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Ras-related C3 botulinum toxin substrate 1 (p21-Rac1)

 RAC1_MOUSE              Reviewed;         192 AA.
P63001; O95501; P15154; Q9BTB4;
31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
31-AUG-2004, sequence version 1.
25-OCT-2017, entry version 157.
RecName: Full=Ras-related C3 botulinum toxin substrate 1;
AltName: Full=p21-Rac1;
Flags: Precursor;
Name=Rac1;
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], AND TISSUE SPECIFICITY.
TISSUE=Thymus;
PubMed=1905006;
Moll J., Sansig G., Fattori E., van der Putten H.;
"The murine rac1 gene: cDNA cloning, tissue distribution and regulated
expression of rac1 mRNA by disassembly of actin microfilaments.";
Oncogene 6:863-866(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Head, Liver, Thymus, and Tongue;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH RASGRF2.
PubMed=9707409; DOI=10.1016/S0960-9822(07)00376-4;
Fan W.-T., Koch C.A., de Hoog C.L., Fam N.P., Moran M.F.;
"The exchange factor Ras-GRF2 activates Ras-dependent and Rac-
dependent mitogen-activated protein kinase pathways.";
Curr. Biol. 8:935-938(1998).
[5]
INTERACTION WITH PARD6A, AND MUTAGENESIS OF GLY-12.
PubMed=10934474; DOI=10.1038/35019573;
Joberty G., Petersen C., Gao L., Macara I.G.;
"The cell-polarity protein Par6 links Par3 and atypical protein kinase
C to Cdc42.";
Nat. Cell Biol. 2:531-539(2000).
[6]
INTERACTION WITH PARD6B.
PubMed=10934475; DOI=10.1038/35019582;
Lin D., Edwards A.S., Fawcett J.P., Mbamalu G., Scott J.D., Pawson T.;
"A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac1 and aPKC
signalling and cell polarity.";
Nat. Cell Biol. 2:540-547(2000).
[7]
INTERACTION WITH PIP5K1A.
PubMed=10679324; DOI=10.1016/S0960-9822(00)00315-8;
Tolias K.F., Hartwig J.H., Ishihara H., Shibasaki Y., Cantley L.C.,
Carpenter C.L.;
"Type Ialpha phosphatidylinositol-4-phosphate 5-kinase mediates Rac-
dependent actin assembly.";
Curr. Biol. 10:153-156(2000).
[8]
INTERACTION WITH MAP3K3; MAP2K3 AND CCM2.
PubMed=14634666; DOI=10.1038/ncb1071;
Uhlik M.T., Abell A.N., Johnson N.L., Sun W., Cuevas B.D.,
Lobel-Rice K.E., Horne E.A., Dell'Acqua M.L., Johnson G.L.;
"Rac-MEKK3-MKK3 scaffolding for p38 MAPK activation during
hyperosmotic shock.";
Nat. Cell Biol. 5:1104-1110(2003).
[9]
INTERACTION WITH NISCH.
PubMed=16002401; DOI=10.1074/jbc.M502546200;
Reddig P.J., Xu D., Juliano R.L.;
"Regulation of p21-activated kinase-independent Rac1 signal
transduction by Nischarin.";
J. Biol. Chem. 280:30994-31002(2005).
[10]
INTERACTION WITH PKN2.
PubMed=17403031; DOI=10.1111/j.1471-4159.2007.04485.x;
Bourguignon L.Y., Gilad E., Peyrollier K., Brightman A., Swanson R.A.;
"Hyaluronan-CD44 interaction stimulates Rac1 signaling and PKN gamma
kinase activation leading to cytoskeleton function and cell migration
in astrocytes.";
J. Neurochem. 101:1002-1017(2007).
[11]
FUNCTION.
PubMed=19029984; DOI=10.1038/nm.1879;
Shibata S., Nagase M., Yoshida S., Kawarazaki W., Kurihara H.,
Tanaka H., Miyoshi J., Takai Y., Fujita T.;
"Modification of mineralocorticoid receptor function by Rac1 GTPase:
implication in proteinuric kidney disease.";
Nat. Med. 14:1370-1376(2008).
[12]
INTERACTION WITH SRGAP2, AND ENZYME REGULATION.
