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

 RAC1_RAT                Reviewed;         192 AA.
31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
16-JAN-2019, entry version 147.
RecName: Full=Ras-related C3 botulinum toxin substrate 1;
AltName: Full=p21-Rac1;
Flags: Precursor;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
STRAIN=Wistar; TISSUE=Bone marrow;
PubMed=16040606; DOI=10.1074/jbc.M414213200;
Sun Y., Bueki K.G., Ettala O., Vaeaeraeniemi J.P., Vaeaenaenen H.K.;
"Possible role of direct Rac1-Rab7 interaction in ruffled border
formation of osteoclasts.";
J. Biol. Chem. 280:32356-32361(2005).
PROTEIN SEQUENCE OF 6-16; 103-116; 133-147; 154-163 AND 167-183, AND
STRAIN=Sprague-Dawley; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
PubMed=16549782; DOI=10.1073/pnas.0600080103;
Gentile S., Darden T., Erxleben C., Romeo C., Russo A., Martin N.,
Rossie S., Armstrong D.L.;
"Rac GTPase signaling through the PP5 protein phosphatase.";
Proc. Natl. Acad. Sci. U.S.A. 103:5202-5206(2006).
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).
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).
PubMed=22128169; DOI=10.1074/jbc.M111.269431;
Wilhelm M., Kukekov N.V., Schmit T.L., Biagas K.V., Sproul A.A.,
Gire S., Maes M.E., Xu Z., Greene L.A.;
"Sh3rf2/POSHER protein promotes cell survival by RING-mediated
proteasomal degradation of the c-Jun N-terminal kinase scaffold POSH
(Plenty of SH3s) protein.";
J. Biol. Chem. 287:2247-2256(2012).
PubMed=24089484; DOI=10.1523/JNEUROSCI.1175-13.2013;
Duffney L.J., Wei J., Cheng J., Liu W., Smith K.R., Kittler J.T.,
Yan Z.;
"Shank3 deficiency induces NMDA receptor hypofunction via an actin-
dependent mechanism.";
J. Neurosci. 33:15767-15778(2013).
-!- 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, neurons adhesion,
migration and differentiation, 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. In podocytes,
promotes nuclear shuttling of NR3C2; this modulation is required
for a proper kidney functioning. 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 synapses, seems to mediate
the regulation of F-actin cluster formation performed by SHANK3.
{ECO:0000250|UniProtKB:P63001, ECO:0000269|PubMed:16040606,
ECO:0000269|PubMed:16549782, ECO:0000269|PubMed:19029984,
ECO:0000269|PubMed:20696765, ECO:0000269|PubMed:24089484}.
-!- ACTIVITY 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 NISCH. Interacts with PIP5K1A. Interacts
with the GTP-bound form of RAB7A. Interacts with SRGAP2. Interacts
with CYFIP1/SRA-1. Interacts with PLXNB3. Interacts with ARHGDIA;
the interaction is induced by SEMA5A, mediated through PLXNB3 and
inactivates and stabilizes RAC1. Interacts (GTP-bound form
preferentially) with PKN2 (via the REM repeats); the interaction
stimulates autophosphorylation and phosphorylation of PKN2.
Interacts with the GEF proteins PREX1, RASGRF2, FARP1, FARP2,
DOCK1, DOCK2 and DOCK7, which promote the exchange between GDP and
GTP, and therefore activate it. Interacts with PARD6A, PARD6B and
PARD6G in a GTP-dependent manner. 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 PLXNB1. Probably found in a
ternary complex composed of DSCAM, PAK1 and RAC1. Interacts with
DSCAM; the interaction requires PAK1. Part of a complex with
MAP2K3, MAP3K3, CCM2 and DEF6. Interacts with BAIAP2, BAIAP2L1 and
DEF6. Interacts with Y.pseudotuberculosis YPKA and PLCB2.
Interacts with NOXA1. Interacts with ARHGEF2. Interacts with
TBC1D2. Interacts with UNKL. Interacts with USP6. Interacts with
SPATA13. Interacts with ARHGEF16; mediates activation of RAC1 by
EPHA2. Interacts with ITGB4. Interacts with S100A8 and
calprotectin (S100A8/9). Interacts with PACSIN2. Interacts with
ITGB1BP1. 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. Interacts with PAK2. Interacts (GTP-bound form) with
SH3RF1 and SH3RF3. Found in a complex with SH3RF1, MAPK8IP1/JIP1,
MAP3K11/MLK3, MAP2K7/MKK7 and MAPK8/JNK1 (By similarity).
Interacts (both active GTP- or inactive GDP-bound forms) with
SH3RF2 (PubMed:22128169). {ECO:0000250|UniProtKB:P63000,
ECO:0000250|UniProtKB:P63001, ECO:0000269|PubMed:16040606,
ECO:0000269|PubMed:16549782, ECO:0000269|PubMed:20696765,
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16040606};
Lipid-anchor {ECO:0000269|PubMed:16040606}; Cytoplasmic side
{ECO:0000269|PubMed:16040606}. Melanosome
{ECO:0000250|UniProtKB:P63000}. Cytoplasm
{ECO:0000250|UniProtKB:P63000}. Cell projection, lamellipodium
{ECO:0000250|UniProtKB:P63001}. Note=Inner surface of plasma
membrane possibly with attachment requiring prenylation of the C-
terminal cysteine (By similarity). Found in the ruffled border (a
late endosomal-like compartment in the plasma membrane) of bone-
resorbing osteoclasts. Localizes to the lamellipodium in a SH3RF1-
dependent manner. {ECO:0000250|UniProtKB:P63000,
-!- TISSUE SPECIFICITY: Osteoclasts. {ECO:0000269|PubMed:16040606}.
-!- DOMAIN: The effector region mediates interaction with DEF6.
-!- 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.
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
EMBL; AY491395; AAR84574.1; -; mRNA.
RefSeq; NP_599193.1; NM_134366.1.
UniGene; Rn.228585; -.
UniGene; Rn.29157; -.
ProteinModelPortal; Q6RUV5; -.
SMR; Q6RUV5; -.
BioGrid; 264467; 6.
DIP; DIP-37114N; -.
IntAct; Q6RUV5; 4.
STRING; 10116.ENSRNOP00000001417; -.
iPTMnet; Q6RUV5; -.
PhosphoSitePlus; Q6RUV5; -.
SwissPalm; Q6RUV5; -.
jPOST; Q6RUV5; -.
PaxDb; Q6RUV5; -.
Ensembl; ENSRNOT00000001417; ENSRNOP00000001417; ENSRNOG00000001068.
GeneID; 363875; -.
KEGG; rno:363875; -.
CTD; 5879; -.
RGD; 619755; Rac1.
eggNOG; KOG0393; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00940000153500; -.
HOGENOM; HOG000233974; -.
HOVERGEN; HBG009351; -.
InParanoid; Q6RUV5; -.
KO; K04392; -.
OrthoDB; 1091615at2759; -.
PhylomeDB; Q6RUV5; -.
Reactome; R-RNO-114604; GPVI-mediated activation cascade.
Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
Reactome; R-RNO-1433557; Signaling by SCF-KIT.
Reactome; R-RNO-193648; NRAGE signals death through JNK.
Reactome; R-RNO-194840; Rho GTPase cycle.
Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-RNO-2424491; DAP12 signaling.
Reactome; R-RNO-2871796; FCERI mediated MAPK activation.
Reactome; R-RNO-376172; DSCAM interactions.
Reactome; R-RNO-389359; CD28 dependent Vav1 pathway.
Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
Reactome; R-RNO-3928664; Ephrin signaling.
Reactome; R-RNO-3928665; EPH-ephrin mediated repulsion of cells.
Reactome; R-RNO-399954; Sema3A PAK dependent Axon repulsion.
Reactome; R-RNO-4086400; PCP/CE pathway.
Reactome; R-RNO-416550; Sema4D mediated inhibition of cell attachment and migration.
Reactome; R-RNO-418885; DCC mediated attractive signaling.
Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-RNO-445144; Signal transduction by L1.
Reactome; R-RNO-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-RNO-5625740; RHO GTPases activate PKNs.
Reactome; R-RNO-5625900; RHO GTPases activate CIT.
Reactome; R-RNO-5625970; RHO GTPases activate KTN1.
Reactome; R-RNO-5626467; RHO GTPases activate IQGAPs.
Reactome; R-RNO-5627123; RHO GTPases activate PAKs.
Reactome; R-RNO-5663213; RHO GTPases Activate WASPs and WAVEs.
Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
Reactome; R-RNO-5668599; RHO GTPases Activate NADPH Oxidases.
Reactome; R-RNO-5687128; MAPK6/MAPK4 signaling.
Reactome; R-RNO-6798695; Neutrophil degranulation.
Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-RNO-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
Reactome; R-RNO-8875555; MET activates RAP1 and RAC1.
Reactome; R-RNO-9032759; NTRK2 activates RAC1.
