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

 RAC1_RAT                Reviewed;         192 AA.
Q6RUV5;
31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
22-NOV-2017, entry version 137.
RecName: Full=Ras-related C3 botulinum toxin substrate 1;
AltName: Full=p21-Rac1;
Flags: Precursor;
Name=Rac1;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND INTERACTION WITH RAB7A.
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).
[2]
PROTEIN SEQUENCE OF 6-16; 103-116; 133-147; 154-163 AND 167-183, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[3]
FUNCTION, INTERACTION WITH PPP5C, AND MUTAGENESIS OF GLN-61.
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).
[4]
FUNCTION, AND MUTAGENESIS OF GLY-12.
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).
[5]
FUNCTION, INTERACTION WITH PLXNB3 AND ARHGDIA, AND SUBCELLULAR
LOCATION.
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).
[6]
FUNCTION IN ACTIN POLYMERIZATION, AND MUTAGENESIS OF THR-17 AND
GLN-61.
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 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:0000269|PubMed:16040606,
ECO:0000269|PubMed:16549782, ECO:0000269|PubMed:19029984,
ECO:0000269|PubMed:20696765, ECO:0000269|PubMed:24089484}.
-!- 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 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 (By similarity). {ECO:0000250|UniProtKB:P63000,
ECO:0000269|PubMed:16040606, ECO:0000269|PubMed:16549782,
ECO:0000269|PubMed:20696765}.
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
side. Melanosome {ECO:0000250}. Cytoplasm. 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. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Osteoclasts. {ECO:0000269|PubMed:16040606}.
-!- 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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Distributed under the Creative Commons Attribution-NoDerivs 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.
CORUM; Q6RUV5; -.
DIP; DIP-37114N; -.
IntAct; Q6RUV5; 4.
MINT; MINT-4577150; -.
STRING; 10116.ENSRNOP00000001417; -.
iPTMnet; Q6RUV5; -.
PhosphoSitePlus; Q6RUV5; -.
SwissPalm; Q6RUV5; -.
PaxDb; Q6RUV5; -.
PRIDE; Q6RUV5; -.
Ensembl; ENSRNOT00000001417; ENSRNOP00000001417; ENSRNOG00000001068.
GeneID; 363875; -.
KEGG; rno:363875; -.
CTD; 5879; -.
RGD; 619755; Rac1.
eggNOG; KOG0393; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00760000118978; -.
HOGENOM; HOG000233974; -.
HOVERGEN; HBG009351; -.
InParanoid; Q6RUV5; -.
KO; K04392; -.
PhylomeDB; Q6RUV5; -.
Reactome; R-RNO-114604; GPVI-mediated activation cascade.
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-416482; G alpha (12/13) signalling events.
Reactome; R-RNO-416550; Sema4D mediated inhibition of cell attachment and migration.
Reactome; R-RNO-416572; Sema4D induced cell migration and growth-cone collapse.
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-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-5668599; RHO GTPases Activate NADPH Oxidases.
Reactome; R-RNO-5687128; MAPK6/MAPK4 signaling.
Reactome; R-RNO-6798695; Neutrophil degranulation.
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-983231; Factors involved in megakaryocyte development and platelet production.
PRO; PR:Q6RUV5; -.
Proteomes; UP000002494; Chromosome 12.
Bgee; ENSRNOG00000001068; -.
ExpressionAtlas; Q6RUV5; baseline and differential.
Genevisible; Q6RUV5; RN.
GO; GO:0005884; C:actin filament; IEA:Ensembl.
GO; GO:0042995; C:cell projection; ISO:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:RGD.
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:0031901; C:early endosome membrane; ISO:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0031012; C:extracellular matrix; ISO:RGD.
GO; GO:0019897; C:extrinsic component of plasma membrane; ISO:RGD.
GO; GO:0005925; C:focal adhesion; ISO:RGD.
GO; GO:0000139; C:Golgi membrane; IDA:RGD.
GO; GO:0060091; C:kinocilium; ISO:RGD.
GO; GO:0030027; C:lamellipodium; ISO:RGD.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; ISO:RGD.
GO; GO:0000242; C:pericentriolar material; ISO:RGD.
GO; GO:0001891; C:phagocytic cup; ISO:RGD.
GO; GO:0005886; C:plasma membrane; ISO:RGD.
GO; GO:0032587; C:ruffle membrane; ISO:RGD.
GO; GO:0005802; C:trans-Golgi network; ISO:RGD.
GO; GO:0051117; F:ATPase binding; IPI:RGD.
GO; GO:0019899; F:enzyme binding; ISO:RGD.
GO; GO:0005525; F:GTP binding; IDA:RGD.
GO; GO:0030742; F:GTP-dependent protein binding; ISO: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:0017137; F:Rab GTPase binding; IPI:RGD.
GO; GO:0051022; F:Rho GDP-dissociation inhibitor binding; IPI:RGD.
GO; GO:0031996; F:thioesterase binding; ISO:RGD.
GO; GO:0030036; P:actin cytoskeleton organization; IDA:RGD.
GO; GO:0007015; P:actin filament organization; IMP:RGD.
