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Protein

Metabotropic glutamate receptor 7

Gene

Grm7

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, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei159GlutamateBy similarity1
Binding sitei230GlutamateBy similarity1
Binding sitei314GlutamateBy similarity1
Binding sitei407GlutamateBy similarity1

GO - Molecular functioni

  • adenylate cyclase inhibiting G-protein coupled glutamate receptor activity Source: RGD
  • adenylate cyclase inhibitor activity Source: RGD
  • calcium channel regulator activity Source: RGD
  • calcium-dependent protein binding Source: RGD
  • calcium ion binding Source: RGD
  • calmodulin binding Source: UniProtKB
  • glutamate binding Source: RGD
  • glutamate receptor activity Source: RGD
  • group III metabotropic glutamate receptor activity Source: RGD
  • PDZ domain binding Source: RGD
  • protein homodimerization activity Source: RGD
  • serine binding Source: RGD
  • voltage-gated calcium channel activity Source: RGD

GO - Biological processi

Keywordsi

Molecular functionG-protein coupled receptor, Receptor, Transducer
Biological processSensory transduction

Names & Taxonomyi

Protein namesi
Recommended name:
Metabotropic glutamate receptor 7
Short name:
mGluR7
Gene namesi
Name:Grm7
Synonyms:Gprc1g, Mglur7
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi619857. Grm7.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini35 – 590ExtracellularSequence analysisAdd BLAST556
Transmembranei591 – 615Helical; Name=1Sequence analysisAdd BLAST25
Topological domaini616 – 627CytoplasmicSequence analysisAdd BLAST12
Transmembranei628 – 648Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini649 – 654ExtracellularSequence analysis6
Transmembranei655 – 675Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini676 – 702CytoplasmicSequence analysisAdd BLAST27
Transmembranei703 – 723Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini724 – 753ExtracellularSequence analysisAdd BLAST30
Transmembranei754 – 775Helical; Name=5Sequence analysisAdd BLAST22
Topological domaini776 – 788CytoplasmicSequence analysisAdd BLAST13
Transmembranei789 – 810Helical; Name=6Sequence analysisAdd BLAST22
Topological domaini811 – 825ExtracellularSequence analysisAdd BLAST15
Transmembranei826 – 850Helical; Name=7Sequence analysisAdd BLAST25
Topological domaini851 – 915CytoplasmicSequence analysisAdd BLAST65

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3879.
GuidetoPHARMACOLOGYi295.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 34Sequence analysisAdd BLAST34
ChainiPRO_000001294035 – 915Metabotropic glutamate receptor 7Add BLAST881

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi67 ↔ 1091 Publication
Glycosylationi98N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi249 ↔ 541By similarity
Disulfide bondi374 ↔ 3901 Publication
Disulfide bondi430 ↔ 4371 Publication
Glycosylationi458N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi486N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi523 ↔ 542By similarity
Disulfide bondi527 ↔ 545By similarity
Disulfide bondi548 ↔ 560By similarity
Disulfide bondi563 ↔ 576By similarity
Glycosylationi572N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei900PhosphoserineBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP35400.
PRIDEiP35400.

PTM databases

iPTMnetiP35400.
PhosphoSitePlusiP35400.

Expressioni

Tissue specificityi

Widely distributed throughout the brain.2 Publications

Interactioni

Subunit structurei

Interacts with PICK1.1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • calcium-dependent protein binding Source: RGD
  • calmodulin binding Source: UniProtKB
  • PDZ domain binding Source: RGD
  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

BioGridi249569. 9 interactors.
DIPiDIP-41145N.
IntActiP35400. 7 interactors.
MINTiMINT-146474.
STRINGi10116.ENSRNOP00000053411.

Chemistry databases

BindingDBiP35400.

Structurei

Secondary structure

1915
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi42 – 45Combined sources4
Beta strandi48 – 55Combined sources8
Beta strandi58 – 60Combined sources3
Beta strandi62 – 64Combined sources3
Beta strandi66 – 70Combined sources5
Helixi72 – 91Combined sources20
Beta strandi93 – 98Combined sources6
Beta strandi101 – 107Combined sources7
Helixi112 – 118Combined sources7
Helixi119 – 126Combined sources8
Beta strandi150 – 154Combined sources5
Helixi159 – 165Combined sources7
Helixi168 – 171Combined sources4
Beta strandi176 – 180Combined sources5
Helixi184 – 187Combined sources4
Turni189 – 192Combined sources4
Beta strandi193 – 199Combined sources7
Helixi202 – 215Combined sources14
Beta strandi221 – 228Combined sources8
Helixi229 – 244Combined sources16
Beta strandi250 – 256Combined sources7
Helixi265 – 274Combined sources10
Beta strandi282 – 286Combined sources5
Helixi289 – 301Combined sources13
Turni305 – 307Combined sources3
Beta strandi308 – 312Combined sources5
Turni314 – 318Combined sources5
Helixi321 – 323Combined sources3
Helixi327 – 330Combined sources4
Beta strandi334 – 339Combined sources6
Helixi344 – 350Combined sources7
Turni355 – 357Combined sources3
Helixi364 – 371Combined sources8
Helixi394 – 397Combined sources4
Helixi408 – 429Combined sources22
Turni438 – 443Combined sources6
Helixi445 – 452Combined sources8
Beta strandi477 – 483Combined sources7
Beta strandi491 – 504Combined sources14
Beta strandi506 – 508Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2E4ZX-ray3.30A33-521[»]
ProteinModelPortaliP35400.
SMRiP35400.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35400.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni180 – 182Glutamate bindingBy similarity3

