RAC1_RAT
ID RAC1_RAT Reviewed; 192 AA.
AC Q6RUV5;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Ras-related C3 botulinum toxin substrate 1 {ECO:0000305};
DE EC=3.6.5.2 {ECO:0000269|PubMed:25498153};
DE AltName: Full=p21-Rac1;
DE Flags: Precursor;
GN Name=Rac1 {ECO:0000312|RGD:619755};
GN Synonyms=Rac {ECO:0000303|PubMed:15800193};
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH RAB7A.
RC STRAIN=Wistar; TISSUE=Bone marrow;
RX PubMed=16040606; DOI=10.1074/jbc.m414213200;
RA Sun Y., Bueki K.G., Ettala O., Vaeaeraeniemi J.P., Vaeaenaenen H.K.;
RT "Possible role of direct Rac1-Rab7 interaction in ruffled border formation
RT of osteoclasts.";
RL J. Biol. Chem. 280:32356-32361(2005).
RN [2]
RP PROTEIN SEQUENCE OF 6-16; 103-116; 133-147; 154-163 AND 167-183, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [3]
RP FUNCTION.
RX PubMed=12695502; DOI=10.1083/jcb.200211002;
RA Zhang H., Webb D.J., Asmussen H., Horwitz A.F.;
RT "Synapse formation is regulated by the signaling adaptor GIT1.";
RL J. Cell Biol. 161:131-142(2003).
RN [4]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-12.
RX PubMed=15800193; DOI=10.1523/jneurosci.3553-04.2005;
RA Zhang H., Webb D.J., Asmussen H., Niu S., Horwitz A.F.;
RT "A GIT1/PIX/Rac/PAK signaling module regulates spine morphogenesis and
RT synapse formation through MLC.";
RL J. Neurosci. 25:3379-3388(2005).
RN [5]
RP FUNCTION, INTERACTION WITH PPP5C, AND MUTAGENESIS OF GLN-61.
RX PubMed=16549782; DOI=10.1073/pnas.0600080103;
RA Gentile S., Darden T., Erxleben C., Romeo C., Russo A., Martin N.,
RA Rossie S., Armstrong D.L.;
RT "Rac GTPase signaling through the PP5 protein phosphatase.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5202-5206(2006).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF GLY-12.
RX PubMed=19029984; DOI=10.1038/nm.1879;
RA Shibata S., Nagase M., Yoshida S., Kawarazaki W., Kurihara H., Tanaka H.,
RA Miyoshi J., Takai Y., Fujita T.;
RT "Modification of mineralocorticoid receptor function by Rac1 GTPase:
RT implication in proteinuric kidney disease.";
RL Nat. Med. 14:1370-1376(2008).
RN [7]
RP FUNCTION, INTERACTION WITH PLXNB3 AND ARHGDIA, AND SUBCELLULAR LOCATION.
RX PubMed=20696765; DOI=10.1074/jbc.m110.120451;
RA Li X., Lee A.Y.;
RT "Semaphorin 5A and plexin-B3 inhibit human glioma cell motility through
RT RhoGDIalpha-mediated inactivation of Rac1 GTPase.";
RL J. Biol. Chem. 285:32436-32445(2010).
RN [8]
RP INTERACTION WITH SH3RF2.
RX PubMed=22128169; DOI=10.1074/jbc.m111.269431;
RA Wilhelm M., Kukekov N.V., Schmit T.L., Biagas K.V., Sproul A.A., Gire S.,
RA Maes M.E., Xu Z., Greene L.A.;
RT "Sh3rf2/POSHER protein promotes cell survival by RING-mediated proteasomal
RT degradation of the c-Jun N-terminal kinase scaffold POSH (Plenty of SH3s)
RT protein.";
RL J. Biol. Chem. 287:2247-2256(2012).
RN [9]
RP FUNCTION IN ACTIN POLYMERIZATION, AND MUTAGENESIS OF THR-17 AND GLN-61.
