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Protein

Metabotropic glutamate receptor 1

Gene

Grm1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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)DescriptionActionsGraphical viewLength
Binding sitei74Glutamate2 Publications1
Binding sitei165Glutamate2 Publications1
Binding sitei236Glutamate2 Publications1
Binding sitei318Glutamate2 Publications1
Binding sitei409Glutamate2 Publications1

GO - Molecular functioni

  • estrogen receptor binding Source: RGD
  • glutamate receptor activity Source: UniProtKB
  • G-protein coupled receptor activity Source: RGD
  • PLC activating G-protein coupled glutamate receptor activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiR-RNO-416476. G alpha (q) signalling events.
R-RNO-420499. Class C/3 (Metabotropic glutamate/pheromone receptors).
R-RNO-6794361. Interactions of neurexins and neuroligins at synapses.

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
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi2742. Grm1.

Subcellular locationi

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini19 – 592ExtracellularBy similarityAdd BLAST574
Transmembranei593 – 615Helical; Name=1By similarityAdd BLAST23
Topological domaini616 – 629CytoplasmicBy similarityAdd BLAST14
Transmembranei630 – 650Helical; Name=2By similarityAdd BLAST21
Topological domaini651 – 658ExtracellularBy similarity8
Transmembranei659 – 680Helical; Name=3By similarityAdd BLAST22
Topological domaini681 – 703CytoplasmicBy similarityAdd BLAST23
Transmembranei704 – 727Helical; Name=4By similarityAdd BLAST24
Topological domaini728 – 750ExtracellularBy similarityAdd BLAST23
Transmembranei751 – 772Helical; Name=5By similarityAdd BLAST22
Topological domaini773 – 785CytoplasmicBy similarityAdd BLAST13
Transmembranei786 – 807Helical; Name=6By similarityAdd BLAST22
Topological domaini808 – 815ExtracellularBy similarity8
Transmembranei816 – 840Helical; Name=7By similarityAdd BLAST25
Topological domaini841 – 1199CytoplasmicBy similarityAdd BLAST359

GO - Cellular componenti

  • axon Source: UniProtKB
  • dendritic spine Source: RGD
  • integral component of plasma membrane Source: UniProtKB
  • postsynaptic density Source: RGD
  • presynaptic membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi67C → S: Impairs protein folding and abolishes location at the cell surface. 1 Publication1
Mutagenesisi109C → S: Impairs protein folding and abolishes location at the cell surface. 1 Publication1
Mutagenesisi140C → S: Impairs homodimerization. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL4477.
GuidetoPHARMACOLOGYi289.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000001292419 – 1199Metabotropic glutamate receptor 1Add BLAST1181

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi67 ↔ 109
Glycosylationi98N-linked (GlcNAc...)1 Publication1
Disulfide bondi140Interchain
Glycosylationi223N-linked (GlcNAc...)1 Publication1
Disulfide bondi289 ↔ 291
Disulfide bondi378 ↔ 394
Glycosylationi397N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi432 ↔ 439
Glycosylationi515N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi657 ↔ 746By similarity
Modified residuei853PhosphoserineBy similarity1
Modified residuei871PhosphothreonineBy similarity1
Modified residuei894PhosphoserineCombined sources1
Modified residuei969PhosphoserineBy similarity1
Modified residuei1098PhosphoserineBy similarity1
Modified residuei1147PhosphoserineCombined sources1
Modified residuei1151PhosphothreonineCombined sources1
Modified residuei1154PhosphoserineBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP23385.
PRIDEiP23385.

PTM databases

iPTMnetiP23385.
PhosphoSitePlusiP23385.

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

ExpressionAtlasiP23385. baseline and differential.

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

GO - Molecular functioni

  • estrogen receptor binding Source: RGD

Protein-protein interaction databases

BioGridi246579. 8 interactors.
DIPiDIP-44897N.
IntActiP23385. 5 interactors.
MINTiMINT-1890098.
STRINGi10116.ENSRNOP00000019319.

Chemistry databases

BindingDBiP23385.

