ID GRM5_RAT Reviewed; 1203 AA. AC P31424; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 24-JAN-2024, entry version 200. DE RecName: Full=Metabotropic glutamate receptor 5; DE Short=mGluR5; DE Flags: Precursor; GN Name=Grm5; Synonyms=Gprc1e, Mglur5; 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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=1320017; DOI=10.1016/s0021-9258(18)42219-3; RA Abe T., Sugihara H., Nawa H., Shigemoto R., Mizuno N., Nakanishi S.; RT "Molecular characterization of a novel metabotropic glutamate receptor RT mGluR5 coupled to inositol phosphate/Ca2+ signal transduction."; RL J. Biol. Chem. 267:13361-13368(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 859-923, AND ALTERNATIVE SPLICING. RC TISSUE=Brain; RX PubMed=7688218; DOI=10.1006/bbrc.1993.1866; RA Minakami R., Katsuki F., Sugiyama H.; RT "A variant of metabotropic glutamate receptor subtype 5: an evolutionally RT conserved insertion with no termination codon."; RL Biochem. Biophys. Res. Commun. 194:622-627(1993). RN [3] RP INTERACTION WITH HOMER1; HOMER2 AND HOMER3, AND MUTAGENESIS OF LEU-1154; RP PRO-1156; PRO-1157; SER-1158; PRO-1159 AND ARG-1161. RX PubMed=9808459; DOI=10.1016/s0896-6273(00)80589-9; RA Tu J.C., Xiao B., Yuan J.P., Lanahan A.A., Leoffert K., Li M., Linden D.J., RA Worley P.F.; RT "Homer binds a novel proline-rich motif and links group 1 metabotropic RT glutamate receptors with IP3 receptors."; RL Neuron 21:717-726(1998). RN [4] RP INTERACTION WITH SIAH1. RX PubMed=10469171; DOI=10.1046/j.1365-2443.1999.00269.x; RA Ishikawa K., Nash S.R., Nishimune A., Neki A., Kaneko S., Nakanishi S.; RT "Competitive interaction of seven in absentia homolog-1A and RT Ca2+/calmodulin with the cytoplasmic tail of group 1 metabotropic glutamate RT receptors."; RL Genes Cells 4:381-390(1999). RN [5] 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 [6] RP INTERACTION WITH NECAB2. RX PubMed=19694902; DOI=10.1111/j.1471-4159.2009.06348.x; RA Canela L., Fernandez-Duenas V., Albergaria C., Watanabe M., Lluis C., RA Mallol J., Canela E.I., Franco R., Lujan R., Ciruela F.; RT "The association of metabotropic glutamate receptor type 5 with the RT neuronal Ca2+-binding protein 2 modulates receptor function."; RL J. Neurochem. 111:555-567(2009). RN [7] RP INTERACTION WITH NCDN. RX PubMed=20007903; DOI=10.1126/science.1178496; RA Wang H., Westin L., Nong Y., Birnbaum S., Bendor J., Brismar H., RA Nestler E., Aperia A., Flajolet M., Greengard P.; RT "Norbin is an endogenous regulator of metabotropic glutamate receptor 5 RT signaling."; RL Science 326:1554-1557(2009). RN [8] RP FUNCTION IN SYNAPTIC ACTIVITY, AND TISSUE SPECIFICITY. RX PubMed=21795692; DOI=10.1074/jbc.m111.258384; RA Verpelli C., Dvoretskova E., Vicidomini C., Rossi F., Chiappalone M., RA Schoen M., Di Stefano B., Mantegazza R., Broccoli V., Boeckers T.M., RA Dityatev A., Sala C.; RT "Importance of Shank3 protein in regulating metabotropic glutamate receptor RT 5 (mGluR5) expression and signaling at synapses."; RL J. Biol. Chem. 286:34839-34850(2011). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-860; SER-1014 AND SER-1016, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). RN [10] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1155-1160 IN COMPLEX WITH HOMER1. RX PubMed=10798399; DOI=10.1016/s0896-6273(00)81145-9; RA Beneken J., Tu J.C., Xiao B., Nuriya M., Yuan J.P., Worley P.F., RA Leahy D.J.; RT "Structure of the Homer EVH1 domain-peptide complex reveals a new twist in RT polyproline recognition."; RL Neuron 26:143-154(2000). 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 activates a phosphatidylinositol- CC calcium second messenger system and generates a calcium-activated CC chloride current. Plays an important role in the regulation of synaptic CC plasticity and the modulation of the neural network activity. CC {ECO:0000269|PubMed:1320017, ECO:0000269|PubMed:21795692}. CC -!