RX PubMed=24089484; DOI=10.1523/jneurosci.1175-13.2013;
RA Duffney L.J., Wei J., Cheng J., Liu W., Smith K.R., Kittler J.T., Yan Z.;
RT "Shank3 deficiency induces NMDA receptor hypofunction via an actin-
RT dependent mechanism.";
RL J. Neurosci. 33:15767-15778(2013).
RN [10]
RP FUNCTION.
RX PubMed=25284783; DOI=10.1016/j.celrep.2014.08.061;
RA Smith K.R., Davenport E.C., Wei J., Li X., Pathania M., Vaccaro V., Yan Z.,
RA Kittler J.T.;
RT "GIT1 and betaPIX are essential for GABA(A) receptor synaptic stability and
RT inhibitory neurotransmission.";
RL Cell Rep. 9:298-310(2014).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=25498153; DOI=10.7554/elife.03116;
RA Galic M., Tsai F.C., Collins S.R., Matis M., Bandara S., Meyer T.;
RT "Dynamic recruitment of the curvature-sensitive protein ArhGAP44 to
RT nanoscale membrane deformations limits exploratory filopodia initiation in
RT neurons.";
RL Elife 3:E03116-E03116(2014).
CC -!- FUNCTION: Plasma membrane-associated small GTPase which cycles between
CC active GTP-bound and inactive GDP-bound states. In its active state,
CC binds to a variety of effector proteins to regulate cellular responses
CC such as secretory processes, phagocytosis of apoptotic cells,
CC epithelial cell polarization, neurons adhesion, migration and
CC differentiation, and growth-factor induced formation of membrane
CC ruffles (PubMed:16040606, PubMed:16549782). Rac1 p21/rho GDI
CC heterodimer is the active component of the cytosolic factor sigma 1,
CC which is involved in stimulation of the NADPH oxidase activity in
CC macrophages. Essential for the SPATA13-mediated regulation of cell
CC migration and adhesion assembly and disassembly. Stimulates PKN2 kinase
CC activity (By similarity). In concert with RAB7A, plays a role in
CC regulating the formation of RBs (ruffled borders) in osteoclasts
CC (PubMed:16040606). In glioma cells, promotes cell migration and
CC invasion (PubMed:20696765). In podocytes, promotes nuclear shuttling of
CC NR3C2; this modulation is required for a proper kidney functioning
CC (PubMed:19029984). Required for atypical chemokine receptor ACKR2-
CC induced LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1) and for
CC up-regulation of ACKR2 from endosomal compartment to cell membrane,
CC increasing its efficiency in chemokine uptake and degradation (By
CC similarity). In neurons, is involved in dendritic spine formation and
CC synaptic plasticity (PubMed:25498153). In hippocampal neurons, involved
CC in spine morphogenesis and synapse formation, through local activation
CC at synapses by guanine nucleotide exchange factors (GEFs), such as
CC ARHGEF6/ARHGEF7/PIX (PubMed:12695502). In synapses, may mediate the
CC regulation of F-actin cluster formation performed by SHANK3
CC (PubMed:24089484). In neurons, plays a crucial role in regulating
CC GABA(A) receptor synaptic stability and hence GABAergic inhibitory
CC synaptic transmission through its role in PAK1 activation and
CC eventually F-actin stabilization (PubMed:25284783).
CC {ECO:0000250|UniProtKB:P63000, ECO:0000250|UniProtKB:P63001,
CC ECO:0000269|PubMed:12695502, ECO:0000269|PubMed:16040606,
CC ECO:0000269|PubMed:16549782, ECO:0000269|PubMed:19029984,
CC ECO:0000269|PubMed:20696765, ECO:0000269|PubMed:24089484,
CC ECO:0000269|PubMed:25284783, ECO:0000269|PubMed:25498153}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000269|PubMed:25498153};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000305|PubMed:25498153};
CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC (GEFs) which promote the exchange of bound GDP for free GTP, GTPase
CC activating proteins (GAPs) which increase the GTP hydrolysis activity,
CC and GDP dissociation inhibitors which inhibit the dissociation of the
CC nucleotide from the GTPase. GTP hydrolysis is stimulated by ARHGAP30
CC and ARHGAP44. {ECO:0000269|PubMed:25498153}.
CC -!- SUBUNIT: Interacts with NISCH. Interacts with PIP5K1A. Interacts with
CC the GTP-bound form of RAB7A. Interacts with SRGAP2. Interacts with
CC CYFIP1/SRA-1. Interacts with PLXNB3. Interacts with ARHGDIA; the
CC interaction is induced by SEMA5A, mediated through PLXNB3 and
CC inactivates and stabilizes RAC1. Interacts (GTP-bound form
CC preferentially) with PKN2 (via the REM repeats); the interaction
CC stimulates autophosphorylation and phosphorylation of PKN2. Interacts
CC with the GEF proteins PREX1, RASGRF2, FARP1, FARP2, DOCK1, DOCK2 and
CC DOCK7, which promote the exchange between GDP and GTP, and therefore
CC activate it. Interacts with PARD6A, PARD6B and PARD6G in a GTP-
CC dependent manner. Part of a quaternary complex containing PARD3, some
CC PARD6 protein (PARD6A, PARD6B or PARD6G) and some atypical PKC protein
CC (PRKCI or PRKCZ), which plays a central role in epithelial cell
CC polarization. Found in a trimeric complex composed of DOCK1 and ELMO1,
CC which plays a central role in phagocytosis of apoptotic cells.
CC Interacts with RALBP1 via its effector domain. Interacts with PLXNB1.
CC Probably found in a ternary complex composed of DSCAM, PAK1 and RAC1.
CC Interacts with DSCAM; the interaction requires PAK1. Part of a complex
CC with MAP2K3, MAP3K3, CCM2 and DEF6. Interacts with BAIAP2, BAIAP2L1 and
CC DEF6. Interacts with Y.pseudotuberculosis YPKA and PLCB2. Interacts
CC with NOXA1. Interacts with ARHGEF2. Interacts with TBC1D2. Interacts
CC with UNKL. Interacts with USP6. Interacts with SPATA13. Interacts with
CC ARHGEF16; mediates activation of RAC1 by EPHA2. Interacts with ITGB4.
CC Interacts with S100A8 and calprotectin (S100A8/9). Interacts with
CC PACSIN2. Interacts with ITGB1BP1. Interacts (when active) with PPP5C
CC (via TPR repeats); activates PPP5C phosphatase activity and
CC translocates PPP5C to the cell membrane. Interacts with RAPH1 (via Ras
CC associating and PH domains) (By similarity). Interacts with MTSS2 (via
CC IMD domain); this interaction may be important to potentiate PDGF-
CC induced RAC1 activation. Interacts with PAK2. Interacts (GTP-bound
CC form) with SH3RF1 and SH3RF3. Found in a complex with SH3RF1,
CC MAPK8IP1/JIP1, MAP3K11/MLK3, MAP2K7/MKK7 and MAPK8/JNK1 (By
CC similarity). Interacts (both active GTP- or inactive GDP-bound forms)
CC with SH3RF2 (PubMed:22128169). Interacts (GTP-bound form
CC preferentially) with CYRIB (By similarity). Interacts with DOCK4 (via
CC DOCKER domain); functions as a guanine nucleotide exchange factor (GEF)
CC for RAC1 (By similarity). Interacts with GARRE1 (By similarity).
