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P23385 (GRM1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Metabotropic glutamate receptor 1

Short name=mGluR1
Gene names
Name:Grm1
Synonyms:Gprc1a, Mglur1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1199 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.4

Subunit structure

Homodimer; disulfide-linked. The PPXXF motif binds HOMER1, HOMER2 and HOMER3. Interacts with RYR1, RYR2, ITPR1, SHANK1 and SHANK3 By similarity. Interacts with SIAH1 and GRASP. Ref.5 Ref.6 Ref.7 Ref.8

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

Predominantly expressed in cerebellar Purkinje cells, CA2-CA3 pyramidal cells of the hippocampus, and mitral and tufted cells of the olfactory bulb. Ref.1 Ref.2

Miscellaneous

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

Sequence similarities

Belongs to the G-protein coupled receptor 3 family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled glutamate receptor signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

calcium-mediated signaling

Inferred from direct assay PubMed 15229243. Source: RGD

membrane depolarization

Traceable author statement PubMed 12514208. Source: UniProtKB

phospholipase C-activating G-protein coupled glutamate receptor signaling pathway

Traceable author statement PubMed 12514208. Source: UniProtKB

positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway

Traceable author statement PubMed 12514208. Source: UniProtKB

protein kinase C-activating G-protein coupled receptor signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of glutamate secretion

Traceable author statement PubMed 11530226. Source: UniProtKB

regulation of synaptic transmission, glutamatergic

Inferred from direct assay PubMed 11530226. Source: UniProtKB

sensory perception of pain

Inferred from expression pattern PubMed 12514201. Source: RGD

synaptic transmission

Inferred from expression pattern PubMed 12514201. Source: RGD

synaptic transmission, GABAergic

Traceable author statement PubMed 11530226. Source: UniProtKB

   Cellular_componentaxon

Inferred from direct assay PubMed 11530226. Source: UniProtKB

dendritic spine

Inferred from direct assay PubMed 18582438. Source: RGD

integral component of plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

postsynaptic density

Inferred from direct assay PubMed 11226670PubMed 18582438. Source: RGD

presynaptic membrane

Inferred from direct assay PubMed 11530226. Source: UniProtKB

   Molecular_functionG-protein coupled receptor activity

Traceable author statement PubMed 12514201. Source: RGD

PLC activating G-protein coupled glutamate receptor activity

Traceable author statement PubMed 12514208. Source: UniProtKB

estrogen receptor binding

Inferred from physical interaction PubMed 18948402. Source: RGD

glutamate receptor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

identical protein binding

Inferred from physical interaction PubMed 19590495. Source: IntAct

protein binding

Inferred from physical interaction PubMed 14519764. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-4410410,EBI-4410410
Ppp1ccP6308815EBI-4410410,EBI-80049

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1A (identifier: P23385-1)

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.
Isoform 1B (identifier: P23385-2)

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.
Isoform 1C (identifier: P23385-3)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 11991181Metabotropic glutamate receptor 1
PRO_0000012924

Regions

Topological domain19 – 592574Extracellular Potential
Transmembrane593 – 61523Helical; Name=1; Potential
Topological domain616 – 62914Cytoplasmic Potential
Transmembrane630 – 65021Helical; Name=2; Potential
Topological domain651 – 66111Extracellular Potential
Transmembrane662 – 68019Helical; Name=3; Potential
Topological domain681 – 70626Cytoplasmic Potential
Transmembrane707 – 72721Helical; Name=4; Potential
Topological domain728 – 75023Extracellular Potential
Transmembrane751 – 77222Helical; Name=5; Potential
Topological domain773 – 78513Cytoplasmic Potential
Transmembrane786 – 80823Helical; Name=6; Potential
Topological domain809 – 8146Extracellular Potential
Transmembrane815 – 84026Helical; Name=7; Potential
Topological domain841 – 1199359Cytoplasmic Potential
Region186 – 1883Glutamate binding
Compositional bias1014 – 103421Gln/Pro-rich
Compositional bias1074 – 10807Gln/Pro-rich
Compositional bias1126 – 113510Asp/Glu-rich (acidic)
Compositional bias1140 – 119960Ser-rich

Sites

Binding site741Glutamate
Binding site1651Glutamate
Binding site2361Glutamate
Binding site3181Glutamate
Binding site4091Glutamate

Amino acid modifications

Glycosylation981N-linked (GlcNAc...) Ref.7
Glycosylation2231N-linked (GlcNAc...) Ref.7
Glycosylation3971N-linked (GlcNAc...) Potential
Glycosylation5151N-linked (GlcNAc...) Potential
Disulfide bond67 ↔ 109 Ref.7 Ref.8
Disulfide bond140Interchain Ref.7 Ref.8
Disulfide bond289 ↔ 291 Ref.7 Ref.8
Disulfide bond378 ↔ 394 Ref.7 Ref.8
Disulfide bond432 ↔ 439 Ref.7 Ref.8

Natural variations

Alternative sequence887 – 90620NSNGK…QAPKG → KKRQPEFSPSSQCPSAHAQL in isoform 1B.
VSP_002026
Alternative sequence888 – 89710SNGKSVSWSE → FALDRQNTVY in isoform 1C.
VSP_002028
Alternative sequence898 – 1199302Missing in isoform 1C.
VSP_002029
Alternative sequence907 – 1199293Missing in isoform 1B.
VSP_002027

Secondary structure

................................................................................... 1199
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1A [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: EEE5A04C50694B9F

FASTA1,199133,236
        10         20         30         40         50         60 
MVRLLLIFFP MIFLEMSILP RMPDRKVLLA GASSQRSVAR MDGDVIIGAL FSVHHQPPAE 

