P48168 (GLRB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glycine receptor subunit beta

Alternative name(s):
Glycine receptor 58 kDa subunit

Gene names

Name:

Glrb

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	496 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 alpha and beta subunits. Interacts with GPHN By similarity.
Subcellular location	Cell junction › synapse › postsynaptic 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	Note=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 process	Ion transport Transport
Cellular component	Cell junction Cell membrane Membrane Postsynaptic cell membrane Synapse
Disease	Disease mutation
Domain	Signal Transmembrane Transmembrane helix
Ligand	Chloride
Molecular function	Chloride channel Ionic channel Ligand-gated ion channel Receptor
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	acrosome reaction Inferred from mutant phenotype. Source: MGI adult walking behavior Inferred from mutant phenotype. Source: MGI nervous system development Inferred from sequence or structural similarity. Source: UniProtKB neuropeptide signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB regulation of membrane potential Inferred from mutant phenotype. Source: MGI righting reflex Inferred from mutant phenotype. Source: MGI startle response Inferred from sequence or structural similarity. Source: UniProtKB synaptic transmission, glycinergic Inferred from mutant phenotype. Source: MGI visual perception Inferred from mutant phenotype. Source: MGI
Cellular component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW chloride channel complex Inferred from electronic annotation. Source: UniProtKB-KW membrane fraction Inferred from direct assay. Source: MGI plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	extracellular-glycine-gated chloride channel activity Inferred from mutant phenotype. Source: MGI glycine binding Inferred from mutant phenotype. Source: MGI receptor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	By similarity
	Chain	23 – 496	474	Glycine receptor subunit beta		PRO_0000000424
Regions
	Topological domain	23 – 265	243	Extracellular Probable
	Transmembrane	266 – 290	25	Helical; Probable
	Transmembrane	299 – 316	18	Helical; Probable
	Transmembrane	331 – 354	24	Helical; Probable
	Topological domain	355 – 477	123	Cytoplasmic Probable
	Transmembrane	478 – 495	18	Helical; Probable
Amino acid modifications
	Glycosylation	54	1	N-linked (GlcNAc...) Potential
	Glycosylation	242	1	N-linked (GlcNAc...) Potential
	Disulfide bond	183 ↔ 197		By similarity
Natural variations
	Natural variant	74 – 83	10	NFKGIPVDVV → TTMLDIQPMI in spastic 1.
	Natural variant	84 – 496	413	Missing in spastic 1.
	Natural variant	143 – 151	9	LFFANEKSA → VSMSWIYNR in spastic 2.
	Natural variant	152 – 496	345	Missing in spastic 2.
Experimental info
	Sequence conflict	365	1	A → R in AAA61874. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P48168 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 554840A6DE9DE7BE	FASTA	496	55,951
	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

References

	« Hide 'large scale' referencesShow '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: 7920630] [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: 7946325] [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. , 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: 16141072] [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: 15489334] [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.
IPI	IPI00108776.
PIR	S46459.
RefSeq	NP_034428.2. NM_010298.5.
UniGene	Mm.275639.
3D structure databases
ProteinModelPortal	P48168.
SMR	P48168. Positions 55-495.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4787310.
STRING	P48168.
PTM databases
PhosphoSite	P48168.
Proteomic databases
PRIDE	P48168.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000029654; ENSMUSP00000029654; ENSMUSG00000028020.
GeneID	14658.
KEGG	mmu:14658.
Organism-specific databases
CTD	2743.
MGI	MGI:95751. Glrb.
Phylogenomic databases
HOGENOM	HBG506497.
HOVERGEN	HBG051707.
InParanoid	P48168.
OrthoDB	EOG4HMJ97.
Gene expression databases
ArrayExpress	P48168.
Bgee	P48168.
CleanEx	MM_GLRB.
Genevestigator	P48168.
GermOnline	ENSMUSG00000028020. Mus musculus.
Family and domain databases
InterPro	IPR008060. Glycine_rcpt_B. IPR006202. Neur_chan_lig-bd. IPR006201. Neur_channel. IPR006029. Neurotrans-gated_channel_TM. IPR018000. Neurotransmitter_ion_chnl_CS. [Graphical view]
Gene3D	G3DSA:2.70.170.10. Neur_chan_lig_bd. 1 hit.
KO	K05196.
PANTHER	PTHR18945:SF29. Glycine_rcpt_B. 1 hit. PTHR18945. Neur_channel. 1 hit.
Pfam	PF02931. Neur_chan_LBD. 1 hit. PF02932. Neur_chan_memb. 1 hit. [Graphical view]
PRINTS	PR01677. GLYRBETA. PR00252. NRIONCHANNEL.
SUPFAM	SSF90112. Neu_channel_TM. 1 hit. SSF63712. Neur_chan_LBD. 1 hit.
TIGRFAMs	TIGR00860. LIC. 1 hit.
PROSITE	PS00236. NEUROTR_ION_CHANNEL. 1 hit. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

GLRB_MOUSE

Accession

Primary (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:	December 14, 2011
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program