- SUBUNIT: Interacts with RYR1, RYR2, ITPR1, SHANK1 and SHANK3. The PPXXF CC motif binds HOMER1, HOMER2 and HOMER3. Interacts with SIAH1 and CC TAMALIN. Interacts with NCDN. Interacts with NECAB2. Interacts with CC CAMK2A (By similarity). {ECO:0000250|UniProtKB:P41594, CC ECO:0000269|PubMed:10469171, ECO:0000269|PubMed:10798399, CC ECO:0000269|PubMed:11850456, ECO:0000269|PubMed:19694902, CC ECO:0000269|PubMed:20007903, ECO:0000269|PubMed:9808459}. CC -!- INTERACTION: CC P31424; P63088: Ppp1cc; NbExp=19; IntAct=EBI-2902734, EBI-80049; CC P31424; Q8R4T5: Tamalin; NbExp=5; IntAct=EBI-2902734, EBI-7361884; CC P31424-1; P29274: ADORA2A; Xeno; NbExp=3; IntAct=EBI-2902778, EBI-2902702; CC P31424-2; P06241: FYN; Xeno; NbExp=2; IntAct=EBI-8830305, EBI-515315; CC P31424-2; Q13526: PIN1; Xeno; NbExp=3; IntAct=EBI-8830305, EBI-714158; CC P31424-2; PRO_0000025675 [P04156]: PRNP; Xeno; NbExp=4; IntAct=EBI-8830305, EBI-8830282; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1320017}; CC Multi-pass membrane protein {ECO:0000269|PubMed:1320017}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=2; Synonyms=5b; CC IsoId=P31424-1; Sequence=Displayed; CC Name=1; Synonyms=5a; CC IsoId=P31424-2; Sequence=VSP_002031; CC -!- TISSUE SPECIFICITY: Widely distributed in neuronal cells of the central CC nervous system. {ECO:0000269|PubMed:1320017, CC ECO:0000269|PubMed:21795692}. CC -!- MISCELLANEOUS: Activated by quisqualate > glutamate > ibotenate > CC trans-1- aminocyclopentyl-1,3-dicarboxylate. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D10891; BAA01711.1; -; mRNA. DR EMBL; S64315; AAB27666.1; -; mRNA. DR PIR; A42916; A42916. DR PIR; PN0549; PN0549. DR RefSeq; NP_058708.1; NM_017012.1. [P31424-2] DR RefSeq; XP_006229721.1; XM_006229659.3. [P31424-1] DR RefSeq; XP_017444267.1; XM_017588778.1. [P31424-1] DR RefSeq; XP_017444268.1; XM_017588779.1. [P31424-1] DR RefSeq; XP_017444269.1; XM_017588780.1. [P31424-1] DR RefSeq; XP_017444270.1; XM_017588781.1. [P31424-2] DR PDB; 1DDV; X-ray; 1.90 A; B=1155-1160. DR PDBsum; 1DDV; -. DR AlphaFoldDB; P31424; -. DR SMR; P31424; -. DR BioGRID; 246583; 11. DR CORUM; P31424; -. DR DIP; DIP-41263N; -. DR ELM; P31424; -. DR IntAct; P31424; 14. DR MINT; P31424; -. DR STRING; 10116.ENSRNOP00000022059; -. DR BindingDB; P31424; -. DR ChEMBL; CHEMBL2564; -. DR DrugCentral; P31424; -. DR GuidetoPHARMACOLOGY; 293; -. DR GlyCosmos; P31424; 6 sites, No reported glycans. DR GlyGen; P31424; 6 sites. DR iPTMnet; P31424; -. DR PhosphoSitePlus; P31424; -. DR PaxDb; 10116-ENSRNOP00000022059; -. DR ABCD; P31424; 2 sequenced antibodies. DR Ensembl; ENSRNOT00000022060.6; ENSRNOP00000022059.5; ENSRNOG00000016429.8. [P31424-1] DR Ensembl; ENSRNOT00000050639.3; ENSRNOP00000040016.3; ENSRNOG00000016429.8. [P31424-2] DR Ensembl; ENSRNOT00055032958; ENSRNOP00055026687; ENSRNOG00055019318. [P31424-1] DR Ensembl; ENSRNOT00060035745; ENSRNOP00060029407; ENSRNOG00060020535. [P31424-1] DR Ensembl; ENSRNOT00065049512; ENSRNOP00065040636; ENSRNOG00065028675. [P31424-1] DR GeneID; 24418; -. DR KEGG; rno:24418; -. DR UCSC; RGD:2746; rat. [P31424-1] DR AGR; RGD:2746; -. DR CTD; 2915; -. DR RGD; 2746; Grm5. DR eggNOG; KOG1056; Eukaryota. DR GeneTree; ENSGT01030000234595; -. DR HOGENOM; CLU_005389_0_1_1; -. DR InParanoid; P31424; -. DR OMA; ECFTPKE; -. DR OrthoDB; 5388627at2759; -. DR PhylomeDB; P31424; -. DR TreeFam; TF313240; -. DR Reactome; R-RNO-416476; G alpha (q) signalling events. DR Reactome; R-RNO-420499; Class C/3 (Metabotropic glutamate/pheromone receptors). DR Reactome; R-RNO-6794361; Neurexins and neuroligins. DR EvolutionaryTrace; P31424; -. DR PRO; PR:P31424; -. DR Proteomes; UP000002494; Chromosome 1. DR GO; GO:0097449; C:astrocyte projection; IDA:RGD. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0043198; C:dendritic shaft; IDA:RGD. DR GO; GO:0043197; C:dendritic spine; IDA:RGD. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0043005; C:neuron projection; ISO:RGD. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO. DR GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD. DR GO; GO:0031687; F:A2A adenosine receptor binding; IPI:RGD. DR GO; GO:0001640; F:adenylate cyclase inhibiting G protein-coupled glutamate receptor activity; IBA:GO_Central. DR GO; GO:0005516; F:calmodulin binding; TAS:UniProtKB. DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB. DR GO; GO:0099530; F:G protein-coupled receptor activity involved in regulation of postsynaptic membrane potential; ISO:RGD. DR GO; GO:0008066; F:glutamate receptor activity; IMP:UniProtKB. DR GO; GO:0042802; F:identical protein binding; ISO:RGD. DR GO; GO:0099583; F:neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration; ISO:RGD. DR GO; GO:0030165; F:PDZ domain binding; TAS:UniProtKB. DR GO; GO:0001639; F:PLC activating G protein-coupled glutamate receptor activity; TAS:UniProtKB. DR GO; GO:1990782; F:protein tyrosine kinase binding; IPI:ARUK-UCL. DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISO:RGD. DR GO; GO:1904646; P:cellular response to amyloid-beta; ISO:RGD. DR GO; GO:0007268; P:chemical synaptic transmission; IMP:RGD. DR GO; GO:0050890; P:cognition; ISO:RGD. DR GO; GO:0002029; P:desensitization of G protein-coupled receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0007612; P:learning; ISO:RGD. DR GO; GO:0007611; P:learning or memory; ISO:RGD. DR GO; GO:0007626; P:locomotory behavior; ISO:RGD. DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD. DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:UniProtKB. DR GO; GO:0007206; P:phospholipase C-activating G protein-coupled glutamate receptor signaling pathway; TAS:UniProtKB. DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; TAS:UniProtKB. DR GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; IDA:RGD. DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:UniProtKB. DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IGI:ARUK-UCL. DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:RGD. DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISO:RGD. DR GO; GO:0001932; P:regulation of protein phosphorylation; ISO:RGD. DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central. DR GO; GO:0006448; P:regulation of translational elongation; ISO:RGD. DR GO; GO:0050808; P:synapse organization; ISO:RGD. DR GO; GO:0099553; P:trans-synaptic signaling by endocannabinoid, modulating synaptic transmission; IMP:SynGO. DR CDD; cd15450; 7tmC_mGluR5; 1. DR CDD; cd06374; PBP1_mGluR_groupI; 1. DR Gene3D; 3.40.50.2300; -; 2. DR Gene3D; 2.10.50.30; GPCR, family 3, nine cysteines domain; 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; IPR000202; GPCR_3_mGluR5. DR InterPro; IPR000162; GPCR_3_mtglu_rcpt. DR InterPro; IPR019588; Metabotropic_Glu_rcpt_Homer-bd. DR InterPro; IPR028082; Peripla_BP_I. DR PANTHER; PTHR24060; METABOTROPIC GLUTAMATE RECEPTOR; 1. DR PANTHER; PTHR24060:SF30; METABOTROPIC GLUTAMATE RECEPTOR 5; 1. DR Pfam; PF00003; 7tm_3; 1. DR Pfam; PF01094; ANF_receptor; 1. DR Pfam; PF10606; GluR_Homer-bdg; 1. DR Pfam; PF07562; NCD3G; 1. DR PRINTS; PR00248; GPCRMGR. DR PRINTS; PR01055; MTABOTROPC5R. DR PRINTS; PR00593; MTABOTROPICR. DR SMART; SM01229; GluR_Homer-bdg; 1. DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 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. DR Genevisible; P31424; RN. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond; KW G-protein coupled receptor; Glycoprotein; Membrane; Methylation; KW Phosphoprotein; Receptor; Reference proteome; Signal; Transducer; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..1203 FT /note="Metabotropic glutamate receptor 5" FT /id="PRO_0000012933" FT TOPO_DOM 21..579 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 580..602 FT /note="Helical; Name=1" FT /evidence="ECO:0000250" FT TOPO_DOM 603..612 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 613..635 FT /note="Helical; Name=2" FT /evidence="ECO:0000250" FT TOPO_DOM 636..643 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 644..666 FT /note="Helical; Name=3" FT /evidence="ECO:0000250" FT TOPO_DOM 667..692 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 693..713 FT /note="Helical; Name=4" FT /evidence="ECO:0000250" FT TOPO_DOM 714..736 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 737..758 FT /note="Helical; Name=5" FT /evidence="ECO:0000250" FT TOPO_DOM 759..771 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 772..794 FT /note="Helical; Name=6" FT /evidence="ECO:0000250" FT TOPO_DOM 795..797 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 798..819 FT /note="Helical; Name=7" FT /evidence="ECO:0000250" FT TOPO_DOM 820..1203 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT REGION 892..970 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1003..1054 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1122..1182 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 900..951 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1040..1054 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1161..1180 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 64 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250" FT BINDING 151 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250" FT BINDING 172..174 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250" FT BINDING 222 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250" FT BINDING 304 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250" FT BINDING 395 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250" FT MOD_RES 860 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 868 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q3UVX5" FT MOD_RES 924 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q3UVX5" FT MOD_RES 1014 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 1016 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT CARBOHYD 88 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 209 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 377 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 381 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 444 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 733 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 57..99 FT /evidence="ECO:0000250" FT DISULFID 240..529 FT /evidence="ECO:0000250" FT DISULFID 275..277 FT /evidence="ECO:0000250" FT DISULFID 364..380 FT /evidence="ECO:0000250" FT DISULFID 418..425 FT /evidence="ECO:0000250" FT DISULFID 510..530 FT /evidence="ECO:0000250" FT DISULFID 514..533 FT /evidence="ECO:0000250" FT DISULFID 536..548 FT /evidence="ECO:0000250" FT DISULFID 551..564 FT /evidence="ECO:0000250" FT DISULFID 643..732 FT /evidence="ECO:0000250" FT VAR_SEQ 876..907 FT /note="Missing (in isoform 1)" FT /evidence="ECO:0000303|PubMed:1320017" FT /id="VSP_002031" FT MUTAGEN 1154 FT /note="L->V: Normal binding to HOMER1." FT /evidence="ECO:0000269|PubMed:9808459" FT MUTAGEN 1156 FT /note="P->K: Disrupts binding to HOMER1." FT /evidence="ECO:0000269|PubMed:9808459" FT MUTAGEN 1157 FT /note="P->E: Disrupts binding to HOMER1." FT /evidence="ECO:0000269|PubMed:9808459" FT MUTAGEN 1157 FT /note="P->L: Disrupts binding to HOMER1." FT /evidence="ECO:0000269|PubMed:9808459" FT MUTAGEN 1158 FT /note="S->F: Normal binding to HOMER1." FT /evidence="ECO:0000269|PubMed:9808459" FT MUTAGEN 1159 FT /note="P->A: Normal binding to HOMER1." FT /evidence="ECO:0000269|PubMed:9808459" FT MUTAGEN 1160 FT /note="F->R: Disrupts binding to HOMER1." FT MUTAGEN 1161 FT /note="R->T: Normal binding to HOMER1." FT /evidence="ECO:0000269|PubMed:9808459" SQ 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 SSL //