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Metabotropic glutamate receptor 5 (mGluR5)

 GRM5_RAT                Reviewed;        1203 AA.
P31424;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 2.
20-JUN-2018, entry version 172.
RecName: Full=Metabotropic glutamate receptor 5;
Short=mGluR5;
Flags: Precursor;
Name=Grm5; Synonyms=Gprc1e, Mglur5;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=1320017;
Abe T., Sugihara H., Nawa H., Shigemoto R., Mizuno N., Nakanishi S.;
"Molecular characterization of a novel metabotropic glutamate receptor
mGluR5 coupled to inositol phosphate/Ca2+ signal transduction.";
J. Biol. Chem. 267:13361-13368(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 859-923, AND ALTERNATIVE SPLICING.
TISSUE=Brain;
PubMed=7688218; DOI=10.1006/bbrc.1993.1866;
Minakami R., Katsuki F., Sugiyama H.;
"A variant of metabotropic glutamate receptor subtype 5: an
evolutionally conserved insertion with no termination codon.";
Biochem. Biophys. Res. Commun. 194:622-627(1993).
[3]
INTERACTION WITH HOMER1; HOMER2 AND HOMER3, AND MUTAGENESIS OF
LEU-1154; PRO-1156; PRO-1157; SER-1158; PRO-1159 AND ARG-1161.
PubMed=9808459; DOI=10.1016/S0896-6273(00)80589-9;
Tu J.C., Xiao B., Yuan J.P., Lanahan A.A., Leoffert K., Li M.,
Linden D.J., Worley P.F.;
"Homer binds a novel proline-rich motif and links group 1 metabotropic
glutamate receptors with IP3 receptors.";
Neuron 21:717-726(1998).
[4]
INTERACTION WITH SIAH1.
PubMed=10469171; DOI=10.1046/j.1365-2443.1999.00269.x;
Ishikawa K., Nash S.R., Nishimune A., Neki A., Kaneko S.,
Nakanishi S.;
"Competitive interaction of seven in absentia homolog-1A and
Ca2+/calmodulin with the cytoplasmic tail of group 1 metabotropic
glutamate receptors.";
Genes Cells 4:381-390(1999).
[5]
INTERACTION WITH GRASP.
PubMed=11850456;
Kitano J., Kimura K., Yamazaki Y., Soda T., Shigemoto R., Nakajima Y.,
Nakanishi S.;
"Tamalin, a PDZ domain-containing protein, links a protein complex
formation of group 1 metabotropic glutamate receptors and the guanine
nucleotide exchange factor cytohesins.";
J. Neurosci. 22:1280-1289(2002).
[6]
INTERACTION WITH NECAB2.
PubMed=19694902; DOI=10.1111/j.1471-4159.2009.06348.x;
Canela L., Fernandez-Duenas V., Albergaria C., Watanabe M., Lluis C.,
Mallol J., Canela E.I., Franco R., Lujan R., Ciruela F.;
"The association of metabotropic glutamate receptor type 5 with the
neuronal Ca2+-binding protein 2 modulates receptor function.";
J. Neurochem. 111:555-567(2009).
[7]
INTERACTION WITH NCDN.
PubMed=20007903; DOI=10.1126/science.1178496;
Wang H., Westin L., Nong Y., Birnbaum S., Bendor J., Brismar H.,
Nestler E., Aperia A., Flajolet M., Greengard P.;
"Norbin is an endogenous regulator of metabotropic glutamate receptor
5 signaling.";
Science 326:1554-1557(2009).
[8]
FUNCTION IN SYNAPTIC ACTIVITY, AND TISSUE SPECIFICITY.