CC Interacts with RAP1GDS1 (By similarity). {ECO:0000250|UniProtKB:P63000,
CC ECO:0000250|UniProtKB:P63001, ECO:0000269|PubMed:16040606,
CC ECO:0000269|PubMed:16549782, ECO:0000269|PubMed:20696765,
CC ECO:0000269|PubMed:22128169}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16040606};
CC Lipid-anchor {ECO:0000269|PubMed:16040606}; Cytoplasmic side
CC {ECO:0000269|PubMed:16040606}. Melanosome
CC {ECO:0000250|UniProtKB:P63000}. Cytoplasm
CC {ECO:0000250|UniProtKB:P63000, ECO:0000250|UniProtKB:P63001}. Cell
CC projection, lamellipodium {ECO:0000250|UniProtKB:P63001}. Cell
CC projection, dendrite {ECO:0000250|UniProtKB:P63001}. Synapse
CC {ECO:0000269|PubMed:15800193}. Nucleus {ECO:0000250|UniProtKB:P63000}.
CC Note=Inner surface of plasma membrane possibly with attachment
CC requiring prenylation of the C-terminal cysteine (By similarity). Found
CC in the ruffled border (a late endosomal-like compartment in the plasma
CC membrane) of bone-resorbing osteoclasts. Localizes to the lamellipodium
CC in a SH3RF1-dependent manner. In macrophages, cytoplasmic location
CC increases upon CSF1 stimulation (By similarity). In hippocampal
CC neurons, localizes at synapses, where it is activated
CC (PubMed:15800193). Activation by GTP-binding promotes nuclear
CC localization (By similarity). {ECO:0000250|UniProtKB:P63000,
CC ECO:0000250|UniProtKB:P63001, ECO:0000269|PubMed:15800193}.
CC -!- TISSUE SPECIFICITY: Osteoclasts. {ECO:0000269|PubMed:16040606}.
CC -!- DOMAIN: The effector region mediates interaction with DEF6.
CC {ECO:0000250|UniProtKB:P63000}.
CC -!- PTM: GTP-bound active form is ubiquitinated by HACE1, leading to its
CC degradation by the proteasome. {ECO:0000250|UniProtKB:P63000}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; AY491395; AAR84574.1; -; mRNA.
DR RefSeq; NP_599193.1; NM_134366.1.
DR AlphaFoldDB; Q6RUV5; -.
DR BMRB; Q6RUV5; -.
DR SMR; Q6RUV5; -.
DR BioGRID; 264467; 9.
DR CORUM; Q6RUV5; -.
DR DIP; DIP-37114N; -.
DR IntAct; Q6RUV5; 5.
DR MINT; Q6RUV5; -.
DR STRING; 10116.ENSRNOP00000001417; -.
DR iPTMnet; Q6RUV5; -.
DR PhosphoSitePlus; Q6RUV5; -.
DR SwissPalm; Q6RUV5; -.
DR jPOST; Q6RUV5; -.
DR PaxDb; Q6RUV5; -.
DR PRIDE; Q6RUV5; -.
DR GeneID; 363875; -.
DR KEGG; rno:363875; -.
DR CTD; 5879; -.
DR RGD; 619755; Rac1.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; Q6RUV5; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; Q6RUV5; -.
DR Reactome; R-RNO-114604; GPVI-mediated activation cascade.
DR Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
DR Reactome; R-RNO-1433557; Signaling by SCF-KIT.
DR Reactome; R-RNO-193648; NRAGE signals death through JNK.
DR Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-RNO-2424491; DAP12 signaling.
DR Reactome; R-RNO-2871796; FCERI mediated MAPK activation.
DR Reactome; R-RNO-376172; DSCAM interactions.
DR Reactome; R-RNO-389359; CD28 dependent Vav1 pathway.
DR Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
DR Reactome; R-RNO-3928664; Ephrin signaling.
DR Reactome; R-RNO-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-RNO-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-RNO-4086400; PCP/CE pathway.
DR Reactome; R-RNO-416550; Sema4D mediated inhibition of cell attachment and migration.
DR Reactome; R-RNO-418885; DCC mediated attractive signaling.
DR Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-RNO-445144; Signal transduction by L1.
DR Reactome; R-RNO-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-RNO-5625740; RHO GTPases activate PKNs.
DR Reactome; R-RNO-5625900; RHO GTPases activate CIT.
DR Reactome; R-RNO-5625970; RHO GTPases activate KTN1.
