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P23385

- GRM1_RAT

UniProt

P23385 - GRM1_RAT

Protein

Metabotropic glutamate receptor 1

Gene

Grm1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 1 (01 Nov 1991)
      Previous versions | rss
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    Functioni

    G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling activates a phosphatidylinositol-calcium second messenger system. May participate in the central action of glutamate in the CNS, such as long-term potentiation in the hippocampus and long-term depression in the cerebellum.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei74 – 741Glutamate2 Publications
    Binding sitei165 – 1651Glutamate2 Publications
    Binding sitei236 – 2361Glutamate2 Publications
    Binding sitei318 – 3181Glutamate2 Publications
    Binding sitei409 – 4091Glutamate2 Publications

    GO - Molecular functioni

    1. estrogen receptor binding Source: RGD
    2. glutamate receptor activity Source: UniProtKB
    3. G-protein coupled receptor activity Source: RGD
    4. identical protein binding Source: IntAct
    5. PLC activating G-protein coupled glutamate receptor activity Source: UniProtKB
    6. protein binding Source: IntAct

    GO - Biological processi

    1. calcium-mediated signaling Source: RGD
    2. dimeric G-protein coupled receptor signaling pathway Source: UniProtKB
    3. G-protein coupled glutamate receptor signaling pathway Source: UniProtKB
    4. G-protein coupled receptor signaling pathway Source: UniProtKB
    5. membrane depolarization Source: UniProtKB
    6. phospholipase C-activating G-protein coupled glutamate receptor signaling pathway Source: UniProtKB
    7. positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway Source: UniProtKB
    8. protein kinase C-activating G-protein coupled receptor signaling pathway Source: RefGenome
    9. regulation of glutamate secretion Source: UniProtKB
    10. regulation of synaptic transmission, glutamatergic Source: UniProtKB
    11. sensory perception of pain Source: RGD
    12. synaptic transmission Source: RGD
    13. synaptic transmission, GABAergic Source: UniProtKB

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Metabotropic glutamate receptor 1
    Short name:
    mGluR1
    Gene namesi
    Name:Grm1
    Synonyms:Gprc1a, Mglur1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi2742. Grm1.

    Subcellular locationi

    Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. axon Source: UniProtKB
    2. dendritic spine Source: RGD
    3. integral component of plasma membrane Source: UniProtKB
    4. postsynaptic density Source: RGD
    5. presynaptic membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi67 – 671C → S: Impairs protein folding and abolishes location at the cell surface. 1 Publication
    Mutagenesisi109 – 1091C → S: Impairs protein folding and abolishes location at the cell surface. 1 Publication
    Mutagenesisi140 – 1401C → S: Impairs homodimerization. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 11991181Metabotropic glutamate receptor 1PRO_0000012924Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi67 ↔ 109
    Glycosylationi98 – 981N-linked (GlcNAc...)1 Publication
    Disulfide bondi140 – 140Interchain
    Glycosylationi223 – 2231N-linked (GlcNAc...)1 Publication
    Disulfide bondi289 ↔ 291
    Disulfide bondi378 ↔ 394
    Glycosylationi397 – 3971N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi432 ↔ 439
    Glycosylationi515 – 5151N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi657 ↔ 746By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP23385.
    PRIDEiP23385.

    PTM databases

    PhosphoSiteiP23385.

    Miscellaneous databases

    PMAP-CutDBP23385.

    Expressioni

    Tissue specificityi

    Predominantly expressed in cerebellar Purkinje cells, CA2-CA3 pyramidal cells of the hippocampus, and mitral and tufted cells of the olfactory bulb.2 Publications

    Gene expression databases

    GenevestigatoriP23385.

    Interactioni

    Subunit structurei

    The PPXXF motif binds HOMER1, HOMER2 and HOMER3. Interacts with RYR1, RYR2, ITPR1, SHANK1 and SHANK3 By similarity. Interacts with SIAH1 and GRASP. Homodimer; disulfide-linked.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-4410410,EBI-4410410
    Ppp1ccP6308815EBI-4410410,EBI-80049

    Protein-protein interaction databases

    BioGridi246579. 7 interactions.
    DIPiDIP-44897N.
    IntActiP23385. 5 interactions.
    MINTiMINT-1890098.

    Structurei

    Secondary structure

    1
    1199
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi39 – 413
    Beta strandi44 – 518
    Turni59 – 657
    Turni72 – 754
    Helixi76 – 9116
    Beta strandi93 – 964
    Beta strandi101 – 1077
    Helixi112 – 12312
    Beta strandi156 – 1605
    Helixi165 – 17511
    Helixi176 – 1783
    Beta strandi182 – 1865
    Helixi190 – 1934
    Turni195 – 1973
    Beta strandi201 – 2055
    Helixi208 – 22114
    Beta strandi226 – 2349
    Helixi235 – 25117
    Beta strandi254 – 2618
    Beta strandi263 – 2653
    Helixi267 – 27812
    Turni279 – 2835
    Beta strandi286 – 2905
    Helixi293 – 30614
    Beta strandi313 – 3164
    Turni318 – 3225
    Helixi324 – 3274
    Helixi331 – 3344
    Beta strandi338 – 3425
    Helixi348 – 3547
    Turni359 – 3613
    Helixi368 – 3758
    Turni400 – 4034
    Helixi410 – 43122
    Helixi440 – 4423
    Helixi447 – 4559
    Beta strandi458 – 4603
    Beta strandi466 – 4683
    Beta strandi479 – 4868
    Beta strandi488 – 4903
    Beta strandi492 – 50110
    Beta strandi504 – 5074
    Turni509 – 5113

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EWKX-ray2.20A/B33-522[»]
    1EWTX-ray3.70A/B33-522[»]
    1EWVX-ray4.00A/B33-522[»]
    1ISRX-ray4.00A33-522[»]
    1ISSX-ray3.30A/B33-522[»]
    ProteinModelPortaliP23385.
    SMRiP23385. Positions 35-512.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23385.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini19 – 592574ExtracellularBy similarityAdd
    BLAST
    Topological domaini616 – 62914CytoplasmicBy similarityAdd
    BLAST
    Topological domaini651 – 6588ExtracellularBy similarity
    Topological domaini681 – 70323CytoplasmicBy similarityAdd
    BLAST
    Topological domaini728 – 75023ExtracellularBy similarityAdd
    BLAST
    Topological domaini773 – 78513CytoplasmicBy similarityAdd
    BLAST
    Topological domaini808 – 8158ExtracellularBy similarity
    Topological domaini841 – 1199359CytoplasmicBy similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei593 – 61523Helical; Name=1By similarityAdd
    BLAST
    Transmembranei630 – 65021Helical; Name=2By similarityAdd
    BLAST
    Transmembranei659 – 68022Helical; Name=3By similarityAdd
    BLAST
    Transmembranei704 – 72724Helical; Name=4By similarityAdd
    BLAST
    Transmembranei751 – 77222Helical; Name=5By similarityAdd
    BLAST
    Transmembranei786 – 80722Helical; Name=6By similarityAdd
    BLAST
    Transmembranei816 – 84025Helical; Name=7By similarityAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni186 – 1883Glutamate binding

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1014 – 103421Gln/Pro-richAdd
    BLAST
    Compositional biasi1074 – 10807Gln/Pro-rich
    Compositional biasi1126 – 113510Asp/Glu-rich (acidic)
    Compositional biasi1140 – 119960Ser-richAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG295200.
    HOGENOMiHOG000218636.
    HOVERGENiHBG107965.
    InParanoidiP23385.
    KOiK04603.
    PhylomeDBiP23385.

