GLRB_RAT
ID GLRB_RAT Reviewed; 496 AA.
AC P20781;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Glycine receptor subunit beta;
DE AltName: Full=Glycine receptor 58 kDa subunit;
DE Flags: Precursor;
GN Name=Glrb;
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 [MRNA], PARTIAL PROTEIN SEQUENCE, AND TISSUE
RP SPECIFICITY.
RX PubMed=2163264; DOI=10.1016/0896-6273(90)90149-a;
RA Grenningloh G., Pribilla I., Prior P., Multhaup G., Beyreuther K.,
RA Taleb O., Betz H.;
RT "Cloning and expression of the 58 kd beta subunit of the inhibitory glycine
RT receptor.";
RL Neuron 4:963-970(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH GLRA1, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=15574743; DOI=10.1523/jneurosci.3424-04.2004;
RA Burzomato V., Beato M., Groot Kormelink P.J., Colquhoun D., Sivilotti L.G.;
RT "Single-channel behavior of heteromeric alpha1beta glycine receptors: an
RT attempt to detect a conformational change before the channel opens.";
RL J. Neurosci. 24:10924-10940(2004).
RN [3]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH GPHN; GLRA1; GLRA2 AND GLRA3.
RX PubMed=8581315; DOI=10.1006/mcne.1995.1033;
RA Kirsch J., Kuhse J., Betz H.;
RT "Targeting of glycine receptor subunits to gephyrin-rich domains in
RT transfected human embryonic kidney cells.";
RL Mol. Cell. Neurosci. 6:450-461(1995).
RN [4]
RP INTERACTION WITH GLRA1, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14551753; DOI=10.1007/s00249-003-0286-y;
RA Mohammadi B., Krampfl K., Cetinkaya C., Moschref H., Grosskreutz J.,
RA Dengler R., Bufler J.;
RT "Kinetic analysis of recombinant mammalian alpha(1) and alpha(1)beta
RT glycine receptor channels.";
RL Eur. Biophys. J. 32:529-536(2003).
RN [5]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=22592841; DOI=10.1002/cne.23139;
RA Weltzien F., Puller C., O'Sullivan G.A., Paarmann I., Betz H.;
RT "Distribution of the glycine receptor beta-subunit in the mouse CNS as
RT revealed by a novel monoclonal antibody.";
RL J. Comp. Neurol. 520:3962-3981(2012).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-391, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 378-426 IN COMPLEX WITH GPHN.
RX PubMed=15201864; DOI=10.1038/sj.emboj.7600256;
RA Sola M., Bavro V.N., Timmins J., Franz T., Ricard-Blum S., Schoehn G.,
RA Ruigrok R.W.H., Paarmann I., Saiyed T., O'Sullivan G.A., Schmitt B.,
RA Betz H., Weissenhorn W.;
RT "Structural basis of dynamic glycine receptor clustering by gephyrin.";
RL EMBO J. 23:2510-2519(2004).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 420-432 IN COMPLEX WITH GPHN.
RX PubMed=16511563; DOI=10.1038/sj.emboj.7601029;
RA Kim E.Y., Schrader N., Smolinsky B., Bedet C., Vannier C., Schwarz G.,
RA Schindelin H.;
RT "Deciphering the structural framework of glycine receptor anchoring by
RT gephyrin.";
RL EMBO J. 25:1385-1395(2006).
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 (PubMed:15574743, PubMed:14551753).
CC Heteropentameric channels composed of GLRB and GLRA1 are activated by
CC lower glycine levels than homopentameric GLRA1. Plays an important role
CC in the down-regulation of neuronal excitability. Contributes to the
CC generation of inhibitory postsynaptic currents (By similarity).
CC {ECO:0000250|UniProtKB:P48167, ECO:0000250|UniProtKB:P48168,
CC ECO:0000269|PubMed:15574743}.
CC -!- SUBUNIT: Heteropentamer composed of GLRB and GLRA1 (PubMed:15574743,
CC PubMed:8581315, PubMed:14551753). Heteropentamer composed of GLRB and
CC GLRA2 (PubMed:8581315). Heteropentamer composed of GLRB and GLRA3
CC (PubMed:8581315). Heteropentamer composed of two GLRA1 and three GLRB
CC subunits. Heteropentamer composed of three GLRA1 and two GLRB subunits
CC (By similarity). Interacts with GPHN (PubMed:8581315, PubMed:15201864,
CC PubMed:16511563). {ECO:0000250|UniProtKB:P48167,
CC ECO:0000269|PubMed:15201864, ECO:0000269|PubMed:15574743,
CC ECO:0000269|PubMed:16511563, ECO:0000269|PubMed:8581315}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000305|PubMed:22592841}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P23415}. Cell membrane
CC {ECO:0000269|PubMed:14551753, ECO:0000269|PubMed:15574743,
CC ECO:0000269|PubMed:22592841, ECO:0000269|PubMed:8581315}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:P23415}. Synapse
CC {ECO:0000269|PubMed:22592841}. Perikaryon
CC {ECO:0000269|PubMed:22592841}. Cell projection, dendrite
CC {ECO:0000269|PubMed:22592841}. Cytoplasm {ECO:0000269|PubMed:8581315}.
