GLRB_BOVIN
ID GLRB_BOVIN Reviewed; 497 AA.
AC Q9GJS9; Q08DZ9;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Glycine receptor subunit beta;
DE AltName: Full=Glycine receptor 58 kDa subunit;
DE Flags: Precursor;
GN Name=GLRB;
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 [GENOMIC DNA / MRNA].
RX PubMed=11178872; DOI=10.1006/mcne.2000.0934;
RA Pierce K.D., Handford C.A., Morris R., Vafa B., Dennis J.A., Healy P.J.,
RA Schofield P.R.;
RT "A nonsense mutation in the alpha1 subunit of the inhibitory glycine
RT receptor associated with bovine myoclonus.";
RL Mol. Cell. Neurosci. 17:354-363(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Glycine receptors are ligand-gated chloride channels. GLRB
CC does not form ligand-gated ion channels by itself, but is part of
CC heteromeric ligand-gated chloride channels. Channel opening is
CC triggered by extracellular glycine. Heteropentameric channels composed
CC of GLRB and GLRA1 are activated by lower glycine levels than
CC homopentameric GLRA1. Plays an important role in the down-regulation of
CC neuronal excitability. Contributes to the generation of inhibitory
CC postsynaptic currents. {ECO:0000250|UniProtKB:P48167,
CC ECO:0000250|UniProtKB:P48168}.
CC -!- SUBUNIT: Heteropentamer composed of GLRB and GLRA1. Heteropentamer
CC composed of GLRB and GLRA2. Heteropentamer composed of GLRB and GLRA3.
CC Heteropentamer composed of two GLRA1 and three GLRB subunits.
CC Heteropentamer composed of three GLRA1 and two GLRB subunits. Interacts
CC with GPHN. {ECO:0000250|UniProtKB:P48167}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:P48168}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P23415}. Synapse {ECO:0000250|UniProtKB:P48168}.
CC Cell projection, dendrite {ECO:0000250|UniProtKB:P48168}. Cell membrane
CC {ECO:0000250|UniProtKB:P48168}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P23415}. Cytoplasm
CC {ECO:0000250|UniProtKB:P48167}. Note=Retained in the cytoplasm upon
CC heterologous expression by itself. Coexpression with GPHN promotes
CC expression at the cell membrane. Coexpression with GLRA1, GLRA2 or
CC GLRA3 promotes expression at the cell membrane.
CC {ECO:0000250|UniProtKB:P20781}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Glycine receptor (TC 1.A.9.3) subfamily. GLRB sub-subfamily.
CC {ECO:0000305}.
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DR EMBL; AF268376; AAG14347.1; -; mRNA.
DR EMBL; AF268374; AAG14345.1; -; Genomic_DNA.
DR EMBL; AF268367; AAG14345.1; JOINED; Genomic_DNA.
DR EMBL; AF268370; AAG14345.1; JOINED; Genomic_DNA.
DR EMBL; AF268369; AAG14345.1; JOINED; Genomic_DNA.
DR EMBL; AF268371; AAG14345.1; JOINED; Genomic_DNA.
DR EMBL; AF268368; AAG14345.1; JOINED; Genomic_DNA.
DR EMBL; AF268372; AAG14345.1; JOINED; Genomic_DNA.
DR EMBL; AF268373; AAG14345.1; JOINED; Genomic_DNA.
DR EMBL; BC123491; AAI23492.1; -; mRNA.
DR RefSeq; NP_776496.1; NM_174071.2.
DR AlphaFoldDB; Q9GJS9; -.
DR SMR; Q9GJS9; -.
DR STRING; 9913.ENSBTAP00000029010; -.
DR PaxDb; Q9GJS9; -.
DR PRIDE; Q9GJS9; -.
DR Ensembl; ENSBTAT00000029010; ENSBTAP00000029010; ENSBTAG00000021764.
DR GeneID; 281198; -.
DR KEGG; bta:281198; -.
DR CTD; 2743; -.
DR VEuPathDB; HostDB:ENSBTAG00000021764; -.
DR VGNC; VGNC:29415; GLRB.
DR eggNOG; KOG3644; Eukaryota.
DR GeneTree; ENSGT00940000156344; -.
DR InParanoid; Q9GJS9; -.
DR OMA; KFFWGIL; -.
DR OrthoDB; 614790at2759; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000021764; Expressed in occipital lobe and 77 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR GO; GO:0016935; C:glycine-gated chloride channel complex; ISS:UniProtKB.
DR GO; GO:0098690; C:glycinergic synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; 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:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0016934; F:extracellularly glycine-gated chloride channel activity; IEA:Ensembl.
DR GO; GO:0016933; F:extracellularly glycine-gated ion channel activity; ISS:UniProtKB.
DR GO; GO:0016594; F:glycine binding; IEA:Ensembl.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0007340; P:acrosome reaction; IEA:Ensembl.
DR GO; GO:0007628; P:adult walking behavior; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; ISS:UniProtKB.
DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR GO; GO:0097112; P:gamma-aminobutyric acid receptor clustering; IEA:Ensembl.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0007218; P:neuropeptide signaling pathway; ISS:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0043200; P:response to amino acid; IBA:GO_Central.
DR GO; GO:0060013; P:righting reflex; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0001964; P:startle response; ISS:UniProtKB.
DR GO; GO:0060012; P:synaptic transmission, glycinergic; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IEA:Ensembl.
DR Gene3D; 1.20.58.390; -; 1.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR008060; Glycine_rcpt_B.
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:SF29; PTHR18945:SF29; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
DR PRINTS; PR01677; GLYRBETA.
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; Cytoplasm;
KW Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..497
FT /note="Glycine receptor subunit beta"
FT /id="PRO_0000236240"
FT TOPO_DOM 23..268
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TRANSMEM 269..290
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TOPO_DOM 291..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TRANSMEM 296..316
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TOPO_DOM 317..327
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TRANSMEM 328..348
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TOPO_DOM 349..475
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TRANSMEM 476..496
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT BINDING 247..253
FT /ligand="strychnine"
FT /ligand_id="ChEBI:CHEBI:90700"
FT /evidence="ECO:0000250|UniProtKB:O93430"
FT SITE 307
FT /note="Important for obstruction of the ion pore in the
FT closed conformation"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT MOD_RES 391
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20781"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 183..197
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT DISULFID 243..255
FT /evidence="ECO:0000250|UniProtKB:P23415"
SQ SEQUENCE 497 AA; 56039 MW; 82F140C115A887E6 CRC64;
MKFLLAVAFF ILISLCIEEA YSKEKSSKKG KGKKKQYLCP SQQSAEDLAR VPANSTSNIL
NRLLVSYDPR IRPNFKGIPV DVVVNIFINS FGSIQETTMD YRVNIFLRQK WNDPRLKLPS
DFRGSDALTV DPTMYKCLWK PDLFFANEKS ANFHDVTQEN ILLFIFRDGD VLVSMRLSIT
LSCPLDLTLF PMDTQRCKMQ LESFGYTTDD LRFIWQSGDP VQLEKIALPQ FDIKKEDIEY
GNCTKYYKGT GYYTCVEVIF TLRRQVGFYM MGVYAPTLLI VVLSWLSFWI NPDASAARVP
LGIFSVLSLA SECTTLAAEL PKVSYVKALD VWLIACLLFG FASLVEYAVV QVMLNNPKRV
EAEKARIAKA EQAVGKGGNV AKKNTVNGAS TPVHISTLQV GETRCKKVCT SKSDLRSNDF
SIVGSLPRDF ELSNYDCYGK PIEVNNGLGK SQAKNNKKPP PAKPVIPTAA KRIDLYARAL
FPFCFLFFNV IYWSIYL