PubMed=19737524; DOI=10.1016/j.cell.2009.06.047;
Guerrier S., Coutinho-Budd J., Sassa T., Gresset A., Jordan N.V.,
Chen K., Jin W.L., Frost A., Polleux F.;
"The F-BAR domain of srGAP2 induces membrane protrusions required for
neuronal migration and morphogenesis.";
Cell 138:990-1004(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
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).
[14]
INTERACTION WITH PLXNB3.
PubMed=20696765; DOI=10.1074/jbc.M110.120451;
Li X., Lee A.Y.;
"Semaphorin 5A and plexin-B3 inhibit human glioma cell motility
through RhoGDIalpha-mediated inactivation of Rac1 GTPase.";
J. Biol. Chem. 285:32436-32445(2010).
[15]
INTERACTION WITH PKN2.
PubMed=20974804; DOI=10.1128/MCB.01001-10;
Wallace S.W., Magalhaes A., Hall A.;
"The Rho target PRK2 regulates apical junction formation in human
bronchial epithelial cells.";
Mol. Cell. Biol. 31:81-91(2011).
-!- FUNCTION: Plasma membrane-associated small GTPase which cycles
between active GTP-bound and inactive GDP-bound states. In its
active state, binds to a variety of effector proteins to regulate
cellular responses such as secretory processes, phagocytosis of
apoptotic cells, epithelial cell polarization and growth-factor
induced formation of membrane ruffles. Rac1 p21/rho GDI
heterodimer is the active component of the cytosolic factor sigma
1, which is involved in stimulation of the NADPH oxidase activity
in macrophages. Essential for the SPATA13-mediated regulation of
cell migration and adhesion assembly and disassembly. Stimulates
PKN2 kinase activity. In concert with RAB7A, plays a role in
regulating the formation of RBs (ruffled borders) in osteoclasts.
In glioma cells, promotes cell migration and invasion. Required
for atypical chemokine receptor ACKR2-induced LIMK1-PAK1-dependent
phosphorylation of cofilin (CFL1) and for up-regulation of ACKR2
from endosomal compartment to cell membrane, increasing its
efficiency in chemokine uptake and degradation. In podocytes,
promotes nuclear shuttling of NR3C2; this modulation is required
for a proper kidney functioning. In synapses, seems to mediate the
regulation of F-actin cluster formation performed by SHANK3.
{ECO:0000269|PubMed:19029984}.
-!- ENZYME REGULATION: Regulated by guanine nucleotide exchange
factors (GEFs) which promote the exchange of bound GDP for free
GTP, GTPase activating proteins (GAPs) which increase the GTP
hydrolysis activity, and GDP dissociation inhibitors which inhibit
the dissociation of the nucleotide from the GTPase. GTP hydrolysis
is stimulated by ARHGAP30 (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with the GEF proteins PREX1, FARP1, FARP2,
DOCK1, DOCK2 and DOCK7, which promote the exchange between GDP and
GTP, and therefore activate it. Part of a quaternary complex
containing PARD3, some PARD6 protein (PARD6A, PARD6B or PARD6G)
and some atypical PKC protein (PRKCI or PRKCZ), which plays a
central role in epithelial cell polarization. Found in a trimeric
complex composed of DOCK1 and ELMO1, which plays a central role in
phagocytosis of apoptotic cells. Interacts with RALBP1 via its
effector domain. Interacts with BAIAP2, BAIAP2L1, PLXNB1,
CYFIP1/SRA-1 and DEF6. Probably found in a ternary complex
composed of DSCAM, PAK1 and RAC1. Interacts with DSCAM; the
interaction requires PAK1. Interacts with TBC1D2. Interacts with
UNKL. Interacts with USP6. Interacts with SPATA13. Interacts with
ITGB4. Interacts with the GTP-bound form of RAB7A. Interacts with
ARHGEF2. Interacts with ARHGEF16; mediates activation of RAC1 by
EPHA2. Interacts with NOXA1. Interacts with S100A8 and
calprotectin (S100A8/9). Interacts with ARHGDIA; the interaction
is induced by SEMA5A, mediated through PLXNB3 and inactivates and
stabilizes RAC1. Interacts with PACSIN2. Interacts with ITGB1BP1
(By similarity). Interacts with the GEF protein RASGRF2, which
promotes the exchange between GDP and GTP, and therefore activates
it. Interacts with PARD6A, PARD6B and PARD6G in a GTP-dependent
manner. Part of a complex with MAP2K3, MAP3K3 and CCM2. Interacts
with NISCH. Interacts with PIP5K1A. Interacts (GTP-bound form
preferentially) with PKN2 (via the REM repeats); the interaction
stimulates autophosphorylation and phosphorylation of PKN2.
Interacts with SRGAP2. Interacts with PLXNB3. Interacts (when
active) with PPP5C (via TPR repeats); activates PPP5C phosphatase
activity and translocates PPP5C to the cell membrane. Interacts
with RAPH1 (via Ras associating and PH domains) (By similarity).
Interacts with MTSS1L (via IMD domain); this interaction may be
important to potentiate PDGF-induced RAC1 activation (By
similarity). {ECO:0000250|UniProtKB:P63000,
ECO:0000269|PubMed:10679324, ECO:0000269|PubMed:10934474,
ECO:0000269|PubMed:10934475, ECO:0000269|PubMed:14634666,
ECO:0000269|PubMed:16002401, ECO:0000269|PubMed:17403031,
ECO:0000269|PubMed:19737524, ECO:0000269|PubMed:20696765,
ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:9707409}.
-!- INTERACTION:
Q62108:Dlg4; NbExp=2; IntAct=EBI-413646, EBI-300895;
Q13153:PAK1 (xeno); NbExp=3; IntAct=EBI-413646, EBI-1307;
P08228:Sod1; NbExp=4; IntAct=EBI-413646, EBI-1635090;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor
{ECO:0000250}; Cytoplasmic side {ECO:0000250}. Melanosome
{ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Inner surface of
plasma membrane possibly with attachment requiring prenylation of
the C-terminal cysteine. Found in the ruffled border (a late
endosomal-like compartment in the plasma membrane) of bone-
resorbing osteoclasts (By similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:1905006}.
-!- DOMAIN: The effector region mediates interaction with DEF6.
{ECO:0000250}.
-!- PTM: GTP-bound active form is ubiquitinated by HACE1, leading to
its degradation by the proteasome. {ECO:0000250}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
{ECO:0000305}.
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EMBL; X57277; CAA40545.1; -; mRNA.
EMBL; AK009017; BAB26027.1; -; mRNA.
EMBL; AK011072; BAB69451.1; -; mRNA.
EMBL; AK034601; BAC28767.1; -; mRNA.
EMBL; AK047969; BAC33203.1; -; mRNA.
EMBL; AK088825; BAC40596.1; -; mRNA.
EMBL; BC003828; AAH03828.1; -; mRNA.
EMBL; BC051053; AAH51053.1; -; mRNA.
CCDS; CCDS19843.1; -.
PIR; A60347; A60347.
RefSeq; NP_033033.1; NM_009007.2.
UniGene; Mm.292510; -.
UniGene; Mm.469963; -.
UniGene; Mm.475073; -.
ProteinModelPortal; P63001; -.
SMR; P63001; -.
BioGrid; 202556; 27.
CORUM; P63001; -.
DIP; DIP-31545N; -.
IntAct; P63001; 29.
MINT; MINT-1602774; -.
STRING; 10090.ENSMUSP00000079380; -.
BindingDB; P63001; -.
ChEMBL; CHEMBL5628; -.
iPTMnet; P63001; -.
PhosphoSitePlus; P63001; -.
SwissPalm; P63001; -.
EPD; P63001; -.
MaxQB; P63001; -.
PaxDb; P63001; -.
PRIDE; P63001; -.
Ensembl; ENSMUST00000080537; ENSMUSP00000079380; ENSMUSG00000001847.
GeneID; 19353; -.
KEGG; mmu:19353; -.
UCSC; uc009akk.1; mouse.
CTD; 5879; -.
MGI; MGI:97845; Rac1.
eggNOG; KOG0393; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00760000118978; -.
HOGENOM; HOG000233974; -.
HOVERGEN; HBG009351; -.
InParanoid; P63001; -.
KO; K04392; -.
PhylomeDB; P63001; -.
