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   08-NOV-2023, entry version 155.
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   GlyCosmos; P22300; 3 sites, No reported glycans.
DR   iPTMnet; P22300; -.
DR   PaxDb; 9913-ENSBTAP00000013543; -.
DR   GeneID; 282240; -.
DR   KEGG; bta:282240; -.
DR   CTD; 2566; -.
DR   eggNOG; KOG3642; Eukaryota.
DR   InParanoid; P22300; -.
DR   OrthoDB; 4265336at2759; -.
DR   Proteomes; UP000009136; Unplaced.
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:0032590; C:dendrite membrane; IBA:GO_Central.
DR   GO; GO:1902711; C:GABA-A receptor complex; ISS:UniProtKB.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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: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 monoatomic ion channel activity; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:1904862; P:inhibitory synapse assembly; ISS:UniProtKB.
DR   GO; GO:0060078; P:regulation of postsynaptic membrane potential; IBA:GO_Central.
DR   GO; GO:0051932; P:synaptic transmission, GABAergic; IBA:GO_Central.
DR   CDD; cd19000; LGIC_ECD_GABAAR_G; 1.
DR   CDD; cd19054; LGIC_TM_GABAAR_gamma; 1.
DR   Gene3D; 2.70.170.10; Neurotransmitter-gated ion-channel ligand-binding domain; 1.
DR   Gene3D; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 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   NCBIfam; TIGR00860; LIC; 1.
DR   PANTHER; PTHR18945:SF498; GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT GAMMA-2; 1.
DR   PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 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; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 1.
DR   SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 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
//