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P48168 (GLRB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycine receptor subunit beta
Alternative name(s):
Glycine receptor 58 kDa subunit
Gene names
Name:Glrb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length496 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The glycine receptor is a neurotransmitter-gated ion channel. Binding of glycine to its receptor increases the chloride conductance and thus produces hyperpolarization (inhibition of neuronal firing).

Subunit structure

Pentamer composed of three alpha and two beta subunits. Homopentamers of alpha subunits also form functional receptors. Interacts with GPHN By similarity.

Subcellular location

Cell junctionsynapsepostsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.

Tissue specificity

High levels of expression in cortex, hippocampus, thalamus and cerebellum.

Involvement in disease

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.

Sequence similarities

Belongs to the ligand-gated ion channel (TC 1.A.9) family. Glycine receptor (TC 1.A.9.3) subfamily. GLRB sub-subfamily. [View classification]

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell junction
Cell membrane
Membrane
Postsynaptic cell membrane
Synapse
   DiseaseDisease mutation
   DomainSignal
Transmembrane
Transmembrane helix
   LigandChloride
   Molecular functionChloride channel
Ion channel
Ligand-gated ion channel
Receptor
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacrosome reaction

Inferred from mutant phenotype PubMed 11076688. Source: MGI

adult walking behavior

Inferred from mutant phenotype PubMed 4323808. Source: MGI

chloride transmembrane transport

Inferred from mutant phenotype PubMed 12809985PubMed 16672662. Source: GOC

ion transmembrane transport

Inferred from sequence or structural similarity PubMed 8717357. Source: GOC

ion transport

Inferred from sequence or structural similarity PubMed 8717357. Source: UniProtKB

nervous system development

Inferred from sequence or structural similarity PubMed 8717357. Source: UniProtKB

neuromuscular process

Inferred from mutant phenotype PubMed 10651857PubMed 8635460PubMed 9087981. Source: MGI

neuropeptide signaling pathway

Inferred from sequence or structural similarity PubMed 8717357. Source: UniProtKB

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

regulation of membrane potential

Inferred from mutant phenotype PubMed 16672662. Source: MGI

righting reflex

Inferred from mutant phenotype PubMed 6285205. Source: MGI

startle response

Inferred from sequence or structural similarity PubMed 8717357. Source: UniProtKB

synaptic transmission

Inferred from sequence or structural similarity PubMed 8717357. Source: UniProtKB

synaptic transmission, glycinergic

Inferred from mutant phenotype PubMed 12809985PubMed 1338094PubMed 16672662. Source: MGI

visual perception

Inferred from mutant phenotype PubMed 1338094. Source: MGI

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

chloride channel complex

Inferred from electronic annotation. Source: UniProtKB-KW

endoplasmic reticulum

Inferred from sequence alignment PubMed 17145751. Source: MGI

external side of plasma membrane

Inferred from sequence alignment PubMed 17145751. Source: MGI

membrane

Inferred from direct assay PubMed 17145751. Source: MGI

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbinding

Inferred from physical interaction PubMed 2983837PubMed 6285205. Source: MGI

extracellular-glycine-gated chloride channel activity

Inferred from mutant phenotype PubMed 12809985PubMed 16672662. Source: MGI

extracellular-glycine-gated ion channel activity

Inferred from sequence or structural similarity PubMed 8717357. Source: UniProtKB

glycine binding

Inferred from mutant phenotype PubMed 2983837PubMed 6285205. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GphnQ035554EBI-7069198,EBI-349317From a different organism.
GphnQ8BUV34EBI-7069198,EBI-771218

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 By similarity
Chain23 – 496474Glycine receptor subunit beta
PRO_0000000424

Regions

Topological domain23 – 265243Extracellular Probable
Transmembrane266 – 29025Helical; Probable
Transmembrane299 – 31618Helical; Probable
Transmembrane331 – 35424Helical; Probable
Topological domain355 – 477123Cytoplasmic Probable
Transmembrane478 – 49518Helical; Probable

Amino acid modifications

Glycosylation541N-linked (GlcNAc...) Potential
Glycosylation2421N-linked (GlcNAc...) Potential
Disulfide bond183 ↔ 197 By similarity

Natural variations

Natural variant74 – 8310NFKGIPVDVV → TTMLDIQPMI in spastic 1.
Natural variant84 – 496413Missing in spastic 1.
Natural variant143 – 1519LFFANEKSA → VSMSWIYNR in spastic 2.
Natural variant152 – 496345Missing in spastic 2.