TreeFam; TF101109; -.
Reactome; R-MMU-114604; GPVI-mediated activation cascade.
Reactome; R-MMU-1433557; Signaling by SCF-KIT.
Reactome; R-MMU-1445148; Translocation of GLUT4 to the plasma membrane.
Reactome; R-MMU-193648; NRAGE signals death through JNK.
Reactome; R-MMU-194840; Rho GTPase cycle.
Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-MMU-2424491; DAP12 signaling.
Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
Reactome; R-MMU-376172; DSCAM interactions.
Reactome; R-MMU-389359; CD28 dependent Vav1 pathway.
Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
Reactome; R-MMU-3928664; Ephrin signaling.
Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
Reactome; R-MMU-399954; Sema3A PAK dependent Axon repulsion.
Reactome; R-MMU-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
Reactome; R-MMU-4086400; PCP/CE pathway.
Reactome; R-MMU-416482; G alpha (12/13) signalling events.
Reactome; R-MMU-416550; Sema4D mediated inhibition of cell attachment and migration.
Reactome; R-MMU-416572; Sema4D induced cell migration and growth-cone collapse.
Reactome; R-MMU-418885; DCC mediated attractive signaling.
Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-MMU-445144; Signal transduction by L1.
Reactome; R-MMU-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-MMU-5625900; RHO GTPases activate CIT.
Reactome; R-MMU-5625970; RHO GTPases activate KTN1.
Reactome; R-MMU-5626467; RHO GTPases activate IQGAPs.
Reactome; R-MMU-5627123; RHO GTPases activate PAKs.
Reactome; R-MMU-5663213; RHO GTPases Activate WASPs and WAVEs.
Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
Reactome; R-MMU-5668599; RHO GTPases Activate NADPH Oxidases.
Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
Reactome; R-MMU-8875555; MET activates RAP1 and RAC1.
Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
ChiTaRS; Rac1; mouse.
PRO; PR:P63001; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000001847; -.
CleanEx; MM_RAC1; -.
ExpressionAtlas; P63001; baseline and differential.
Genevisible; P63001; MM.
GO; GO:0042995; C:cell projection; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0043197; C:dendritic spine; ISO:MGI.
GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0031012; C:extracellular matrix; ISO:MGI.
GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0060091; C:kinocilium; IDA:MGI.
GO; GO:0030027; C:lamellipodium; IDA:MGI.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000242; C:pericentriolar material; IDA:MGI.
GO; GO:0001891; C:phagocytic cup; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0005525; F:GTP binding; IDA:MGI.
GO; GO:0030742; F:GTP-dependent protein binding; IPI:UniProtKB.
GO; GO:0003924; F:GTPase activity; IDA:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0051022; F:Rho GDP-dissociation inhibitor binding; ISS:UniProtKB.
GO; GO:0031996; F:thioesterase binding; ISO:MGI.
GO; GO:0030036; P:actin cytoskeleton organization; ISO:MGI.
GO; GO:0030041; P:actin filament polymerization; IDA:MGI.
GO; GO:0048532; P:anatomical structure arrangement; IMP:MGI.
GO; GO:0002093; P:auditory receptor cell morphogenesis; IMP:MGI.
GO; GO:0007411; P:axon guidance; IMP:MGI.
GO; GO:0007155; P:cell adhesion; IDA:MGI.
GO; GO:0016477; P:cell migration; IDA:MGI.
GO; GO:0048870; P:cell motility; ISS:UniProtKB.
GO; GO:0045216; P:cell-cell junction organization; IMP:MGI.
GO; GO:0021894; P:cerebral cortex GABAergic interneuron development; IGI:MGI.
GO; GO:0021799; P:cerebral cortex radially oriented cell migration; IMP:MGI.
GO; GO:0090103; P:cochlea morphogenesis; IMP:MGI.
GO; GO:0007010; P:cytoskeleton organization; IDA:MGI.
GO; GO:0016358; P:dendrite development; IDA:MGI.
GO; GO:0048813; P:dendrite morphogenesis; IGI:MGI.
GO; GO:0071542; P:dopaminergic neuron differentiation; IGI:MGI.
GO; GO:0021831; P:embryonic olfactory bulb interneuron precursor migration; IMP:MGI.