    Family and domain databases

    InterProiIPR001828. ANF_lig-bd_rcpt.
    IPR000337. GPCR_3.
    IPR011500. GPCR_3_9-Cys_dom.
    IPR017978. GPCR_3_C.
    IPR017979. GPCR_3_CS.
    IPR000162. GPCR_3_mtglu_rcpt.
    IPR001256. GPCR_3_mtglu_rcpt_1.
    IPR019588. Metabotropic_Glu_rcpt_Homer-bd.
    IPR028082. Peripla_BP_I.
    [Graphical view]
    PfamiPF00003. 7tm_3. 1 hit.
    PF01094. ANF_receptor. 1 hit.
    PF10606. GluR_Homer-bdg. 1 hit.
    PF07562. NCD3G. 1 hit.
    [Graphical view]
    PRINTSiPR00248. GPCRMGR.
    PR01051. MTABOTROPC1R.
    PR00593. MTABOTROPICR.
    SUPFAMiSSF53822. SSF53822. 1 hit.
    PROSITEiPS00979. G_PROTEIN_RECEP_F3_1. 1 hit.
    PS00980. G_PROTEIN_RECEP_F3_2. 1 hit.
    PS00981. G_PROTEIN_RECEP_F3_3. 1 hit.
    PS50259. G_PROTEIN_RECEP_F3_4. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1A (identifier: P23385-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MVRLLLIFFP MIFLEMSILP RMPDRKVLLA GASSQRSVAR MDGDVIIGAL     50
    FSVHHQPPAE KVPERKCGEI REQYGIQRVE AMFHTLDKIN ADPVLLPNIT 100
    LGSEIRDSCW HSSVALEQSI EFIRDSLISI RDEKDGLNRC LPDGQTLPPG 150
    RTKKPIAGVI GPGSSSVAIQ VQNLLQLFDI PQIAYSATSI DLSDKTLYKY 200
    FLRVVPSDTL QARAMLDIVK RYNWTYVSAV HTEGNYGESG MDAFKELAAQ 250
    EGLCIAHSDK IYSNAGEKSF DRLLRKLRER LPKARVVVCF CEGMTVRGLL 300
    SAMRRLGVVG EFSLIGSDGW ADRDEVIEGY EVEANGGITI KLQSPEVRSF 350
    DDYFLKLRLD TNTRNPWFPE FWQHRFQCRL PGHLLENPNF KKVCTGNESL 400
    EENYVQDSKM GFVINAIYAM AHGLQNMHHA LCPGHVGLCD AMKPIDGRKL 450
    LDFLIKSSFV GVSGEEVWFD EKGDAPGRYD IMNLQYTEAN RYDYVHVGTW 500
    HEGVLNIDDY KIQMNKSGMV RSVCSEPCLK GQIKVIRKGE VSCCWICTAC 550
    KENEFVQDEF TCRACDLGWW PNAELTGCEP IPVRYLEWSD IESIIAIAFS 600
    CLGILVTLFV TLIFVLYRDT PVVKSSSREL CYIILAGIFL GYVCPFTLIA 650
    KPTTTSCYLQ RLLVGLSSAM CYSALVTKTN RIARILAGSK KKICTRKPRF 700
    MSAWAQVIIA SILISVQLTL VVTLIIMEPP MPILSYPSIK EVYLICNTSN 750
    LGVVAPVGYN GLLIMSCTYY AFKTRNVPAN FNEAKYIAFT MYTTCIIWLA 800
    FVPIYFGSNY KIITTCFAVS LSVTVALGCM FTPKMYIIIA KPERNVRSAF 850
    TTSDVVRMHV GDGKLPCRSN TFLNIFRRKK PGAGNANSNG KSVSWSEPGG 900
    RQAPKGQHVW QRLSVHVKTN ETACNQTAVI KPLTKSYQGS GKSLTFSDAS 950
    TKTLYNVEEE DNTPSAHFSP PSSPSMVVHR RGPPVATTPP LPPHLTAEET 1000
    PLFLADSVIP KGLPPPLPQQ QPQQPPPQQP PQQPKSLMDQ LQGVVTNFGS 1050
    GIPDFHAVLA GPGTPGNSLR SLYPPPPPPQ HLQMLPLHLS TFQEESISPP 1100
    GEDIDDDSER FKLLQEFVYE REGNTEEDEL EEEEDLPTAS KLTPEDSPAL 1150
    TPPSPFRDSV ASGSSVPSSP VSESVLCTPP NVTYASVILR DYKQSSSTL 1199
    Length:1,199
    Mass (Da):133,236
    Last modified:November 1, 1991 - v1
    Checksum:iEEE5A04C50694B9F
    GO
    Isoform 1B (identifier: P23385-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         887-906: NSNGKSVSWSEPGGRQAPKG → KKRQPEFSPSSQCPSAHAQL
         907-1199: Missing.