Structurei

Secondary structure

11199
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi39 – 41Combined sources3
Beta strandi44 – 51Combined sources8
Turni59 – 65Combined sources7
Turni72 – 75Combined sources4
Helixi76 – 91Combined sources16
Beta strandi93 – 96Combined sources4
Beta strandi101 – 107Combined sources7
Helixi112 – 123Combined sources12
Beta strandi156 – 160Combined sources5
Helixi165 – 175Combined sources11
Helixi176 – 178Combined sources3
Beta strandi182 – 186Combined sources5
Helixi190 – 193Combined sources4
Turni195 – 197Combined sources3
Beta strandi201 – 205Combined sources5
Helixi208 – 221Combined sources14
Beta strandi226 – 234Combined sources9
Helixi235 – 251Combined sources17
Beta strandi254 – 261Combined sources8
Beta strandi263 – 265Combined sources3
Helixi267 – 278Combined sources12
Turni279 – 283Combined sources5
Beta strandi286 – 290Combined sources5
Helixi293 – 306Combined sources14
Beta strandi313 – 316Combined sources4
Turni318 – 322Combined sources5
Helixi324 – 327Combined sources4
Helixi331 – 334Combined sources4
Beta strandi338 – 342Combined sources5
Helixi348 – 354Combined sources7
Turni359 – 361Combined sources3
Helixi368 – 375Combined sources8
Turni400 – 403Combined sources4
Helixi410 – 431Combined sources22
Helixi440 – 442Combined sources3
Helixi447 – 455Combined sources9
Beta strandi458 – 460Combined sources3
Beta strandi466 – 468Combined sources3
Beta strandi479 – 486Combined sources8
Beta strandi488 – 490Combined sources3
Beta strandi492 – 501Combined sources10
Beta strandi504 – 507Combined sources4
Turni509 – 511Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23385.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni186 – 188Glutamate binding3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1014 – 1034Gln/Pro-richAdd BLAST21
Compositional biasi1074 – 1080Gln/Pro-rich7
Compositional biasi1126 – 1135Asp/Glu-rich (acidic)10
Compositional biasi1140 – 1199Ser-richAdd BLAST60

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1056. Eukaryota.
ENOG410XR6W. LUCA.
GeneTreeiENSGT00760000118884.
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.
SMARTiSM01229. GluR_Homer-bdg. 1 hit.
[Graphical view]
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. AlignAdd to basket

