GBRA2_BOVIN
ID GBRA2_BOVIN Reviewed; 451 AA.
AC P10063;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 158.
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;
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], FUNCTION, AND ACTIVITY REGULATION.
RC TISSUE=Brain;
RX PubMed=2842688; DOI=10.1038/335076a0;
RA Levitan E.S., Schofield P.R., Burt D.R., Rhee L.M., Wisdes W., Koehler M.,
RA Rodriguez H., Stephenson F.A., Darlison M.G., Barnard E.A., Seeburg P.H.;
RT "Structural and functional basis for GABAA receptor heterogeneity.";
RL Nature 335:76-79(1988).
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 (PubMed:2842688). 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 ECO:0000269|PubMed:2842688}.
CC -!- ACTIVITY REGULATION: Activated by pentobarbital (PubMed:2842688).
CC Inhibited by the antagonist bicuculline (PubMed:2842688).
CC {ECO:0000269|PubMed:2842688}.
CC -!- SUBUNIT: Heteropentamer, formed by a combination of alpha, beta, gamma,
CC delta and rho chains. Interacts with UBQLN1 (By similarity). Interacts
CC with KIF21B (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:P23576,
CC ECO:0000250|UniProtKB:P26048}.
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:0000250|UniProtKB:P23576}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P26048}.
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; X12361; CAA30924.1; -; mRNA.
DR PIR; S12510; ACBOG2.
DR RefSeq; NP_776966.1; NM_174541.2.
DR RefSeq; XP_010804413.1; XM_010806111.1.
DR RefSeq; XP_015319236.1; XM_015463750.1.
DR AlphaFoldDB; P10063; -.
DR SMR; P10063; -.
DR STRING; 9913.ENSBTAP00000015688; -.
DR ChEMBL; CHEMBL2094107; -.
DR DrugCentral; P10063; -.
DR PaxDb; P10063; -.
DR GeneID; 282236; -.
DR KEGG; bta:282236; -.
DR CTD; 2555; -.
DR eggNOG; KOG3642; Eukaryota.
DR InParanoid; P10063; -.
DR OrthoDB; 1057372at2759; -.
DR PRO; PR:P10063; -.
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:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IEA:InterPro.
DR GO; GO:0004890; F:GABA-A receptor activity; IEA:InterPro.
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; IPR001390; GABAAa_rcpt.
DR InterPro; IPR005432; GABBAa2_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 PANTHER; PTHR18945:SF218; PTHR18945:SF218; 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; 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; 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_0000000432"
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 CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 166..180
FT /evidence="ECO:0000250"
SQ SEQUENCE 451 AA; 51146 MW; 74DBDA860E6EB551 CRC64;
MKTKLNSSNM QLLLFVFLAW DPARLVLANI QEDEAKNNIT IFTRILDRLL DGYDNRLRPG
LGDSITEVFT NIYVTSFGPV SDTDMEYTID VFFRQKWKDE RLKFKGPMNI LRLNNLMASK
IWTPDTFFHN GKKSVAHNMT MPNKLLRIQD DGTLLYTMRL TVQAECPMHL EDFPMDAHSC
PLKFGSYAYT TSEVTYIWTY NASDSVQVAP DGSRLNQYDL PGQSIGKETI KSSTGEYTVM
TAHFHLKRKI GYFVIQTYLP CIMTVILSQV SFWLNRESVP ARTVFGVTTV LTMTTLSISA
RNSLPKVAYA TAMDWFIAVC YAFVFSALIE FATVNYFTKR GWAWDGKSVV NDKKKEKASV
MIQNNAYAVA VANYAPNLSK DPVLSTISKS ATTPEPNKKP ENKPAEAKKT FNSVSKIDRM
SRIVFPVLFG TFNLVYWATY LNREPVLGVS P
