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UniProtKB - Q6RUV5 (RAC1_RAT)

Entry version 165 (29 Sep 2021)
Sequence version 1 (05 Jul 2004)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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, neurons adhesion, migration and differentiation, and growth-factor induced formation of membrane ruffles (PubMed:16040606, PubMed:16549782).

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 (By similarity).

In concert with RAB7A, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts (PubMed:16040606).

In glioma cells, promotes cell migration and invasion (PubMed:20696765).

In podocytes, promotes nuclear shuttling of NR3C2; this modulation is required for a proper kidney functioning (PubMed:19029984).

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 (By similarity).

In neurons, is involved in dendritic spine formation and synaptic plasticity (PubMed:25498153).

In hippocampal neurons, involved in spine morphogenesis and synapse formation, through local activation at synapses by guanine nucleotide exchange factors (GEFs), such as ARHGEF6/ARHGEF7/PIX (PubMed:12695502).

In synapses, may mediate the regulation of F-actin cluster formation performed by SHANK3 (PubMed:24089484).

In neurons, plays a crucial role in regulating GABA(A) receptor synaptic stability and hence GABAergic inhibitory synaptic transmission through its role in PAK1 activation and eventually F-actin stabilization (PubMed:25284783).

By similarity8 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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 and ARHGAP44.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei60GTP; via amide nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi13 – 18GTPBy similarity6
Nucleotide bindingi30 – 35GTPBy similarity6
Nucleotide bindingi116 – 118GTPBy similarity3
Nucleotide bindingi159 – 160GTPBy similarity2

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-RNO-114604, GPVI-mediated activation cascade
R-RNO-1257604, PIP3 activates AKT signaling
R-RNO-1433557, Signaling by SCF-KIT
R-RNO-193648, NRAGE signals death through JNK
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-416550, Sema4D mediated inhibition of cell attachment and migration
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-5625740, RHO GTPases activate PKNs
R-RNO-5625900, RHO GTPases activate CIT
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-5663220, RHO GTPases Activate Formins
R-RNO-5668599, RHO GTPases Activate NADPH Oxidases
R-RNO-5687128, MAPK6/MAPK4 signaling
R-RNO-6798695, Neutrophil degranulation
R-RNO-6811558, PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-RNO-8849471, PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases
R-RNO-8875555, MET activates RAP1 and RAC1
R-RNO-9013149, RAC1 GTPase cycle
R-RNO-9032759, NTRK2 activates RAC1
R-RNO-983231, Factors involved in megakaryocyte development and platelet production

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Ras-related C3 botulinum toxin substrate 1Curated (EC:3.6.5.21 Publication)
Alternative name(s):
p21-Rac1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Rac1Imported
Synonyms:Rac1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 12

Organism-specific databases

Rat genome database

More...RGDi		619755, Rac1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane, Synapse

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi12G → V: Constitutively active. Increases PAK1 and LIMK1 phosphorylation and NR3C2 nuclear localization in podocytes. In hippocampal neurons, increases the amount of dendritic protrusions and decreases the number of normal spines and synapses. 2 Publications1
Mutagenesisi17T → N: Dominant negatif. Reduces NMDA receptor-mediated synaptic currents. 1 Publication1
Mutagenesisi61Q → L: Constitutively active. Interacts with PPP5C. 2 Publications1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000420401 – 189Ras-related C3 botulinum toxin substrate 1Add BLAST189
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000042041190 – 192Removed in mature formBy similarity3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki147Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei189Cysteine methyl esterBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi189S-geranylgeranyl cysteineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q6RUV5

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q6RUV5

PRoteomics IDEntifications database

More...PRIDEi		Q6RUV5

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q6RUV5

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q6RUV5

SwissPalm database of S-palmitoylation events

More...SwissPalmi		Q6RUV5

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Osteoclasts.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSRNOG00000001068, Expressed in cerebellum and 21 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q6RUV5, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q6RUV5, RN

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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).

Interacts with MTSS2 (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).

Interacts (GTP-bound form preferentially) with CYRIB (By similarity).

Interacts with DOCK4 (via DOCKER domain); functions as a guanine nucleotide exchange factor (GEF) for RAC1 (By similarity).

Interacts with GARRE1 (By similarity).

