GRAP1_MOUSE
ID GRAP1_MOUSE Reviewed; 806 AA.
AC Q8VD04; A2AEW7; O35693; Q3T9C3; Q69ZP9;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=GRIP1-associated protein 1;
DE Short=GRASP-1;
DE AltName: Full=HCMV-interacting protein;
DE Contains:
DE RecName: Full=GRASP-1 C-terminal chain {ECO:0000250|UniProtKB:Q9JHZ4};
DE AltName: Full=30kDa C-terminus form;
GN Name=Gripap1; Synonyms=DXImx47e, Kiaa1167;
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 [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-106.
RA Weber B.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 318-776.
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631 AND SER-634, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-620; SER-631; SER-633;
RP SER-634; SER-656 AND SER-657, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [7]
RP TISSUE SPECIFICITY, AND INTERACTION WITH STX12.
RX PubMed=20098723; DOI=10.1371/journal.pbio.1000283;
RA Hoogenraad C.C., Popa I., Futai K., Martinez-Sanchez E.,
RA Sanchez-Martinez E., Wulf P.S., van Vlijmen T., Dortland B.R., Oorschot V.,
RA Govers R., Monti M., Heck A.J., Sheng M., Klumperman J., Rehmann H.,
RA Jaarsma D., Kapitein L.C., van der Sluijs P.;
RT "Neuron specific Rab4 effector GRASP-1 coordinates membrane specialization
RT and maturation of recycling endosomes.";
RL PLoS Biol. 8:E1000283-E1000283(2010).
CC -!- FUNCTION: Regulates the endosomal recycling back to the neuronal plasma
CC membrane, possibly by connecting early and late recycling endosomal
CC domains and promoting segregation of recycling endosomes from early
CC endosomal membranes. Involved in the localization of recycling
CC endosomes to dendritic spines, thereby playing a role in the
CC maintenance of dendritic spine morphology. Required for the activity-
CC induced AMPA receptor recycling to dendrite membranes and for long-term
CC potentiation and synaptic plasticity (By similarity).
CC {ECO:0000250|UniProtKB:Q9JHZ4}.
CC -!- FUNCTION: [GRASP-1 C-terminal chain]: Functions as a scaffold protein
CC to facilitate MAP3K1/MEKK1-mediated activation of the JNK1 kinase by
CC phosphorylation, possibly by bringing MAP3K1/MEKK1 and JNK1 in close
CC proximity (By similarity). {ECO:0000250|UniProtKB:Q4V328}.
CC -!- SUBUNIT: Interacts with GRIP1, GRIP2 and AMPA receptors. Interacts (via
CC C-terminus) with MAPK8/JNK1 and MAP3K1/MEKK1; the interaction promotes
CC MAP3K1-mediated phosphorylation of MAPK8. Interacts (via N-terminus)
CC with RAB4A (in GTP-bound form) (By similarity). Interacts (via C-
CC terminus) with STX12 (PubMed:20098723). {ECO:0000250|UniProtKB:Q9JHZ4,
CC ECO:0000269|PubMed:20098723}.
CC -!- INTERACTION:
CC Q8VD04; A3KBF5: Mapk8; NbExp=2; IntAct=EBI-7585099, EBI-7585074;
CC Q8VD04; Q9NRI5: DISC1; Xeno; NbExp=2; IntAct=EBI-7585099, EBI-529989;
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000250|UniProtKB:Q9JHZ4}; Peripheral membrane protein
CC {ECO:0000305}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:Q9JHZ4}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9JHZ4}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q9JHZ4}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9JHZ4}. Synapse {ECO:0000250|UniProtKB:Q9JHZ4}.
CC Note=Localizes to recycling endosomal tubules that are emanating from
CC early endosomes. {ECO:0000250|UniProtKB:Q9JHZ4}.
CC -!- TISSUE SPECIFICITY: Expressed in the central nervous system, including
CC cortex, cerebellum, midbrain and spinal cord, and in primary cultured
CC hippocampal neurons but absent in non-neuronal tissues and cell types
CC with the exception of neuroendocrine insulinoma cells.
CC {ECO:0000269|PubMed:20098723}.
CC -!- PTM: Proteolytically cleaved by caspase-3. A minor C-terminal
CC proteolytic fragment of 30 kDa is produced. Proteolytic cleavage is
CC required for JNK signaling activation. {ECO:0000250|UniProtKB:Q9JHZ4}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA66184.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK156165; BAE33608.1; -; mRNA.
DR EMBL; AK172623; BAE43101.1; -; mRNA.
DR EMBL; AK172699; BAE43133.1; -; mRNA.
DR EMBL; AL671995; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X97571; CAA66184.1; ALT_INIT; mRNA.
DR EMBL; AK173119; BAD32397.1; -; Transcribed_RNA.
DR CCDS; CCDS40844.1; -.
DR RefSeq; NP_997553.1; NM_207670.2.
DR AlphaFoldDB; Q8VD04; -.
DR SMR; Q8VD04; -.
DR BioGRID; 207707; 6.
DR IntAct; Q8VD04; 4.
DR MINT; Q8VD04; -.
DR STRING; 10090.ENSMUSP00000068789; -.
DR iPTMnet; Q8VD04; -.
