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RAC2
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	1DS6, 2W2T, 2W2V, 2W2X
Identifikatori
Aliasi	RAC2
Vanjski ID-jevi	OMIM: 602049 MGI: 97846 HomoloGene: 55699 GeneCards: RAC2
EC broj	3.6.5.2
Lokacija gena (čovjek)
Hrom.	Hromosom 22 (čovjek)
Kraj	37,244,448 bp
Lokacija gena (miš)
Hrom.	Hromosom 15 (miš)
Kraj	78,456,983 bp
Obrazac RNK ekspresije
	Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija	• nucleotide binding; • GTP binding; • protein kinase regulator activity; • GO:0006184 GTPase activity; • GO:0001948, GO:0016582 vezivanje za proteine;
Ćelijska komponenta	• citoplazma; • citosol; • phagocytic vesicle membrane; • nuclear envelope; • membrana; • focal adhesion; • ćelijska membrana; • Mikronit; • Egzosom; • lamellipodium; • intracellular anatomical structure;
Biološki proces	• 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; • Hemotaksija; • cell projection assembly; • positive regulation of cell population 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; • GO:0072468 Transdukcija signala; • small GTPase mediated signal transduction; • G protein-coupled receptor signaling pathway;
	Izvori:Amigo / QuickGO
Ortolozi
	5880
	19354
	ENSG00000128340
	ENSMUSG00000033220
	P15153
	Q05144
	NM_002872
	NM_009008
	NP_002863
	NP_033034
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Rac2 (Ras-srodni C3 botulinum toksinski sustrat) je mali (~21 kDa) signalni G-protein (specifična GTPaza), član potporodice Rac-proteina u porodici Rho GTPaza, jest protein koji je kod ljudi kodiran genom sa hromosoma 22.^[5]^[6]

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 192 aminokiseline, a molekulska težina 21.429 Da.^[6]

C: Cistein

D: Asparaginska kiselina

E: Glutaminska kiselina

F: Fenilalanin

G: Glicin

H: Histidin

I: Izoleucin

K: Lizin

L: Leucin

M: Metionin

N: Asparagin

P: Prolin

Q: Glutamin

R: Arginin

S: Serin

T: Treonin

V: Valin

W: Triptofan

Y: Tirozin

10	20	30	40	50
MQAIKCVVVG	DGAVGKTCLL	ISYTTNAFPG	EYIPTVFDNY	SANVMVDSKP
VNLGLWDTAG	QEDYDRLRPL	SYPQTDVFLI	CFSLVSPASY	ENVRAKWFPE
VRHHCPSTPI	ILVGTKLDLR	DDKDTIEKLK	EKKLAPITYP	QGLALAKEID
SVKYLECSAL	TQRGLKTVFD	EAIRAVLCPQ	PTRQQKRACS	LL

Funkcija

Članovi Rho porodice GTPaza reguliraju raznolik niz ćelijskih događaja, uključujući kontrolu rasta ćelija, reorganizaciju citoskeleta i aktivaciju protein ]]kinaza]].^[6]

Interakcije

Pokazalo se da Rac2 reaguje sa ARHGDIA^[7]^[8] i dušik-oksid sintazom 2A.^[9]

Također pogledajte

NADPH oksidaza

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000128340 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000033220 - Ensembl, maj 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ ^a ^b ^c "Entrez Gene: RAC2 ras-related C3 botulinum toxin substrate 2 (rho family, small GTP binding protein Rac2)".
^ Gorvel JP, Chang TC, Boretto J, Azuma T, Chavrier P (januar 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. S2CID 10817327.
^ Fauré J, Dagher MC (maj 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.
^ 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. doi:10.1152/ajprenal.2001.281.2.F326. PMID 11457725.

Dopunska literatura

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. doi:10.1016/S0021-9258(19)50005-9. 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. doi:10.1016/S0021-9258(18)92889-9. 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. doi:10.1016/S0021-9258(19)84716-6. 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. S2CID 10817327.
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. S2CID 6759163.
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. S2CID 4324211.

Vanjski linkovi

RAC2 Info with links in the Cell Migration Gateway Arhivirano 11. 12. 2014. na Wayback Machine

Šablon:Rho porodica GTPaza

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000128340 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000033220 - Ensembl, maj 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.

[Ridley-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.

[entrez-6] "Entrez Gene: RAC2 ras-related C3 botulinum toxin substrate 2 (rho family, small GTP binding protein Rac2)".

[pmid9490022-7] Gorvel JP, Chang TC, Boretto J, Azuma T, Chavrier P (januar 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. S2CID 10817327.

[pmid11368848-8] Fauré J, Dagher MC (maj 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.

[pmid11457725-9] 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. doi:10.1152/ajprenal.2001.281.2.F326. PMID 11457725.

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RAC2