ID GRASP_RAT Reviewed; 394 AA. AC Q8R4T5; DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 24-JAN-2024, entry version 137. DE RecName: Full=General receptor for phosphoinositides 1-associated scaffold protein; DE Short=GRP1-associated scaffold protein; DE AltName: Full=95 kDa postsynaptic density protein discs-large ZO-1 domain-containing protein; DE AltName: Full=PSD-95 PDZ domain-containing protein; DE AltName: Full=Tamalin {ECO:0000303|PubMed:11850456}; GN Name=Tamalin {ECO:0000303|PubMed:11850456}; Synonyms=Grasp; 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], TISSUE SPECIFICITY, INTERACTION WITH GRM1; RP GRM2; GRM3; GRM5 AND CYTH2, SUBCELLULAR LOCATION, AND FUNCTION. RC TISSUE=Brain; 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 [2] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93 AND SER-386, AND RP 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). CC -!- FUNCTION: Plays a role in intracellular trafficking and contributes to CC the macromolecular organization of group 1 metabotropic glutamate CC receptors (mGluRs) at synapses. {ECO:0000269|PubMed:11850456}. CC -!- SUBUNIT: Heteromer. Composed of TAMALIN, CYTH2 and at least one GRM1. CC Also interacts with CYTH3, GRM2, GRM3 and GRM5. CC {ECO:0000250|UniProtKB:Q9JJA9, ECO:0000269|PubMed:11850456}. CC -!- INTERACTION: CC Q8R4T5; O35431: Apba2; NbExp=4; IntAct=EBI-7361884, EBI-2028211; CC Q8R4T5; P31016: Dlg4; NbExp=3; IntAct=EBI-7361884, EBI-375655; CC Q8R4T5; P97838: Dlgap3; NbExp=3; IntAct=EBI-7361884, EBI-375673; CC Q8R4T5; P31424: Grm5; NbExp=5; IntAct=EBI-7361884, EBI-2902734; CC Q8R4T5; O88382: Magi2; NbExp=5; IntAct=EBI-7361884, EBI-696179; CC Q8R4T5; Q8R4T5: Tamalin; NbExp=3; IntAct=EBI-7361884, EBI-7361884; CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region CC {ECO:0000269|PubMed:11850456}. Cell membrane CC {ECO:0000269|PubMed:11850456}; Peripheral membrane protein CC {ECO:0000269|PubMed:11850456}; Cytoplasmic side CC {ECO:0000269|PubMed:11850456}. Postsynaptic cell membrane CC {ECO:0000269|PubMed:11850456}. CC -!- TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:11850456}. 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; AF374272; AAL87038.1; -; mRNA. DR RefSeq; NP_620249.1; NM_138894.1. DR PDB; 2EGK; X-ray; 2.85 A; A/B/C/D=96-189. DR PDB; 2EGN; X-ray; 2.40 A; A=96-189. DR PDB; 2EGO; X-ray; 1.80 A; A/B=96-189. DR PDBsum; 2EGK; -. DR PDBsum; 2EGN; -. DR PDBsum; 2EGO; -. DR AlphaFoldDB; Q8R4T5; -. DR SMR; Q8R4T5; -. DR BioGRID; 251380; 19. DR CORUM; Q8R4T5; -. DR ELM; Q8R4T5; -. DR IntAct; Q8R4T5; 16. DR MINT; Q8R4T5; -. DR STRING; 10116.ENSRNOP00000009979; -. DR iPTMnet; Q8R4T5; -. DR PhosphoSitePlus; Q8R4T5; -. DR PaxDb; 10116-ENSRNOP00000009979; -. DR Ensembl; ENSRNOT00000009979.4; ENSRNOP00000009979.1; ENSRNOG00000007346.4. DR Ensembl; ENSRNOT00065039388; ENSRNOP00065032016; ENSRNOG00065023049. DR GeneID; 192254; -. DR KEGG; rno:192254; -. DR UCSC; RGD:70554; rat. DR AGR; RGD:70554; -. DR CTD; 160622; -. DR RGD; 70554; Tamalin. DR eggNOG; KOG3528; Eukaryota. DR GeneTree; ENSGT00530000063734; -. DR HOGENOM; CLU_058640_0_0_1; -. DR InParanoid; Q8R4T5; -. DR OMA; KVHNDSP; -. DR OrthoDB; 5356422at2759; -. DR PhylomeDB; Q8R4T5; -. DR TreeFam; TF316315; -. DR EvolutionaryTrace; Q8R4T5; -. DR PRO; PR:Q8R4T5; -. DR Proteomes; UP000002494; Chromosome 7. DR Bgee; ENSRNOG00000007346; Expressed in frontal cortex and 18 other cell types or tissues. DR ExpressionAtlas; Q8R4T5; baseline and differential. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; ISO:RGD. DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO. DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0030165; F:PDZ domain binding; IDA:RGD. DR GO; GO:0031267; F:small GTPase binding; IDA:RGD. DR GO; GO:0099152; P:regulation of neurotransmitter receptor transport, endosome to postsynaptic membrane; ISO:RGD. DR GO; GO:0007165; P:signal transduction; ISO:RGD. DR CDD; cd00992; PDZ_signaling; 1. DR Gene3D; 2.30.42.10; -; 1. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR PANTHER; PTHR15963; GENERAL RECEPTOR FOR PHOSPHOINOSITIDES 1-ASSOCIATED SCAFFOLD PROTEIN-RELATED; 1. DR PANTHER; PTHR15963:SF3; PROTEIN TAMALIN; 1. DR Pfam; PF00595; PDZ; 1. DR SMART; SM00228; PDZ; 1. DR SUPFAM; SSF50156; PDZ domain-like; 1. DR PROSITE; PS50106; PDZ; 1. DR Genevisible; Q8R4T5; RN. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Cytoplasm; Membrane; Methylation; KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Synapse. FT CHAIN 1..394 FT /note="General receptor for phosphoinositides 1-associated FT scaffold protein" FT /id="PRO_0000087586" FT DOMAIN 100..189 FT /note="PDZ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT REGION 1..51 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 180..257 FT /note="Interaction with PSCD3" FT /evidence="ECO:0000250" FT REGION 293..318 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 294..309 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 76 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9JJA9" FT MOD_RES 93 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 236 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q7Z6J2" FT MOD_RES 269 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q9JJA9" FT MOD_RES 386 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT STRAND 98..104 FT /evidence="ECO:0007829|PDB:2EGO" FT STRAND 107..109 FT /evidence="ECO:0007829|PDB:2EGK" FT STRAND 112..119 FT /evidence="ECO:0007829|PDB:2EGO" FT STRAND 130..137 FT /evidence="ECO:0007829|PDB:2EGO" FT HELIX 142..145 FT /evidence="ECO:0007829|PDB:2EGO" FT STRAND 153..157 FT /evidence="ECO:0007829|PDB:2EGO" FT HELIX 167..176 FT /evidence="ECO:0007829|PDB:2EGO" FT TURN 177..179 FT /evidence="ECO:0007829|PDB:2EGO" FT STRAND 180..186 FT /evidence="ECO:0007829|PDB:2EGO" SQ SEQUENCE 394 AA; 42321 MW; 520D0AD23CB2B70D CRC64; MTLRRLRKLQ QKEEATAAPD LAGRAPDSEA ARAAPTPSGP PAAAAPPGAP GDELYAALED YHPAELYRAL AVSGGTLPRR KGSGFRWKNF TQSPEQQRKV LTLEKGDNQT FGFEIQTYGL HHREEQRVEM VTFVCRVHES SPAQLAGLTP GDTIASVNGL NVEGIRHREI VDIIKASGNV LRLETLYGTS IRKAELEARL QYLKQTLYEK WGEYRSLMVQ EQRLVHGLVV KDPSIYDTLE SVRSCLYGAG LLPGSLPFGP LLAAPGGARG GSRRAKGDTD DAVYHTCFFG GAEPQALPPP PPPARAPGPG SAETPASVLC PAPRATLSRS ASVRCAGPGG GGGGGAPGAL WTEAREQALC GAGLRKTKYR SFRRRLLKFI PGLNRSLEEE ESQL //