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P31422 (GRM3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 102. Feed History...

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

Names and origin

Protein namesRecommended name:
Metabotropic glutamate receptor 3
Short name=mGluR3
Gene names
Name:Grm3
Synonyms:Gprc1c, Mglur3
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length879 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for glutamate. The activity of this receptor is mediated by a G-protein that inhibits adenylate cyclase activity.

Subunit structure

Interacts with GRASP. Ref.2

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

Is widely distributed in the CNS. Predominant expression is seen in the neuronal cells of the cerebral cortex, dentate gyrus, and glial cells throughout brain regions.

Sequence similarities

Belongs to the G-protein coupled receptor 3 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 879857Metabotropic glutamate receptor 3
PRO_0000012929

Regions

Topological domain23 – 576554Extracellular Potential
Transmembrane577 – 59923Helical; Name=1; Potential
Topological domain600 – 61314Cytoplasmic Potential
Transmembrane614 – 63421Helical; Name=2; Potential
Topological domain635 – 64511Extracellular Potential
Transmembrane646 – 66419Helical; Name=3; Potential
Topological domain665 – 68824Cytoplasmic Potential
Transmembrane689 – 70921Helical; Name=4; Potential
Topological domain710 – 73425Extracellular Potential
Transmembrane735 – 75622Helical; Name=5; Potential
Topological domain757 – 76913Cytoplasmic Potential
Transmembrane770 – 79223Helical; Name=6; Potential
Topological domain793 – 80210Extracellular Potential
Transmembrane803 – 82826Helical; Name=7; Potential
Topological domain829 – 87951Cytoplasmic Potential

Amino acid modifications

Glycosylation2091N-linked (GlcNAc...) Ref.3
Glycosylation2921N-linked (GlcNAc...) Potential
Glycosylation4141N-linked (GlcNAc...) Potential
Glycosylation4391N-linked (GlcNAc...) Potential
Disulfide bond57 ↔ 99 Ref.3
Disulfide bond240 ↔ 527 Ref.3
Disulfide bond361 ↔ 373 Ref.3
Disulfide bond412 ↔ 419 Ref.3
Disulfide bond509 ↔ 528 Ref.3
Disulfide bond513 ↔ 531 Ref.3
Disulfide bond534 ↔ 546 Ref.3
Disulfide bond549 ↔ 562 Ref.3

Secondary structure

1 ............................................................................................................ 879
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P31422 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 3E5965EDD5E6DEED

FASTA87998,960
        10         20         30         40         50         60 
MKMLTRLQIL MLALFSKGFL LSLGDHNFMR REIKIEGDLV LGGLFPINEK GTGTEECGRI 

        70         80         90        100        110        120 
NEDRGIQRLE AMLFAIDEIN KDNYLLPGVK LGVHILDTCS RDTYALEQSL EFVRASLTKV 

       130        140        150        160        170        180 
DEAEYMCPDG SYAIQENIPL LIAGVIGGSY SSVSIQVANL LRLFQIPQIS YASTSAKLSD 

       190        200        210        220        230        240 
KSRYDYFART VPPDFYQAKA MAEILRFFNW TYVSTVASEG DYGETGIEAF EQEARLRNIC 

       250        260        270        280        290        300 
IATAEKVGRS NIRKSYDSVI RELLQKPNAR VVVLFMRSDD SRELIAAANR VNASFTWVAS 

       310        320        330        340        350        360 
DGWGAQESIV KGSEHVAYGA ITLELASHPV RQFDRYFQSL NPYNNHRNPW FRDFWEQKFQ 

       370        380        390        400        410        420 
CSLQNKRNHR QVCDKHLAID SSNYEQESKI MFVVNAVYAM AHALHKMQRT LCPNTTKLCD 

       430        440        450        460        470        480 
AMKILDGKKL YKEYLLKINF TAPFNPNKGA DSIVKFDTFG DGMGRYNVFN LQQTGGKYSY 

       490        500        510        520        530        540 
LKVGHWAETL SLDVDSIHWS RNSVPTSQCS DPCAPNEMKN MQPGDVCCWI CIPCEPYEYL 

       550        560        570        580        590        600 
VDEFTCMDCG PGQWPTADLS GCYNLPEDYI KWEDAWAIGP VTIACLGFLC TCIVITVFIK 

       610        620        630        640        650        660 
HNNTPLVKAS GRELCYILLF GVSLSYCMTF FFIAKPSPVI CALRRLGLGT SFAICYSALL 

       670        680        690        700        710        720 
TKTNCIARIF DGVKNGAQRP KFISPSSQVF ICLGLILVQI VMVSVWLILE TPGTRRYTLP 

       730        740        750        760        770        780 
EKRETVILKC NVKDSSMLIS LTYDVVLVIL CTVYAFKTRK CPENFNEAKF IGFTMYTTCI 

       790        800        810        820        830        840 
IWLAFLPIFY VTSSDYRVQT TTMCISVSLS GFVVLGCLFA PKVHIVLFQP QKNVVTHRLH 

       850        860        870 
LNRFSVSGTA TTYSQSSAST YVPTVCNGRE VLDSTTSSL

« Hide

References

[1]"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: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"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.
[3]"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 (2.35 ANGSTROMS) OF 25-575, GLYCOSYLATION AT ASN-209, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M92076 mRNA. No translation available.
IPIIPI00769125.
PIRJH0562.
RefSeqNP_001099182.1. NM_001105712.1.
UniGeneRn.41715.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E4UX-ray2.35A/B25-575[»]
2E4VX-ray2.40A/B25-575[»]
2E4WX-ray2.40A/B25-575[»]
2E4XX-ray2.75A/B25-575[»]
2E4YX-ray3.40A/B25-575[»]
ProteinModelPortalP31422.
SMRP31422. Positions 28-567.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-1773162.
STRING10116.ENSRNOP00000007572.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP31422.

Proteomic databases

PaxDbP31422.
PRIDEP31422.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000007572; ENSRNOP00000007572; ENSRNOG00000005519.
GeneID24416.
KEGGrno:24416.

Organism-specific databases

CTD2913.
RGD2744. Grm3.

Phylogenomic databases

eggNOGNOG295200.
GeneTreeENSGT00640000091090.
HOGENOMHOG000218635.
HOVERGENHBG107965.
InParanoidP31422.
KOK04605.
OrthoDBEOG49ZXNJ.

Gene expression databases

GenevestigatorP31422.

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.
IPR001234. GPCR_3_mtglu_rcpt_3.
[Graphical view]
PfamPF00003. 7tm_3. 1 hit.
PF01094. ANF_receptor. 1 hit.
PF07562. NCD3G. 1 hit.
[Graphical view]
PRINTSPR00248. GPCRMGR.
PR01053. MTABOTROPC3R.
PR00593. MTABOTROPICR.
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

BindingDBP31422.
ChEMBLCHEMBL3067.
EvolutionaryTraceP31422.
NextBio603257.

Entry information

Entry nameGRM3_RAT
AccessionPrimary (citable) accession number: P31422
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: May 1, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents