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P35400 (GRM7_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Metabotropic glutamate receptor 7

Short name=mGluR7
Gene names
Name:Grm7
Synonyms:Gprc1g, Mglur7
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length915 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, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Ref.1 Ref.2

Subunit structure

Interacts with PICK1. Ref.3

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

Widely distributed throughout the brain. Ref.1 Ref.2

Sequence similarities

Belongs to the G-protein coupled receptor 3 family.

Ontologies

Keywords
   Biological processOlfaction
Sensory transduction
   Cellular componentCell membrane
Membrane
   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_processadenylate cyclase-inhibiting G-protein coupled glutamate receptor signaling pathway

Inferred from direct assay PubMed 11825890. Source: RGD

learning or memory

Traceable author statement PubMed 12021391. Source: UniProtKB

negative regulation of glutamate secretion

Inferred from direct assay PubMed 11825890PubMed 12692128. Source: RGD

sensory perception of smell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 9300765. Source: RGD

asymmetric synapse

Inferred from direct assay PubMed 9300765. Source: RGD

axon

Inferred from direct assay PubMed 9300765. Source: RGD

axon terminus

Inferred from direct assay PubMed 11825890. Source: RGD

cell surface

Inferred from direct assay PubMed 16890965. Source: UniProtKB

dendrite

Inferred from direct assay PubMed 9300765. Source: RGD

dendritic shaft

Inferred from direct assay PubMed 12823458. Source: RGD

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred from direct assay PubMed 9300765. Source: RGD

neuronal cell body

Inferred from direct assay PubMed 8929965PubMed 9300765. Source: RGD

postsynaptic membrane

Inferred from direct assay PubMed 8764662. Source: UniProtKB

presynaptic active zone

Inferred from direct assay PubMed 8764662. Source: UniProtKB

presynaptic membrane

Inferred from direct assay PubMed 9300765. Source: RGD

protein complex

Inferred from direct assay PubMed 11007882. Source: RGD

rough endoplasmic reticulum

Inferred from direct assay PubMed 9300765. Source: RGD

synapse

Inferred from direct assay PubMed 11007882. Source: RGD

terminal bouton

Inferred from direct assay PubMed 12823458. Source: RGD

   Molecular_functionPDZ domain binding

Inferred from physical interaction PubMed 11007882. Source: RGD

adenylate cyclase inhibiting G-protein coupled glutamate receptor activity

Inferred from direct assay PubMed 11825890. Source: RGD

calcium-dependent protein binding

Inferred from physical interaction PubMed 21855531. Source: RGD

calmodulin binding

Inferred from physical interaction PubMed 12021391. Source: UniProtKB

glutamate binding

Inferred from direct assay PubMed 11825890PubMed 12692128PubMed 17620729. Source: RGD

group III metabotropic glutamate receptor activity

Inferred from direct assay PubMed 12692128. Source: RGD

protein homodimerization activity

Inferred from direct assay PubMed 17620729. Source: RGD

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3434 Potential
Chain35 – 915881Metabotropic glutamate receptor 7
PRO_0000012940

Regions

Topological domain35 – 590556Extracellular Potential
Transmembrane591 – 61525Helical; Name=1; Potential
Topological domain616 – 62712Cytoplasmic Potential
Transmembrane628 – 64821Helical; Name=2; Potential
Topological domain649 – 6546Extracellular Potential
Transmembrane655 – 67521Helical; Name=3; Potential
Topological domain676 – 70227Cytoplasmic Potential
Transmembrane703 – 72321Helical; Name=4; Potential
Topological domain724 – 75330Extracellular Potential
Transmembrane754 – 77522Helical; Name=5; Potential
Topological domain776 – 78813Cytoplasmic Potential
Transmembrane789 – 81022Helical; Name=6; Potential
Topological domain811 – 82515Extracellular Potential
Transmembrane826 – 85025Helical; Name=7; Potential
Topological domain851 – 91565Cytoplasmic Potential
Region180 – 1823Glutamate binding By similarity

Sites

Binding site1591Glutamate By similarity
Binding site2301Glutamate By similarity
Binding site3141Glutamate By similarity
Binding site4071Glutamate By similarity

Amino acid modifications

Glycosylation981N-linked (GlcNAc...) Potential
Glycosylation4581N-linked (GlcNAc...) Potential
Glycosylation4861N-linked (GlcNAc...) Potential
Glycosylation5721N-linked (GlcNAc...) Potential
Disulfide bond67 ↔ 109 Ref.4
Disulfide bond249 ↔ 541 By similarity
Disulfide bond374 ↔ 390 Ref.4
Disulfide bond430 ↔ 437 Ref.4
Disulfide bond523 ↔ 542 By similarity
Disulfide bond527 ↔ 545 By similarity
Disulfide bond548 ↔ 560 By similarity
Disulfide bond563 ↔ 576 By similarity

Secondary structure

............................................................................. 915
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P35400 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: F28AFC4C6454A6C2

FASTA915102,232
        10         20         30         40         50         60 
MVQLGKLLRV LTLMKFPCCV LEVLLCVLAA AARGQEMYAP HSIRIEGDVT LGGLFPVHAK 

        70         80         90        100        110        120 
GPSGVPCGDI KRENGIHRLE AMLYALDQIN SDPNLLPNVT LGARILDTCS RDTYALEQSL 

