GBRB_LYMST
ID GBRB_LYMST Reviewed; 499 AA.
AC P26714;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Gamma-aminobutyric acid receptor subunit beta;
DE AltName: Full=GABA(A) receptor;
DE Flags: Precursor;
OS Lymnaea stagnalis (Great pond snail) (Helix stagnalis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Lymnaeidae; Lymnaea.
OX NCBI_TaxID=6523;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1655414; DOI=10.1002/j.1460-2075.1991.tb04887.x;
RA Harvey R.J., Vreugdenhil E., Zaman S.H., Bhandal N.S., Usherwood P.N.R.,
RA Barnard E.A., Darlison M.G.;
RT "Sequence of a functional invertebrate GABAA receptor subunit which can
RT form a chimeric receptor with a vertebrate alpha subunit.";
RL EMBO J. 10:3239-3245(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 201-334.
RX PubMed=2164988; DOI=10.1042/bst0180438;
RA Harvey R.J., Vreugdenhil E., Barnard E.A., Darlison M.G.;
RT "Cloning of genomic and cDNA sequences encoding an invertebrate gamma-
RT aminobutyric acid A receptor subunit.";
RL Biochem. Soc. Trans. 18:438-439(1990).
CC -!- FUNCTION: GABA, an inhibitory neurotransmitter, mediates neuronal
CC inhibition by binding to the GABA/benzodiazepine receptor and opening
CC an integral chloride channel.
CC -!- SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor
CC chains: alpha, beta, gamma, delta, and rho.
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. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X58638; CAA41495.1; -; mRNA.
DR PIR; S17785; S17785.
DR AlphaFoldDB; P26714; -.
DR SMR; P26714; -.
DR TCDB; 1.A.9.5.13; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
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 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; 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; 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 Postsynaptic cell membrane; Receptor; Signal; Synapse; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..499
FT /note="Gamma-aminobutyric acid receptor subunit beta"
FT /id="PRO_0000000467"
FT TOPO_DOM 24..251
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 252..273
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 278..299
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 311..333
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 334..475
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 476..499
FT /note="Helical"
FT /evidence="ECO:0000305"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 167..181
FT /evidence="ECO:0000250"
FT CONFLICT 232
FT /note="S -> L (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 499 AA; 57082 MW; F81C9F2A850D62F4 CRC64;
MWGIIVPFFS ASLMCSLVAV VRCQQDTDHF ANVTNTIDSL LKGYDIRLRP SFGGAPLEIG
IEVILASFDS ISEVDMDYTI TMYLNQYWRD ERLQFIFNES LDLGENRSVT TMTLTGAFAE
KIWVPDTFLA NDKNSFLHDI TEKNKMVRLY GNGSLVYGMR FTTTLACMMD LHNYPLDHQE
CTVEIESYGY TMDDIVLYWL NDRGAVTGVE DVSLPQFSIT NYATINKIEE LSTGDYQRLS
LIFQLQRNIG YFIFQTYLPS ILIVMLSWVS FWINHEATSA RVALGITTVL TMTTISNGVR
SSLPRISYVK AIDIYLVMCF VFVFAALLEY AAVNYTYWGA RAKRKAKRLR ERATSVRKRV
DDGDQMNNTN MDTVELKEVH MVPTSVGVTN SQSFNLDLDD GSGDDTGFRV VPPIPRSFTH
SHATTHGYIP TNVVRRRSSS HVPPRRRRLL SHFRQKAKSI KVKIPRVQDV NTIDKYARLM
FPLLFIIFNT SYWSVYLLT
