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Ras-specific guanine nucleotide-releasing factor 1 (Ras-GRF1) (CDC25Mm) (Guanine nucleotide-releasing protein) (GNRP) (Ras-specific nucleotide exchange factor CDC25)

 RGRF1_MOUSE             Reviewed;        1262 AA.
P27671;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
18-JUL-2018, entry version 177.
RecName: Full=Ras-specific guanine nucleotide-releasing factor 1;
Short=Ras-GRF1;
AltName: Full=CDC25Mm;
AltName: Full=Guanine nucleotide-releasing protein;
Short=GNRP;
AltName: Full=Ras-specific nucleotide exchange factor CDC25;
Name=Rasgrf1; Synonyms=Cdc25, Grf1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ;
PubMed=1396590;
Cen H., Lowy D.D.;
"Isolation of multiple mouse cDNAs with coding homology to
Saccharomyces cerevisiae CDC25: identification of a region related to
Bcr, Vav, Dbl and CDC24.";
EMBO J. 11:4007-4015(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 791-1262.
STRAIN=SWR/J; TISSUE=Brain;
PubMed=1376246;
Martegani E., Vanoni M., Zippel R., Coccetti P., Brambilla R.,
Ferrari C., Sturani E.P., Alberghina L.;
"Cloning by functional complementation of a mouse cDNA encoding a
homologue of CDC25, a Saccharomyces cerevisiae RAS activator.";
EMBO J. 11:2151-2157(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1031-1226.
PubMed=1379731; DOI=10.1073/pnas.89.15.7100;
Wei W., Mosteller R.D., Sanyal P., Gonzales E., McKinney D.,
Dasgupta C., Li P., Liu B.-X., Broek D.;
"Identification of a mammalian gene structurally and functionally
related to the CDC25 gene of Saccharomyces cerevisiae.";
Proc. Natl. Acad. Sci. U.S.A. 89:7100-7104(1992).
[4]
FUNCTION, OLIGOMERIZATION, INTERACTION WITH RASGRF2, AND MUTAGENESIS
OF LEU-263 AND 394-LEU--LEU-400.
PubMed=10373510; DOI=10.1128/MCB.19.7.4611;
Anborgh P.H., Qian X., Papageorge A.G., Vass W.C., DeClue J.E.,
Lowy D.R.;
"Ras-specific exchange factor GRF: oligomerization through its Dbl
homology domain and calcium-dependent activation of Raf.";
Mol. Cell. Biol. 19:4611-4622(1999).
[5]
UBIQUITINATION, AND INTERACTION WITH USP8.
PubMed=11500497; DOI=10.1074/jbc.M103454200;
Gnesutta N., Ceriani M., Innocenti M., Mauri I., Zippel R.,
Sturani E., Borgonovo B., Berruti G., Martegani E.;
"Cloning and characterization of mouse UBPy, a deubiquitinating enzyme
that interacts with the ras guanine nucleotide exchange factor
CDC25(Mm)/Ras-GRF1.";
J. Biol. Chem. 276:39448-39454(2001).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-745, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Promotes the exchange of Ras-bound GDP by GTP.
{ECO:0000269|PubMed:10373510}.
-!- SUBUNIT: Homooligomer and heterooligomer with RASGRF2. Interacts
with USP8, thereby regulating its stability.
{ECO:0000269|PubMed:10373510, ECO:0000269|PubMed:11500497}.
-!- INTERACTION:
P01112:HRAS (xeno); NbExp=2; IntAct=EBI-645522, EBI-350145;
P35739:Ntrk1 (xeno); NbExp=3; IntAct=EBI-645522, EBI-976667;
Q63604:Ntrk2 (xeno); NbExp=2; IntAct=EBI-645522, EBI-7287667;
Q03351:Ntrk3 (xeno); NbExp=2; IntAct=EBI-645522, EBI-7365348;
-!- TISSUE SPECIFICITY: Brain.
-!- DOMAIN: The DH (DBL-homology) domain mediates interaction with
RASGRF2.
-!- PTM: Phosphorylated by PLK2, leading to ubiquitination and
degradation by the proteasome. {ECO:0000250}.
-!- PTM: Ubiquitinated and degraded following phosphorylation by PLK2.
{ECO:0000305|PubMed:11500497}.
-!- PTM: Phosphorylated by SRC and LCK. Phosphorylation by LCK
increases its capacity to stimulate the GDP/GTP exchange on Ras,
whereas its phosphorylation by SRC seems not to have an effect on
stimulation activity (By similarity). {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; L20899; AAA02741.1; -; mRNA.
EMBL; X59868; CAA42525.1; -; mRNA.
CCDS; CCDS40722.1; -.
PIR; S28407; S28407.
RefSeq; NP_035375.1; NM_011245.2.
UniGene; Mm.44561; -.
PDB; 2IJE; X-ray; 2.20 A; S=1028-1262.
PDBsum; 2IJE; -.
ProteinModelPortal; P27671; -.
SMR; P27671; -.
BioGrid; 202600; 4.
DIP; DIP-41194N; -.
ELM; P27671; -.
IntAct; P27671; 5.
MINT; P27671; -.
STRING; 10090.ENSMUSP00000034912; -.
iPTMnet; P27671; -.
PhosphoSitePlus; P27671; -.
MaxQB; P27671; -.
PaxDb; P27671; -.
PRIDE; P27671; -.
Ensembl; ENSMUST00000034912; ENSMUSP00000034912; ENSMUSG00000032356.
GeneID; 19417; -.
KEGG; mmu:19417; -.
UCSC; uc009qzt.1; mouse.
CTD; 5923; -.
MGI; MGI:99694; Rasgrf1.
eggNOG; ENOG410IQ6Q; Eukaryota.
eggNOG; ENOG410XPWA; LUCA.
GeneTree; ENSGT00910000143985; -.
HOGENOM; HOG000046000; -.
HOVERGEN; HBG005208; -.
InParanoid; P27671; -.
KO; K04349; -.
OMA; DPGDNQI; -.
OrthoDB; EOG091G09V6; -.
PhylomeDB; P27671; -.
TreeFam; TF317296; -.
Reactome; R-MMU-442982; Ras activation upon Ca2+ influx through NMDA receptor.
Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
ChiTaRS; Rasgrf1; mouse.
EvolutionaryTrace; P27671; -.
PRO; PR:P27671; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032356; -.
ExpressionAtlas; P27671; baseline and differential.
Genevisible; P27671; MM.
GO; GO:0097440; C:apical dendrite; ISO:MGI.
GO; GO:0016327; C:apicolateral plasma membrane; ISO:MGI.
GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; IDA:HGNC.
GO; GO:0030426; C:growth cone; IDA:HGNC.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0035254; F:glutamate receptor binding; IPI:MGI.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0017016; F:Ras GTPase binding; ISO:MGI.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; ISO:MGI.
GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:MGI.
GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
GO; GO:0090630; P:activation of GTPase activity; IDA:HGNC.
GO; GO:0008283; P:cell proliferation; IMP:MGI.
GO; GO:0031175; P:neuron projection development; IDA:HGNC.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:MGI.
GO; GO:0043547; P:positive regulation of GTPase activity; IDA:HGNC.
GO; GO:0046579; P:positive regulation of Ras protein signal transduction; ISS:UniProtKB.
GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IMP:MGI.
GO; GO:2000310; P:regulation of NMDA receptor activity; IGI:MGI.
GO; GO:0035020; P:regulation of Rac protein signal transduction; IDA:HGNC.
GO; GO:0046578; P:regulation of Ras protein signal transduction; IDA:HGNC.
GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:MGI.
GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
CDD; cd00155; RasGEF; 1.
CDD; cd00160; RhoGEF; 1.
Gene3D; 1.10.840.10; -; 1.
Gene3D; 1.20.900.10; -; 1.
Gene3D; 2.30.29.30; -; 2.
InterPro; IPR035899; DBL_dom_sf.
InterPro; IPR000219; DH-domain.
InterPro; IPR001331; GDS_CDC24_CS.
InterPro; IPR000048; IQ_motif_EF-hand-BS.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
InterPro; IPR023578; Ras_GEF_dom_sf.
InterPro; IPR001895; RASGEF_cat_dom.
InterPro; IPR036964; RASGEF_cat_dom_sf.
InterPro; IPR030745; RasGRF1.
PANTHER; PTHR23113:SF193; PTHR23113:SF193; 1.
Pfam; PF00169; PH; 2.
Pfam; PF00617; RasGEF; 1.
Pfam; PF00618; RasGEF_N; 1.
Pfam; PF00621; RhoGEF; 1.
SMART; SM00233; PH; 2.
SMART; SM00147; RasGEF; 1.
SMART; SM00229; RasGEFN; 2.
SMART; SM00325; RhoGEF; 1.
SUPFAM; SSF48065; SSF48065; 1.
SUPFAM; SSF48366; SSF48366; 2.
PROSITE; PS00741; DH_1; 1.
PROSITE; PS50010; DH_2; 1.
PROSITE; PS50096; IQ; 1.
PROSITE; PS50003; PH_DOMAIN; 2.
PROSITE; PS00720; RASGEF; 1.
PROSITE; PS50009; RASGEF_CAT; 1.
PROSITE; PS50212; RASGEF_NTER; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Guanine-nucleotide releasing factor;
Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
CHAIN 1 1262 Ras-specific guanine nucleotide-releasing
factor 1.
/FTId=PRO_0000068881.
DOMAIN 22 130 PH 1. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 208 233 IQ. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 244 430 DH. {ECO:0000255|PROSITE-
ProRule:PRU00062}.
DOMAIN 460 588 PH 2. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 635 749 N-terminal Ras-GEF. {ECO:0000255|PROSITE-
ProRule:PRU00135}.
DOMAIN 1027 1259 Ras-GEF. {ECO:0000255|PROSITE-
ProRule:PRU00168}.
MOD_RES 71 71 Phosphoserine; by PLK2.
{ECO:0000250|UniProtKB:P28818}.
MOD_RES 581 581 Phosphoserine; by PLK2.
{ECO:0000250|UniProtKB:P28818}.
MOD_RES 617 617 Phosphoserine; by PLK2.
{ECO:0000250|UniProtKB:P28818}.
MOD_RES 745 745 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 766 766 Phosphoserine; by PLK2.
{ECO:0000250|UniProtKB:P28818}.
MUTAGEN 263 263 L->Q: Loss of function and
oligomerization.
{ECO:0000269|PubMed:10373510}.
MUTAGEN 394 400 LTLHELL->IIIRDII: Partial loss of
function. No effect on oligomerization.
{ECO:0000269|PubMed:10373510}.
CONFLICT 1033 1033 E -> D (in Ref. 3). {ECO:0000305}.
HELIX 1028 1044 {ECO:0000244|PDB:2IJE}.
HELIX 1048 1057 {ECO:0000244|PDB:2IJE}.
HELIX 1061 1064 {ECO:0000244|PDB:2IJE}.
HELIX 1066 1087 {ECO:0000244|PDB:2IJE}.
HELIX 1092 1111 {ECO:0000244|PDB:2IJE}.
HELIX 1115 1125 {ECO:0000244|PDB:2IJE}.
HELIX 1128 1131 {ECO:0000244|PDB:2IJE}.
HELIX 1134 1138 {ECO:0000244|PDB:2IJE}.
HELIX 1142 1154 {ECO:0000244|PDB:2IJE}.
HELIX 1158 1169 {ECO:0000244|PDB:2IJE}.
HELIX 1179 1192 {ECO:0000244|PDB:2IJE}.
HELIX 1204 1222 {ECO:0000244|PDB:2IJE}.
HELIX 1231 1238 {ECO:0000244|PDB:2IJE}.
HELIX 1246 1256 {ECO:0000244|PDB:2IJE}.
SEQUENCE 1262 AA; 144102 MW; 38BFE68F7C228DC8 CRC64;
MQKAIRLNDG HVVTLGLLAQ KDGTRKGYLS KRSADNPKWQ TKWFALLQNL LFYFESDSSP
RPSGLYLLEG SICKRAPSPK RGTSSKESGE KQQHYFTVNF SNDSQKTLEL RTEDAKDCDE
WVAAIARASY KILATEHEAL MQKYLHLLQV VETEKTVAKQ LRQQLEDGEV EIERLKTEVT
ITNLIKDNDR IQSSNKAGSA DDEDSDIKKI KKVQSFLRGW LCRRKWKNII QDYIRSPHAD
SMRKRNQVVF SMLEAEAEYV QQLHILVNNF LRPLRMAASS KKPPITHDDV SSIFLNSETI
MFLHQIFYQG LKARISSWPT LVLADLFDIL LPMLNIYQEF VRNHQYSLQI LAHCKQNRDF
DKLLKQYEAK PDCEERTLET FLTYPMFQIP RYILTLHELL AHTPHEHVER NSLDYAKSKL
EELSRIMHDE VSETENIRKN LAIERMITEG CEILLDTSQT FVRQGSLMQM SLSEKSKSSR
GRLGSLSTKK EGERQCFLFS KHLIICTRGS GGKLHLTKNG VISLIDCTLL DEPENLDDEA
KGAGPEIEHL EFKIGVEPKD SLPFTVILVA STRQEKAAWT SDIIQCVDNI RCNGLMMNAF
EENSKVTVPQ MIKSDASLYC DDVDIRFSKT MNSCKVLQIR YASVERLLER LTDLRFLSID
FLNTFLHSYR VFTNAMVVLD KLINIYRKPM SAIPARSLEL LFSSSHNAKL LYGDAPKSPR
ASRKFSSPPP LAIGTSSPSR RRKLSLNIPI ITGGKALELA SLGCSSDSYA NIHSPISPFG
KTTLDTGKLC MASSLPKTPE EIDVPATIPE KPGELSASRK HSSDVLKEES EDDQNHSDED
NTEVSPVKSP PTPKSFLNRT ITEFPFFNYN NGILMTTCRD LVDNNRSTLS ATSAFAIATA
GANEGPSNKE VFRRMSLANT GFSSDQRNID KEFVIRRAAT NRVLNVLRHW VTKHTQDFDT
DDTLKYRVIC FLEEVMHDPD LLTQERKAAA NIIRTLTLEE TTEQHSMLEE VILMTEGVKT
EPFENHPALE IAEQLTLLDH LVFKSIPYEE FFGQGWMKAE KYERTPYIMK TTKHFNHVSN
FIASEIIRNE DISARASAIE KWVAVADICR CLHNYNAVLE ITSSINRSAI FRLKKTWLKV
SKQTKSLLDK LQKLVSSDGR FKNLRESLRN CDPPCVPYLG MYLTDLVFIE EGTPNYTEDG
LVNFSKMRMI SHIIREIRQF QQTTYKIDPQ PKVIQYLLDE SFMLDEESLY ESSLLIEPKL
PT


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