Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glycine receptor subunit beta

Gene

Glrb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Glycine receptors are ligand-gated chloride channels. GLRB does not form ligand-gated ion channels by itself, but is part of heteromeric ligand-gated chloride channels. Channel opening is triggered by extracellular glycine (PubMed:12809985). Heteropentameric channels composed of GLRB and GLRA1 are activated by lower glycine levels than homopentameric GLRA1. Plays an important role in the down-regulation of neuronal excitability. Contributes to the generation of inhibitory postsynaptic currents (PubMed:12809985, PubMed:16672662).By similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei307 – 3071Important for obstruction of the ion pore in the closed conformationBy similarity

GO - Molecular functioni

  • drug binding Source: MGI
  • extracellular-glycine-gated chloride channel activity Source: MGI
  • extracellular-glycine-gated ion channel activity Source: UniProtKB
  • glycine binding Source: MGI

GO - Biological processi

  • acrosome reaction Source: MGI
  • adult walking behavior Source: MGI
  • chloride transmembrane transport Source: UniProtKB
  • gamma-aminobutyric acid receptor clustering Source: MGI
  • ion transport Source: UniProtKB
  • nervous system development Source: UniProtKB
  • neuromuscular process Source: MGI
  • neuropeptide signaling pathway Source: UniProtKB
  • neurotransmitter-gated ion channel clustering Source: MGI
  • protein heterooligomerization Source: Ensembl
  • regulation of membrane potential Source: MGI
  • righting reflex Source: MGI
  • startle response Source: UniProtKB
  • synaptic transmission Source: UniProtKB
  • synaptic transmission, glycinergic Source: MGI
  • visual perception Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Chloride channel, Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

Keywords - Ligandi

Chloride

Enzyme and pathway databases

ReactomeiR-MMU-975298. Ligand-gated ion channel transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycine receptor subunit beta
Alternative name(s):
Glycine receptor 58 kDa subunit
Gene namesi
Name:Glrb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:95751. Glrb.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 268246ExtracellularBy similarityAdd
BLAST
Transmembranei269 – 29022Helical; Name=1By similarityAdd
BLAST
Topological domaini291 – 2955CytoplasmicBy similarity
Transmembranei296 – 31621Helical; Name=2By similarityAdd
BLAST
Topological domaini317 – 32711ExtracellularBy similarityAdd
BLAST
Transmembranei328 – 34821Helical; Name=3By similarityAdd
BLAST
Topological domaini349 – 474126CytoplasmicBy similarityAdd
BLAST
Transmembranei475 – 49521Helical; Name=4By similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Involvement in diseasei

Defects in Glrb cause the spastic condition which is characterized by muscle rigidity, tremors, myoclonic jerks, pronounced startle reaction, abnormal gait and impaired righting ability (PubMed:7920630). Neurons from the ventral horn of the spinal cord display reduced inhibitory postsynaptic currents (PubMed:12809985). Likewise, hypoglossal neurons display a dramatic reduction in the frequency and amplitude of postsynaptic inhibitory currents (PubMed:16672662).

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222By similarityAdd
BLAST
Chaini23 – 496474Glycine receptor subunit betaPRO_0000000424Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi54 – 541N-linked (GlcNAc...)Sequence analysis
Disulfide bondi183 ↔ 197By similarity
Glycosylationi242 – 2421N-linked (GlcNAc...)Sequence analysis
Disulfide bondi243 ↔ 255By similarity
Modified residuei391 – 3911PhosphothreonineBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP48168.
PaxDbiP48168.
PRIDEiP48168.

PTM databases

iPTMnetiP48168.
PhosphoSiteiP48168.

Expressioni

Tissue specificityi

Detected in spinal cord, brain and brain stem, especially in the periolivary region, spinal nuclei, trigeminal nucleus, medulla oblongata, pons and midbrain. Detected in the inner plexiform layer of the retina (at protein level) (PubMed:22592841). High levels of expression in cortex, hippocampus, thalamus and cerebellum (PubMed:7920630). Detected in spinal cord (PubMed:7946325).3 Publications

Gene expression databases

BgeeiP48168.
CleanExiMM_GLRB.
ExpressionAtlasiP48168. baseline and differential.
GenevisibleiP48168. MM.

