GRM3_RAT
ID GRM3_RAT Reviewed; 879 AA.
AC P31422;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Metabotropic glutamate receptor 3;
DE Short=mGluR3;
DE Flags: Precursor;
GN Name=Grm3; Synonyms=Gprc1c, Mglur3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1309649; DOI=10.1016/0896-6273(92)90118-w;
RA Tanabe Y., Masu M., Ishii T., Shigemoto R., Nakanishi S.;
RT "A family of metabotropic glutamate receptors.";
RL Neuron 8:169-179(1992).
RN [2]
RP INTERACTION WITH TAMALIN.
RX PubMed=11850456; DOI=10.1523/jneurosci.22-04-01280.2002;
RA Kitano J., Kimura K., Yamazaki Y., Soda T., Shigemoto R., Nakajima Y.,
RA Nakanishi S.;
RT "Tamalin, a PDZ domain-containing protein, links a protein complex
RT formation of group 1 metabotropic glutamate receptors and the guanine
RT nucleotide exchange factor cytohesins.";
RL J. Neurosci. 22:1280-1289(2002).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-439, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 25-575 IN COMPLEXES WITH
RP GLUTAMATE, GLYCOSYLATION AT ASN-209, AND DISULFIDE BONDS.
RX PubMed=17360426; DOI=10.1073/pnas.0611577104;
RA Muto T., Tsuchiya D., Morikawa K., Jingami H.;
RT "Structures of the extracellular regions of the group II/III metabotropic
RT glutamate receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:3759-3764(2007).
CC -!- FUNCTION: G-protein coupled receptor for glutamate. Ligand binding
CC causes a conformation change that triggers signaling via guanine
CC nucleotide-binding proteins (G proteins) and modulates the activity of
CC down-stream effectors. Signaling inhibits adenylate cyclase activity.
CC -!- SUBUNIT: Interacts with TAMALIN. {ECO:0000269|PubMed:11850456}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Is widely distributed in the CNS. Predominant
CC expression is seen in the neuronal cells of the cerebral cortex,
CC dentate gyrus, and glial cells throughout brain regions.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
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DR EMBL; M92076; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; JH0562; JH0562.
DR RefSeq; NP_001099182.1; NM_001105712.1.
DR PDB; 2E4U; X-ray; 2.35 A; A/B=25-575.
DR PDB; 2E4V; X-ray; 2.40 A; A/B=25-575.
DR PDB; 2E4W; X-ray; 2.40 A; A/B=25-575.
DR PDB; 2E4X; X-ray; 2.75 A; A/B=25-575.
DR PDB; 2E4Y; X-ray; 3.40 A; A/B=25-575.
DR PDBsum; 2E4U; -.
DR PDBsum; 2E4V; -.
DR PDBsum; 2E4W; -.
DR PDBsum; 2E4X; -.
DR PDBsum; 2E4Y; -.
DR AlphaFoldDB; P31422; -.
DR SMR; P31422; -.
DR BioGRID; 246581; 2.
DR DIP; DIP-41143N; -.
DR IntAct; P31422; 4.
DR MINT; P31422; -.
DR STRING; 10116.ENSRNOP00000007572; -.
DR BindingDB; P31422; -.
DR ChEMBL; CHEMBL3067; -.
DR DrugCentral; P31422; -.
DR GuidetoPHARMACOLOGY; 291; -.
DR GlyGen; P31422; 4 sites, 9 N-linked glycans (2 sites).
DR iPTMnet; P31422; -.
DR PhosphoSitePlus; P31422; -.
DR PaxDb; P31422; -.
DR PRIDE; P31422; -.
DR Ensembl; ENSRNOT00000007572; ENSRNOP00000007572; ENSRNOG00000005519.
DR GeneID; 24416; -.
DR KEGG; rno:24416; -.
DR CTD; 2913; -.
DR RGD; 2744; Grm3.
DR eggNOG; KOG1056; Eukaryota.
DR GeneTree; ENSGT01030000234595; -.
DR HOGENOM; CLU_005389_0_0_1; -.
DR InParanoid; P31422; -.
DR OrthoDB; 1154468at2759; -.
DR PhylomeDB; P31422; -.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR Reactome; R-RNO-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
DR EvolutionaryTrace; P31422; -.