DR PhosphoSitePlus; Q8VD04; -.
DR EPD; Q8VD04; -.
DR jPOST; Q8VD04; -.
DR MaxQB; Q8VD04; -.
DR PaxDb; Q8VD04; -.
DR PeptideAtlas; Q8VD04; -.
DR PRIDE; Q8VD04; -.
DR ProteomicsDB; 271289; -.
DR Antibodypedia; 355; 230 antibodies from 32 providers.
DR DNASU; 54645; -.
DR Ensembl; ENSMUST00000065932; ENSMUSP00000068789; ENSMUSG00000031153.
DR GeneID; 54645; -.
DR KEGG; mmu:54645; -.
DR UCSC; uc009smo.2; mouse.
DR CTD; 56850; -.
DR MGI; MGI:1859616; Gripap1.
DR VEuPathDB; HostDB:ENSMUSG00000031153; -.
DR eggNOG; ENOG502QTUD; Eukaryota.
DR GeneTree; ENSGT00720000108868; -.
DR InParanoid; Q8VD04; -.
DR OrthoDB; 1273136at2759; -.
DR PhylomeDB; Q8VD04; -.
DR TreeFam; TF329006; -.
DR BioGRID-ORCS; 54645; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Gripap1; mouse.
DR PRO; PR:Q8VD04; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8VD04; protein.
DR Bgee; ENSMUSG00000031153; Expressed in granulocyte and 268 other tissues.
DR ExpressionAtlas; Q8VD04; baseline and differential.
DR Genevisible; Q8VD04; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0098998; C:extrinsic component of postsynaptic early endosome membrane; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0098837; C:postsynaptic recycling endosome; ISO:MGI.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; ISO:MGI.
DR GO; GO:1905244; P:regulation of modification of synaptic structure; ISO:MGI.
DR GO; GO:0099152; P:regulation of neurotransmitter receptor transport, endosome to postsynaptic membrane; ISO:MGI.
DR GO; GO:0099158; P:regulation of recycling endosome localization within postsynapse; ISO:MGI.
DR InterPro; IPR026204; GRIPAP1.
DR PANTHER; PTHR18978; PTHR18978; 2.
PE 1: Evidence at protein level;
KW Acetylation; Cell projection; Coiled coil; Endosome; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Synapse; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q4V328"
FT CHAIN 2..806
FT /note="GRIP1-associated protein 1"
FT /id="PRO_0000087582"
FT CHAIN 564..806
FT /note="GRASP-1 C-terminal chain"
FT /id="PRO_0000441812"
FT REGION 616..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 4..158
FT /evidence="ECO:0000255"
FT COILED 204..606
FT /evidence="ECO:0000255"
FT COILED 666..700
FT /evidence="ECO:0000255"
FT COILED 750..779
FT /evidence="ECO:0000255"
FT COMPBIAS 649..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 563..564
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250|UniProtKB:Q9JHZ4"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q4V328"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JHZ4"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4V328"
FT MOD_RES 656
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 795
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JHZ4"
FT CONFLICT 4
FT /note="A -> R (in Ref. 3; CAA66184)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="Q -> L (in Ref. 1; BAE33608/BAE43101/BAE43133)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 806 AA; 92715 MW; 766F7C5B44589020 CRC64;
MAQALSEEEF QRMQTQLLEL RTNNYQLSDE LRKNGVELSS LRQKVAYLDK EFSKAQKALS
KSKKAQEVEV LLSENEMLQA KLHSQEEDFR LQNSTLMAEF SKLCSQLEQL ELENRQLKEG
VPGAAGAHVD GELLRLQAEN TALQKNMAAL QERYGKEAVR PSAVGEGQGD PPGDVLPTPL
APMPLAEVEL KWEMEREEKK LLWEQLQGLE SSKQAETSRL QEELAKLSEK LKKKQESFCR
LQTEKETLFN DSRNKIEELQ QRKEADLKAQ LARTQKLQQE LEAANQSLAE LRDQRQGERL
EHAAALRALQ DQIQTAKTQE LNMLREQTSE LASELQHRQA EYEELMGQKD DLNSQLQESL
RANSRLLEQL QEIGQEKEQL TQDLQEARKS AEKRKVMLDE LAMETLQEKS QHKEELGAVR
LRHEKELLGV RARYERELRE LHEDKKRQEE ELRGQIREEK ARTRELENLQ HTVEELQAQV
HSMDGAKGWF ERRLKEAEES LQQQQQEQEE TLKLCREEHA AELKGKDEEL QNVREQLQQA
QEERDGHVKT ISNLKQEVKD TVDGQRILEK KGSAVLKDLK RQLHLERKRA DKLQERLQEI
LTNSKSRTGL EELVLSEMNS PSRTQTGDSS SVSSFSYREI LKEKESSAIP ARSLSSSPQA
QPPRPAELSD EEVAELFQRL AETQQEKWML EEKVKHLEVS SASMAEDLCR KSAIIETYVM
DSRIDVSVAA GHTDRSGLGS VLRDLVKPGD ENLREMNKKL QNMLEEQLTK NMHLHKDMEV
LSQEIVRLSK ECVGSPDPDL EPGEAN
