RAC2

Rac2 (Ras-related C3 botulinum toxin substrate 2) is a small (~21 kDa) signaling G protein (to be specific, a GTPase), and is a member of the Rac subfamily of the family Rho family of GTPases.[5] It is encoded by the gene RAC2.[6]

RAC2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1DS6, 2W2T, 2W2V, 2W2X
Identifiers
Aliases	RAC2, EN-7, Gx, HSPC022, p21-Rac2, ras-related C3 botulinum toxin substrate 2 (rho family, small GTP binding protein Rac2), Rac family small GTPase 2
External IDs	OMIM: 602049 MGI: 97846 HomoloGene: 55699 GeneCards: RAC2
Gene location (Human) Chr. Chromosome 22 (human)[1] Band 22q13.1 Start 37,225,270 bp[1] End 37,244,448 bp[1]
Gene location (Mouse) Chr. Chromosome 15 (mouse)[2] Band 15|15 E1 Start 78,559,167 bp[2] End 78,572,783 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • nucleotide binding • GTP binding • protein kinase regulator activity • GTPase activity • GO:0001948 protein binding Cellular component • cytoplasm • cytosol • phagocytic vesicle membrane • nuclear envelope • membrane • focal adhesion • cell membrane • actin filament • extracellular exosome • lamellipodium • intracellular Biological process • regulation of respiratory burst • lymphocyte aggregation • regulation of T cell proliferation • positive regulation of protein targeting to mitochondrion • regulation of hydrogen peroxide metabolic process • actin filament organization • regulation of cell-substrate adhesion • regulation of neutrophil migration • bone resorption • platelet activation • chemotaxis • cell projection assembly • positive regulation of cell proliferation • regulation of mast cell chemotaxis • positive regulation of neutrophil chemotaxis • regulation of mast cell degranulation • regulation of protein kinase activity • positive regulation of lamellipodium assembly • regulation of small GTPase mediated signal transduction • actin cytoskeleton organization • signal transduction • small GTPase mediated signal transduction • G-protein coupled receptor signaling pathway Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	5880	19354
Ensembl	ENSG00000128340	ENSMUSG00000033220
UniProt	P15153	Q05144
RefSeq (mRNA)	NM_002872	NM_009008
RefSeq (protein)	NP_002863	NP_033034
Location (UCSC)	Chr 22: 37.23 – 37.24 Mb	Chr 15: 78.56 – 78.57 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Members of Rho family of GTPases appear to regulate a diverse array of cellular events, including the control of cell growth, cytoskeletal reorganization, and the activation of protein kinases.[6]

Interactions

Rac2 has been shown to interact with ARHGDIA[7][8] and Nitric oxide synthase 2A.[9]

See also

• NADPH oxidase

References

1. GRCh38: Ensembl release 89: ENSG00000128340 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000033220 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Ridley AJ (2006). "Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking". Trends Cell Biol. 16 (10): 522–9. doi:10.1016/j.tcb.2006.08.006. PMID 16949823.
6. "Entrez Gene: RAC2 ras-related C3 botulinum toxin substrate 2 (rho family, small GTP binding protein Rac2)".
7. Gorvel JP, Chang TC, Boretto J, Azuma T, Chavrier P (January 1998). "Differential properties of D4/LyGDI versus RhoGDI: phosphorylation and rho GTPase selectivity". FEBS Lett. 422 (2): 269–73. doi:10.1016/S0014-5793(98)00020-9. PMID 9490022.
8. Fauré J, Dagher MC (May 2001). "Interactions between Rho GTPases and Rho GDP dissociation inhibitor (Rho-GDI)". Biochimie. 83 (5): 409–14. doi:10.1016/S0300-9084(01)01263-9. PMID 11368848.
9. Kuncewicz T, Balakrishnan P, Snuggs MB, Kone BC (August 2001). "Specific association of nitric oxide synthase-2 with Rac isoforms in activated murine macrophages". Am. J. Physiol. Renal Physiol. 281 (2): F326-36. PMID 11457725.

