GRM5_RAT
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 03-AUG-2022, entry version 192.
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}.
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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 GlyGen; P31424; 6 sites.
DR iPTMnet; P31424; -.
DR PhosphoSitePlus; P31424; -.
DR PaxDb; P31424; -.
DR PRIDE; P31424; -.
DR ABCD; P31424; 2 sequenced antibodies.
DR Ensembl; ENSRNOT00000022060; ENSRNOP00000022059; ENSRNOG00000016429. [P31424-1]
DR Ensembl; ENSRNOT00000050639; ENSRNOP00000040016; ENSRNOG00000016429. [P31424-2]
DR GeneID; 24418; -.
DR KEGG; rno:24418; -.
DR UCSC; RGD:2746; rat. [P31424-1]
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 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 Genevisible; P31424; RN.
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:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0016020; C:membrane; IDA: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; IDA:RGD.
DR GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0045211; C:postsynaptic membrane; TAS:UniProtKB.
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:0040013; P:negative regulation of locomotion; IDA: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:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled 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:0099170; P:postsynaptic modulation of chemical synaptic transmission; ISO:RGD.
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:1902938; P:regulation of intracellular calcium activated chloride channel activity; ISO: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:0006355; P:regulation of transcription, DNA-templated; IDA:RGD.
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 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; 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 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; 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; 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
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