ID   GRASP_MOUSE             Reviewed;         392 AA.
AC   Q9JJA9; Q9JKL0;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   24-JAN-2024, entry version 130.
DE   RecName: Full=General receptor for phosphoinositides 1-associated scaffold protein;
DE            Short=GRP1-associated scaffold protein;
GN   Name=Tamalin {ECO:0000303|PubMed:11850456}; Synonyms=Grasp;
GN   ORFNames=MNCb-4428;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH CYTH3, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=10828067; DOI=10.1074/jbc.275.22.16827;
RA   Nevrivy D.J., Peterson V.J., Avram D., Ishmael J.E., Hansen S.G.,
RA   Dowell P., Hruby D.E., Dawson M.I., Leid M.;
RT   "Interaction of GRASP, a protein encoded by a novel retinoic acid-induced
RT   gene, with members of the cytohesin family of guanine nucleotide exchange
RT   factors.";
RL   J. Biol. Chem. 275:16827-16836(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT   oligo-capping method.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-76 AND SER-384, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Kidney;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-269, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
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:0000250}.
CC   -!- SUBUNIT: Heteromer. Composed of TAMALIN, CYTH2 and at least one GRM1.
CC       Also interacts with GRM2, GRM3 and GRM5 (By similarity). Interacts with
CC       CYTH3 (PubMed:10828067). {ECO:0000250|UniProtKB:Q8R4T5,
CC       ECO:0000269|PubMed:10828067}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000250|UniProtKB:Q8R4T5}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q8R4T5}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q8R4T5}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q8R4T5}. Postsynaptic cell membrane
CC       {ECO:0000250|UniProtKB:Q8R4T5}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain, heart and lung, and to a
CC       lower extent in embryo, kidney and ovary. {ECO:0000269|PubMed:10828067,
CC       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; AF236099; AAF36997.1; -; mRNA.
DR   EMBL; AB041603; BAA95086.1; -; mRNA.
DR   EMBL; BC046307; AAH46307.1; -; mRNA.
DR   CCDS; CCDS27847.1; -.
DR   RefSeq; NP_062391.3; NM_019518.3.
DR   AlphaFoldDB; Q9JJA9; -.
DR   SMR; Q9JJA9; -.
DR   BioGRID; 207817; 5.
DR   IntAct; Q9JJA9; 1.
DR   MINT; Q9JJA9; -.
DR   STRING; 10090.ENSMUSP00000000543; -.
DR   iPTMnet; Q9JJA9; -.
DR   PhosphoSitePlus; Q9JJA9; -.
DR   MaxQB; Q9JJA9; -.
DR   PaxDb; 10090-ENSMUSP00000000543; -.
DR   PeptideAtlas; Q9JJA9; -.
DR   ProteomicsDB; 271054; -.
DR   Antibodypedia; 26519; 105 antibodies from 24 providers.
DR   DNASU; 56149; -.
DR   Ensembl; ENSMUST00000000543.6; ENSMUSP00000000543.5; ENSMUSG00000000531.6.
DR   GeneID; 56149; -.
DR   KEGG; mmu:56149; -.
DR   UCSC; uc007xsu.1; mouse.
DR   AGR; MGI:1860303; -.
DR   CTD; 160622; -.
DR   MGI; MGI:1860303; Tamalin.
DR   VEuPathDB; HostDB:ENSMUSG00000000531; -.
DR   eggNOG; KOG3528; Eukaryota.
DR   GeneTree; ENSGT00530000063734; -.
DR   HOGENOM; CLU_058640_0_0_1; -.
DR   InParanoid; Q9JJA9; -.
DR   OMA; KVHNDSP; -.
DR   OrthoDB; 5356422at2759; -.
DR   PhylomeDB; Q9JJA9; -.
DR   TreeFam; TF316315; -.
DR   BioGRID-ORCS; 56149; 5 hits in 77 CRISPR screens.
DR   ChiTaRS; Grasp; mouse.
DR   PRO; PR:Q9JJA9; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q9JJA9; Protein.
DR   Bgee; ENSMUSG00000000531; Expressed in dorsal pancreas and 198 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0005641; C:nuclear envelope lumen; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR   GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR   GO; GO:0006886; P:intracellular protein transport; ISO:MGI.
DR   GO; GO:0099152; P:regulation of neurotransmitter receptor transport, endosome to postsynaptic membrane; IDA:SynGO.
DR   GO; GO:0007165; P:signal transduction; IPI:MGI.
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; Q9JJA9; MM.
PE   1: Evidence at protein level;
KW   Cell membrane; Cytoplasm; Membrane; Methylation; Phosphoprotein;
KW   Postsynaptic cell membrane; Reference proteome; Synapse.
FT   CHAIN           1..392
FT                   /note="General receptor for phosphoinositides 1-associated
FT                   scaffold protein"
FT                   /id="PRO_0000087585"
FT   DOMAIN          100..189
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          180..257
FT                   /note="Interaction with PSCD3"
FT                   /evidence="ECO:0000269|PubMed:10828067"
FT   REGION          294..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..308
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         76
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         93
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R4T5"
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:0007744|PubMed:24129315"
FT   MOD_RES         384
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        299
FT                   /note="P -> L (in Ref. 2; BAA95086)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   392 AA;  42337 MW;  52144F07D36B57FE CRC64;
     MTLRRLRKLQ QKEEATAAPD PAGRAPDSEA ARAAPLPSGP PAAAAPPGAP GEELYAALED
     YHPAELYRAL AVSGGTLPRR KGSGFRWKNF TQSPEQQRKV LTLEKGDNQT FGFEIQTYGL
     HHREEQRVEM VTFVCRVHES SPAQLAGLTP GDTIASVNGL NVEGIRHREI VDIIKASGNV
     LRLETLYGTS IRKAELEARL QYLKQTLYEK WGEYRSLMVQ EQRLVHGLVV KDPSIYDTLE
     SVRSCLYGAG LLPGSLPFGP LLAAPGSARG GARRAKGDTD DAVYHTCFFG GAEPQALPPP
     PPPARALGPS SAETPASVLF PAPRSTLSRS ASVRCAGPGG GGGAPGALWT EAREQALCGA
     GLRKTKYRSF RRRLLKFIPG LNRSLEEEES QL
//