Further reading

• Mizuno T, Kaibuchi K, Ando S, Musha T, Hiraoka K, Takaishi K, Asada M, Nunoi H, Matsuda I, Takai Y (1992). "Regulation of the superoxide-generating NADPH oxidase by a small GTP-binding protein and its stimulatory and inhibitory GDP/GTP exchange proteins". J. Biol. Chem. 267 (15): 10215–8. PMID 1316893.
• Reibel L, Dorseuil O, Stancou R, Bertoglio J, Gacon G (1991). "A hemopoietic specific gene encoding a small GTP binding protein is overexpressed during T cell activation". Biochem. Biophys. Res. Commun. 175 (2): 451–8. doi:10.1016/0006-291X(91)91585-Z. PMID 1902092.
• Kinsella BT, Erdman RA, Maltese WA (1991). "Carboxyl-terminal isoprenylation of ras-related GTP-binding proteins encoded by rac1, rac2, and ralA". J. Biol. Chem. 266 (15): 9786–94. PMID 1903399.
• Didsbury J, Weber RF, Bokoch GM, Evans T, Snyderman R (1989). "rac, a novel ras-related family of proteins that are botulinum toxin substrates". J. Biol. Chem. 264 (28): 16378–82. PMID 2674130.
• Kwong CH, Malech HL, Rotrosen D, Leto TL (1993). "Regulation of the human neutrophil NADPH oxidase by rho-related G-proteins". Biochemistry. 32 (21): 5711–7. doi:10.1021/bi00072a029. PMID 8504089.
• Courjal F, Chuchana P, Theillet C, Fort P (1997). "Structure and chromosomal assignment to 22q12 and 17qter of the ras-related Rac2 and Rac3 human genes". Genomics. 44 (2): 242–6. doi:10.1006/geno.1997.4871. PMID 9299243.
• Gorvel JP, Chang TC, Boretto J, Azuma T, Chavrier P (1998). "Differential properties of D4/LyGDI versus RhoGDI: phosphorylation and rho GTPase selectivity". FEBS Lett. 422 (2): 269–73. doi:10.1016/S0014-5793(98)00020-9. PMID 9490022.
• Dai Q, Choy E, Chiu V, Romano J, Slivka SR, Steitz SA, Michaelis S, Philips MR (1998). "Mammalian prenylcysteine carboxyl methyltransferase is in the endoplasmic reticulum". J. Biol. Chem. 273 (24): 15030–4. doi:10.1074/jbc.273.24.15030. PMID 9614111.
• Ahmed S, Prigmore E, Govind S, Veryard C, Kozma R, Wientjes FB, Segal AW, Lim L (1998). "Cryptic Rac-binding and p21(Cdc42Hs/Rac)-activated kinase phosphorylation sites of NADPH oxidase component p67(phox)". J. Biol. Chem. 273 (25): 15693–701. doi:10.1074/jbc.273.25.15693. PMID 9624165.
• Faris SL, Rinckel LA, Huang J, Hong YR, Kleinberg ME (1998). "Phagocyte NADPH oxidase p67-phox possesses a novel carboxylterminal binding site for the GTPases Rac2 and Cdc42". Biochem. Biophys. Res. Commun. 247 (2): 271–6. doi:10.1006/bbrc.1998.8775. PMID 9642115.
• Zhang B, Zheng Y (1998). "Negative regulation of Rho family GTPases Cdc42 and Rac2 by homodimer formation". J. Biol. Chem. 273 (40): 25728–33. doi:10.1074/jbc.273.40.25728. PMID 9748241.
• Nishihara H, Kobayashi S, Hashimoto Y, Ohba F, Mochizuki N, Kurata T, Nagashima K, Matsuda M (1999). "Non-adherent cell-specific expression of DOCK2, a member of the human CDM-family proteins". Biochim. Biophys. Acta. 1452 (2): 179–87. doi:10.1016/S0167-4889(99)00133-0. PMID 10559471.
• Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP (1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–95. doi:10.1038/990031. PMID 10591208.
• Scheffzek K, Stephan I, Jensen ON, Illenberger D, Gierschik P (2000). "The Rac-RhoGDI complex and the structural basis for the regulation of Rho proteins by RhoGDI". Nat. Struct. Biol. 7 (2): 122–6. doi:10.1038/72392. PMID 10655614.
• Ambruso DR, Knall C, Abell AN, Panepinto J, Kurkchubasche A, Thurman G, Gonzalez-Aller C, Hiester A, deBoer M, Harbeck RJ, Oyer R, Johnson GL, Roos D (2000). "Human neutrophil immunodeficiency syndrome is associated with an inhibitory Rac2 mutation". Proc. Natl. Acad. Sci. U.S.A. 97 (9): 4654–9. doi:10.1073/pnas.080074897. PMC 18288. PMID 10758162.
• Williams DA, Tao W, Yang F, Kim C, Gu Y, Mansfield P, Levine JE, Petryniak B, Derrow CW, Harris C, Jia B, Zheng Y, Ambruso DR, Lowe JB, Atkinson SJ, Dinauer MC, Boxer L (2000). "Dominant negative mutation of the hematopoietic-specific Rho GTPase, Rac2, is associated with a human phagocyte immunodeficiency". Blood. 96 (5): 1646–54. PMID 10961859.
• Tamura M, Kai T, Tsunawaki S, Lambeth JD, Kameda K (2000). "Direct interaction of actin with p47(phox) of neutrophil NADPH oxidase". Biochem. Biophys. Res. Commun. 276 (3): 1186–90. doi:10.1006/bbrc.2000.3598. PMID 11027608.
• Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z (2000). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Res. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152.
• Lapouge K, Smith SJ, Walker PA, Gamblin SJ, Smerdon SJ, Rittinger K (2000). "Structure of the TPR domain of p67phox in complex with Rac.GTP". Mol. Cell. 6 (4): 899–907. doi:10.1016/S1097-2765(05)00091-2. PMID 11090627.
• Tarricone C, Xiao B, Justin N, Walker PA, Rittinger K, Gamblin SJ, Smerdon SJ (2001). "The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways". Nature. 411 (6834): 215–9. doi:10.1038/35075620. PMID 11346801.

External links

• RAC2 Info with links in the Cell Migration Gateway