    Note: C-terminally truncated forms of isoform 1A.

    Show »
    Length:906
    Mass (Da):101,638
    Checksum:i93201A86AD366DB3
    GO
    Isoform 1C (identifier: P23385-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         888-897: SNGKSVSWSE → FALDRQNTVY
         898-1199: Missing.

    Note: C-terminally truncated forms of isoform 1A.

    Show »
    Length:897
    Mass (Da):100,752
    Checksum:i6F1E809C2AC521B9
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei887 – 90620NSNGK…QAPKG → KKRQPEFSPSSQCPSAHAQL in isoform 1B. CuratedVSP_002026Add
    BLAST
    Alternative sequencei888 – 89710SNGKSVSWSE → FALDRQNTVY in isoform 1C. CuratedVSP_002028
    Alternative sequencei898 – 1199302Missing in isoform 1C. CuratedVSP_002029Add
    BLAST
    Alternative sequencei907 – 1199293Missing in isoform 1B. CuratedVSP_002027Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57569 mRNA. Translation: CAA40799.1.
    M61099 mRNA. Translation: AAA19497.1.
    S48085 mRNA. Translation: AAB24138.1.
    PIRiA41939.
    RefSeqiNP_001107802.1. NM_001114330.1. [P23385-2]
    NP_058707.1. NM_017011.1. [P23385-1]
    UniGeneiRn.87787.

    Genome annotation databases

    GeneIDi24414.
    KEGGirno:24414.
    UCSCiRGD:2742. rat. [P23385-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57569 mRNA. Translation: CAA40799.1 .
    M61099 mRNA. Translation: AAA19497.1 .
    S48085 mRNA. Translation: AAB24138.1 .
    PIRi A41939.
    RefSeqi NP_001107802.1. NM_001114330.1. [P23385-2 ]
    NP_058707.1. NM_017011.1. [P23385-1 ]
    UniGenei Rn.87787.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EWK X-ray 2.20 A/B 33-522 [» ]
    1EWT X-ray 3.70 A/B 33-522 [» ]
    1EWV X-ray 4.00 A/B 33-522 [» ]
    1ISR X-ray 4.00 A 33-522 [» ]
    1ISS X-ray 3.30 A/B 33-522 [» ]
    ProteinModelPortali P23385.
    SMRi P23385. Positions 35-512.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 246579. 7 interactions.
    DIPi DIP-44897N.
    IntActi P23385. 5 interactions.
    MINTi MINT-1890098.

    Chemistry

    BindingDBi P23385.
    ChEMBLi CHEMBL2111335.
    GuidetoPHARMACOLOGYi 289.

    Protein family/group databases

    GPCRDBi Search...

    PTM databases

    PhosphoSitei P23385.

    Proteomic databases

    PaxDbi P23385.
    PRIDEi P23385.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 24414.
    KEGGi rno:24414.
    UCSCi RGD:2742. rat. [P23385-1 ]

    Organism-specific databases

    CTDi 2911.
    RGDi 2742. Grm1.

    Phylogenomic databases

    eggNOGi NOG295200.
    HOGENOMi HOG000218636.
    HOVERGENi HBG107965.
    InParanoidi P23385.
    KOi K04603.
    PhylomeDBi P23385.

    Miscellaneous databases

    EvolutionaryTracei P23385.
    NextBioi 603247.
    PMAP-CutDB P23385.
    PROi P23385.

    Gene expression databases

    Genevestigatori P23385.

