1FOE,1E96,1I4D,1HE1,1G4U,1HH4,2C2H


Conserved Protein Domain Family
Rac1_like

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cd01871: Rac1_like 
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Ras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1)-like consists of Rac1, Rac2 and Rac3
The Rac1-like subfamily consists of Rac1, Rac2, and Rac3 proteins, plus the splice variant Rac1b that contains a 19-residue insertion near switch II relative to Rac1. While Rac1 is ubiquitously expressed, Rac2 and Rac3 are largely restricted to hematopoietic and neural tissues respectively. Rac1 stimulates the formation of actin lamellipodia and membrane ruffles. It also plays a role in cell-matrix adhesion and cell anoikis. In intestinal epithelial cells, Rac1 is an important regulator of migration and mediates apoptosis. Rac1 is also essential for RhoA-regulated actin stress fiber and focal adhesion complex formation. In leukocytes, Rac1 and Rac2 have distinct roles in regulating cell morphology, migration, and invasion, but are not essential for macrophage migration or chemotaxis. Rac3 has biochemical properties that are closely related to Rac1, such as effector interaction, nucleotide binding, and hydrolysis; Rac2 has a slower nucleotide association and is more efficiently activated by the RacGEF Tiam1. Both Rac1 and Rac3 have been implicated in the regulation of cell migration and invasion in human metastatic breast cancer. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.
Statistics
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PSSM-Id: 206663
Aligned: 19 rows
Threshold Bit Score: 362.207
Created: 6-Jan-2012
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
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Conserved site includes 9 residues -Click on image for an interactive view with Cn3D
Feature 1:GTP/Mg2+ binding site [chemical binding site]
Evidence:
  • Comment:Rac molecules assume an active conformation when bound to GTP and inactive when GTP is hydrolyzed to GDP
  • Comment:Mg2+ ion plays a key role in bringing together the functional regions of the phosphate-binding, switches I and II
  • Citation:PMID 9545299
  • Structure:1I4D: Human Rac1 binds GDP and Mg2+, defined using 3.5 A contacts
  • Structure:1E96: Human Rac1 binds GTP and Mg2+, defined using 3.5 A contacts

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                  # ####                                                                
1FOE_B         3 AIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICF 82  human
1I4D_D         3 AIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICF 82  human
AAP22281       3 AIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPINLGLWDTAGQEDYDRLRPLSYPQTDVFLICF 82  California sea ...
P40792         3 AIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDAKPINLGLWDTAGQEDYDRLRPLSYPQTDVFLICF 82  fruit fly
Q94124         3 AIKCVVVGDGAVGKTCLLLSYTTNAFPGEYILTVFDTYSTNVMVDGRPINLSLWDTAGQDDYDQFRHLSFPQTDVFLVCF 82  Caenorhabditis ...
NP_990347      3 AIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICF 82  chicken
XP_650831      3 AVKCVIVGDGAVGKTCLLISYTTNAFPNEYIPTVFDNYSATVMVDSKPINLGLWDTAGQEDYDRLRPLSYPQTDVFLICF 82  Entamoeba histo...
XP_640169      3 AIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPINLGLWDTAGQEDYDRLRPLSYPQTDVFLICF 82  Dictyostelium d...
NP_001027692   3 AIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGRPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICF 82  Ciona intestinalis
AAW42478       6 NIKCVVVGDGAVGKTCLLISYTTNAFPGEYVPTVFDNYSSQVIVDGMTVSLGLWDTAGQEDYDRLRPLSYPQTDVFLLCF 85  Cryptococcus ne...
Feature 1                                         # ##                                       #   
1FOE_B        83 SLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLRDDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQ 162 human
1I4D_D        83 SLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLRDDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQ 162 human
AAP22281      83 SLISPTSFENVRAKWFPEVSHHCPHTPIILVGTKLDLREDKETIEKLRDKKLSPITYPQGLAMAREISAVKYLECSALTQ 162 California sea ...
P40792        83 SLVNPASFENVRAKWYPEVRHHCPSTPIILVGTKLDLRDDKNTIEKLRDKKLAPITYPQGLAMAKEIGAVKYLECSALTQ 162 fruit fly
Q94124        83 ALNNPASFENVRAKWYPEVSHHCPNTPIILVGTKADLREDRDTIERLRERRLQPVSHTQGYVMAKEIKAVKYLECSALTQ 162 Caenorhabditis ...
NP_990347     83 SLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLRDDKDTIERLRDKKLAPITYPQGLAMAREIGSVKYLECSALTQ 162 chicken
XP_650831     83 SVVSPPSFDNVSSKWQPEVSHHCPKTPCLLVGTKLDMREDKEQLKRLEEKKITPITTEQGEAKCKDIGAVKYIECSALTQ 162 Entamoeba histo...
XP_640169     83 SIISPSSYENVSGKWGPEVFHHAPNVPIILVGTKMDMREDKETQDRLKEKKLYPVSYEQGLLKMKEINAFKYLECSALTQ 162 Dictyostelium d...
NP_001027692  83 SLVSPASFENVRAKWYPEVAHHCPDTPVILVGTKLDLRDDQETIQKLKEKKLAPILYPQGLQMAKEVNAVKYLECSALTQ 162 Ciona intestinalis
AAW42478      86 SVVSPASFENVRTKWYPEIQHHSPGTPIILVGTKLDLRDDPMQIEKLRERRQAPIGYSQGSSMANDIKAAKYLECSALTQ 165 Cryptococcus ne...
Feature 1                      
1FOE_B       163 RGLKTVFDEAIRAV 176 human
1I4D_D       163 RGLKTVFDEAIRAV 176 human
AAP22281     163 KGLKNVFDEAIRAV 176 California sea hare
P40792       163 KGLKTVFDEAIRSV 176 fruit fly
Q94124       163 IGLKQVFDEAIRTG 176 Caenorhabditis elegans
NP_990347    163 RGLKTVFDEAIRAV 176 chicken
XP_650831    163 KNLRLVFDEAVRAV 176 Entamoeba histolytica HM-1:IMSS
XP_640169    163 KGLKTVFDEAIRSV 176 Dictyostelium discoideum AX4
NP_001027692 163 KGLKTVFDEAIRAV 176 Ciona intestinalis
AAW42478     166 KNLKSVFDEAIRTV 179 Cryptococcus neoformans var. neoformans JEC21

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