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Protein

Ras-related C3 botulinum toxin substrate 1

Gene

Rac1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 SHANK3.5 Publications

Enzyme regulationi

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).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 178GTPBy similarity
Nucleotide bindingi57 – 615GTPBy similarity
Nucleotide bindingi115 – 1184GTPBy similarity

GO - Molecular functioni

  • GTPase activity Source: RGD
  • GTP binding Source: RGD
  • histone deacetylase binding Source: RGD
  • protein kinase binding Source: BHF-UCL
  • Rab GTPase binding Source: RGD
  • Rho GDP-dissociation inhibitor binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-114604. GPVI-mediated activation cascade.
R-RNO-1433557. Signaling by SCF-KIT.
R-RNO-193648. NRAGE signals death through JNK.
R-RNO-194840. Rho GTPase cycle.
R-RNO-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-RNO-2424491. DAP12 signaling.
R-RNO-2871796. FCERI mediated MAPK activation.
R-RNO-376172. DSCAM interactions.
R-RNO-389359. CD28 dependent Vav1 pathway.
R-RNO-3928662. EPHB-mediated forward signaling.
R-RNO-3928664. Ephrin signaling.
R-RNO-3928665. EPH-ephrin mediated repulsion of cells.
R-RNO-399954. Sema3A PAK dependent Axon repulsion.
R-RNO-4086400. PCP/CE pathway.
R-RNO-416482. G alpha (12/13) signalling events.
R-RNO-416550. Sema4D mediated inhibition of cell attachment and migration.
R-RNO-416572. Sema4D induced cell migration and growth-cone collapse.
R-RNO-418885. DCC mediated attractive signaling.
R-RNO-4420097. VEGFA-VEGFR2 Pathway.
R-RNO-445144. Signal transduction by L1.
R-RNO-5218920. VEGFR2 mediated vascular permeability.
R-RNO-5625970. RHO GTPases activate KTN1.
R-RNO-5626467. RHO GTPases activate IQGAPs.
R-RNO-5627123. RHO GTPases activate PAKs.
R-RNO-5663213. RHO GTPases Activate WASPs and WAVEs.
R-RNO-5668599. RHO GTPases Activate NADPH Oxidases.
R-RNO-5687128. MAPK6/MAPK4 signaling.
R-RNO-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
R-RNO-983231. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related C3 botulinum toxin substrate 1
Alternative name(s):
p21-Rac1
Gene namesi
Name:Rac1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 12

Organism-specific databases

RGDi619755. Rac1.

Subcellular locationi

  • Cell membrane; Lipid-anchor; Cytoplasmic side
  • Melanosome By similarity
  • 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.By similarity

GO - Cellular componenti

  • actin filament Source: Ensembl
  • cytoplasm Source: RGD
  • cytoplasmic ribonucleoprotein granule Source: Ensembl
  • cytoplasmic vesicle Source: RGD
  • cytosol Source: UniProtKB
  • early endosome membrane Source: Ensembl
  • extracellular exosome Source: Ensembl
  • extrinsic component of plasma membrane Source: Ensembl
  • focal adhesion Source: Ensembl
  • Golgi membrane Source: RGD
  • lamellipodium Source: Ensembl
  • melanosome Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • nucleus Source: Ensembl
  • phagocytic cup Source: Ensembl
  • ruffle membrane Source: Ensembl
  • trans-Golgi network Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi12 – 121G → V: Constitutively active. Increases PAK1 and LIMK1 phosphorylation and NR3C2 nuclear localization in podocytes. 1 Publication
Mutagenesisi17 – 171T → N: Dominant negatif. Reduces NMDA receptor-mediated synaptic currents. 1 Publication
Mutagenesisi61 – 611Q → L: Constitutively active. Interacts with PPP5C. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 189189Ras-related C3 botulinum toxin substrate 1PRO_0000042040Add
BLAST
Propeptidei190 – 1923Removed in mature formBy similarityPRO_0000042041

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki147 – 147Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei189 – 1891Cysteine methyl esterBy similarity
Lipidationi189 – 1891S-geranylgeranyl cysteineBy similarity

Post-translational modificationi

GTP-bound active form is ubiquitinated by HACE1, leading to its degradation by the proteasome.By similarity

Keywords - PTMi

Isopeptide bond, Lipoprotein, Methylation, Prenylation, Ubl conjugation

Proteomic databases

PaxDbiQ6RUV5.
PRIDEiQ6RUV5.

PTM databases

iPTMnetiQ6RUV5.
PhosphoSiteiQ6RUV5.
SwissPalmiQ6RUV5.

Expressioni

Tissue specificityi

Osteoclasts.1 Publication

Gene expression databases

ExpressionAtlasiQ6RUV5. baseline and differential.
GenevisibleiQ6RUV5. RN.

Interactioni

Subunit structurei

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).By similarity3 Publications

GO - Molecular functioni

  • histone deacetylase binding Source: RGD
  • protein kinase binding Source: BHF-UCL
  • Rab GTPase binding Source: RGD
  • Rho GDP-dissociation inhibitor binding Source: RGD

Protein-protein interaction databases

BioGridi264467. 6 interactions.
DIPiDIP-37114N.
IntActiQ6RUV5. 1 interaction.
MINTiMINT-4577150.
STRINGi10116.ENSRNOP00000001417.