Experimental info

Sequence conflict3651A → R in AAA61874. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P48168 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 554840A6DE9DE7BE

FASTA49655,951
        10         20         30         40         50         60 
MKFSLAISFF ILMSLLFEDA CAKEKSSKKG KGKKKQYLCP SQQSPEDLAR VPPNSTSNIL 

        70         80         90        100        110        120 
NRLLVSYDPR IRPNFKGIPV DVVVNIFINS FGSIQETTMD YRVNIFLRQK WNDPRLKLPS 

       130        140        150        160        170        180 
DFRGSDALTV DPTMYKCLWK PDLFFANEKS ANFHDVTQEN ILLFIFRDGD VLVSMRLSIT 

       190        200        210        220        230        240 
LSCPLDLTLF PMDTQRCKMQ LESFGYTTDD LRFIWQSGDP VQLEKIALPQ FDIKKEDIEY 

       250        260        270        280        290        300 
GNCTKYYKGT GYYTCVEVIF TLRRQVGFYM MGVYAPTLLI VVLSWLSFWI NPDASAARVP 

       310        320        330        340        350        360 
LGIFSVLSLA SECTTLAAEL PKVSYVKALD VWLIACLLFG FASLVEYAVV QVMLNNPKRV 

       370        380        390        400        410        420 
EAEKARIAKA EQADGKGGNA AKKNTVNGTG TPVHISTLQV GETRCKKVCT SKSDLRSNDF 

       430        440        450        460        470        480 
SIVGSLPRDF ELSNYDCYGK PIEVNNGLGK PQAKNKKPPP AKPVIPTAAK RIDLYARALF 

       490 
PFCFLFFNVI YWSIYL 

« Hide

References

« Hide 'large scale' references
[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].
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.
Strain: BALB/c 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS46459.
RefSeqNP_034428.2. NM_010298.6.
UniGeneMm.275639.

3D structure databases

ProteinModelPortalP48168.
SMRP48168. Positions 55-496.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP48168. 5 interactions.
MINTMINT-4787310.
STRING10090.ENSMUSP00000029654.

PTM databases

PhosphoSiteP48168.

Proteomic databases

PaxDbP48168.
PRIDEP48168.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029654; ENSMUSP00000029654; ENSMUSG00000028020.
GeneID14658.
KEGGmmu:14658.
UCSCuc008pog.1. mouse.

Organism-specific databases

CTD2743.
MGIMGI:95751. Glrb.

Phylogenomic databases

eggNOGNOG295166.
GeneTreeENSGT00550000074453.
HOGENOMHOG000231336.
HOVERGENHBG051707.
InParanoidQ5U5X3.
KOK05196.
OMAPTMFKCL.
OrthoDBEOG712TVZ.
TreeFamTF315453.

Gene expression databases

ArrayExpressP48168.
BgeeP48168.
CleanExMM_GLRB.
GenevestigatorP48168.

Family and domain databases

Gene3D2.70.170.10. 1 hit.
InterProIPR008060. Glycine_rcpt_B.
IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
IPR018000. Neurotransmitter_ion_chnl_CS.
[Graphical view]
PANTHERPTHR18945. PTHR18945. 1 hit.
PTHR18945:SF29. PTHR18945:SF29. 1 hit.
PfamPF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 1 hit.
[Graphical view]
PRINTSPR01677. GLYRBETA.
PR00252. NRIONCHANNEL.
SUPFAMSSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 1 hit.
TIGRFAMsTIGR00860. LIC. 1 hit.
PROSITEPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio286522.
PROP48168.
SOURCESearch...

Entry information

Entry nameGLRB_MOUSE
AccessionPrimary (citable) accession number: P48168
Secondary accession number(s): Q5U5X3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot