ID GBRA2_RAT Reviewed; 451 AA.
AC P23576;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 27-MAR-2024, entry version 164.
DE RecName: Full=Gamma-aminobutyric acid receptor subunit alpha-2;
DE AltName: Full=GABA(A) receptor subunit alpha-2;
DE Flags: Precursor;
GN Name=Gabra2; Synonyms=Gabra-2;
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=1849552; DOI=10.1111/j.1471-4159.1991.tb02072.x;
RA Khrestchatisky M., Maclennan A.J., Tillakaratne N.J.K., Chiang M.Y.,
RA Tobin A.J.;
RT "Sequence and regional distribution of the mRNA encoding the alpha 2
RT polypeptide of rat gamma-aminobutyric acidA receptors.";
RL J. Neurochem. 56:1717-1722(1991).
RN [2]
RP INTERACTION WITH KIF21B, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25172774; DOI=10.1016/j.ejcb.2014.07.007;
RA Labonte D., Thies E., Kneussel M.;
RT "The kinesin KIF21B participates in the cell surface delivery of gamma2
RT subunit-containing GABAA receptors.";
RL Eur. J. Cell Biol. 93:338-346(2014).
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 alpha2/beta2/gamma2 receptor exhibits synaptogenic activity whereas the
CC alpha2/beta3/gamma2 receptor shows very little or no synaptogenic
CC activity (By similarity). {ECO:0000250|UniProtKB:P26048}.
CC -!- ACTIVITY REGULATION: Activated by pentobarbital (By similarity).
CC Inhibited by the antagonist bicuculline (By similarity).
CC {ECO:0000250|UniProtKB:P10063}.
CC -!- SUBUNIT: Heteropentamer, formed by a combination of alpha, beta, gamma,
CC delta and rho chains (By similarity). Binds UBQLN1 (By similarity).
CC Interacts with KIF21B (PubMed:25172774). Interacts with LHFPL4 (By
CC similarity). Interacts with SHISA7; interaction leads to the regulation
CC of GABA(A) receptor trafficking, channel deactivation kinetics and
CC pharmacology (By similarity). {ECO:0000250|UniProtKB:P26048,
CC ECO:0000269|PubMed:25172774}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:P26048}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P26048}; Multi-pass
CC membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:25172774}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P26048}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:25172774}.
CC -!- DOMAIN: The extracellular domain contributes to synaptic contact
CC formation. {ECO:0000250|UniProtKB:P26048}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P26048}.
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. GABRA2 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; L08491; AAC42030.1; ALT_SEQ; Genomic_DNA.
DR PIR; JH0370; JH0370.
DR AlphaFoldDB; P23576; -.
DR SMR; P23576; -.
DR ComplexPortal; CPX-412; GABA-A receptor, alpha-2/beta-3/gamma-2.
DR CORUM; P23576; -.
DR STRING; 10116.ENSRNOP00000003197; -.
DR BindingDB; P23576; -.
DR ChEMBL; CHEMBL341; -.
DR DrugCentral; P23576; -.
DR GlyCosmos; P23576; 3 sites, 12 glycans.
DR GlyGen; P23576; 3 sites, 12 N-linked glycans (1 site).
DR iPTMnet; P23576; -.
DR PhosphoSitePlus; P23576; -.
DR PaxDb; 10116-ENSRNOP00000060621; -.
DR ABCD; P23576; 2 sequenced antibodies.
DR UCSC; RGD:61856; rat.
DR AGR; RGD:61856; -.
DR RGD; 61856; Gabra2.
DR eggNOG; KOG3642; Eukaryota.
DR InParanoid; P23576; -.
DR PhylomeDB; P23576; -.
DR Reactome; R-RNO-977443; GABA receptor activation.
DR PRO; PR:P23576; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0032590; C:dendrite membrane; IDA:BHF-UCL.
DR GO; GO:1902711; C:GABA-A receptor complex; ISO:RGD.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0060077; C:inhibitory synapse; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; ISO:RGD.
DR GO; GO:0099634; C:postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:0048787; C:presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:RGD.
DR GO; GO:0008503; F:benzodiazepine receptor activity; ISO:RGD.
DR GO; GO:0004890; F:GABA-A receptor activity; TAS:RGD.
DR GO; GO:0022851; F:GABA-gated chloride ion channel activity; ISO:RGD.
DR GO; GO:0005237; F:inhibitory extracellular ligand-gated monoatomic ion channel activity; IBA:GO_Central.
DR GO; GO:0099507; F:ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential; ISO:RGD.
DR GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; ISO:RGD.
DR GO; GO:1902476; P:chloride transmembrane transport; ISO:RGD.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; ISO:RGD.
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; cd19052; LGIC_TM_GABAAR_alpha; 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; IPR001390; GABAAa_rcpt.
DR InterPro; IPR005432; GABBAa2_rcpt.
DR InterPro; IPR047024; Gabra-1-6_TM.
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:SF218; GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT ALPHA-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; PR01079; GABAARALPHA.
DR PRINTS; PR01615; GABAARALPHA2.
DR PRINTS; PR00253; GABAARECEPTR.
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 1: Evidence at protein level;
KW Cell membrane; Cell projection; Chloride; Chloride channel;
KW Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Ligand-gated ion channel; Membrane;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..451
FT /note="Gamma-aminobutyric acid receptor subunit alpha-2"
FT /id="PRO_0000000435"
FT TOPO_DOM 29..251
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 252..273
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 279..300
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 313..334
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 335..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 420..441
FT /note="Helical"
FT /evidence="ECO:0000305"
FT REGION 389..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 166..180
FT /evidence="ECO:0000250"
SQ SEQUENCE 451 AA; 51182 MW; 47F507F015DAE5DD CRC64;
MRTKLSTCNV WFPLLVLLVW NPARLVLANI QEDEAKNNIT IFTRILDRLL DGYDNRLRPG
LGDSITEVFT NIYVTSFGPV SDTDMEYTID VFFRQKWKDE RLKFKGPMNI LRLNNSMASK
IWTPDTFFHN GKKSVAHNMT MPNKLLRIQD DGTLLYTMRL TVQAECPMHL EDFPMDAHSC
PLKFGSYAYT TSEVTYIWTY NPSDSVQVAP DGSRLNQYDL LGQSIGKETI KSSTGEYTVM
TAHFHLKRKI GYFVIQTYLP CIMTVILSQV SFWLNRESVP ARTVFGVTTV LTMTTLSISA
RNSLPKVAYA TAMDWFIAVC YAFVFSALIE FATVNYFTKR GWAWDGKSVV NDKKKEKGSV
MIQNNAYAVA VANYAPNLSK DPVLSTISKS ATTPEPNKKP ENKPAEAKKT FNSVSKIDRM
SRIVFPVLFG TFNLVYWATY LNREPVLGVS P
//
