1LB1,1CC0,1X86,1CXZ,1S1C,1Z2C


Conserved Protein Domain Family
RhoA_like

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cd01870: RhoA_like 
Click on image for an interactive view with Cn3D
Ras homology family A (RhoA)-like includes RhoA, RhoB and RhoC
The RhoA subfamily consists of RhoA, RhoB, and RhoC. RhoA promotes the formation of stress fibers and focal adhesions, regulating cell shape, attachment, and motility. RhoA can bind to multiple effector proteins, thereby triggering different downstream responses. In many cell types, RhoA mediates local assembly of the contractile ring, which is necessary for cytokinesis. RhoA is vital for muscle contraction; in vascular smooth muscle cells, RhoA plays a key role in cell contraction, differentiation, migration, and proliferation. RhoA activities appear to be elaborately regulated in a time- and space-dependent manner to control cytoskeletal changes. 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. RhoA and RhoC are observed only in geranylgeranylated forms; however, RhoB can be present in palmitoylated, farnesylated, and geranylgeranylated forms. RhoA and RhoC are highly relevant for tumor progression and invasiveness; however, RhoB has recently been suggested to be a tumor suppressor. 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: 206662
Aligned: 27 rows
Threshold Bit Score: 318.218
Created: 6-Jan-2012
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
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Conserved site includes 15 residues -Click on image for an interactive view with Cn3D
Feature 1:GTP/Mg2+ binding site [chemical binding site]
Evidence:
  • Structure:1CC0: Human RhoA binds GDP and Mg2+, defined using 3.5 A contacts
  • Comment:Mg2+ ion plays a key role in bringing together the functional regions of the phosphate-binding, switches I and II
  • Comment:Rho molecules assume an active conformation when bound to GTP and inactive when GTP is hydrolyzed to GDP
  • Citation:PMID 9545299

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                  ######             ## #                     ##                        
1LB1_F         7 RKKLVIVGDGACGKTCLLIVFSKDQfpevYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCF 86  human
1CC0_A         5 RKKLVIVGDGACGKTCLLIVNSKDQfpevYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCF 84  human
AAD31508       6 RKKLVIVGDGACGKTCLLIVFSKDQfpevYVPTVFENYVADIEVDNRQVELALWDTAGQEDYDRLRPLSYPDTDVVLLCY 85  Schistosoma man...
Q09914         6 RRKLVIVGDGACGKTCLLIVFSKGTfpevYVPTVFENYVADVEVDGRHVELALWDTAGQEDYDRLRPLSYPDSHVILICF 85  fission yeast
CAC82554       5 RKKLKIDGEGACGKTCLLIXFSKDQfpevYVPTVFENYVADIEVDSKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCF 84  Ciona intestinalis
AAW44712       6 RRKLVIVGDGACGKTCLLIVFSKGMfpevYVPTVFENYVADVEVDGKKVELALWDTAGQEDYDRLRPLSYPDSHVILICF 85  Cryptococcus ne...
NP_001229582   5 RKKLVIVGDGACGKTCLLIVFSKDQfpevYVPTVFENYVADIEVDSKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCF 84  purple urchin
AEO34010       5 RKKLVIVGDGACGKTCLLIVFSKDQfpevYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCF 84  Amblyomma macul...
BAE95627       5 RKKLVIVGDGACGKTCLLIVFSKDQfpevYVPTVFENYVADIEVDGKLVELALWDTAGQEDYDRLRPLSYPDTDVILMCF 84  Japanese lancelet
XP_003385965   5 RKKLVIVGDGACGKTCLLIVFSKDQfpevYVPTVFENYVADIEVDGKCVELALWDTAGQEDYDRLRPLSYPDTDVILMCF 84  Amphimedon quee...
Feature 1                                         # #                                        ##  
1LB1_F        87 SIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTK 166 human
1CC0_A        85 SIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTK 164 human
AAD31508      86 SIDSPDSFANIEEKWLPEIRHFCPDVPIVLVGNKKDLRHDEATKNELHRTKQLPVTFNEGKQVAEKISAYAFFECSAKTK 165 Schistosoma man...
Q09914        86 AVDSPDSLDNVQEKWISEVLHFCSSLPILLVACKADLRNDPKIIEELSKTNQHPVTTEEGQAVAQKIGAYKYLECSAKTN 165 fission yeast
CAC82554      85 SIDSPDSLENIPEKWTPEVRHFCPSVPIILVGNKKDLRNGSSTIKELAKMKQSAVSNEDGMAMADKIGAYGYMECSARTK 164 Ciona intestinalis
AAW44712      86 AIDSPDSLDNVQEKWISEVLHFCQGLPIVLVACKKDLRDDGKTIQDLARMNQRPVSRAEGMAVAQKIGAQGYVECSAKTG 165 Cryptococcus ne...
NP_001229582  85 AIDNPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRNDDNTKMELQRTKQTPVTYDEGHQMSVKINAAKYMECSAKTN 164 purple urchin
AEO34010      85 SIDSPDSLENILEKWHPEVKHFCPSVPIVLVANKKDLRSDPATVKELGKMKQEPVKSDEGRAMADRISAFGYLECSAKTK 164 Amblyomma macul...
BAE95627      85 SIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRNDETTKRELAKMKQEPVKTEEGRHMAEMINAFAYLECSAKTK 164 Japanese lancelet
XP_003385965  85 SIDSPDSLENIPEKWTPEVRHFCPTVPIVLVGNKKDLRYDEGTRRELSKSKQEPVKTEEGRAMADKIGAYNYLECSAKLN 164 Amphimedon quee...
Feature 1                       
1LB1_F       167 DGVREVFEMATRAAL 181 human
1CC0_A       165 DGVREVFEMATRAAL 179 human
AAD31508     166 EGVSDVFVAATRAAL 180 Schistosoma mansoni
Q09914       166 EGVREVFESATRAAM 180 fission yeast
CAC82554     165 EGVREVFELATKAAL 179 Ciona intestinalis
AAW44712     166 EGVREVFQTATRHAL 180 Cryptococcus neoformans var. neoformans JEC21
NP_001229582 165 DGVREVFETATRAAL 179 purple urchin
AEO34010     165 EGVREVFEMATRAAL 179 Amblyomma maculatum
BAE95627     165 EGVREVFETATKAAL 179 Japanese lancelet
XP_003385965 165 EGVREVFETATRAAL 179 Amphimedon queenslandica

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