GBRB3_CHICK
ID GBRB3_CHICK Reviewed; 476 AA.
AC P19019;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Gamma-aminobutyric acid receptor subunit beta-3;
DE AltName: Full=GABA(A) receptor subunit beta-3;
DE Flags: Precursor;
GN Name=GABRB3;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Commercial Rhode Island cross; TISSUE=Brain;
RX PubMed=2170940; DOI=10.1093/nar/18.18.5557;
RA Bateson A.N., Harvey R.J., Blocks C.C.M., Darlison M.G.;
RT "Sequence of the chicken GABAA receptor beta 3-subunit cDNA.";
RL Nucleic Acids Res. 18:5557-5557(1990).
CC -!- FUNCTION: Ligand-gated chloride channel which is a component of the
CC heteropentameric receptor for GABA, the major inhibitory
CC neurotransmitter in the brain (By similarity). Plays an important role
CC in the formation of functional inhibitory GABAergic synapses in
CC addition to mediating synaptic inhibition as a GABA- gated ion channel
CC (By similarity). {ECO:0000250|UniProtKB:P28472}.
CC -!- SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor
CC chains: alpha, beta, gamma, delta, and rho.
CC {ECO:0000250|UniProtKB:P28472}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:P28472}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P28472}. Cell membrane
CC {ECO:0000250|UniProtKB:P28472}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P28472}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:P63079}.
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. GABRB3 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; X54243; CAA38147.1; -; mRNA.
DR PIR; S11440; S11440.
DR RefSeq; NP_990677.1; NM_205346.3.
DR AlphaFoldDB; P19019; -.
DR SMR; P19019; -.
DR STRING; 9031.ENSGALP00000026977; -.
DR PaxDb; P19019; -.
DR PRIDE; P19019; -.
DR Ensembl; ENSGALT00000077202; ENSGALP00000050049; ENSGALG00000029392.
DR GeneID; 396290; -.
DR KEGG; gga:396290; -.
DR CTD; 2562; -.
DR VEuPathDB; HostDB:geneid_396290; -.
DR eggNOG; KOG3643; Eukaryota.
DR GeneTree; ENSGT00940000154713; -.
DR HOGENOM; CLU_010920_0_1_1; -.
DR InParanoid; P19019; -.
DR OMA; MYWKDTP; -.
DR OrthoDB; 480926at2759; -.
DR PhylomeDB; P19019; -.
DR Reactome; R-GGA-977443; GABA receptor activation.
DR PRO; PR:P19019; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000029392; Expressed in brain.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1902711; C:GABA-A receptor complex; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR GO; GO:0022851; F:GABA-gated chloride ion channel activity; ISS:UniProtKB.
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; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:1904862; P:inhibitory synapse assembly; ISS:UniProtKB.
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:0007165; P:signal transduction; 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; IPR002289; GABAAb_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; PR01160; GABAARBETA.
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 2: Evidence at transcript level;
KW Cell membrane; Chloride; Chloride channel; Cytoplasmic vesicle;
KW Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..476
FT /note="Gamma-aminobutyric acid receptor subunit beta-3"
FT /id="PRO_0000000465"
FT TOPO_DOM 26..245
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 246..267
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 271..293
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 305..327
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 328..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 454..475
FT /note="Helical"
FT /evidence="ECO:0000305"
FT REGION 402..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 161..175
FT /evidence="ECO:0000250"
SQ SEQUENCE 476 AA; 54433 MW; 8DD0AB7CF7BB3698 CRC64;
MWGFGGGRIF GIFSAPVLVA VVCCAQSVND PGNMSFVKET VDKLLKGYDI RLRPDFGGPP
VCVGMNIDIA SIDMVSEVNM DYTLTMYFQQ YWRDKRLAYA GIPLNLTLDN RVADQLWVPD
TYFLNDKKSF VHGVTVKNRM IRLHPDGTVL YGLRITTTAA CMMDLRRYPL DEQNCTLEIE
SYGYTTDDIE FYWRGGDNAV TGVERIELPQ FSIVEYRLVS KNVVFATGAY PRLSLSFRLK
RNIGYFILQT YMPSILITIL SWVSFWINYD ASAARVALGI TTVLTMTTIN THLRETLPKI
PYVKAIDMYL MGCFVFVFLA LLEYAFVNYI FFGKGPQRQK KLAEKSAKAN NDRSRFEGSR
VDTHGNILLT SLEIHNEVAS NEVTTSVTDA RNSTISFDNS GIQYRKQSSH RESLGRRSSD
RTGSHSKRGH LRRRSSQLKI KIPDLTDVNA IDRWSRMVFP FTFSLFNLIY WLYYVN
