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P23385

- GRM1_RAT

UniProt

P23385 - GRM1_RAT

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Protein

Metabotropic glutamate receptor 1

Gene

Grm1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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)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

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
Complete GO annotation...

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
Complete GO annotation...

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

        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)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 29, 2014
This is version 146 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