By similarity4 Publications

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		264467, 9 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q6RUV5

Database of interacting proteins

More...DIPi		DIP-37114N

Protein interaction database and analysis system

More...IntActi		Q6RUV5, 5 interactors

Molecular INTeraction database

More...MINTi		Q6RUV5

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000001417

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		Q6RUV5

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q6RUV5

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi32 – 40Effector regionSequence analysis9

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The effector region mediates interaction with DEF6.By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the small GTPase superfamily. Rho family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0393, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000153500

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_041217_21_3_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q6RUV5

Identification of Orthologs from Complete Genome Data

More...OMAi		WLPEITH

Database of Orthologous Groups

More...OrthoDBi		1091615at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q6RUV5

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.300, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR027417, P-loop_NTPase
IPR005225, Small_GTP-bd_dom
IPR001806, Small_GTPase
IPR003578, Small_GTPase_Rho

The PANTHER Classification System

More...PANTHERi		PTHR24072, PTHR24072, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00071, Ras, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00174, RHO, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52540, SSF52540, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00231, small_GTP, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51420, RHO, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iACEDF83A45E5EA67
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2K0X4A0A0G2K0X4_RAT
Ras-related C3 botulinum toxin subs...
Rac1
217Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0U1RS21A0A0U1RS21_RAT
Ras-related C3 botulinum toxin subs...
Rac1
115Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0U1RS18A0A0U1RS18_RAT
Ras-related C3 botulinum toxin subs...
Rac1
22Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AY491395 mRNA Translation: AAR84574.1

NCBI Reference Sequences

More...RefSeqi		NP_599193.1, NM_134366.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSRNOT00000001417; ENSRNOP00000001417; ENSRNOG00000001068

Database of genes from NCBI RefSeq genomes

More...GeneIDi		363875

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:363875

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

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

3D structure databases

BMRBiQ6RUV5
SMRiQ6RUV5
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi264467, 9 interactors
CORUMiQ6RUV5
DIPiDIP-37114N
IntActiQ6RUV5, 5 interactors
MINTiQ6RUV5
STRINGi10116.ENSRNOP00000001417

PTM databases

iPTMnetiQ6RUV5
PhosphoSitePlusiQ6RUV5
SwissPalmiQ6RUV5

Proteomic databases

jPOSTiQ6RUV5
PaxDbiQ6RUV5
PRIDEiQ6RUV5

Genome annotation databases

EnsembliENSRNOT00000001417; ENSRNOP00000001417; ENSRNOG00000001068
GeneIDi363875
KEGGirno:363875

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5879
RGDi619755, Rac1

Phylogenomic databases

eggNOGiKOG0393, Eukaryota
GeneTreeiENSGT00940000153500
HOGENOMiCLU_041217_21_3_1
InParanoidiQ6RUV5
OMAiWLPEITH
OrthoDBi1091615at2759
PhylomeDBiQ6RUV5

Enzyme and pathway databases

ReactomeiR-RNO-114604, GPVI-mediated activation cascade
R-RNO-1257604, PIP3 activates AKT signaling
R-RNO-1433557, Signaling by SCF-KIT
R-RNO-193648, NRAGE signals death through JNK
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-416550, Sema4D mediated inhibition of cell attachment and migration
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-5625740, RHO GTPases activate PKNs
R-RNO-5625900, RHO GTPases activate CIT
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-5663220, RHO GTPases Activate Formins
R-RNO-5668599, RHO GTPases Activate NADPH Oxidases
R-RNO-5687128, MAPK6/MAPK4 signaling
R-RNO-6798695, Neutrophil degranulation
R-RNO-6811558, PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-RNO-8849471, PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases
R-RNO-8875555, MET activates RAP1 and RAC1
R-RNO-9013149, RAC1 GTPase cycle
R-RNO-9032759, NTRK2 activates RAC1
R-RNO-983231, Factors involved in megakaryocyte development and platelet production

Miscellaneous databases

Protein Ontology

More...PROi		PR:Q6RUV5

Gene expression databases

BgeeiENSRNOG00000001068, Expressed in cerebellum and 21 other tissues
ExpressionAtlasiQ6RUV5, baseline and differential
GenevisibleiQ6RUV5, RN

Family and domain databases

Gene3Di3.40.50.300, 1 hit
InterProiView protein in InterPro
IPR027417, P-loop_NTPase
IPR005225, Small_GTP-bd_dom
IPR001806, Small_GTPase
IPR003578, Small_GTPase_Rho
PANTHERiPTHR24072, PTHR24072, 1 hit
PfamiView protein in Pfam
PF00071, Ras, 1 hit
SMARTiView protein in SMART
SM00174, RHO, 1 hit
SUPFAMiSSF52540, SSF52540, 1 hit
TIGRFAMsiTIGR00231, small_GTP, 1 hit
PROSITEiView protein in PROSITE
PS51420, RHO, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRAC1_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q6RUV5
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: July 5, 2004
Last modified: September 29, 2021
This is version 165 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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