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GRIP1-associated protein 1 (GRASP-1) [Cleaved into: GRASP-1 C-terminal chain (30kDa C-terminus form)]

 GRAP1_RAT               Reviewed;         837 AA.
Q9JHZ4; Q9JHZ3;
27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
12-SEP-2018, entry version 104.
RecName: Full=GRIP1-associated protein 1;
Short=GRASP-1;
Contains:
RecName: Full=GRASP-1 C-terminal chain {ECO:0000305|PubMed:10896157};
AltName: Full=30kDa C-terminus form;
Name=Gripap1; Synonyms=Grasp1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH
GRIP1; GRIP2 AND AMPA RECEPTORS, CLEAVAGE BY CASPASE-3, AND
MUTAGENESIS OF ASP-591 AND ASP-594.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
PubMed=10896157; DOI=10.1016/S0896-6273(00)81198-8;
Ye B., Liao D., Zhang X., Zhang P., Dong H., Huganir R.L.;
"GRASP-1: a neuronal RasGEF associated with the AMPA receptor/GRIP
complex.";
Neuron 26:603-617(2000).
[2]
FUNCTION, INTERACTION WITH MAPK8 AND MAP3K1, AND CLEAVAGE BY
CASPASE-3.
PubMed=17761173; DOI=10.1016/j.febslet.2007.08.008;
Ye B., Yu W.P., Thomas G.M., Huganir R.L.;
"GRASP-1 is a neuronal scaffold protein for the JNK signaling
pathway.";
FEBS Lett. 581:4403-4410(2007).
[3]
FUNCTION, INTERACTION WITH RAB4A AND STX12, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF ASP-591 AND ASP-594.
PubMed=20098723; DOI=10.1371/journal.pbio.1000283;
Hoogenraad C.C., Popa I., Futai K., Martinez-Sanchez E.,
Sanchez-Martinez E., Wulf P.S., van Vlijmen T., Dortland B.R.,
Oorschot V., Govers R., Monti M., Heck A.J., Sheng M., Klumperman J.,
Rehmann H., Jaarsma D., Kapitein L.C., van der Sluijs P.;
"Neuron specific Rab4 effector GRASP-1 coordinates membrane
specialization and maturation of recycling endosomes.";
PLoS Biol. 8:E1000283-E1000283(2010).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-684; SER-688 AND
SER-826, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Regulates the endosomal recycling back to the neuronal
plasma membrane, possibly by connecting early and late recycling
endosomal domains and promoting segregation of recycling endosomes
from early endosomal membranes. Involved in the localization of
recycling endosomes to dendritic spines, thereby playing a role in
the maintenance of dendritic spine morphology. Required for the
activity-induced AMPA receptor recycling to dendrite membranes and
for long-term potentiation and synaptic plasticity.
{ECO:0000269|PubMed:20098723}.
-!- FUNCTION: GRASP-1 C-terminal chain: Functions as a scaffold
protein in neurons to facilitate MAP3K1/MEKK1-mediated activation
of the JNK1 kinase by phosphorylation, possibly by bringing
MAP3K1/MEKK1 and JNK1 in close proximity.
{ECO:0000269|PubMed:17761173}.
-!- SUBUNIT: Interacts with GRIP1, GRIP2 and AMPA receptors
(PubMed:10896157). Interacts (via C-terminus) with MAPK8/JNK1 and
with MAP3K1/MEKK1; the interaction promotes MAP3K1-mediated
phosphorylation of MAPK8 (PubMed:17761173). Interacts (via N-
terminus) with RAB4A (in GTP-bound form) (PubMed:20098723).
Interacts (via C-terminus) with STX12 (PubMed:20098723).
{ECO:0000269|PubMed:10896157, ECO:0000269|PubMed:17761173,
ECO:0000269|PubMed:20098723}.
-!- SUBCELLULAR LOCATION: Early endosome membrane
{ECO:0000269|PubMed:20098723}; Peripheral membrane protein
{ECO:0000305}. Recycling endosome membrane
{ECO:0000269|PubMed:20098723}; Peripheral membrane protein
{ECO:0000305}. Cell projection, axon
{ECO:0000269|PubMed:20098723}. Cell projection, dendrite
{ECO:0000269|PubMed:20098723}. Cell junction, synapse
{ECO:0000269|PubMed:20098723}. Note=Localizes to recycling
endosomal tubules that are emanating from early endosomes.
{ECO:0000269|PubMed:20098723}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=long form;
IsoId=Q9JHZ4-1; Sequence=Displayed;
Name=2; Synonyms=short form;
IsoId=Q9JHZ4-2; Sequence=VSP_015706;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in the central nervous system;
especially in neurons. {ECO:0000269|PubMed:10896157}.
-!- PTM: Proteolytically cleaved by caspase-3 (PubMed:10896157). A
minor C-terminal proteolytic fragment of 30 kDa is produced
(PubMed:10896157). Proteolytic cleavage is required for JNK
signaling activation (PubMed:17761173).
{ECO:0000269|PubMed:10896157, ECO:0000269|PubMed:17761173}.
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EMBL; AF274057; AAF82298.1; -; mRNA.
EMBL; AF274058; AAF82299.1; -; mRNA.
RefSeq; NP_446259.1; NM_053807.1. [Q9JHZ4-1]
UniGene; Rn.53868; -.
ProteinModelPortal; Q9JHZ4; -.
SMR; Q9JHZ4; -.
BioGrid; 250467; 1.
CORUM; Q9JHZ4; -.
IntAct; Q9JHZ4; 1.
MINT; Q9JHZ4; -.
iPTMnet; Q9JHZ4; -.
PhosphoSitePlus; Q9JHZ4; -.
PeptideAtlas; Q9JHZ4; -.
PRIDE; Q9JHZ4; -.
Ensembl; ENSRNOT00000012646; ENSRNOP00000012646; ENSRNOG00000009071. [Q9JHZ4-1]
GeneID; 116493; -.
KEGG; rno:116493; -.
UCSC; RGD:621249; rat. [Q9JHZ4-1]
CTD; 56850; -.
RGD; 621249; Gripap1.
GeneTree; ENSGT00720000108868; -.
HOGENOM; HOG000231369; -.
HOVERGEN; HBG080243; -.
InParanoid; Q9JHZ4; -.
OMA; SMAEDIC; -.
OrthoDB; EOG091G0AQ8; -.
PhylomeDB; Q9JHZ4; -.
TreeFam; TF329006; -.
PRO; PR:Q9JHZ4; -.
Proteomes; UP000002494; Chromosome X.
Bgee; ENSRNOG00000009071; Expressed in 10 organ(s), highest expression level in brain.
Genevisible; Q9JHZ4; RN.
GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0098837; C:postsynaptic recycling endosome; IDA:SynGO.
GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; IMP:SynGO.
GO; GO:1905244; P:regulation of modification of synaptic structure; IMP:SynGO.
InterPro; IPR026204; GRIPAP1.
PANTHER; PTHR18978; PTHR18978; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell junction; Cell projection;
Coiled coil; Complete proteome; Endosome; Membrane; Phosphoprotein;
Protein transport; Reference proteome; Synapse; Transport.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q4V328}.
CHAIN 2 837 GRIP1-associated protein 1.
/FTId=PRO_0000087583.
CHAIN 595 837 GRASP-1 C-terminal chain.
/FTId=PRO_0000441813.
COILED 4 158 {ECO:0000255}.
COILED 204 637 {ECO:0000255}.
COILED 697 731 {ECO:0000255}.
COILED 781 810 {ECO:0000255}.
SITE 594 595 Cleavage; by caspase-3.
{ECO:0000269|PubMed:10896157}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q4V328}.
MOD_RES 651 651 Phosphoserine.
{ECO:0000250|UniProtKB:Q4V328}.
MOD_RES 662 662 Phosphoserine.
{ECO:0000250|UniProtKB:Q4V328}.
MOD_RES 664 664 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VD04}.
MOD_RES 665 665 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VD04}.
MOD_RES 684 684 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 686 686 Phosphoserine.
{ECO:0000250|UniProtKB:Q4V328}.
MOD_RES 687 687 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VD04}.
MOD_RES 688 688 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 826 826 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
VAR_SEQ 57 101 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_015706.
MUTAGEN 591 591 D->E: No in vitro cleavage by caspase-3;
when associated with E-594. Results in
loss of JNK activation; when associated
with E-594. {ECO:0000269|PubMed:10896157,
ECO:0000269|PubMed:20098723}.
MUTAGEN 594 594 D->E: No in vitro cleavage by caspase-3;
when associated with E-591. Results in
loss of JNK activation; when associated
with E-591. {ECO:0000269|PubMed:10896157,
ECO:0000269|PubMed:20098723}.
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


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