       130        140        150        160        170        180 
TFVQALIQKD TSDVRCTNGE PPVFVKPEKV VGVIGASGSS VSIMVANILR LFQIPQISYA 

       190        200        210        220        230        240 
STAPELSDDR RYDFFSRVVP PDSFQAQAMV DIVKALGWNY VSTLASEGSY GEKGVESFTQ 

       250        260        270        280        290        300 
ISKEAGGLCI AQSVRIPQER KDRTIDFDRI IKQLLDTPNS RAVVIFANDE DIKQILAAAK 

       310        320        330        340        350        360 
RADQVGHFLW VGSDSWGSKI NPLHQHEDIA EGAITIQPKR ATVEGFDAYF TSRTLENNRR 

       370        380        390        400        410        420 
NVWFAEYWEE NFNCKLTISG SKKEDTDRKC TGQERIGKDS NYEQEGKVQF VIDAVYAMAH 

       430        440        450        460        470        480 
ALHHMNKDLC ADYRGVCPEM EQAGGKKLLK YIRHVNFNGS AGTPVMFNKN GDAPGRYDIF 

       490        500        510        520        530        540 
QYQTTNTTNP GYRLIGQWTD ELQLNIEDMQ WGKGVREIPS SVCTLPCKPG QRKKTQKGTP 

       550        560        570        580        590        600 
CCWTCEPCDG YQYQFDEMTC QHCPYDQRPN ENRTGCQNIP IIKLEWHSPW AVIPVFLAML 

       610        620        630        640        650        660 
GIIATIFVMA TFIRYNDTPI VRASGRELSY VLLTGIFLCY IITFLMIAKP DVAVCSFRRV 

       670        680        690        700        710        720 
FLGLGMCISY AALLTKTNRI YRIFEQGKKS VTAPRLISPT SQLAITSSLI SVQLLGVFIW 

       730        740        750        760        770        780 
FGVDPPNIII DYDEHKTMNP EQARGVLKCD ITDLQIICSL GYSILLMVTC TVYAIKTRGV 

       790        800        810        820        830        840 
PENFNEAKPI GFTMYTTCIV WLAFIPIFFG TAQSAEKLYI QTTTLTISMN LSASVALGML 

       850        860        870        880        890        900 
YMPKVYIIIF HPELNVQKRK RSFKAVVTAA TMSSRLSHKP SDRPNGEAKT ELCENVDPNS 

       910 
PAAKKKYVSY NNLVI 

« Hide

References

[1]"Molecular characterization of a new metabotropic glutamate receptor mGluR7 coupled to inhibitory cyclic AMP signal transduction."
Okamoto N., Hori S., Akazawa C., Hayashi Y., Shigemoto R., Mizuno N., Nakanishi S.
J. Biol. Chem. 269:1231-1236(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Strain: Sprague-Dawley.
Tissue: Brain.
[2]"Cloning and expression of a new member of the L-2-amino-4-phosphonobutyric acid-sensitive class of metabotropic glutamate receptors."
Saugstad J.A., Kinzie J.M., Mulvihill E.R., Segerson T.P., Westbrook G.L.
Mol. Pharmacol. 45:367-372(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Strain: Sprague-Dawley.
Tissue: Olfactory bulb.
[3]"Interaction of the C-terminal tail region of the metabotropic glutamate receptor 7 with the protein kinase C substrate PICK1."
El Far O., Airas J., Wischmeyer E., Nehring R.B., Karschin A., Betz H.
Eur. J. Neurosci. 12:4215-4221(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PICK1.
[4]"Structures of the extracellular regions of the group II/III metabotropic glutamate receptors."
Muto T., Tsuchiya D., Morikawa K., Jingami H.
Proc. Natl. Acad. Sci. U.S.A. 104:3759-3764(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 33-521, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D16817 mRNA. Translation: BAA04092.1.
U06832 mRNA. Translation: AAA20655.1.
PIRA49874.
RefSeqNP_112302.1. NM_031040.1.
UniGeneRn.10409.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E4ZX-ray3.30A33-521[»]
ProteinModelPortalP35400.
SMRP35400. Positions 40-511.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid249569. 10 interactions.
DIPDIP-41145N.
IntActP35400. 6 interactions.
MINTMINT-146474.
STRING10116.ENSRNOP00000053411.

Chemistry

BindingDBP35400.
ChEMBLCHEMBL2111335.
GuidetoPHARMACOLOGY295.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP35400.

Proteomic databases

PRIDEP35400.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID81672.
KEGGrno:81672.

Organism-specific databases

CTD2917.
RGD619857. Grm7.

Phylogenomic databases

eggNOGNOG295200.
HOVERGENHBG107965.
KOK04608.
PhylomeDBP35400.

Gene expression databases

GenevestigatorP35400.

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.
IPR001883. GPCR_3_mtglu_rcpt_7.
IPR028082. Peripla_BP_I.
[Graphical view]
PfamPF00003. 7tm_3. 1 hit.
PF01094. ANF_receptor. 1 hit.
PF07562. NCD3G. 1 hit.
[Graphical view]
PRINTSPR00248. GPCRMGR.
PR01057. MTABOTROPC7R.
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

EvolutionaryTraceP35400.
NextBio615264.

Entry information

Entry nameGRM7_RAT
AccessionPrimary (citable) accession number: P35400
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 104 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