Conserved Protein Domain Family
RhoG

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cd01875: RhoG 
Ras homolog family, member G (RhoG) of small guanosine triphosphatases (GTPases)
RhoG is a GTPase with high sequence similarity to members of the Rac subfamily, including the regions involved in effector recognition and binding. However, RhoG does not bind to known Rac1 and Cdc42 effectors, including proteins containing a Cdc42/Rac interacting binding (CRIB) motif. Instead, RhoG interacts directly with Elmo, an upstream regulator of Rac1, in a GTP-dependent manner and forms a ternary complex with Dock180 to induce activation of Rac1. The RhoG-Elmo-Dock180 pathway is required for activation of Rac1 and cell spreading mediated by integrin, as well as for neurite outgrowth induced by nerve growth factor. Thus RhoG activates Rac1 through Elmo and Dock180 to control cell morphology. RhoG has also been shown to play a role in caveolar trafficking and has a novel role in signaling the neutrophil respiratory burst stimulated by G protein-coupled receptor (GPCR) agonists. 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.
Statistics
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PSSM-Id: 133277
View PSSM: cd01875
Aligned: 4 rows
Threshold Bit Score: 422.11
Threshold Setting Gi: 27881890
Created: 6-Jan-2012
Updated: 17-Jan-2013
Structure
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Aligned Rows:
  next features
Feature 1:GTP/Mg2+ binding site [chemical binding site]
Evidence:
  • Comment:Rho 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

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                   ######                                      ## #                    
gi 51338611   1 MQSIKCVVVGDGAVGKTCLLICYTTNAFPKEYIPTVFDNYSAQSAVDGRTVNLNLWDTAGQEEYDRLRTLSYPQTNVFVI 80
gi 37589358   1 MQSIKCVVVGDGAVGKTCLLICFTTNAFPKEYIPTVFDNYSAQTAVDGRTVSLNLWDTAGQEEYDRLRTLSYPQTNVFII 80
gi 27881890   1 MQTIKCVVVGDGAVGKTCLLISYTTNAFPDEYIPTVFDNYSTQTCVDGRAVSLNLWDTAGQEEYDRLRTLSYPQTHVFII 80
gi 53127384   1 MQTIKCVVVGDGAVGKTCLLISYTTNAFPEEYIPTVFDNYSAQMTVDGRTVSLNLWDTAGQEEYDRLRTLSYPQTNVFVI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                          # #                                        ##
gi 51338611  81 CFSIASPPSYENVRHKWHPEVCHHCPDVPILLVGTKKDLRAQPDTLRRLKEQGQAPITPQQGQALAKQIHAVRYLECSAL 160
gi 37589358  81 CFSIASPTSYENVKHKWYPEVGHHCPNVPILLVGTKKDLRNNADVIKKLKEQNQMPITNHQGGNLAKQIHAVKYMECSAL 160
gi 27881890  81 CFSVASPSSHANVRHKWHPEVCHHCPGVPVLLVGTKRDLRGDKETLEKLKEQGMSPTTPQQGSALARSIGAVRYLECSAL 160
gi 53127384  81 CFSIGSPSSYANVRHKWHPEVSHHCPNVPILLVGTKRDLRNDLETVKKLKEQSLAPTTPQQGTSLAKQIGAVKYLECSAL 160
                       170       180       190
                ....*....|....*....|....*....|.
Feature 1                                      
gi 51338611 161 QQDGVKEVFAEAVRAVLNPTPIKRGRSCILL 191
gi 37589358 161 NQDGIKEVFADAVRAVLNPTPIKDKKSCFIL 191
gi 27881890 161 LQEGVREVFNEAVRAVLYPNAKKHTKKCVLL 191
gi 53127384 161 NQEGVREVFAEAVRAVLYPVTKKNTRKCVLL 191

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