PubMed=21795692; DOI=10.1074/jbc.M111.258384;
Verpelli C., Dvoretskova E., Vicidomini C., Rossi F., Chiappalone M.,
Schoen M., Di Stefano B., Mantegazza R., Broccoli V., Boeckers T.M.,
Dityatev A., Sala C.;
"Importance of Shank3 protein in regulating metabotropic glutamate
receptor 5 (mGluR5) expression and signaling at synapses.";
J. Biol. Chem. 286:34839-34850(2011).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-860; SER-1014 AND
SER-1016, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[10]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1155-1160 IN COMPLEX WITH
HOMER1.
PubMed=10798399; DOI=10.1016/S0896-6273(00)81145-9;
Beneken J., Tu J.C., Xiao B., Nuriya M., Yuan J.P., Worley P.F.,
Leahy D.J.;
"Structure of the Homer EVH1 domain-peptide complex reveals a new
twist in polyproline recognition.";
Neuron 26:143-154(2000).
-!- FUNCTION: 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 and generates
a calcium-activated chloride current. Plays an important role in
the regulation of synaptic plasticity and the modulation of the
neural network activity. {ECO:0000269|PubMed:1320017,
ECO:0000269|PubMed:21795692}.
-!- SUBUNIT: Interacts with RYR1, RYR2, ITPR1, SHANK1 and SHANK3. The
PPXXF motif binds HOMER1, HOMER2 and HOMER3. Interacts with SIAH1
and GRASP. Interacts with NCDN. Interacts with NECAB2.
{ECO:0000269|PubMed:10469171, ECO:0000269|PubMed:10798399,
ECO:0000269|PubMed:11850456, ECO:0000269|PubMed:19694902,
ECO:0000269|PubMed:20007903, ECO:0000269|PubMed:9808459}.
-!- INTERACTION:
P29274:ADORA2A (xeno); NbExp=3; IntAct=EBI-2902778, EBI-2902702;
P06241:FYN (xeno); NbExp=2; IntAct=EBI-8830305, EBI-515315;
Q8R4T5:Grasp; NbExp=5; IntAct=EBI-2902734, EBI-7361884;
Q13526:PIN1 (xeno); NbExp=3; IntAct=EBI-8830305, EBI-714158;
P63088:Ppp1cc; NbExp=19; IntAct=EBI-2902734, EBI-80049;
P04156:PRNP (xeno); NbExp=4; IntAct=EBI-8830305, EBI-8830282;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1320017};
Multi-pass membrane protein {ECO:0000269|PubMed:1320017}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=2; Synonyms=5b;
IsoId=P31424-1; Sequence=Displayed;
Name=1; Synonyms=5a;
IsoId=P31424-2; Sequence=VSP_002031;
-!- TISSUE SPECIFICITY: Widely distributed in neuronal cells of the
central nervous system. {ECO:0000269|PubMed:1320017,
ECO:0000269|PubMed:21795692}.
-!- MISCELLANEOUS: Activated by quisqualate > glutamate > ibotenate >
trans-1- aminocyclopentyl-1,3-dicarboxylate.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
{ECO:0000305}.
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EMBL; D10891; BAA01711.1; -; mRNA.
EMBL; S64315; AAB27666.1; -; mRNA.
PIR; A42916; A42916.
PIR; PN0549; PN0549.
RefSeq; NP_058708.1; NM_017012.1. [P31424-2]
RefSeq; XP_006229721.1; XM_006229659.3. [P31424-1]
RefSeq; XP_017444267.1; XM_017588778.1. [P31424-1]
RefSeq; XP_017444268.1; XM_017588779.1. [P31424-1]
RefSeq; XP_017444269.1; XM_017588780.1. [P31424-1]
RefSeq; XP_017444270.1; XM_017588781.1. [P31424-2]
UniGene; Rn.29972; -.
PDB; 1DDV; X-ray; 1.90 A; B=1155-1160.
PDBsum; 1DDV; -.
ProteinModelPortal; P31424; -.
SMR; P31424; -.
BioGrid; 246583; 8.
CORUM; P31424; -.
DIP; DIP-41263N; -.
ELM; P31424; -.
