GRASP_RAT
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 03-AUG-2022, entry version 129.
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}.
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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; Q8R4T5; -.
DR PRIDE; Q8R4T5; -.
DR Ensembl; ENSRNOT00000009979; ENSRNOP00000009979; ENSRNOG00000007346.
DR GeneID; 192254; -.
DR KEGG; rno:192254; -.
DR UCSC; RGD:70554; rat.
DR CTD; 160622; -.
DR RGD; 70554; Grasp.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00530000063734; -.
DR HOGENOM; CLU_058640_0_0_1; -.
DR InParanoid; Q8R4T5; -.
DR OMA; YQTCIYQ; -.
DR OrthoDB; 966869at2759; -.
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 tissues.
DR ExpressionAtlas; Q8R4T5; baseline and differential.
DR Genevisible; Q8R4T5; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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; IDA: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:0008104; P:protein localization; 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 Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
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