Reactome; R-RNO-983231; Factors involved in megakaryocyte development and platelet production.
PRO; PR:Q6RUV5; -.
Proteomes; UP000002494; Chromosome 12.
Bgee; ENSRNOG00000001068; Expressed in 10 organ(s), highest expression level in lung.
ExpressionAtlas; Q6RUV5; baseline and differential.
Genevisible; Q6RUV5; RN.
GO; GO:0005884; C:actin filament; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IEA:Ensembl.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0043197; C:dendritic spine; IDA:SynGO.
GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
GO; GO:0000139; C:Golgi membrane; IDA:RGD.
GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0055038; C:recycling endosome membrane; IEA:Ensembl.
GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
GO; GO:0051117; F:ATPase binding; IPI:RGD.
GO; GO:0005525; F:GTP binding; IDA:RGD.
GO; GO:0003924; F:GTPase activity; IDA:RGD.
GO; GO:0042826; F:histone deacetylase binding; IPI:RGD.
GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
GO; GO:0017137; F:Rab GTPase binding; IPI:RGD.
GO; GO:0051022; F:Rho GDP-dissociation inhibitor binding; IPI:RGD.
GO; GO:0031996; F:thioesterase binding; IEA:Ensembl.
GO; GO:0030036; P:actin cytoskeleton organization; IDA:RGD.
GO; GO:0007015; P:actin filament organization; IMP:RGD.
GO; GO:0045453; P:bone resorption; IDA:RGD.
GO; GO:0048870; P:cell motility; ISS:UniProtKB.
GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
GO; GO:0008283; P:cell proliferation; IMP:RGD.
GO; GO:0071260; P:cellular response to mechanical stimulus; IDA:RGD.
GO; GO:0006935; P:chemotaxis; IMP:RGD.
GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0030032; P:lamellipodium assembly; IEA:Ensembl.
GO; GO:0051668; P:localization within membrane; IEA:Ensembl.
GO; GO:0002551; P:mast cell chemotaxis; IMP:RGD.
GO; GO:0032707; P:negative regulation of interleukin-23 production; IEA:Ensembl.
GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
GO; GO:0045740; P:positive regulation of DNA replication; IMP:RGD.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; IEA:Ensembl.
GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:RGD.
GO; GO:0031116; P:positive regulation of microtubule polymerization; IEA:Ensembl.
GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IEA:Ensembl.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
GO; GO:0016601; P:Rac protein signal transduction; IDA:SynGO.
GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
GO; GO:0008361; P:regulation of cell size; IEA:Ensembl.
GO; GO:0045428; P:regulation of nitric oxide biosynthetic process; IGI:ARUK-UCL.
GO; GO:0060263; P:regulation of respiratory burst; IEA:Ensembl.
GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
GO; GO:0097178; P:ruffle assembly; IEA:Ensembl.
GO; GO:0071526; P:semaphorin-plexin signaling pathway; IMP:UniProtKB.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
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; Cell projection; Complete proteome; Cytoplasm;
Direct protein sequencing; GTP-binding; Isopeptide bond; Lipoprotein;
Membrane; Methylation; Nucleotide-binding; Prenylation;
Reference proteome; Ubl conjugation.
CHAIN 1 189 Ras-related C3 botulinum toxin substrate
PROPEP 190 192 Removed in mature form. {ECO:0000250}.
NP_BIND 13 18 GTP. {ECO:0000250|UniProtKB:P63000}.
NP_BIND 30 35 GTP. {ECO:0000250|UniProtKB:P63000}.
NP_BIND 116 118 GTP. {ECO:0000250|UniProtKB:P63000}.
NP_BIND 159 160 GTP. {ECO:0000250|UniProtKB:P63000}.
MOTIF 32 40 Effector region. {ECO:0000255}.
BINDING 60 60 GTP; via amide nitrogen.
MOD_RES 189 189 Cysteine methyl ester. {ECO:0000250}.
LIPID 189 189 S-geranylgeranyl cysteine.
CROSSLNK 147 147 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
MUTAGEN 12 12 G->V: Constitutively active. Increases
PAK1 and LIMK1 phosphorylation and NR3C2
nuclear localization in podocytes.
MUTAGEN 17 17 T->N: Dominant negatif. Reduces NMDA
receptor-mediated synaptic currents.
MUTAGEN 61 61 Q->L: Constitutively active. Interacts
with PPP5C. {ECO:0000269|PubMed:16549782,
SEQUENCE 192 AA; 21450 MW; ACEDF83A45E5EA67 CRC64;

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