DR PRO; PR:P31422; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000005519; Expressed in Ammon's horn and 4 other tissues.
DR ExpressionAtlas; P31422; baseline and differential.
DR Genevisible; P31422; RN.
DR GO; GO:0097449; C:astrocyte projection; IDA:ARUK-UCL.
DR GO; GO:0030424; C:axon; IDA:ARUK-UCL.
DR GO; GO:0043197; C:dendritic spine; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:RGD.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR GO; GO:0042734; C:presynaptic membrane; ISO:RGD.
DR GO; GO:0001640; F:adenylate cyclase inhibiting G protein-coupled glutamate receptor activity; IBA:GO_Central.
DR GO; GO:0005246; F:calcium channel regulator activity; ISO:RGD.
DR GO; GO:0001641; F:group II metabotropic glutamate receptor activity; IMP:RGD.
DR GO; GO:0097110; F:scaffold protein binding; IPI:ARUK-UCL.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:RGD.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
DR GO; GO:0019233; P:sensory perception of pain; TAS:UniProtKB.
DR Gene3D; 2.10.50.30; -; 1.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR000337; GPCR_3.
DR InterPro; IPR011500; GPCR_3_9-Cys_dom.
DR InterPro; IPR038550; GPCR_3_9-Cys_sf.
DR InterPro; IPR017978; GPCR_3_C.
DR InterPro; IPR017979; GPCR_3_CS.
DR InterPro; IPR001234; GPCR_3_mGluR3.
DR InterPro; IPR000162; GPCR_3_mtglu_rcpt.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF00003; 7tm_3; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF07562; NCD3G; 1.
DR PRINTS; PR00248; GPCRMGR.
DR PRINTS; PR01053; MTABOTROPC3R.
DR PRINTS; PR00593; MTABOTROPICR.
DR SUPFAM; SSF53822; SSF53822; 1.
DR PROSITE; PS00979; G_PROTEIN_RECEP_F3_1; 1.
DR PROSITE; PS00980; G_PROTEIN_RECEP_F3_2; 1.
DR PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; 1.
DR PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Signal; Transducer;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..879
FT /note="Metabotropic glutamate receptor 3"
FT /id="PRO_0000012929"
FT TOPO_DOM 23..576
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 577..599
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 600..613
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 614..634
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 635..645
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 646..664
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 665..688
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 689..709
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 710..734
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 735..756
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 757..769
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 770..792
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 793..802
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 803..828
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 829..879
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 68
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 151
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 172..174
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 222
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 301
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 389
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17360426"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT DISULFID 57..99
FT /evidence="ECO:0000269|PubMed:17360426"
FT DISULFID 240..527
FT /evidence="ECO:0000269|PubMed:17360426"
FT DISULFID 361..373
FT /evidence="ECO:0000269|PubMed:17360426"
FT DISULFID 412..419
FT /evidence="ECO:0000269|PubMed:17360426"
FT DISULFID 509..528
FT /evidence="ECO:0000269|PubMed:17360426"
FT DISULFID 513..531
FT /evidence="ECO:0000269|PubMed:17360426"
FT DISULFID 534..546
FT /evidence="ECO:0000269|PubMed:17360426"
FT DISULFID 549..562
FT /evidence="ECO:0000269|PubMed:17360426"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:2E4U"
FT STRAND 38..45