        70         80         90        100        110        120 
KVPERKCGEI REQYGIQRVE AMFHTLDKIN ADPVLLPNIT LGSEIRDSCW HSSVALEQSI 

       130        140        150        160        170        180 
EFIRDSLISI RDEKDGLNRC LPDGQTLPPG RTKKPIAGVI GPGSSSVAIQ VQNLLQLFDI 

       190        200        210        220        230        240 
PQIAYSATSI DLSDKTLYKY FLRVVPSDTL QARAMLDIVK RYNWTYVSAV HTEGNYGESG 

       250        260        270        280        290        300 
MDAFKELAAQ EGLCIAHSDK IYSNAGEKSF DRLLRKLRER LPKARVVVCF CEGMTVRGLL 

       310        320        330        340        350        360 
SAMRRLGVVG EFSLIGSDGW ADRDEVIEGY EVEANGGITI KLQSPEVRSF DDYFLKLRLD 

       370        380        390        400        410        420 
TNTRNPWFPE FWQHRFQCRL PGHLLENPNF KKVCTGNESL EENYVQDSKM GFVINAIYAM 

       430        440        450        460        470        480 
AHGLQNMHHA LCPGHVGLCD AMKPIDGRKL LDFLIKSSFV GVSGEEVWFD EKGDAPGRYD 

       490        500        510        520        530        540 
IMNLQYTEAN RYDYVHVGTW HEGVLNIDDY KIQMNKSGMV RSVCSEPCLK GQIKVIRKGE 

       550        560        570        580        590        600 
VSCCWICTAC KENEFVQDEF TCRACDLGWW PNAELTGCEP IPVRYLEWSD IESIIAIAFS 

       610        620        630        640        650        660 
CLGILVTLFV TLIFVLYRDT PVVKSSSREL CYIILAGIFL GYVCPFTLIA KPTTTSCYLQ 

       670        680        690        700        710        720 
RLLVGLSSAM CYSALVTKTN RIARILAGSK KKICTRKPRF MSAWAQVIIA SILISVQLTL 

       730        740        750        760        770        780 
VVTLIIMEPP MPILSYPSIK EVYLICNTSN LGVVAPVGYN GLLIMSCTYY AFKTRNVPAN 

       790        800        810        820        830        840 
FNEAKYIAFT MYTTCIIWLA FVPIYFGSNY KIITTCFAVS LSVTVALGCM FTPKMYIIIA 

       850        860        870        880        890        900 
KPERNVRSAF TTSDVVRMHV GDGKLPCRSN TFLNIFRRKK PGAGNANSNG KSVSWSEPGG 

       910        920        930        940        950        960 
RQAPKGQHVW QRLSVHVKTN ETACNQTAVI KPLTKSYQGS GKSLTFSDAS TKTLYNVEEE 

       970        980        990       1000       1010       1020 
DNTPSAHFSP PSSPSMVVHR RGPPVATTPP LPPHLTAEET PLFLADSVIP KGLPPPLPQQ 

      1030       1040       1050       1060       1070       1080 
QPQQPPPQQP PQQPKSLMDQ LQGVVTNFGS GIPDFHAVLA GPGTPGNSLR SLYPPPPPPQ 

      1090       1100       1110       1120       1130       1140 
HLQMLPLHLS TFQEESISPP GEDIDDDSER FKLLQEFVYE REGNTEEDEL EEEEDLPTAS 

      1150       1160       1170       1180       1190 
KLTPEDSPAL TPPSPFRDSV ASGSSVPSSP VSESVLCTPP NVTYASVILR DYKQSSSTL 

« Hide

Isoform 1B [UniParc].

Checksum: 93201A86AD366DB3
Show »

FASTA906101,638
Isoform 1C [UniParc].

Checksum: 6F1E809C2AC521B9
Show »

FASTA897100,752

References

[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]"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.
[7]"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.
[8]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X57569 mRNA. Translation: CAA40799.1.
M61099 mRNA. Translation: AAA19497.1.
S48085 mRNA. Translation: AAB24138.1.
PIRA41939.
RefSeqNP_001107802.1. NM_001114330.1. [P23385-2]
NP_058707.1. NM_017011.1. [P23385-1]
UniGeneRn.87787.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP23385.
SMRP23385. Positions 35-512.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246579. 7 interactions.
DIPDIP-44897N.
IntActP23385. 5 interactions.
MINTMINT-1890098.

Chemistry

BindingDBP23385.
ChEMBLCHEMBL2111335.
GuidetoPHARMACOLOGY289.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP23385.

Proteomic databases

PaxDbP23385.
PRIDEP23385.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID24414.
KEGGrno:24414.
UCSCRGD:2742. rat. [P23385-1]

Organism-specific databases

CTD2911.
RGD2742. Grm1.

Phylogenomic databases

eggNOGNOG295200.
HOGENOMHOG000218636.
HOVERGENHBG107965.
InParanoidP23385.
KOK04603.
PhylomeDBP23385.

Gene expression databases

GenevestigatorP23385.

Family and domain databases

InterProIPR001828. 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]
PfamPF00003. 7tm_3. 1 hit.
PF01094. ANF_receptor. 1 hit.
PF10606. GluR_Homer-bdg. 1 hit.
PF07562. NCD3G. 1 hit.
[Graphical view]
PRINTSPR00248. GPCRMGR.
PR01051. MTABOTROPC1R.
PR00593. MTABOTROPICR.
SUPFAMSSF53822. SSF53822. 1 hit.
PROSITEPS00979. 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]
ProtoNetSearch...

Other

EvolutionaryTraceP23385.
NextBio603247.
PMAP-CutDBP23385.
PROP23385.

Entry information

Entry nameGRM1_RAT
AccessionPrimary (citable) accession number: P23385
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: July 9, 2014
This is version 144 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries