR   GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR   GO; GO:0060078; P:regulation of postsynaptic membrane potential; IBA:GO_Central.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0051932; P:synaptic transmission, GABAergic; IBA:GO_Central.
DR   Gene3D; 1.20.58.390; -; 1.
DR   Gene3D; 2.70.170.10; -; 1.
DR   InterPro; IPR006028; GABAA/Glycine_rcpt.
DR   InterPro; IPR008099; GABAAe_rcpt.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR   InterPro; IPR038050; Neuro_actylchol_rec.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   PANTHER; PTHR18945; PTHR18945; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR00253; GABAARECEPTR.
DR   PRINTS; PR01723; GABAAREPSLON.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF63712; SSF63712; 1.
DR   SUPFAM; SSF90112; SSF90112; 1.
DR   TIGRFAMs; TIGR00860; LIC; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Chloride; Chloride channel; Disulfide bond; Glycoprotein;
KW   Ion channel; Ion transport; Membrane; Postsynaptic cell membrane;
KW   Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..506
FT                   /note="Gamma-aminobutyric acid receptor subunit epsilon"
FT                   /id="PRO_0000000472"
FT   TOPO_DOM        23..254
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        255..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        282..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        345..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        366..485
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        486..506
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          32..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        253
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        196..210
FT                   /evidence="ECO:0000250"
FT   CONFLICT        133
FT                   /note="R -> C (in Ref. 2; AAB93879)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        467
FT                   /note="N -> S (in Ref. 2; AAB93879)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   506 AA;  59219 MW;  8C2FBECF10686E57 CRC64;
     MLPKVLLMLL NMFLALQWRV GPHIKLENKP PAQDKVVFGP QPQPSGKKLP ARETELTADH
     TTERPRGKLT RASQILNTIL SNYDHKLRPS IGEKPTVVTV KVFVNSLGPI SILDMEYSID
     IIFYQTWYDE RLRYNDTFET LILHGNVVSQ LWIPDTFFRN SKRTQEYDIT IPNQMALIHK
     DGKVLYTVRM TIDARCSLHM LNFPMDSHSC PLSFSSFSYD EHEMIYKWEN FKLKIDAKNT
     WKLLEFDFTG VNNKTEIIST PVGDFMVMTF FFNVSRRFGF IVFQNYIPSS VTTMLSWVSF
     WIKIEAAAAR ASVGVSSVLT MATLGTFSRK NFPRVSYLTA LDFYIAICFV LCFCTLLEFT
     VLNFLTYNNI ERQASPKFYQ FPTNSRANAR TRARARTRAR ARARARQQQE VFVCEIVTYE
     ENAEEGYQWS PRSRRPQCPW RRCGRSYVCF RVLRKYFCMV PGCEGNNWQR GRICIHVYRL
     DNYSRVLFPI TFFFFNVVYW VICLNL
 
 
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