GO; GO:0030041; P:actin filament polymerization; ISO:RGD.
GO; GO:0048532; P:anatomical structure arrangement; ISO:RGD.
GO; GO:0002093; P:auditory receptor cell morphogenesis; ISO:RGD.
GO; GO:0007411; P:axon guidance; ISO:RGD.
GO; GO:0045453; P:bone resorption; IDA:RGD.
GO; GO:0007155; P:cell adhesion; ISO:RGD.
GO; GO:0016477; P:cell migration; ISO:RGD.
GO; GO:0048870; P:cell motility; ISS:UniProtKB.
GO; GO:0008283; P:cell proliferation; IMP:RGD.
GO; GO:0045216; P:cell-cell junction organization; ISO:RGD.
GO; GO:0071260; P:cellular response to mechanical stimulus; IDA:RGD.
GO; GO:0021894; P:cerebral cortex GABAergic interneuron development; ISO:RGD.
GO; GO:0021799; P:cerebral cortex radially oriented cell migration; ISO:RGD.
GO; GO:0006935; P:chemotaxis; IMP:RGD.
GO; GO:0090103; P:cochlea morphogenesis; ISO:RGD.
GO; GO:0007010; P:cytoskeleton organization; ISO:RGD.
GO; GO:0016358; P:dendrite development; ISO:RGD.
GO; GO:0048813; P:dendrite morphogenesis; ISO:RGD.
GO; GO:0071542; P:dopaminergic neuron differentiation; ISO:RGD.
GO; GO:0021831; P:embryonic olfactory bulb interneuron precursor migration; ISO:RGD.
GO; GO:0006897; P:endocytosis; ISO:RGD.
GO; GO:0043652; P:engulfment of apoptotic cell; ISO:RGD.
GO; GO:0003382; P:epithelial cell morphogenesis; ISO:RGD.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISO:RGD.
GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; ISO:RGD.
GO; GO:0048873; P:homeostasis of number of cells within a tissue; ISO:RGD.
GO; GO:0006972; P:hyperosmotic response; ISO:RGD.
GO; GO:0030032; P:lamellipodium assembly; ISO:RGD.
GO; GO:0051668; P:localization within membrane; ISO:RGD.
GO; GO:0002551; P:mast cell chemotaxis; IMP:RGD.
GO; GO:1904948; P:midbrain dopaminergic neuron differentiation; ISO:RGD.
GO; GO:0032707; P:negative regulation of interleukin-23 production; ISO:RGD.
GO; GO:0048812; P:neuron projection morphogenesis; ISO:RGD.
GO; GO:0035567; P:non-canonical Wnt signaling pathway; ISO:RGD.
GO; GO:0006911; P:phagocytosis, engulfment; ISO:RGD.
GO; GO:0030838; P:positive regulation of actin filament polymerization; ISO:RGD.
GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISO:RGD.
GO; GO:0060999; P:positive regulation of dendritic spine development; ISO:RGD.
GO; GO:0045740; P:positive regulation of DNA replication; IMP:RGD.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISO:RGD.
GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:RGD.
GO; GO:0031116; P:positive regulation of microtubule polymerization; ISO:RGD.
GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; ISO:RGD.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISO:RGD.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:RGD.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:RGD.
GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
GO; GO:0016601; P:Rac protein signal transduction; IDA:SynGO.
GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
GO; GO:0022604; P:regulation of cell morphogenesis; ISO:RGD.
GO; GO:0008361; P:regulation of cell size; ISO:RGD.
GO; GO:0010762; P:regulation of fibroblast migration; ISO:RGD.
GO; GO:0010591; P:regulation of lamellipodium assembly; ISO:RGD.
GO; GO:0014041; P:regulation of neuron maturation; ISO:RGD.
GO; GO:0048168; P:regulation of neuronal synaptic plasticity; ISO:RGD.
GO; GO:0060263; P:regulation of respiratory burst; ISO:RGD.
GO; GO:0051492; P:regulation of stress fiber assembly; ISO:RGD.
GO; GO:0097178; P:ruffle assembly; ISO:RGD.
GO; GO:0031529; P:ruffle organization; ISO:RGD.
GO; GO:0071526; P:semaphorin-plexin signaling pathway; IMP:UniProtKB.
GO; GO:0007264; P:small GTPase mediated signal transduction; ISO:RGD.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:RGD.
GO; GO:0051932; P:synaptic transmission, GABAergic; ISO:RGD.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; ISO:RGD.
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;
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
1.
/FTId=PRO_0000042040.
PROPEP 190 192 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000042041.
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. Increases
PAK1 and LIMK1 phosphorylation and NR3C2
nuclear localization in podocytes.
{ECO:0000269|PubMed:19029984}.
MUTAGEN 17 17 T->N: Dominant negatif. Reduces NMDA
receptor-mediated synaptic currents.
{ECO:0000269|PubMed:24089484}.
MUTAGEN 61 61 Q->L: Constitutively active. Interacts
with PPP5C. {ECO:0000269|PubMed:16549782,
ECO:0000269|PubMed:24089484}.
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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