FT /evidence="ECO:0007829|PDB:2E4U"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:2E4U"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:2E4U"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:2E4U"
FT HELIX 66..81
FT /evidence="ECO:0007829|PDB:2E4U"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:2E4X"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:2E4U"
FT HELIX 102..114
FT /evidence="ECO:0007829|PDB:2E4U"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:2E4U"
FT HELIX 151..161
FT /evidence="ECO:0007829|PDB:2E4U"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:2E4U"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:2E4U"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:2E4U"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:2E4U"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:2E4U"
FT HELIX 194..207
FT /evidence="ECO:0007829|PDB:2E4U"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:2E4U"
FT HELIX 223..235
FT /evidence="ECO:0007829|PDB:2E4U"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:2E4U"
FT STRAND 240..247
FT /evidence="ECO:0007829|PDB:2E4U"
FT HELIX 253..264
FT /evidence="ECO:0007829|PDB:2E4U"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:2E4U"
FT HELIX 278..290
FT /evidence="ECO:0007829|PDB:2E4U"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:2E4U"
FT TURN 301..305
FT /evidence="ECO:0007829|PDB:2E4U"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:2E4U"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:2E4U"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:2E4U"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:2E4U"
FT HELIX 331..338
FT /evidence="ECO:0007829|PDB:2E4U"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:2E4U"
FT HELIX 351..358
FT /evidence="ECO:0007829|PDB:2E4U"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:2E4V"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:2E4U"
FT HELIX 390..411
FT /evidence="ECO:0007829|PDB:2E4U"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:2E4U"
FT HELIX 427..434
FT /evidence="ECO:0007829|PDB:2E4U"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:2E4U"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:2E4U"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:2E4U"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:2E4U"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:2E4X"
FT STRAND 466..472
FT /evidence="ECO:0007829|PDB:2E4U"
FT STRAND 474..477
FT /evidence="ECO:0007829|PDB:2E4X"
FT STRAND 479..491
FT /evidence="ECO:0007829|PDB:2E4U"
FT HELIX 494..496
FT /evidence="ECO:0007829|PDB:2E4U"
FT HELIX 500..502
FT /evidence="ECO:0007829|PDB:2E4V"
FT TURN 515..517
FT /evidence="ECO:0007829|PDB:2E4U"
FT STRAND 518..521
FT /evidence="ECO:0007829|PDB:2E4U"
FT STRAND 524..527
FT /evidence="ECO:0007829|PDB:2E4U"
FT STRAND 530..533
FT /evidence="ECO:0007829|PDB:2E4U"
FT STRAND 538..542
FT /evidence="ECO:0007829|PDB:2E4U"
FT STRAND 545..548
FT /evidence="ECO:0007829|PDB:2E4U"
FT STRAND 553..555
FT /evidence="ECO:0007829|PDB:2E4U"
FT STRAND 559..564
FT /evidence="ECO:0007829|PDB:2E4U"
SQ SEQUENCE 879 AA; 98960 MW; 3E5965EDD5E6DEED CRC64;
MKMLTRLQIL MLALFSKGFL LSLGDHNFMR REIKIEGDLV LGGLFPINEK GTGTEECGRI
NEDRGIQRLE AMLFAIDEIN KDNYLLPGVK LGVHILDTCS RDTYALEQSL EFVRASLTKV
DEAEYMCPDG SYAIQENIPL LIAGVIGGSY SSVSIQVANL LRLFQIPQIS YASTSAKLSD
KSRYDYFART VPPDFYQAKA MAEILRFFNW TYVSTVASEG DYGETGIEAF EQEARLRNIC
IATAEKVGRS NIRKSYDSVI RELLQKPNAR VVVLFMRSDD SRELIAAANR VNASFTWVAS
DGWGAQESIV KGSEHVAYGA ITLELASHPV RQFDRYFQSL NPYNNHRNPW FRDFWEQKFQ
CSLQNKRNHR QVCDKHLAID SSNYEQESKI MFVVNAVYAM AHALHKMQRT LCPNTTKLCD
AMKILDGKKL YKEYLLKINF TAPFNPNKGA DSIVKFDTFG DGMGRYNVFN LQQTGGKYSY
LKVGHWAETL SLDVDSIHWS RNSVPTSQCS DPCAPNEMKN MQPGDVCCWI CIPCEPYEYL
VDEFTCMDCG PGQWPTADLS GCYNLPEDYI KWEDAWAIGP VTIACLGFLC TCIVITVFIK
HNNTPLVKAS GRELCYILLF GVSLSYCMTF FFIAKPSPVI CALRRLGLGT SFAICYSALL
TKTNCIARIF DGVKNGAQRP KFISPSSQVF ICLGLILVQI VMVSVWLILE TPGTRRYTLP
EKRETVILKC NVKDSSMLIS LTYDVVLVIL CTVYAFKTRK CPENFNEAKF IGFTMYTTCI
IWLAFLPIFY VTSSDYRVQT TTMCISVSLS GFVVLGCLFA PKVHIVLFQP QKNVVTHRLH
LNRFSVSGTA TTYSQSSAST YVPTVCNGRE VLDSTTSSL
