GRAP1_RAT
ID GRAP1_RAT Reviewed; 837 AA.
AC Q9JHZ4; Q9JHZ3;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=GRIP1-associated protein 1;
DE Short=GRASP-1;
DE Contains:
DE RecName: Full=GRASP-1 C-terminal chain {ECO:0000305|PubMed:10896157};
DE AltName: Full=30kDa C-terminus form;
GN Name=Gripap1; Synonyms=Grasp1;
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 GRIP1;
RP GRIP2 AND AMPA RECEPTORS, CLEAVAGE BY CASPASE-3, AND MUTAGENESIS OF ASP-591
RP AND ASP-594.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RX PubMed=10896157; DOI=10.1016/s0896-6273(00)81198-8;
RA Ye B., Liao D., Zhang X., Zhang P., Dong H., Huganir R.L.;
RT "GRASP-1: a neuronal RasGEF associated with the AMPA receptor/GRIP
RT complex.";
RL Neuron 26:603-617(2000).
RN [2]
RP FUNCTION, INTERACTION WITH MAPK8 AND MAP3K1, AND CLEAVAGE BY CASPASE-3.
RX PubMed=17761173; DOI=10.1016/j.febslet.2007.08.008;
RA Ye B., Yu W.P., Thomas G.M., Huganir R.L.;
RT "GRASP-1 is a neuronal scaffold protein for the JNK signaling pathway.";
RL FEBS Lett. 581:4403-4410(2007).
RN [3]
RP FUNCTION, INTERACTION WITH RAB4A AND STX12, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ASP-591 AND ASP-594.
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-684; SER-688 AND SER-826, 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: 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. {ECO:0000269|PubMed:20098723}.
CC -!- FUNCTION: [GRASP-1 C-terminal chain]: Functions as a scaffold protein
CC in neurons to facilitate MAP3K1/MEKK1-mediated activation of the JNK1
CC kinase by phosphorylation, possibly by bringing MAP3K1/MEKK1 and JNK1
CC in close proximity. {ECO:0000269|PubMed:17761173}.
CC -!- SUBUNIT: Interacts with GRIP1, GRIP2 and AMPA receptors
CC (PubMed:10896157). Interacts (via C-terminus) with MAPK8/JNK1 and with
CC MAP3K1/MEKK1; the interaction promotes MAP3K1-mediated phosphorylation
CC of MAPK8 (PubMed:17761173). Interacts (via N-terminus) with RAB4A (in
CC GTP-bound form) (PubMed:20098723). Interacts (via C-terminus) with
CC STX12 (PubMed:20098723). {ECO:0000269|PubMed:10896157,
CC ECO:0000269|PubMed:17761173, ECO:0000269|PubMed:20098723}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000269|PubMed:20098723}; Peripheral membrane protein
CC {ECO:0000305}. Recycling endosome membrane
CC {ECO:0000269|PubMed:20098723}; Peripheral membrane protein
CC {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:20098723}.
CC Cell projection, dendrite {ECO:0000269|PubMed:20098723}. Synapse
CC {ECO:0000269|PubMed:20098723}. Note=Localizes to recycling endosomal
CC tubules that are emanating from early endosomes.
CC {ECO:0000269|PubMed:20098723}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=long form;
CC IsoId=Q9JHZ4-1; Sequence=Displayed;
CC Name=2; Synonyms=short form;
CC IsoId=Q9JHZ4-2; Sequence=VSP_015706;
CC -!- TISSUE SPECIFICITY: Expressed in the central nervous system; especially
CC in neurons. {ECO:0000269|PubMed:10896157}.
CC -!- PTM: Proteolytically cleaved by caspase-3 (PubMed:10896157). A minor C-
CC terminal proteolytic fragment of 30 kDa is produced (PubMed:10896157).
CC Proteolytic cleavage is required for JNK signaling activation
CC (PubMed:17761173). {ECO:0000269|PubMed:10896157,
CC ECO:0000269|PubMed:17761173}.
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; AF274057; AAF82298.1; -; mRNA.
DR EMBL; AF274058; AAF82299.1; -; mRNA.
DR RefSeq; NP_446259.1; NM_053807.1. [Q9JHZ4-1]
DR AlphaFoldDB; Q9JHZ4; -.
DR SMR; Q9JHZ4; -.
DR BioGRID; 250467; 1.
DR CORUM; Q9JHZ4; -.
DR IntAct; Q9JHZ4; 1.
DR MINT; Q9JHZ4; -.
DR STRING; 10116.ENSRNOP00000012646; -.
DR iPTMnet; Q9JHZ4; -.
DR PhosphoSitePlus; Q9JHZ4; -.
DR jPOST; Q9JHZ4; -.
DR PeptideAtlas; Q9JHZ4; -.
DR PRIDE; Q9JHZ4; -.
DR Ensembl; ENSRNOT00000012646; ENSRNOP00000012646; ENSRNOG00000009071. [Q9JHZ4-1]
DR Ensembl; ENSRNOT00000111277; ENSRNOP00000085406; ENSRNOG00000009071. [Q9JHZ4-2]
DR GeneID; 116493; -.
DR KEGG; rno:116493; -.
DR UCSC; RGD:621249; rat. [Q9JHZ4-1]
DR CTD; 56850; -.
DR RGD; 621249; Gripap1.
DR eggNOG; ENOG502QTUD; Eukaryota.
DR GeneTree; ENSGT00720000108868; -.
DR HOGENOM; CLU_019728_1_0_1; -.
DR InParanoid; Q9JHZ4; -.
DR OMA; LQKNVAX; -.
DR OrthoDB; 1273136at2759; -.
DR PhylomeDB; Q9JHZ4; -.
DR TreeFam; TF329006; -.
DR PRO; PR:Q9JHZ4; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000009071; Expressed in frontal cortex and 20 other tissues.
DR Genevisible; Q9JHZ4; RN.
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; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0098998; C:extrinsic component of postsynaptic early endosome membrane; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0098837; C:postsynaptic recycling endosome; IDA:SynGO.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; IMP:SynGO.
DR GO; GO:1905244; P:regulation of modification of synaptic structure; IMP:SynGO.
DR GO; GO:0099152; P:regulation of neurotransmitter receptor transport, endosome to postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099158; P:regulation of recycling endosome localization within postsynapse; IDA:SynGO.
DR InterPro; IPR026204; GRIPAP1.
DR PANTHER; PTHR18978; PTHR18978; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Coiled coil; Endosome;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Synapse;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q4V328"
FT CHAIN 2..837
FT /note="GRIP1-associated protein 1"
FT /id="PRO_0000087583"
FT CHAIN 595..837
FT /note="GRASP-1 C-terminal chain"
FT /id="PRO_0000441813"
FT REGION 161..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 4..158
FT /evidence="ECO:0000255"
FT COILED 204..637
FT /evidence="ECO:0000255"
FT COILED 697..731
FT /evidence="ECO:0000255"
FT COILED 781..810
FT /evidence="ECO:0000255"
FT COMPBIAS 680..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 594..595
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000269|PubMed:10896157"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q4V328"
FT MOD_RES 651
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4V328"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4V328"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD04"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD04"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4V328"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD04"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 826
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 57..101
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_015706"
FT MUTAGEN 591
FT /note="D->E: No in vitro cleavage by caspase-3; when
FT associated with E-594. Results in loss of JNK activation;
FT when associated with E-594."
FT /evidence="ECO:0000269|PubMed:10896157,
FT ECO:0000269|PubMed:20098723"
FT MUTAGEN 594
FT /note="D->E: No in vitro cleavage by caspase-3; when
FT associated with E-591. Results in loss of JNK activation;
FT when associated with E-591."
FT /evidence="ECO:0000269|PubMed:10896157,
FT ECO:0000269|PubMed:20098723"
SQ SEQUENCE 837 AA; 96074 MW; A746AE4FD09D3AD2 CRC64;
MAQALSEEEF QRMQTQLLEL RTNNYQLSDE LRKNGVELSS LRQKVAYLDK EFSKAQKALS
KSKKAQEVEV LLSEKEMLQA KLHSQEEDFR LQNSTLMAEF SKLCSQLEQL ELENRQLKEG
VPGAAGPHVD GELLRLQAEN TALQKNMAAL QERYGKEAVR PSAVSEGQGD PPGDVLPISL
SPMPLAEVEL KWEMEREEKK LLWEQLQGLE SSKQAETSRL QEELAKLSEK LKKKQESFCR
LQTEKETLFN DSRNKIEELQ QRKEADLKAQ LARTQKLQQE LEAANQSLAE LRDQRQGERL
EHAAALRALQ DQVSSQSADA QEQVEGLLAE NNALRTSLAA LEQIQTAKTQ ELNMLREQNT
ELAAELKHRQ ADYEELMGQK DDLNSQLQES LRANSRLLEQ LQEMGQEKEQ LIQDLQEARK
SAEKRKVMLD ELAMETLQEK SQHKEELGAV RLRHEKEMLG VRARYERELR ELHEDKKRQE
EELRGQIREE KARTRELENL QHTVEELQAQ VHSMDGAKGW FERRLKEAEE SLLQQEQEQE
ETLKQCREQH AAELKGKEEE LQNVRDQLQQ AQEERDGHVK TISNLKQEVK DTVDGQRILE
KKGSAVLKDL KRQLHLERKR ADKLQERLQE ILTNSKSRTG LEELVLSEMN SPSRTQTGDS
SSVSSFSYRE ILKEKESSAI PARSLSSSPQ AQPPRPAELS DEEVAELFQR LAETQQEKWM
LEEKVKHLEV SSASMAEDLC RKSAIIETYV MDSRIDVSVA AGHTDRSGLG SVLRDLVKPG
DENLREMNKK LQNMLEEQLT KNMHLHKDME VLSQEIVRLS KECVGSPDPD LEPGEAN