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

        10         20         30         40         50
MVRLLLIFFP MIFLEMSILP RMPDRKVLLA GASSQRSVAR MDGDVIIGAL
60 70 80 90 100
FSVHHQPPAE KVPERKCGEI REQYGIQRVE AMFHTLDKIN ADPVLLPNIT
110 120 130 140 150
LGSEIRDSCW HSSVALEQSI EFIRDSLISI RDEKDGLNRC LPDGQTLPPG
160 170 180 190 200
RTKKPIAGVI GPGSSSVAIQ VQNLLQLFDI PQIAYSATSI DLSDKTLYKY
210 220 230 240 250
FLRVVPSDTL QARAMLDIVK RYNWTYVSAV HTEGNYGESG MDAFKELAAQ
260 270 280 290 300
EGLCIAHSDK IYSNAGEKSF DRLLRKLRER LPKARVVVCF CEGMTVRGLL
310 320 330 340 350
SAMRRLGVVG EFSLIGSDGW ADRDEVIEGY EVEANGGITI KLQSPEVRSF
360 370 380 390 400
DDYFLKLRLD TNTRNPWFPE FWQHRFQCRL PGHLLENPNF KKVCTGNESL
410 420 430 440 450
EENYVQDSKM GFVINAIYAM AHGLQNMHHA LCPGHVGLCD AMKPIDGRKL
460 470 480 490 500
LDFLIKSSFV GVSGEEVWFD EKGDAPGRYD IMNLQYTEAN RYDYVHVGTW
510 520 530 540 550
HEGVLNIDDY KIQMNKSGMV RSVCSEPCLK GQIKVIRKGE VSCCWICTAC
560 570 580 590 600
KENEFVQDEF TCRACDLGWW PNAELTGCEP IPVRYLEWSD IESIIAIAFS
610 620 630 640 650
CLGILVTLFV TLIFVLYRDT PVVKSSSREL CYIILAGIFL GYVCPFTLIA
660 670 680 690 700
KPTTTSCYLQ RLLVGLSSAM CYSALVTKTN RIARILAGSK KKICTRKPRF
710 720 730 740 750
MSAWAQVIIA SILISVQLTL VVTLIIMEPP MPILSYPSIK EVYLICNTSN
760 770 780 790 800
LGVVAPVGYN GLLIMSCTYY AFKTRNVPAN FNEAKYIAFT MYTTCIIWLA
810 820 830 840 850
FVPIYFGSNY KIITTCFAVS LSVTVALGCM FTPKMYIIIA KPERNVRSAF
860 870 880 890 900
TTSDVVRMHV GDGKLPCRSN TFLNIFRRKK PGAGNANSNG KSVSWSEPGG
910 920 930 940 950
RQAPKGQHVW QRLSVHVKTN ETACNQTAVI KPLTKSYQGS GKSLTFSDAS
960 970 980 990 1000
TKTLYNVEEE DNTPSAHFSP PSSPSMVVHR RGPPVATTPP LPPHLTAEET
1010 1020 1030 1040 1050
PLFLADSVIP KGLPPPLPQQ QPQQPPPQQP PQQPKSLMDQ LQGVVTNFGS
1060 1070 1080 1090 1100
GIPDFHAVLA GPGTPGNSLR SLYPPPPPPQ HLQMLPLHLS TFQEESISPP
1110 1120 1130 1140 1150
GEDIDDDSER FKLLQEFVYE REGNTEEDEL EEEEDLPTAS KLTPEDSPAL
1160 1170 1180 1190
TPPSPFRDSV ASGSSVPSSP VSESVLCTPP NVTYASVILR DYKQSSSTL
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)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_002026887 – 906NSNGK…QAPKG → KKRQPEFSPSSQCPSAHAQL in isoform 1B. CuratedAdd BLAST20
Alternative sequenceiVSP_002028888 – 897SNGKSVSWSE → FALDRQNTVY in isoform 1C. Curated10
Alternative sequenceiVSP_002029898 – 1199Missing in isoform 1C. CuratedAdd BLAST302
Alternative sequenceiVSP_002027907 – 1199Missing in isoform 1B. CuratedAdd BLAST293

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

EnsembliENSRNOT00000044325; ENSRNOP00000047790; ENSRNOG00000014290. [P23385-2]
GeneIDi24414.
KEGGirno:24414.
UCSCiRGD:2742. rat. [P23385-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246579. 8 interactors.
DIPiDIP-44897N.
IntActiP23385. 5 interactors.
MINTiMINT-1890098.
STRINGi10116.ENSRNOP00000019319.

Chemistry databases

BindingDBiP23385.
ChEMBLiCHEMBL4477.
GuidetoPHARMACOLOGYi289.

Protein family/group databases

GPCRDBiSearch...

PTM databases

iPTMnetiP23385.
PhosphoSitePlusiP23385.

Proteomic databases

PaxDbiP23385.
PRIDEiP23385.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000044325; ENSRNOP00000047790; ENSRNOG00000014290. [P23385-2]
GeneIDi24414.
KEGGirno:24414.
UCSCiRGD:2742. rat. [P23385-1]

Organism-specific databases

CTDi2911.
RGDi2742. Grm1.

Phylogenomic databases

eggNOGiKOG1056. Eukaryota.
ENOG410XR6W. LUCA.
GeneTreeiENSGT00760000118884.
HOGENOMiHOG000218636.
HOVERGENiHBG107965.
InParanoidiP23385.
KOiK04603.
PhylomeDBiP23385.

Enzyme and pathway databases

ReactomeiR-RNO-416476. G alpha (q) signalling events.
R-RNO-420499. Class C/3 (Metabotropic glutamate/pheromone receptors).
R-RNO-6794361. Interactions of neurexins and neuroligins at synapses.

Miscellaneous databases

EvolutionaryTraceiP23385.
PMAP-CutDBP23385.
PROiP23385.

Gene expression databases

ExpressionAtlasiP23385. baseline and differential.

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.
SMARTiSM01229. GluR_Homer-bdg. 1 hit.
[Graphical view]
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]
ProtoNetiSearch...

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: November 2, 2016
This is version 163 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.