IntAct; P31424; 13.
MINT; P31424; -.
STRING; 10116.ENSRNOP00000022059; -.
BindingDB; P31424; -.
ChEMBL; CHEMBL2564; -.
GuidetoPHARMACOLOGY; 293; -.
iPTMnet; P31424; -.
PhosphoSitePlus; P31424; -.
PaxDb; P31424; -.
PRIDE; P31424; -.
GeneID; 24418; -.
KEGG; rno:24418; -.
UCSC; RGD:2746; rat. [P31424-1]
CTD; 2915; -.
RGD; 2746; Grm5.
eggNOG; KOG1056; Eukaryota.
eggNOG; ENOG410XR6W; LUCA.
HOGENOM; HOG000218636; -.
HOVERGEN; HBG107965; -.
InParanoid; P31424; -.
KO; K04604; -.
OrthoDB; EOG091G177R; -.
PhylomeDB; P31424; -.
TreeFam; TF313240; -.
EvolutionaryTrace; P31424; -.
PRO; PR:P31424; -.
Proteomes; UP000002494; Unplaced.
Genevisible; P31424; RN.
GO; GO:0097449; C:astrocyte projection; IDA:RGD.
GO; GO:0043198; C:dendritic shaft; IDA:RGD.
GO; GO:0043197; C:dendritic spine; IDA:RGD.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0014069; C:postsynaptic density; IDA:RGD.
GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO.
GO; GO:0045211; C:postsynaptic membrane; TAS:UniProtKB.
GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central.
GO; GO:0031687; F:A2A adenosine receptor binding; IPI:RGD.
GO; GO:0005516; F:calmodulin binding; TAS:UniProtKB.
GO; GO:0004930; F:G-protein coupled receptor activity; ISS:UniProtKB.
GO; GO:0008066; F:glutamate receptor activity; IMP:UniProtKB.
GO; GO:0030165; F:PDZ domain binding; TAS:UniProtKB.
GO; GO:0001639; F:PLC activating G-protein coupled glutamate receptor activity; TAS:UniProtKB.
GO; GO:1990782; F:protein tyrosine kinase binding; IPI:ARUK-UCL.
GO; GO:0000185; P:activation of MAPKKK activity; IDA:UniProtKB.
GO; GO:0007196; P:adenylate cyclase-inhibiting G-protein coupled glutamate receptor signaling pathway; IBA:GO_Central.
GO; GO:0007268; P:chemical synaptic transmission; IMP:RGD.
GO; GO:0002029; P:desensitization of G-protein coupled receptor protein signaling pathway; IDA:UniProtKB.
GO; GO:0007216; P:G-protein coupled glutamate receptor signaling pathway; IMP:UniProtKB.
GO; GO:0040013; P:negative regulation of locomotion; IDA:RGD.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:UniProtKB.
GO; GO:0007206; P:phospholipase C-activating G-protein coupled glutamate receptor signaling pathway; TAS:UniProtKB.
GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway; TAS:UniProtKB.
GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; IDA:RGD.
GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IGI:ARUK-UCL.
GO; GO:0007205; P:protein kinase C-activating G-protein coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:RGD.
GO; GO:0099553; P:trans-synaptic signaling by endocannabinoid, modulating synaptic transmission; IMP:SynGO.
Gene3D; 2.10.50.30; -; 1.
InterPro; IPR001828; ANF_lig-bd_rcpt.
InterPro; IPR000337; GPCR_3.
InterPro; IPR011500; GPCR_3_9-Cys_dom.
InterPro; IPR038550; GPCR_3_9-Cys_sf.
InterPro; IPR017978; GPCR_3_C.
InterPro; IPR017979; GPCR_3_CS.
InterPro; IPR000162; GPCR_3_mtglu_rcpt.
InterPro; IPR000202; GPCR_3_mtglu_rcpt_5.
