GBRA3_BOVIN
ID GBRA3_BOVIN Reviewed; 492 AA.
AC P10064;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Gamma-aminobutyric acid receptor subunit alpha-3;
DE AltName: Full=GABA(A) receptor subunit alpha-3;
DE Flags: Precursor;
GN Name=GABRA3;
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].
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: GABA, the major inhibitory neurotransmitter in the vertebrate
CC brain, mediates neuronal inhibition by binding to the
CC GABA/benzodiazepine receptor and opening an integral chloride channel.
CC -!- SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor
CC chains: alpha, beta, gamma, delta, and rho. Binds UBQLN1 (By
CC similarity). Interacts with GPHN (By similarity).
CC {ECO:0000250|UniProtKB:P26049, ECO:0000250|UniProtKB:P34903}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC protein. Cell membrane; Multi-pass membrane protein.
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. GABRA3 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; X12362; CAA30925.1; -; mRNA.
DR PIR; S12511; CHBOA3.
DR RefSeq; NP_776967.1; NM_174542.2.
DR AlphaFoldDB; P10064; -.
DR SMR; P10064; -.
DR STRING; 9913.ENSBTAP00000008798; -.
DR ChEMBL; CHEMBL2094107; -.
DR DrugCentral; P10064; -.
DR PaxDb; P10064; -.
DR PRIDE; P10064; -.
DR GeneID; 282237; -.
DR KEGG; bta:282237; -.
DR CTD; 2556; -.
DR eggNOG; KOG3642; Eukaryota.
DR InParanoid; P10064; -.
DR OrthoDB; 1057372at2759; -.
DR PRO; PR:P10064; -.
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: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 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; IPR005433; GABBAa3_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 Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
DR PRINTS; PR01079; GABAARALPHA.
DR PRINTS; PR01616; GABAARALPHA3.
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; Chloride; Chloride channel; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW Phosphoprotein; Postsynaptic cell membrane; Receptor; Reference proteome;
KW Signal; Synapse; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..492
FT /note="Gamma-aminobutyric acid receptor subunit alpha-3"
FT /id="PRO_0000000436"
FT TOPO_DOM 29..276
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 277..298
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 304..325
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 338..359
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 360..457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 458..479
FT /note="Helical"
FT /evidence="ECO:0000305"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26049"
FT MOD_RES 427
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P26049"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26049"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 191..205
FT /evidence="ECO:0000250"
SQ SEQUENCE 492 AA; 55284 MW; 5C79AAA6F22F3413 CRC64;
MIITQMSQFY MAGLGLLFLI NILPGTTGQV ESRRQEPGDF VKQDIGGLSP KHAPDIPDDS
TDNITIFTRI LDRLLDGYDN RLRPGLGDAV TEVKTDIYVT SFGPVSDTDM EYTIDVFFRQ
TWHDERLKFD GPMKILPLNN LLASKIWTPD TFFHNGKKSV AHNMTTPNKL LRLVDNGTLL
YTMRLTIHAE CPMHLEDFPM DVHACPLKFG SYAYTTAEVV YSWTLGKNKS VEVAQDGSRL
NQYDLLGHVV GTEIIRSSTG EYVVMTTHFH LKRKIGYFVI QTYLPCIMTV ILSQVSFWLN
RESVPARTVF GVTTVLTMTT LSISARNSLP KVAYATAMDW FMAVCYAFVF SALIEFATVN
YFTKRSWAWE GKKVPEALEM KKKTPAVPTK KTSTTFNIVG TTYPINLAKD TEFSAISKGA
APSTSSTPTI IASPKTTCVQ DIPTETKTYN SVSKVDKISR IIFPVLFAIF NLVYWATYVN
RESAIKGMIR KQ
