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GBRA6_RAT
ID   GBRA6_RAT               Reviewed;         453 AA.
AC   P30191;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 156.
DE   RecName: Full=Gamma-aminobutyric acid receptor subunit alpha-6;
DE   AltName: Full=GABA(A) receptor subunit alpha-6;
DE   Flags: Precursor;
GN   Name=Gabra6; Synonyms=Gabra-6;
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 [GENOMIC DNA].
RC   TISSUE=Brain;
RX   PubMed=2166916; DOI=10.1038/346648a0;
RA   Lueddens H., Pritchett D., Khler M., Killisch I., Keinaenen K., Monyer H.,
RA   Sprengel R., Seeburg P.H.;
RT   "Cerebellar GABAA receptor selective for a behavioural alcohol
RT   antagonist.";
RL   Nature 346:648-651(1990).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-403, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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   -!- SUBUNIT: Binds UBQLN1 (By similarity). Generally pentameric. There are
CC       five types of GABA(A) receptor chains: alpha, beta, gamma, delta, and
CC       rho. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC       protein. Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Only found in cerebellar granule cells.
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. GABRA6 sub-
CC       subfamily. {ECO:0000305}.
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DR   EMBL; L08495; AAC42034.1; -; Genomic_DNA.
DR   EMBL; X55742; CAA39273.1; -; Genomic_DNA.
DR   PIR; S11087; S11087.
DR   RefSeq; NP_068613.1; NM_021841.1.
DR   AlphaFoldDB; P30191; -.
DR   SMR; P30191; -.
DR   ComplexPortal; CPX-405; GABA-A receptor, alpha-6/beta-3/gamma-2.
DR   ComplexPortal; CPX-406; GABA-A receptor, alpha-6/beta-3/delta.
DR   ComplexPortal; CPX-407; GABA-A receptor, alpha-6/beta-2/delta.
DR   STRING; 10116.ENSRNOP00000004877; -.
DR   BindingDB; P30191; -.
DR   ChEMBL; CHEMBL293; -.
DR   DrugCentral; P30191; -.
DR   GlyGen; P30191; 3 sites.
DR   iPTMnet; P30191; -.
DR   PhosphoSitePlus; P30191; -.
DR   PaxDb; P30191; -.
DR   PRIDE; P30191; -.
DR   ABCD; P30191; 2 sequenced antibodies.
DR   GeneID; 29708; -.
DR   KEGG; rno:29708; -.
DR   UCSC; RGD:61861; rat.
DR   CTD; 2559; -.
DR   RGD; 61861; Gabra6.
DR   eggNOG; KOG3642; Eukaryota.
DR   InParanoid; P30191; -.
DR   OrthoDB; 1057372at2759; -.
DR   PhylomeDB; P30191; -.
DR   Reactome; R-RNO-977443; GABA receptor activation.
DR   PRO; PR:P30191; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0099192; C:cerebellar Golgi cell to granule cell synapse; IDA:SynGO.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0032590; C:dendrite membrane; IBA:GO_Central.
DR   GO; GO:1902711; C:GABA-A receptor complex; IBA:GO_Central.
DR   GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR   GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:RGD.
DR   GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IDA:SynGO.
DR   GO; GO:0016020; C:membrane; IDA:RGD.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0032809; C:neuronal cell body membrane; IDA:RGD.
DR   GO; GO:0098794; C:postsynapse; IBA:GO_Central.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:RGD.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:RGD.
DR   GO; GO:0043235; C:receptor complex; IDA:RGD.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0050809; F:diazepam binding; IDA:RGD.
DR   GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR   GO; GO:0004890; F:GABA-A receptor activity; IEA:InterPro.
DR   GO; GO:1901363; F:heterocyclic compound binding; IDA:RGD.
DR   GO; GO:0005237; F:inhibitory extracellular ligand-gated ion channel activity; IMP:RGD.
DR   GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR   GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR   GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; ISO:RGD.
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:0007214; P:gamma-aminobutyric acid signaling pathway; IBA:GO_Central.
DR   GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
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:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0051932; P:synaptic transmission, GABAergic; IMP:RGD.
DR   Gene3D; 1.20.58.390; -; 1.
DR   Gene3D; 2.70.170.10; -; 1.
DR   InterPro; IPR006028; GABAA/Glycine_rcpt.
DR   InterPro; IPR001390; GABAAa_rcpt.
DR   InterPro; IPR005436; GABBAa6_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; PR01079; GABAARALPHA.
DR   PRINTS; PR01619; GABAARALPHA6.
DR   PRINTS; PR00253; GABAARECEPTR.
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   1: Evidence at protein level;
KW   Cell membrane; Chloride; Chloride channel; Disulfide bond; Glycoprotein;
KW   Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW   Phosphoprotein; Postsynaptic cell membrane; Receptor; Reference proteome;
KW   Signal; Synapse; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..453
FT                   /note="Gamma-aminobutyric acid receptor subunit alpha-6"
FT                   /id="PRO_0000000449"
FT   TOPO_DOM        20..242
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        243..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        269..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        301..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        325..419
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        420..441
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         375
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16305"
FT   MOD_RES         403
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        128
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        156..170
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   453 AA;  51184 MW;  77EF2636A8B116F2 CRC64;
     MLLLLPWLFS LLWIENAQAQ LEDEGNFYSE NVSRILDNLL EGYDNRLRPG FGGAVTEVKT
     DIYVTSFGPV SDVEMEYTMD VFFRQTWTDE RLKFKGPAEI LSLNNLMVSK IWTPDTFFRN
     GKKSIAHNMT TPNKLFRLMH NGTILYTMRL TINADCPMRL VNFPMDGHAC PLKFGSYAYP
     KSEIIYTWKK GPLYSVEVPE ESSSLLQYDL IGQTVSSETI KSNTGEYVIM TVYFHLQRKM
     GYFMIQIYTP CIMTVILSQV SFWINKESVP ARTVFGITTV LTMTTLSISA RHSLPKVSYA
     TAMDWFIAVC FAFVFSALIE FAAVNYFTNL QSQKAERQAQ TAAKPPVAKS KTTESLEAEI
     VVHSDSKYHL KKRISSLTLP IVPSSEASKV LSRTPILPST PVTPPLLLPA IGGTSKIDQY
     SRILFPVAFA GFNLVYWIVY LSKDTMEVSS TVE
 
 
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