InterPro; IPR019588; Metabotropic_Glu_rcpt_Homer-bd.
InterPro; IPR028082; Peripla_BP_I.
Pfam; PF00003; 7tm_3; 1.
Pfam; PF01094; ANF_receptor; 1.
Pfam; PF10606; GluR_Homer-bdg; 1.
Pfam; PF07562; NCD3G; 1.
PRINTS; PR00248; GPCRMGR.
PRINTS; PR01055; MTABOTROPC5R.
PRINTS; PR00593; MTABOTROPICR.
SMART; SM01229; GluR_Homer-bdg; 1.
SUPFAM; SSF53822; SSF53822; 1.
PROSITE; PS00979; G_PROTEIN_RECEP_F3_1; 1.
PROSITE; PS00980; G_PROTEIN_RECEP_F3_2; 1.
PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; 1.
PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
Methylation; Phosphoprotein; Receptor; Reference proteome; Signal;
Transducer; Transmembrane; Transmembrane helix.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 1203 Metabotropic glutamate receptor 5.
/FTId=PRO_0000012933.
TOPO_DOM 21 579 Extracellular. {ECO:0000250}.
TRANSMEM 580 602 Helical; Name=1. {ECO:0000250}.
TOPO_DOM 603 612 Cytoplasmic. {ECO:0000250}.
TRANSMEM 613 635 Helical; Name=2. {ECO:0000250}.
TOPO_DOM 636 643 Extracellular. {ECO:0000250}.
TRANSMEM 644 666 Helical; Name=3. {ECO:0000250}.
TOPO_DOM 667 692 Cytoplasmic. {ECO:0000250}.
TRANSMEM 693 713 Helical; Name=4. {ECO:0000250}.
TOPO_DOM 714 736 Extracellular. {ECO:0000250}.
TRANSMEM 737 758 Helical; Name=5. {ECO:0000250}.
TOPO_DOM 759 771 Cytoplasmic. {ECO:0000250}.
TRANSMEM 772 794 Helical; Name=6. {ECO:0000250}.
TOPO_DOM 795 797 Extracellular. {ECO:0000250}.
TRANSMEM 798 819 Helical; Name=7. {ECO:0000250}.
TOPO_DOM 820 1203 Cytoplasmic. {ECO:0000250}.
REGION 172 174 Glutamate binding. {ECO:0000250}.
REGION 804 808 Allosteric effector binding.
{ECO:0000250}.
BINDING 64 64 Glutamate. {ECO:0000250}.
BINDING 151 151 Glutamate. {ECO:0000250}.
BINDING 222 222 Glutamate. {ECO:0000250}.
BINDING 304 304 Glutamate. {ECO:0000250}.
BINDING 395 395 Glutamate. {ECO:0000250}.
MOD_RES 860 860 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 868 868 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q3UVX5}.
MOD_RES 924 924 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q3UVX5}.
MOD_RES 1014 1014 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1016 1016 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 88 88 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 209 209 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 377 377 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 381 381 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 444 444 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 733 733 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 57 99 {ECO:0000250}.
DISULFID 240 529 {ECO:0000250}.
DISULFID 275 277 {ECO:0000250}.
DISULFID 364 380 {ECO:0000250}.
DISULFID 418 425 {ECO:0000250}.
DISULFID 510 530 {ECO:0000250}.
DISULFID 514 533 {ECO:0000250}.
DISULFID 536 548 {ECO:0000250}.
DISULFID 551 564 {ECO:0000250}.
DISULFID 643 732 {ECO:0000250}.
VAR_SEQ 876 907 Missing (in isoform 1).
{ECO:0000303|PubMed:1320017}.
/FTId=VSP_002031.
MUTAGEN 1154 1154 L->V: Normal binding to HOMER1.
{ECO:0000269|PubMed:9808459}.
MUTAGEN 1156 1156 P->K: Disrupts binding to HOMER1.