    Family and domain databases

    InterProi IPR001828. ANF_lig-bd_rcpt.
    IPR000337. GPCR_3.
    IPR011500. GPCR_3_9-Cys_dom.
    IPR017978. GPCR_3_C.
    IPR017979. GPCR_3_CS.
    IPR000162. GPCR_3_mtglu_rcpt.
    IPR001256. GPCR_3_mtglu_rcpt_1.
    IPR019588. Metabotropic_Glu_rcpt_Homer-bd.
    IPR028082. Peripla_BP_I.
    [Graphical view ]
    Pfami PF00003. 7tm_3. 1 hit.
    PF01094. ANF_receptor. 1 hit.
    PF10606. GluR_Homer-bdg. 1 hit.
    PF07562. NCD3G. 1 hit.
    [Graphical view ]
    PRINTSi PR00248. GPCRMGR.
    PR01051. MTABOTROPC1R.
    PR00593. MTABOTROPICR.
    SUPFAMi SSF53822. SSF53822. 1 hit.
    PROSITEi PS00979. G_PROTEIN_RECEP_F3_1. 1 hit.
    PS00980. G_PROTEIN_RECEP_F3_2. 1 hit.
    PS00981. G_PROTEIN_RECEP_F3_3. 1 hit.
    PS50259. G_PROTEIN_RECEP_F3_4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and expression of a metabotropic glutamate receptor."
      Masu M., Tanabe Y., Tsuchida K., Shigemoto R., Nakanishi S.
      Nature 349:760-765(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Strain: Sprague-Dawley.
      Tissue: Brain.
    2. "Cloning, expression, and gene structure of a G protein-coupled glutamate receptor from rat brain."
      Houamed K.M., Kuijper J.L., Gilbert T.L., Haldeman B.A., O'Hara P.J., Mulvihill E.R., Almers W., Hagen F.S.
      Science 252:1318-1321(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Tissue: Brain.
    3. "A family of metabotropic glutamate receptors."
      Tanabe Y., Masu M., Ishii T., Shigemoto R., Nakanishi S.
      Neuron 8:169-179(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 1B).
      Tissue: Brain.
    4. "Alternative splicing generates metabotropic glutamate receptors inducing different patterns of calcium release in Xenopus oocytes."
      Pin J.-P., Waeber C., Prezeau L., Bockaert J., Heinemann S.F.
      Proc. Natl. Acad. Sci. U.S.A. 89:10331-10335(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 1C), FUNCTION.
      Tissue: Brain.
    5. "Competitive interaction of seven in absentia homolog-1A and Ca2+/calmodulin with the cytoplasmic tail of group 1 metabotropic glutamate receptors."
      Ishikawa K., Nash S.R., Nishimune A., Neki A., Kaneko S., Nakanishi S.
      Genes Cells 4:381-390(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SIAH1.
    6. "Cys-140 is critical for metabotropic glutamate receptor-1 dimerization."
      Ray K., Hauschild B.C.
      J. Biol. Chem. 275:34245-34251(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERCHAIN DISULFIDE BOND, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-67; CYS-109 AND CYS-140.
    7. "Tamalin, a PDZ domain-containing protein, links a protein complex formation of group 1 metabotropic glutamate receptors and the guanine nucleotide exchange factor cytohesins."
      Kitano J., Kimura K., Yamazaki Y., Soda T., Shigemoto R., Nakajima Y., Nakanishi S.
      J. Neurosci. 22:1280-1289(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GRASP.
    8. "Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor."
      Kunishima N., Shimada Y., Tsuji Y., Sato T., Yamamoto M., Kumasaka T., Nakanishi S., Jingami H., Morikawa K.
      Nature 407:971-977(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 33-522 ALONE AND IN COMPLEX WITH GLUTAMATE, SUBUNIT, GLYCOSYLATION AT ASN-98 AND ASN-223, GLUTAMATE-BINDING SITES, DISULFIDE BONDS.
    9. "Structural views of the ligand-binding cores of a metabotropic glutamate receptor complexed with an antagonist and both glutamate and Gd3+."
      Tsuchiya D., Kunishima N., Kamiya N., Jingami H., Morikawa K.
      Proc. Natl. Acad. Sci. U.S.A. 99:2660-2665(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 33-522 IN COMPLEX WITH GLUTAMATE AND ANTAGONIST, SUBUNIT, DISULFIDE BONDS.

    Entry informationi

    Entry nameiGRM1_RAT
    AccessioniPrimary (citable) accession number: P23385
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 145 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Activated by quisqualate > glutamate > ibotenate > trans-1- aminocyclopentyl-1,3-dicarboxylate; inhibited by 2-amino-3-phosphonopropionate.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3