Interactioni

Subunit structurei

Heteropentamer composed of GLRB and GLRA1. Heteropentamer composed of GLRB and GLRA2. Heteropentamer composed of GLRB and GLRA3. Heteropentamer composed of two GLRA1 and three GLRB subunits. Heteropentamer composed of three GLRA1 and two GLRB subunits. Interacts with GPHN.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
GphnQ035554EBI-7069198,EBI-349317From a different organism.
GphnQ8BUV34EBI-7069198,EBI-771218

Protein-protein interaction databases

IntActiP48168. 5 interactions.
MINTiMINT-4787310.
STRINGi10090.ENSMUSP00000029654.

Structurei

3D structure databases

ProteinModelPortaliP48168.
SMRiP48168. Positions 55-496.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni247 – 2537Strychnine-bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3644. Eukaryota.
ENOG410XP43. LUCA.
GeneTreeiENSGT00760000118821.
HOGENOMiHOG000231336.
HOVERGENiHBG051707.
InParanoidiP48168.
KOiK05196.
OMAiPRLKLPN.
OrthoDBiEOG712TVZ.
TreeFamiTF315453.

Family and domain databases

Gene3Di2.70.170.10. 1 hit.
InterProiIPR008060. Glycine_rcpt_B.
IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
IPR018000. Neurotransmitter_ion_chnl_CS.
[Graphical view]
PANTHERiPTHR18945. PTHR18945. 2 hits.
PTHR18945:SF29. PTHR18945:SF29. 2 hits.
PfamiPF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 1 hit.
[Graphical view]
PRINTSiPR01677. GLYRBETA.
PR00252. NRIONCHANNEL.
SUPFAMiSSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 1 hit.
TIGRFAMsiTIGR00860. LIC. 1 hit.
PROSITEiPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P48168-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFSLAISFF ILMSLLFEDA CAKEKSSKKG KGKKKQYLCP SQQSPEDLAR
60 70 80 90 100
VPPNSTSNIL NRLLVSYDPR IRPNFKGIPV DVVVNIFINS FGSIQETTMD
110 120 130 140 150
YRVNIFLRQK WNDPRLKLPS DFRGSDALTV DPTMYKCLWK PDLFFANEKS
160 170 180 190 200
ANFHDVTQEN ILLFIFRDGD VLVSMRLSIT LSCPLDLTLF PMDTQRCKMQ
210 220 230 240 250
LESFGYTTDD LRFIWQSGDP VQLEKIALPQ FDIKKEDIEY GNCTKYYKGT
260 270 280 290 300
GYYTCVEVIF TLRRQVGFYM MGVYAPTLLI VVLSWLSFWI NPDASAARVP
310 320 330 340 350
LGIFSVLSLA SECTTLAAEL PKVSYVKALD VWLIACLLFG FASLVEYAVV
360 370 380 390 400
QVMLNNPKRV EAEKARIAKA EQADGKGGNA AKKNTVNGTG TPVHISTLQV
410 420 430 440 450
GETRCKKVCT SKSDLRSNDF SIVGSLPRDF ELSNYDCYGK PIEVNNGLGK
460 470 480 490
PQAKNKKPPP AKPVIPTAAK RIDLYARALF PFCFLFFNVI YWSIYL
Length:496
Mass (Da):55,951
Last modified:July 27, 2011 - v2
Checksum:i554840A6DE9DE7BE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti365 – 3651A → R in AAA61874 (PubMed:7920630).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti74 – 8310NFKGIPVDVV → TTMLDIQPMI in spastic 1. 1 Publication
Natural varianti84 – 496413Missing in spastic 1. 1 Publication
Add
BLAST
Natural varianti143 – 1519LFFANEKSA → VSMSWIYNR in spastic 2. 1 Publication
Natural varianti152 – 496345Missing in spastic 2. 1 Publication
Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09399 mRNA. Translation: AAA61874.1.
X81202 mRNA. Translation: CAA57076.1.
X81201 Genomic DNA. Translation: CAA57075.1.
L32594 Genomic DNA. Translation: AAA65966.1.
AK083251 mRNA. Translation: BAC38831.1.
CH466547 Genomic DNA. Translation: EDL15445.1.
BC037605 mRNA. Translation: AAH37605.1.
CCDSiCCDS17424.1.
PIRiS46459.
RefSeqiNP_034428.2. NM_010298.6.
UniGeneiMm.275639.