CC Note=Retained in the cytoplasm upon heterologous expression by itself.
CC Coexpression with GPHN promotes expression at the cell membrane.
CC Coexpression with GLRA1, GLRA2 or GLRA3 promotes expression at the cell
CC membrane. {ECO:0000269|PubMed:8581315}.
CC -!- TISSUE SPECIFICITY: Detected in spinal cord and brain stem (at protein
CC level) (PubMed:22592841). Detected in spinal cord, cerebellum and brain
CC cortex (PubMed:2163264). {ECO:0000269|PubMed:2163264,
CC ECO:0000269|PubMed:22592841}.
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; AJ310839; CAC35983.1; -; mRNA.
DR PIR; JH0165; JH0165.
DR RefSeq; NP_445748.1; NM_053296.1.
DR RefSeq; XP_006232568.1; XM_006232506.2.
DR PDB; 1T3E; X-ray; 3.25 A; P=378-426.
DR PDB; 2FTS; X-ray; 2.41 A; P=420-432.
DR PDB; 4PD1; X-ray; 1.98 A; C=419-433.
DR PDBsum; 1T3E; -.
DR PDBsum; 2FTS; -.
DR PDBsum; 4PD1; -.
DR AlphaFoldDB; P20781; -.
DR SMR; P20781; -.
DR BioGRID; 247490; 6.
DR CORUM; P20781; -.
DR IntAct; P20781; 1.
DR STRING; 10116.ENSRNOP00000014170; -.
DR ChEMBL; CHEMBL3392921; -.
DR GuidetoPHARMACOLOGY; 427; -.
DR GlyGen; P20781; 2 sites.
DR iPTMnet; P20781; -.
DR PhosphoSitePlus; P20781; -.
DR PaxDb; P20781; -.
DR PRIDE; P20781; -.
DR Ensembl; ENSRNOT00000014170; ENSRNOP00000014170; ENSRNOG00000010199.
DR GeneID; 25456; -.
DR KEGG; rno:25456; -.
DR UCSC; RGD:2706; rat.
DR CTD; 2743; -.
DR RGD; 2706; Glrb.
DR eggNOG; KOG3644; Eukaryota.
DR GeneTree; ENSGT00940000156344; -.
DR HOGENOM; CLU_010920_1_4_1; -.
DR InParanoid; P20781; -.
DR OMA; KFFWGIL; -.
DR OrthoDB; 614790at2759; -.
DR PhylomeDB; P20781; -.
DR TreeFam; TF315453; -.
DR Reactome; R-RNO-112314; Neurotransmitter receptors and postsynaptic signal transmission.
DR EvolutionaryTrace; P20781; -.
DR PRO; PR:P20781; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000010199; Expressed in cerebellum and 6 other tissues.
DR Genevisible; P20781; RN.
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; ISO:RGD.
DR GO; GO:0016935; C:glycine-gated chloride channel complex; ISS:UniProtKB.
DR GO; GO:0098690; C:glycinergic synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; TAS:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045211; C:postsynaptic membrane; TAS:RGD.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
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; ISO:RGD.
DR GO; GO:0016933; F:extracellularly glycine-gated ion channel activity; IDA:RGD.
DR GO; GO:0016594; F:glycine binding; IDA:RGD.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0007340; P:acrosome reaction; ISO:RGD.
DR GO; GO:0007628; P:adult walking behavior; ISO:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; ISS:UniProtKB.
DR GO; GO:1902476; P:chloride transmembrane transport; ISS:UniProtKB.
DR GO; GO:0097112; P:gamma-aminobutyric acid receptor clustering; ISO:RGD.
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:0050905; P:neuromuscular process; ISO:RGD.
DR GO; GO:0007218; P:neuropeptide signaling pathway; ISS:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0043200; P:response to amino acid; IBA:GO_Central.
DR GO; GO:0060013; P:righting reflex; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0007601; P:visual perception; ISO:RGD.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Chloride; Chloride channel;
KW Cytoplasm; Direct protein sequencing; 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..22
FT CHAIN 23..496
FT /note="Glycine receptor subunit beta"
FT /id="PRO_0000000425"
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..474
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TRANSMEM 475..495
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:0007744|PubMed:22673903"
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"
FT HELIX 429..431
FT /evidence="ECO:0007829|PDB:2FTS"
SQ SEQUENCE 496 AA; 55927 MW; F77CE96105EF8ACF CRC64;
MKFSLAVSFF ILMSLLFEDA CSKEKSSKKG KGKKKQYLCP SQQSAEDLAR VPPNSTSNIL
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 EQADGKGGNA AKKNTVNGTG TPVHISTLQV GETRCKKVCT SKSDLRSNDF
SIVGSLPRDF ELSNYDCYGK PIEVNNGLGK PQAKNKKPPP AKPVIPTAAK RIDLYARALF
PFCFLFFNVI YWSIYL