GO; GO:0006897; P:endocytosis; IDA:MGI.
GO; GO:0043652; P:engulfment of apoptotic cell; IDA:BHF-UCL.
GO; GO:0003382; P:epithelial cell morphogenesis; IMP:MGI.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IGI:MGI.
GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; ISO:MGI.
GO; GO:0048873; P:homeostasis of number of cells within a tissue; IGI:MGI.
GO; GO:0006972; P:hyperosmotic response; IDA:MGI.
GO; GO:0030032; P:lamellipodium assembly; IDA:MGI.
GO; GO:0051668; P:localization within membrane; ISO:MGI.
GO; GO:1904948; P:midbrain dopaminergic neuron differentiation; IMP:ParkinsonsUK-UCL.
GO; GO:0032707; P:negative regulation of interleukin-23 production; ISO:MGI.
GO; GO:0048812; P:neuron projection morphogenesis; IGI:ParkinsonsUK-UCL.
GO; GO:0035567; P:non-canonical Wnt signaling pathway; IGI:ParkinsonsUK-UCL.
GO; GO:0006911; P:phagocytosis, engulfment; IMP:UniProtKB.
GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:MGI.
GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISO:MGI.
GO; GO:0060999; P:positive regulation of dendritic spine development; IMP:MGI.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISO:MGI.
GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISO:MGI.
GO; GO:0031116; P:positive regulation of microtubule polymerization; ISO:MGI.
GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IMP:UniProtKB.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IMP:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
GO; GO:0072659; P:protein localization to plasma membrane; IDA:MGI.
GO; GO:0030334; P:regulation of cell migration; IMP:MGI.
GO; GO:0022604; P:regulation of cell morphogenesis; IGI:MGI.
GO; GO:0008361; P:regulation of cell size; ISO:MGI.
GO; GO:0010762; P:regulation of fibroblast migration; IMP:UniProtKB.
GO; GO:0010591; P:regulation of lamellipodium assembly; ISO:MGI.
GO; GO:0014041; P:regulation of neuron maturation; IGI:MGI.
GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IMP:MGI.
GO; GO:0060263; P:regulation of respiratory burst; ISO:MGI.
GO; GO:0051492; P:regulation of stress fiber assembly; ISO:MGI.
GO; GO:0097178; P:ruffle assembly; IMP:UniProtKB.
GO; GO:0031529; P:ruffle organization; ISO:MGI.
GO; GO:0071526; P:semaphorin-plexin signaling pathway; ISS:UniProtKB.
GO; GO:0007264; P:small GTPase mediated signal transduction; IDA:MGI.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:MGI.
GO; GO:0051932; P:synaptic transmission, GABAergic; IGI:MGI.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IGI:MGI.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR003578; Small_GTPase_Rho.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51420; RHO; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Cytoplasm; GTP-binding;
Isopeptide bond; Lipoprotein; Membrane; Methylation;
Nucleotide-binding; Prenylation; Reference proteome; Ubl conjugation.
CHAIN 1 189 Ras-related C3 botulinum toxin substrate
1.
/FTId=PRO_0000042038.
PROPEP 190 192 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000042039.
NP_BIND 10 17 GTP. {ECO:0000250}.
NP_BIND 57 61 GTP. {ECO:0000250}.
NP_BIND 115 118 GTP. {ECO:0000250}.
MOTIF 32 40 Effector region. {ECO:0000255}.
MOD_RES 189 189 Cysteine methyl ester. {ECO:0000250}.
LIPID 189 189 S-geranylgeranyl cysteine. {ECO:0000250}.
CROSSLNK 147 147 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P63000}.
MUTAGEN 12 12 G->V: Constitutively active. Interacts
with PARD6 proteins.
{ECO:0000269|PubMed:10934474}.
SEQUENCE 192 AA; 21450 MW; ACEDF83A45E5EA67 CRC64;
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP VNLGLWDTAG
QEDYDRLRPL SYPQTDVFLI CFSLVSPASF ENVRAKWYPE VRHHCPNTPI ILVGTKLDLR
DDKDTIEKLK EKKLTPITYP QGLAMAKEIG AVKYLECSAL TQRGLKTVFD EAIRAVLCPP
PVKKRKRKCL LL


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