DR Reactome; R-RNO-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-RNO-5627123; RHO GTPases activate PAKs.
DR Reactome; R-RNO-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-RNO-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-RNO-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-RNO-8875555; MET activates RAP1 and RAC1.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9032759; NTRK2 activates RAC1.
DR Reactome; R-RNO-9748787; Azathioprine ADME.
DR Reactome; R-RNO-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:Q6RUV5; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001068; Expressed in cerebellum and 20 other tissues.
DR ExpressionAtlas; Q6RUV5; baseline and differential.
DR Genevisible; Q6RUV5; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IDA:SynGO.
DR GO; GO:0031901; C:early endosome membrane; ISO:RGD.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISO:RGD.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IDA:RGD.
DR GO; GO:0060091; C:kinocilium; ISO:RGD.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000242; C:pericentriolar material; ISO:RGD.
DR GO; GO:0001891; C:phagocytic cup; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; ISO:RGD.
DR GO; GO:0055038; C:recycling endosome membrane; ISO:RGD.
DR GO; GO:0032587; C:ruffle membrane; ISO:RGD.
DR GO; GO:0005802; C:trans-Golgi network; ISO:RGD.
DR GO; GO:0051117; F:ATPase binding; IPI:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IDA:RGD.
DR GO; GO:0030742; F:GTP-dependent protein binding; ISO:RGD.
DR GO; GO:0003924; F:GTPase activity; IDA:RGD.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0051022; F:Rho GDP-dissociation inhibitor binding; IPI:RGD.
DR GO; GO:0031267; F:small GTPase binding; IPI:RGD.
DR GO; GO:0031996; F:thioesterase binding; ISO:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:RGD.
DR GO; GO:0007015; P:actin filament organization; IMP:RGD.
DR GO; GO:0030041; P:actin filament polymerization; ISO:RGD.
DR GO; GO:0048532; P:anatomical structure arrangement; ISO:RGD.
DR GO; GO:0086098; P:angiotensin-activated signaling pathway involved in heart process; ISO:RGD.
DR GO; GO:0002093; P:auditory receptor cell morphogenesis; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; ISO:RGD.
DR GO; GO:0045453; P:bone resorption; IDA:RGD.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0048870; P:cell motility; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IMP:RGD.
DR GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR GO; GO:0045216; P:cell-cell junction organization; ISO:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IDA:RGD.
DR GO; GO:0021894; P:cerebral cortex GABAergic interneuron development; ISO:RGD.
DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; ISO:RGD.
DR GO; GO:0006935; P:chemotaxis; IMP:RGD.
DR GO; GO:0090103; P:cochlea morphogenesis; ISO:RGD.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; ISO:RGD.
DR GO; GO:0016358; P:dendrite development; ISO:RGD.
DR GO; GO:0048813; P:dendrite morphogenesis; ISO:RGD.
DR GO; GO:0071542; P:dopaminergic neuron differentiation; ISO:RGD.
DR GO; GO:0021831; P:embryonic olfactory bulb interneuron precursor migration; ISO:RGD.
DR GO; GO:0006897; P:endocytosis; ISO:RGD.
DR GO; GO:0043652; P:engulfment of apoptotic cell; ISO:RGD.
DR GO; GO:0003382; P:epithelial cell morphogenesis; ISO:RGD.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0030900; P:forebrain development; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; ISO:RGD.
DR GO; GO:0006972; P:hyperosmotic response; ISO:RGD.
DR GO; GO:0030032; P:lamellipodium assembly; ISO:RGD.
DR GO; GO:0051668; P:localization within membrane; ISO:RGD.
DR GO; GO:0002551; P:mast cell chemotaxis; IMP:RGD.
DR GO; GO:1904948; P:midbrain dopaminergic neuron differentiation; ISO:RGD.
DR GO; GO:0008045; P:motor neuron axon guidance; IBA:GO_Central.
DR GO; GO:0010764; P:negative regulation of fibroblast migration; ISO:RGD.