{ECO:0000269|PubMed:9808459}.
MUTAGEN 1157 1157 P->E: Disrupts binding to HOMER1.
{ECO:0000269|PubMed:9808459}.
MUTAGEN 1157 1157 P->L: Disrupts binding to HOMER1.
{ECO:0000269|PubMed:9808459}.
MUTAGEN 1158 1158 S->F: Normal binding to HOMER1.
{ECO:0000269|PubMed:9808459}.
MUTAGEN 1159 1159 P->A: Normal binding to HOMER1.
{ECO:0000269|PubMed:9808459}.
MUTAGEN 1160 1160 F->R: Disrupts binding to HOMER1.
MUTAGEN 1161 1161 R->T: Normal binding to HOMER1.
{ECO:0000269|PubMed:9808459}.
SEQUENCE 1203 AA; 131885 MW; 99CA51E9E11C1EA4 CRC64;
MVLLLILSVL LLKEDVRGSA QSSERRVVAH MPGDIIIGAL FSVHHQPTVD KVHERKCGAV
REQYGIQRVE AMLHTLERIN SDPTLLPNIT LGCEIRDSCW HSAVALEQSI EFIRDSLISS
EEEEGLVRCV DGSSSFRSKK PIVGVIGPGS SSVAIQVQNL LQLFNIPQIA YSATSMDLSD
KTLFKYFMRV VPSDAQQARA MVDIVKRYNW TYVSAVHTEG NYGESGMEAF KDMSAKEGIC
IAHSYKIYSN AGEQSFDKLL KKLRSHLPKA RVVACFCEGM TVRGLLMAMR RLGLAGEFLL
LGSDGWADRY DVTDGYQREA VGGITIKLQS PDVKWFDDYY LKLRPETNLR NPWFQEFWQH
RFQCRLEGFA QENSKYNKTC NSSLTLRTHH VQDSKMGFVI NAIYSMAYGL HNMQMSLCPG
YAGLCDAMKP IDGRKLLDSL MKTNFTGVSG DMILFDENGD SPGRYEIMNF KEMGKDYFDY
INVGSWDNGE LKMDDDEVWS KKNNIIRSVC SEPCEKGQIK VIRKGEVSCC WTCTPCKENE
YVFDEYTCKA CQLGSWPTDD LTGCDLIPVQ YLRWGDPEPI AAVVFACLGL LATLFVTVIF
IIYRDTPVVK SSSRELCYII LAGICLGYLC TFCLIAKPKQ IYCYLQRIGI GLSPAMSYSA
LVTKTNRIAR ILAGSKKKIC TKKPRFMSAC AQLVIAFILI CIQLGIIVAL FIMEPPDIMH
DYPSIREVYL ICNTTNLGVV TPLGYNGLLI LSCTFYAFKT RNVPANFNEA KYIAFTMYTT
CIIWLAFVPI YFGSNYKIIT MCFSVSLSAT VALGCMFVPK VYIILAKPER NVRSAFTTST
VVRMHVGDGK SSSAASRSSS LVNLWKRRGS SGETLRYKDR RLAQHKSEIE CFTPKGSMGN
GGRATMSSSN GKSVTWAQNE KSTRGQHLWQ RLSVHINKKE NPNQTAVIKP FPKSTENRGP
GAAAGGGSGP GVAGAGNAGC TATGGPEPPD AGPKALYDVA EAEESFPAAA RPRSPSPIST
LSHLAGSAGR TDDDAPSLHS ETAARSSSSQ GSLMEQISSV VTRFTANISE LNSMMLSTAA
TPGPPGTPIC SSYLIPKEIQ LPTTMTTFAE IQPLPAIEVT GGAQGATGVS PAQETPTGAE
SAPGKPDLEE LVALTPPSPF RDSVDSGSTT PNSPVSESAL CIPSSPKYDT LIIRDYTQSS
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Genprice Inc, Invoices and accounting
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