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1056. Eukaryota.
ENOG410XR6W. LUCA.
HOVERGENiHBG107965.
InParanoidiP35400.
KOiK04608.
PhylomeDBiP35400.

Family and domain databases

InterProiView protein in InterPro
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.
IPR001883. GPCR_3_mtglu_rcpt_7.
IPR028082. Peripla_BP_I.
PfamiView protein in Pfam
PF00003. 7tm_3. 1 hit.
PF01094. ANF_receptor. 1 hit.
PF07562. NCD3G. 1 hit.
PRINTSiPR00248. GPCRMGR.
PR01057. MTABOTROPC7R.
PR00593. MTABOTROPICR.
SUPFAMiSSF53822. SSF53822. 1 hit.
PROSITEiView protein in PROSITE
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.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P35400-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVQLGKLLRV LTLMKFPCCV LEVLLCVLAA AARGQEMYAP HSIRIEGDVT
60 70 80 90 100
LGGLFPVHAK GPSGVPCGDI KRENGIHRLE AMLYALDQIN SDPNLLPNVT
110 120 130 140 150
LGARILDTCS RDTYALEQSL TFVQALIQKD TSDVRCTNGE PPVFVKPEKV
160 170 180 190 200
VGVIGASGSS VSIMVANILR LFQIPQISYA STAPELSDDR RYDFFSRVVP
210 220 230 240 250
PDSFQAQAMV DIVKALGWNY VSTLASEGSY GEKGVESFTQ ISKEAGGLCI
260 270 280 290 300
AQSVRIPQER KDRTIDFDRI IKQLLDTPNS RAVVIFANDE DIKQILAAAK
310 320 330 340 350
RADQVGHFLW VGSDSWGSKI NPLHQHEDIA EGAITIQPKR ATVEGFDAYF
360 370 380 390 400
TSRTLENNRR NVWFAEYWEE NFNCKLTISG SKKEDTDRKC TGQERIGKDS
410 420 430 440 450
NYEQEGKVQF VIDAVYAMAH ALHHMNKDLC ADYRGVCPEM EQAGGKKLLK
460 470 480 490 500
YIRHVNFNGS AGTPVMFNKN GDAPGRYDIF QYQTTNTTNP GYRLIGQWTD
510 520 530 540 550
ELQLNIEDMQ WGKGVREIPS SVCTLPCKPG QRKKTQKGTP CCWTCEPCDG
560 570 580 590 600
YQYQFDEMTC QHCPYDQRPN ENRTGCQNIP IIKLEWHSPW AVIPVFLAML
610 620 630 640 650
GIIATIFVMA TFIRYNDTPI VRASGRELSY VLLTGIFLCY IITFLMIAKP
660 670 680 690 700
DVAVCSFRRV FLGLGMCISY AALLTKTNRI YRIFEQGKKS VTAPRLISPT
710 720 730 740 750
SQLAITSSLI SVQLLGVFIW FGVDPPNIII DYDEHKTMNP EQARGVLKCD
760 770 780 790 800
ITDLQIICSL GYSILLMVTC TVYAIKTRGV PENFNEAKPI GFTMYTTCIV
810 820 830 840 850
WLAFIPIFFG TAQSAEKLYI QTTTLTISMN LSASVALGML YMPKVYIIIF
860 870 880 890 900
HPELNVQKRK RSFKAVVTAA TMSSRLSHKP SDRPNGEAKT ELCENVDPNS
910
PAAKKKYVSY NNLVI
Length:915
Mass (Da):102,232
Last modified:June 1, 1994 - v1
Checksum:iF28AFC4C6454A6C2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16817 mRNA. Translation: BAA04092.1.
U06832 mRNA. Translation: AAA20655.1.
PIRiA49874.
RefSeqiNP_112302.1. NM_031040.1.
UniGeneiRn.10409.

Genome annotation databases

GeneIDi81672.
KEGGirno:81672.

Similar proteinsi

Entry informationi

Entry nameiGRM7_RAT
AccessioniPrimary (citable) accession number: P35400
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 22, 2017
This is version 128 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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