Genome annotation databases

EnsembliENSMUST00000029654; ENSMUSP00000029654; ENSMUSG00000028020.
GeneIDi14658.
KEGGimmu:14658.
UCSCiuc008pog.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09399 mRNA. Translation: AAA61874.1.
X81202 mRNA. Translation: CAA57076.1.
X81201 Genomic DNA. Translation: CAA57075.1.
L32594 Genomic DNA. Translation: AAA65966.1.
AK083251 mRNA. Translation: BAC38831.1.
CH466547 Genomic DNA. Translation: EDL15445.1.
BC037605 mRNA. Translation: AAH37605.1.
CCDSiCCDS17424.1.
PIRiS46459.
RefSeqiNP_034428.2. NM_010298.6.
UniGeneiMm.275639.

3D structure databases

ProteinModelPortaliP48168.
SMRiP48168. Positions 55-496.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP48168. 5 interactions.
MINTiMINT-4787310.
STRINGi10090.ENSMUSP00000029654.

PTM databases

iPTMnetiP48168.
PhosphoSiteiP48168.

Proteomic databases

MaxQBiP48168.
PaxDbiP48168.
PRIDEiP48168.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029654; ENSMUSP00000029654; ENSMUSG00000028020.
GeneIDi14658.
KEGGimmu:14658.
UCSCiuc008pog.2. mouse.

Organism-specific databases

CTDi2743.
MGIiMGI:95751. Glrb.

Phylogenomic databases

eggNOGiKOG3644. Eukaryota.
ENOG410XP43. LUCA.
GeneTreeiENSGT00760000118821.
HOGENOMiHOG000231336.
HOVERGENiHBG051707.
InParanoidiP48168.
KOiK05196.
OMAiPRLKLPN.
OrthoDBiEOG712TVZ.
TreeFamiTF315453.

Enzyme and pathway databases

ReactomeiR-MMU-975298. Ligand-gated ion channel transport.

Miscellaneous databases

PROiP48168.
SOURCEiSearch...

Gene expression databases

BgeeiP48168.
CleanExiMM_GLRB.
ExpressionAtlasiP48168. baseline and differential.
GenevisibleiP48168. MM.

Family and domain databases

Gene3Di2.70.170.10. 1 hit.
InterProiIPR008060. Glycine_rcpt_B.
IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
IPR018000. Neurotransmitter_ion_chnl_CS.
[Graphical view]
PANTHERiPTHR18945. PTHR18945. 2 hits.
PTHR18945:SF29. PTHR18945:SF29. 2 hits.
PfamiPF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 1 hit.
[Graphical view]
PRINTSiPR01677. GLYRBETA.
PR00252. NRIONCHANNEL.
SUPFAMiSSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 1 hit.
TIGRFAMsiTIGR00860. LIC. 1 hit.
PROSITEiPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Glycine receptor beta-subunit gene mutation in spastic mouse associated with LINE-1 element insertion."
    Kingsmore S.F., Giros B., Suh D., Bieniarz M., Caron M.G., Seldin M.F.
    Nat. Genet. 7:136-141(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DISEASE, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "The spastic mouse: aberrant splicing of glycine receptor beta subunit mRNA caused by intronic insertion of L1 element."
    Muelhardt C., Fischer M., Gass P., Simon-Chazottes D., Guenet J.-L., Kuhse J., Betz H., Becker C.M.
    Neuron 13:1003-1015(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS SPASTIC, TISSUE SPECIFICITY.
    Strain: BALB/cJ and C57BL/6.
    Tissue: Brain and Liver.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Hippocampus.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Eye.
  6. "Spinal inhibitory synaptic transmission in the glycine receptor mouse mutant spastic."
    von Wegerer J., Becker K., Glockenhammer D., Becker C.M., Zeilhofer H.U., Swandulla D.
    Neurosci. Lett. 345:45-48(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISEASE, FUNCTION.
  7. "Distinct physiological mechanisms underlie altered glycinergic synaptic transmission in the murine mutants spastic, spasmodic, and oscillator."
    Graham B.A., Schofield P.R., Sah P., Margrie T.W., Callister R.J.
    J. Neurosci. 26:4880-4890(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISEASE, FUNCTION.
  8. Cited for: SUBCELLULAR LOCATION.
  9. "Distribution of the glycine receptor beta-subunit in the mouse CNS as revealed by a novel monoclonal antibody."
    Weltzien F., Puller C., O'Sullivan G.A., Paarmann I., Betz H.
    J. Comp. Neurol. 520:3962-3981(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiGLRB_MOUSE
AccessioniPrimary (citable) accession number: P48168
Secondary accession number(s): Q5U5X3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.