GRASP_MOUSE
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 03-AUG-2022, entry version 123.
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}.
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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; Q9JJA9; -.
DR PeptideAtlas; Q9JJA9; -.
DR PRIDE; Q9JJA9; -.
DR ProteomicsDB; 271054; -.
DR Antibodypedia; 26519; 95 antibodies from 23 providers.
DR DNASU; 56149; -.
DR Ensembl; ENSMUST00000000543; ENSMUSP00000000543; ENSMUSG00000000531.
DR GeneID; 56149; -.
DR KEGG; mmu:56149; -.
DR UCSC; uc007xsu.1; mouse.
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; YQTCIYQ; -.
DR OrthoDB; 966869at2759; -.
DR PhylomeDB; Q9JJA9; -.
DR TreeFam; TF316315; -.
DR BioGRID-ORCS; 56149; 5 hits in 72 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 195 other tissues.
DR Genevisible; Q9JJA9; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0008104; P:protein localization; 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 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 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
