GBRG2_BOVIN
ID GBRG2_BOVIN Reviewed; 475 AA.
AC P22300;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 150.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2L AND 2S).
RC TISSUE=Brain cortex;
RX PubMed=1702226; DOI=10.1073/pnas.87.24.9966;
RA Whiting P.J., McKernan R.M., Iversen L.L.;
RT "Another mechanism for creating diversity in gamma-aminobutyrate type A
RT receptors: RNA splicing directs expression of two forms of gamma 2
RT phosphorylation site.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:9966-9970(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). The gamma2 subunit is necessary but not sufficient for
CC a rapid formation of active synaptic contacts and the synaptogenic
CC effect of this subunit is influenced by the type of alpha and beta
CC subunits present in the receptor pentamer (By similarity). The
CC alpha1/beta2/gamma2 receptor, alpha2/beta2/gamma2 receptor and the
CC alpha1/beta3/gamma2 receptor exhibit synaptogenic activity whereas the
CC alpha2/beta3/gamma2 receptor shows very little or no synaptogenic
CC activity (By similarity). Functions also as histamine receptor and
CC mediates 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 (By similarity). Interacts with GABARAP (By
CC similarity). Interacts with KIF21B (By similarity). Identified in a
CC complex of 720 kDa composed of LHFPL4, NLGN2, GABRA1, GABRB2, GABRG2
CC and GABRB3 (By similarity). Interacts with LHFPL4 (By similarity).
CC Interacts with SHISA7; interaction leads to the regulation of GABA(A)
CC receptor trafficking, channel deactivation kinetics and pharmacology
CC (By similarity). {ECO:0000250|UniProtKB:P18507,
CC ECO:0000250|UniProtKB:P18508, ECO:0000250|UniProtKB:P22723}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:P18507}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P18507}; Multi-pass
CC membrane protein {ECO:0000255}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P22723}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:P18508}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2L;
CC IsoId=P22300-1; Sequence=Displayed;
CC Name=2S;
CC IsoId=P22300-2; Sequence=VSP_000090;
CC -!- DOMAIN: The extracellular domain contributes to synaptic contact
CC formation. {ECO:0000250|UniProtKB:P22723}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P22723}.
CC -!- PTM: Palmitoylated by ZDHHC3/GODZ; required for the accumulation of
CC GABA(A) receptors at the postsynaptic membrane of inhibitory GABAergic
CC synapses. {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; M55563; AAA30531.1; -; mRNA.
DR PIR; B39272; B39272.
DR RefSeq; NP_776970.1; NM_174545.1. [P22300-1]
DR AlphaFoldDB; P22300; -.
DR SMR; P22300; -.
DR STRING; 9913.ENSBTAP00000013543; -.
DR ChEMBL; CHEMBL2094107; -.
DR DrugCentral; P22300; -.
DR iPTMnet; P22300; -.
DR PaxDb; P22300; -.
DR GeneID; 282240; -.
DR KEGG; bta:282240; -.
DR CTD; 2566; -.
DR eggNOG; KOG3642; Eukaryota.
DR InParanoid; P22300; -.
DR OrthoDB; 1057372at2759; -.
DR Proteomes; UP000009136; 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:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:1902711; C:GABA-A receptor complex; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005254; F:chloride channel activity; ISS:UniProtKB.
DR GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IEA:InterPro.
DR GO; GO:0004890; F:GABA-A receptor activity; ISS:UniProtKB.
DR GO; GO:0071420; P:cellular response to histamine; ISS:UniProtKB.
DR GO; GO:1902476; P:chloride transmembrane transport; ISS:UniProtKB.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IEA:InterPro.
DR GO; GO:1904862; P:inhibitory synapse assembly; ISS:UniProtKB.
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 Alternative splicing; Cell membrane; Cell projection; Chloride;
KW Chloride channel; Cytoplasmic vesicle; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Signal;
KW Synapse; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT CHAIN 40..475
FT /note="Gamma-aminobutyric acid receptor subunit gamma-2"
FT /id="PRO_0000000476"
FT TOPO_DOM 40..273
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 274..296
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 300..322
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 334..356
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 357..451
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 452..475
FT /note="Helical"
FT /evidence="ECO:0000305"
FT MOD_RES 382
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000305"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 190..204
FT /evidence="ECO:0000250"
FT VAR_SEQ 377..384
FT /note="Missing (in isoform 2S)"
FT /evidence="ECO:0000303|PubMed:1702226"
FT /id="VSP_000090"
FT VARIANT 230
FT /note="S -> G"
SQ SEQUENCE 475 AA; 55265 MW; A881082D3990197F CRC64;
MSSPNIWSTG SSVYSTPVFS QKMTLWILLL LSLYPGLTRQ KSDDDYEDYA SNKTWVLTPK
VPEGDVTVIL NNLLEGYDNK LRPDIGVKPT LIHTDMYVNS IGPVNAINME YTIDIFFGQT
WYDRRLKFNS TIKVLRLNSN MVGKIWIPDT FFRNSKKADA HWITTPNRML RIWNDGRVLY
TLRLTIDAEC QLQLHNFPMD EHSCPLEFSS YGYPREEIVY QWKRSSVEVS DTRSWRLYQF
SFVGLRNTTE VVKTTSGDYV VMTVYFDLSR RMGYFTIQTY IPCTLIVVLS WVSFWINKDA
VPARTSLGIT TVLTMTTLST IARKSLPKVS YVTAMDLFVS VCFIFVFSAL VEYGTLHYFV
SNRKPSKDKD KKKKNPLLRM FSFKAPTIDI RPRSATIQMN NATHLQERDE EYGYECLDGK
DCASFFCCFE DCRTGAWRHG RIHIRIAKMD SYARIFFPTA FCLFNLVYWV SYLYL
