GBRG2_CHICK
ID GBRG2_CHICK Reviewed; 474 AA.
AC P21548;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Gamma-aminobutyric acid receptor subunit gamma-2;
DE AltName: Full=GABA(A) receptor subunit gamma-2;
DE Flags: Precursor;
GN Name=GABRG2;
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=2175889; DOI=10.1093/nar/18.23.7157;
RA Glencorse T.A., Bateson A.N., Darlison M.G.;
RT "Sequence of the chicken GABAA receptor gamma 2-subunit cDNA.";
RL Nucleic Acids Res. 18:7157-7157(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). Functions also as histamine receptor and mediates
CC cellular responses to histamine (By similarity).
CC {ECO:0000250|UniProtKB:P22723}.
CC -!- ACTIVITY REGULATION: Allosterically activated by benzodiazepines (By
CC similarity). Activated by pentobarbitol (By similarity). Inhibited by
CC the antagonist bicuculline (By similarity). Inhibited by zinc ions (By
CC similarity). {ECO:0000250|UniProtKB:P18507,
CC ECO:0000250|UniProtKB:P18508}.
CC -!- SUBUNIT: Heteropentamer, formed by a combination of alpha, beta, gamma,
CC delta and rho chains. {ECO:0000250|UniProtKB:P22723}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:P22723}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P22723}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- DOMAIN: The extracellular domain contributes to synaptic contact
CC formation. {ECO:0000250|UniProtKB:P22723}.
CC -!- MISCELLANEOUS: This subunit carries the benzodiazepine binding site.
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. GABRG2 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; X54944; CAA38704.1; -; mRNA.
DR PIR; S13086; S13086.
DR RefSeq; NP_990676.1; NM_205345.2.
DR AlphaFoldDB; P21548; -.
DR SMR; P21548; -.
DR STRING; 9031.ENSGALP00000034151; -.
DR iPTMnet; P21548; -.
DR PaxDb; P21548; -.
DR Ensembl; ENSGALT00000065912; ENSGALP00000053851; ENSGALG00000038042.
DR GeneID; 396289; -.
DR KEGG; gga:396289; -.
DR CTD; 2566; -.
DR VEuPathDB; HostDB:geneid_396289; -.
DR eggNOG; KOG3642; Eukaryota.
DR GeneTree; ENSGT00940000156685; -.
DR HOGENOM; CLU_010920_2_0_1; -.
DR InParanoid; P21548; -.
DR OMA; PMDVHSC; -.
DR OrthoDB; 1057372at2759; -.
DR PhylomeDB; P21548; -.
DR PRO; PR:P21548; -.
DR Proteomes; UP000000539; Chromosome 13.
DR Bgee; ENSGALG00000038042; Expressed in brain and 1 other tissue.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
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; ISS:UniProtKB.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005254; F:chloride channel activity; ISS:UniProtKB.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0004890; F:GABA-A receptor activity; ISS:UniProtKB.
DR GO; GO:0022851; F:GABA-gated chloride ion channel activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0030534; P:adult behavior; IEA:Ensembl.
DR GO; GO:0071420; P:cellular response to histamine; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; ISS:UniProtKB.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IBA:GO_Central.
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:0009791; P:post-embryonic development; IEA:Ensembl.
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; 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; IPR005439; GABBAg2_rcpt.
DR InterPro; IPR005437; GABRG-1/4.
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; PR01620; GABAARGAMMA.
DR PRINTS; PR01622; GABAARGAMMA2.
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..38
FT /evidence="ECO:0000255"
FT CHAIN 39..474
FT /note="Gamma-aminobutyric acid receptor subunit gamma-2"
FT /id="PRO_0000000480"
FT TOPO_DOM 39..272
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 273..295
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 299..321
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 333..355
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 356..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 451..474
FT /note="Helical"
FT /evidence="ECO:0000305"
FT REGION 376..383
FT /note="Insertion, similar to human gamma-2 sequence which
FT is proposed to be caused by alternative splicing"
FT CARBOHYD 51
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 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 189..203
FT /evidence="ECO:0000250"
SQ SEQUENCE 474 AA; 54970 MW; 79A172CCEA59C9CF CRC64;
MTPSNPTRLG STALLNPAFS LKMMVWALVF LSLIQCSTQK GDDDYEDYTS NKTWVLTPKV
HESDVTLILN GLLEGYDNKL RPDIGVKPTV IHTDMYVNSI GPVNAINMEY TIDIFFAQTW
YDRRLKFNST IKVLRLNSNM VGKIWIPDTF FRNSKKADAH WITTPNRMLR IWNDGRVLYT
LRLTIDAECQ LQLHNFPMDA HSCPLEFSSY GYPREEIIYQ WKRSSVEVGD TRSWRLYQFS
FTGLRNTTEV VKTTSGDYVV MSVYFNLSRR MGYFTIQTYI PCTLIVVLSW VSFWINKDAV
PARTSLGITT VLTMTTLSTI ARKSLPKVSY VTAMDLFVSV CFIFVFSALV EYGTLHYFVS
NRKPSKDKDK KKKNPLLRMF SFKAPTIDIR PRSATIQMNN ATHLQERDEE YGYECLDGKD
CASFFCCFED CRTGAWRHGR IHIRIAKMDS YARIFFPTAF CLFNLVYWVS YLYL