DR GO; GO:0032707; P:negative regulation of interleukin-23 production; ISO:RGD.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISO:RGD.
DR GO; GO:0035567; P:non-canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISO:RGD.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISO:RGD.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISO:RGD.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; ISO:RGD.
DR GO; GO:0045740; P:positive regulation of DNA replication; IMP:RGD.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:RGD.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISO:RGD.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:RGD.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:RGD.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISO:RGD.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; ISO:RGD.
DR GO; GO:2000386; P:positive regulation of ovarian follicle development; ISO:RGD.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:RGD.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0016601; P:Rac protein signal transduction; IDA:SynGO.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0061344; P:regulation of cell adhesion involved in heart morphogenesis; ISO:RGD.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISO:RGD.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0008361; P:regulation of cell size; ISO:RGD.
DR GO; GO:0070376; P:regulation of ERK5 cascade; ISO:RGD.
DR GO; GO:0010762; P:regulation of fibroblast migration; ISO:RGD.
DR GO; GO:0010591; P:regulation of lamellipodium assembly; ISO:RGD.
DR GO; GO:0014041; P:regulation of neuron maturation; ISO:RGD.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; ISO:RGD.
DR GO; GO:1902622; P:regulation of neutrophil migration; IBA:GO_Central.
DR GO; GO:0045428; P:regulation of nitric oxide biosynthetic process; IGI:ARUK-UCL.
DR GO; GO:0046425; P:regulation of receptor signaling pathway via JAK-STAT; ISO:RGD.
DR GO; GO:0060263; P:regulation of respiratory burst; ISO:RGD.
DR GO; GO:0051492; P:regulation of stress fiber assembly; ISO:RGD.
DR GO; GO:0097178; P:ruffle assembly; ISO:RGD.
DR GO; GO:0031529; P:ruffle organization; ISO:RGD.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IMP:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISO:RGD.
DR GO; GO:0003376; P:sphingosine-1-phosphate receptor signaling pathway; ISO:RGD.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; ISO:RGD.
DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; ISO:RGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003578; Small_GTPase_Rho.
DR PANTHER; PTHR24072; PTHR24072; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51420; RHO; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cytoplasm; Direct protein sequencing;
KW GTP-binding; Hydrolase; Isopeptide bond; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Nucleus; Prenylation; Reference proteome;
KW Synapse; Ubl conjugation.
FT CHAIN 1..189
FT /note="Ras-related C3 botulinum toxin substrate 1"
FT /id="PRO_0000042040"
FT PROPEP 190..192
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P63000"
FT /id="PRO_0000042041"
FT MOTIF 32..40
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT MOTIF 179..188
FT /note="Polybasic region; required for nuclear import"
FT /evidence="ECO:0000250|UniProtKB:P63000"
FT BINDING 13..18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P63000"
FT BINDING 30..35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P63000"
FT BINDING 60
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P63000"
FT BINDING 116..118
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P63000"
FT BINDING 159..160
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P63000"
FT MOD_RES 189
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P63000"
FT LIPID 189
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P63000"
FT CROSSLNK 147
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P63000"
FT MUTAGEN 12
FT /note="G->V: Constitutively active. Increases PAK1 and
FT LIMK1 phosphorylation and NR3C2 nuclear localization in
FT podocytes. In hippocampal neurons, increases the amount of
FT dendritic protrusions and decreases the number of normal
FT spines and synapses."
FT /evidence="ECO:0000269|PubMed:15800193,
FT ECO:0000269|PubMed:19029984"
FT MUTAGEN 17
FT /note="T->N: Dominant negative. Reduces NMDA receptor-
FT mediated synaptic currents."
FT /evidence="ECO:0000269|PubMed:24089484"
FT MUTAGEN 61
FT /note="Q->L: Constitutively active. Interacts with PPP5C."
FT /evidence="ECO:0000269|PubMed:16549782,
FT ECO:0000269|PubMed:24089484"
SQ 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
