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P48168

- GLRB_MOUSE

UniProt

P48168 - GLRB_MOUSE

Protein

Glycine receptor subunit beta

Gene

Glrb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    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).

    GO - Molecular functioni

    1. binding Source: MGI
    2. extracellular-glycine-gated chloride channel activity Source: MGI
    3. extracellular-glycine-gated ion channel activity Source: UniProtKB
    4. glycine binding Source: MGI
    5. protein binding Source: IntAct

    GO - Biological processi

    1. acrosome reaction Source: MGI
    2. adult walking behavior Source: MGI
    3. chloride transmembrane transport Source: GOC
    4. ion transmembrane transport Source: GOC
    5. ion transport Source: UniProtKB
    6. nervous system development Source: UniProtKB
    7. neuromuscular process Source: MGI
    8. neuropeptide signaling pathway Source: UniProtKB
    9. protein heterooligomerization Source: Ensembl
    10. regulation of membrane potential Source: MGI
    11. righting reflex Source: MGI
    12. startle response Source: UniProtKB
    13. synaptic transmission Source: UniProtKB
    14. synaptic transmission, glycinergic Source: MGI
    15. visual perception Source: MGI

    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

    ReactomeiREACT_198558. 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
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:95751. Glrb.

    Subcellular locationi

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. chloride channel complex Source: UniProtKB-KW
    3. endoplasmic reticulum Source: MGI
    4. external side of plasma membrane Source: MGI
    5. membrane Source: MGI
    6. postsynaptic membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, 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.

    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

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP48168.
    PRIDEiP48168.

    PTM databases

    PhosphoSiteiP48168.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP48168.
    BgeeiP48168.
    CleanExiMM_GLRB.
    GenevestigatoriP48168.

    Interactioni

    Subunit structurei

    Pentamer composed of three alpha and two beta subunits. Homopentamers of alpha subunits also form functional receptors. Interacts with GPHN By similarity.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 55-374.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 265243ExtracellularCuratedAdd
    BLAST
    Topological domaini355 – 477123CytoplasmicCuratedAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei266 – 29025HelicalCuratedAdd
    BLAST
    Transmembranei299 – 31618HelicalCuratedAdd
    BLAST
    Transmembranei331 – 35424HelicalCuratedAdd
    BLAST
    Transmembranei478 – 49518HelicalCuratedAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG295166.
    GeneTreeiENSGT00550000074453.
    HOGENOMiHOG000231336.
    HOVERGENiHBG051707.
    InParanoidiQ5U5X3.
    KOiK05196.
    OMAiPTMFKCL.
    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. 1 hit.
    PTHR18945:SF29. PTHR18945:SF29. 1 hit.
    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

    MKFSLAISFF ILMSLLFEDA CAKEKSSKKG KGKKKQYLCP SQQSPEDLAR    50
    VPPNSTSNIL NRLLVSYDPR IRPNFKGIPV DVVVNIFINS FGSIQETTMD 100
    YRVNIFLRQK WNDPRLKLPS DFRGSDALTV DPTMYKCLWK PDLFFANEKS 150
    ANFHDVTQEN ILLFIFRDGD VLVSMRLSIT LSCPLDLTLF PMDTQRCKMQ 200
    LESFGYTTDD LRFIWQSGDP VQLEKIALPQ FDIKKEDIEY GNCTKYYKGT 250
    GYYTCVEVIF TLRRQVGFYM MGVYAPTLLI VVLSWLSFWI NPDASAARVP 300
    LGIFSVLSLA SECTTLAAEL PKVSYVKALD VWLIACLLFG FASLVEYAVV 350
    QVMLNNPKRV EAEKARIAKA EQADGKGGNA AKKNTVNGTG TPVHISTLQV 400
    GETRCKKVCT SKSDLRSNDF SIVGSLPRDF ELSNYDCYGK PIEVNNGLGK 450
    PQAKNKKPPP AKPVIPTAAK RIDLYARALF PFCFLFFNVI YWSIYL 496
    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.
    Natural varianti84 – 496413Missing in spastic 1.
    Add
    BLAST
    Natural varianti143 – 1519LFFANEKSA → VSMSWIYNR in spastic 2.
    Natural varianti152 – 496345Missing in spastic 2.
    Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS17424.1.
    PIRi S46459.
    RefSeqi NP_034428.2. NM_010298.6.
    UniGenei Mm.275639.

    3D structure databases

    ProteinModelPortali P48168.
    SMRi P48168. Positions 55-374.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P48168. 5 interactions.
    MINTi MINT-4787310.
    STRINGi 10090.ENSMUSP00000029654.

    Chemistry

    GuidetoPHARMACOLOGYi 427.

    PTM databases

    PhosphoSitei P48168.

    Proteomic databases

    PaxDbi P48168.
    PRIDEi P48168.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029654 ; ENSMUSP00000029654 ; ENSMUSG00000028020 .
    GeneIDi 14658.
    KEGGi mmu:14658.
    UCSCi uc008pog.1. mouse.

    Organism-specific databases

    CTDi 2743.
    MGIi MGI:95751. Glrb.

    Phylogenomic databases

    eggNOGi NOG295166.
    GeneTreei ENSGT00550000074453.
    HOGENOMi HOG000231336.
    HOVERGENi HBG051707.
    InParanoidi Q5U5X3.
    KOi K05196.
    OMAi PTMFKCL.
    OrthoDBi EOG712TVZ.
    TreeFami TF315453.

    Enzyme and pathway databases

    Reactomei REACT_198558. Ligand-gated ion channel transport.

    Miscellaneous databases

    NextBioi 286522.
    PROi P48168.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P48168.
    Bgeei P48168.
    CleanExi MM_GLRB.
    Genevestigatori P48168.

    Family and domain databases

    Gene3Di 2.70.170.10. 1 hit.
    InterProi IPR008060. Glycine_rcpt_B.
    IPR006202. Neur_chan_lig-bd.
    IPR006201. Neur_channel.
    IPR006029. Neurotrans-gated_channel_TM.
    IPR018000. Neurotransmitter_ion_chnl_CS.
    [Graphical view ]
    PANTHERi PTHR18945. PTHR18945. 1 hit.
    PTHR18945:SF29. PTHR18945:SF29. 1 hit.
    Pfami PF02931. Neur_chan_LBD. 1 hit.
    PF02932. Neur_chan_memb. 1 hit.
    [Graphical view ]
    PRINTSi PR01677. GLYRBETA.
    PR00252. NRIONCHANNEL.
    SUPFAMi SSF63712. SSF63712. 1 hit.
    SSF90112. SSF90112. 1 hit.
    TIGRFAMsi TIGR00860. LIC. 1 hit.
    PROSITEi PS00236. NEUROTR_ION_CHANNEL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    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: October 1, 2014
    This is version 124 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

    External Data

    Dasty 3