Structurei

3D structure databases

ProteinModelPortaliQ6RUV5.
SMRiQ6RUV5. Positions 1-177.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi32 – 409Effector regionSequence analysis

Domaini

The effector region mediates interaction with DEF6.By similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rho family.Curated

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00760000118978.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiQ6RUV5.
KOiK04392.
OMAiSPRRHKC.
OrthoDBiEOG764747.
PhylomeDBiQ6RUV5.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6RUV5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP
60 70 80 90 100
VNLGLWDTAG QEDYDRLRPL SYPQTDVFLI CFSLVSPASF ENVRAKWYPE
110 120 130 140 150
VRHHCPNTPI ILVGTKLDLR DDKDTIEKLK EKKLTPITYP QGLAMAKEIG
160 170 180 190
AVKYLECSAL TQRGLKTVFD EAIRAVLCPP PVKKRKRKCL LL
Length:192
Mass (Da):21,450
Last modified:July 5, 2004 - v1
Checksum:iACEDF83A45E5EA67
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY491395 mRNA. Translation: AAR84574.1.
RefSeqiNP_599193.1. NM_134366.1.
UniGeneiRn.29157.

Genome annotation databases

EnsembliENSRNOT00000001417; ENSRNOP00000001417; ENSRNOG00000001068.
GeneIDi363875.
KEGGirno:363875.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY491395 mRNA. Translation: AAR84574.1.
RefSeqiNP_599193.1. NM_134366.1.
UniGeneiRn.29157.

3D structure databases

ProteinModelPortaliQ6RUV5.
SMRiQ6RUV5. Positions 1-177.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi264467. 6 interactions.
DIPiDIP-37114N.
IntActiQ6RUV5. 1 interaction.
MINTiMINT-4577150.
STRINGi10116.ENSRNOP00000001417.

PTM databases

iPTMnetiQ6RUV5.
PhosphoSiteiQ6RUV5.
SwissPalmiQ6RUV5.

Proteomic databases

PaxDbiQ6RUV5.
PRIDEiQ6RUV5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000001417; ENSRNOP00000001417; ENSRNOG00000001068.
GeneIDi363875.
KEGGirno:363875.

Organism-specific databases

CTDi5879.
RGDi619755. Rac1.

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00760000118978.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiQ6RUV5.
KOiK04392.
OMAiSPRRHKC.
OrthoDBiEOG764747.
PhylomeDBiQ6RUV5.

Enzyme and pathway databases

ReactomeiR-RNO-114604. GPVI-mediated activation cascade.
R-RNO-1433557. Signaling by SCF-KIT.
R-RNO-193648. NRAGE signals death through JNK.
R-RNO-194840. Rho GTPase cycle.
R-RNO-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-RNO-2424491. DAP12 signaling.
R-RNO-2871796. FCERI mediated MAPK activation.
R-RNO-376172. DSCAM interactions.
R-RNO-389359. CD28 dependent Vav1 pathway.
R-RNO-3928662. EPHB-mediated forward signaling.
R-RNO-3928664. Ephrin signaling.
R-RNO-3928665. EPH-ephrin mediated repulsion of cells.
R-RNO-399954. Sema3A PAK dependent Axon repulsion.
R-RNO-4086400. PCP/CE pathway.
R-RNO-416482. G alpha (12/13) signalling events.
R-RNO-416550. Sema4D mediated inhibition of cell attachment and migration.
R-RNO-416572. Sema4D induced cell migration and growth-cone collapse.
R-RNO-418885. DCC mediated attractive signaling.
R-RNO-4420097. VEGFA-VEGFR2 Pathway.
R-RNO-445144. Signal transduction by L1.
R-RNO-5218920. VEGFR2 mediated vascular permeability.
R-RNO-5625970. RHO GTPases activate KTN1.
R-RNO-5626467. RHO GTPases activate IQGAPs.
R-RNO-5627123. RHO GTPases activate PAKs.
R-RNO-5663213. RHO GTPases Activate WASPs and WAVEs.
R-RNO-5668599. RHO GTPases Activate NADPH Oxidases.
R-RNO-5687128. MAPK6/MAPK4 signaling.
R-RNO-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
R-RNO-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

PROiQ6RUV5.

Gene expression databases

ExpressionAtlasiQ6RUV5. baseline and differential.
GenevisibleiQ6RUV5. RN.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Possible role of direct Rac1-Rab7 interaction in ruffled border formation of osteoclasts."
    Sun Y., Bueki K.G., Ettala O., Vaeaeraeniemi J.P., Vaeaenaenen H.K.
    J. Biol. Chem. 280:32356-32361(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH RAB7A.
    Strain: Wistar.
    Tissue: Bone marrow.
  2. Lubec G., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 6-16; 103-116; 133-147; 154-163 AND 167-183, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  3. Cited for: FUNCTION, INTERACTION WITH PPP5C, MUTAGENESIS OF GLN-61.
  4. "Modification of mineralocorticoid receptor function by Rac1 GTPase: implication in proteinuric kidney disease."
    Shibata S., Nagase M., Yoshida S., Kawarazaki W., Kurihara H., Tanaka H., Miyoshi J., Takai Y., Fujita T.
    Nat. Med. 14:1370-1376(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLY-12.
  5. "Semaphorin 5A and plexin-B3 inhibit human glioma cell motility through RhoGDIalpha-mediated inactivation of Rac1 GTPase."
    Li X., Lee A.Y.
    J. Biol. Chem. 285:32436-32445(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PLXNB3 AND ARHGDIA, SUBCELLULAR LOCATION.
  6. "Shank3 deficiency induces NMDA receptor hypofunction via an actin-dependent mechanism."
    Duffney L.J., Wei J., Cheng J., Liu W., Smith K.R., Kittler J.T., Yan Z.
    J. Neurosci. 33:15767-15778(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACTIN POLYMERIZATION, MUTAGENESIS OF THR-17 AND GLN-61.

Entry informationi

Entry nameiRAC1_RAT
AccessioniPrimary (citable) accession number: Q6RUV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: July 5, 2004
Last modified: July 6, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.