Conserved Protein Domain Family
Rab24

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cd04118: Rab24 
Rab GTPase family 24 (Rab24)
Rab24 is distinct from other Rabs in several ways. It exists primarily in the GTP-bound state, having a low intrinsic GTPase activity; it is not efficiently geranyl-geranylated at the C-terminus; it does not form a detectable complex with Rab GDP-dissociation inhibitors (GDIs); and it has recently been shown to undergo tyrosine phosphorylation when overexpressed in vitro. The specific function of Rab24 still remains unknown. It is found in a transport route between ER-cis-Golgi and late endocytic compartments. It is putatively involved in an autophagic pathway, possibly directing misfolded proteins in the ER to degradative pathways. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins.
Statistics
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PSSM-Id: 133318
View PSSM: cd04118
Aligned: 5 rows
Threshold Bit Score: 313.34
Threshold Setting Gi: 66828159
Created: 9-Aug-2005
Updated: 17-Jan-2013
Structure
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Aligned Rows:
  next features
Feature 1:GTP/Mg2+ binding site [chemical binding site]
Evidence:
  • Comment:Based on sequence similarity with other Rab isoforms.
  • Comment:The active conformation of Rab is stabilized by interations between the gamma phosphate of GTP and two critically conserved residues, Thr in switch I and Gly in switch II

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1               #######         #      ##                         #                     
gi 8953548    7 AKVVMLGKESVGKTSLVERYVHHRFLvgpyQNTIGAAFVAKPIQVGDKVVTLGIWDTAGSERYEAMSRIYYRGARAAIVC 86
gi 66828159   8 LKVVLLGYASVGKTCIVTRYTSGQFGd--tHTTIGGAFSSKRVVVGETEVLLGIWDTAGTERYQAVNVSYYRRANAAIVC 85
gi 23396831   8 VKVVMLGKEYVGKTSLVERYVHDRFLvgpyQNTIGAAFVAKVMSVGDRTVTLGIWDTAGSERYEAMSRIYYRGAKAAIVC 87
gi 71480086   8 AKVVMLGKESVGKTSLVERYVHRRFLvgpyQNTIGAAFVAKALNVGEKVITLGIWDTAGSERYEAMSRIYYRGARAAIVC 87
gi 46250042   8 VKVVMLGKESVGKTSLVERYVHHRFLhgpcQNTIGAAFVAKTMYVEGRSLTLGIWDTAGSERYEAMSRIYYRGAKAAIVC 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                       ## #                              ###           
gi 8953548   87 YDLTDISSFQRAKFWVKEVQNCEEHCKIYLCGTKVDLIesdrglRQVDYHDVQDFADEIGAQHFETSSKTGNNVDELFQK 166
gi 66828159  86 YDLTNRESWEKVTFWAEELTQNEPEIEIYIVGTKLDLIqqg-diKAVPEEEVKQTARRYKAHIFETSSRTGENVSLLFQT 164
gi 23396831  88 YDLTDSSSFERAKFWVKELRSLEEGCQIYLCGTKSDLLeedrrrRRVDFHDVQDYADNIKAQLFETSSKTGQSVDELFQK 167
gi 71480086  88 YDLTDSSSFGRARFWVKELQNCEEHCKIYLCGTKSDLIeadrstRQVDYHDVQDFADEIGAQHFETSSKTGKNVDEVFQK 167
gi 46250042  88 YDLTDASSFERVKFWVNELQNLEEHCRIYICGTKSDLLendkslRQVDFHDVQDFAEEIKAHVCETSSKTGQSVDELFQK 167
                       170       180       190
                ....*....|....*....|....*....|....*...
Feature 1                                             
gi 8953548  167 VAEDFnsisfqfmtee-----agidlgqkkdsYFYSCC 199
gi 66828159 165 IAEDFckrtnngtnpvnsnpsnvvnvntqtqkKKGGCC 202
gi 23396831 168 VAEDYvsvaafqvmted----kgvdlgqkpnpYFYSCC 201
gi 71480086 168 VAEDFsscalefmqee-----kgvdlgqkkdsYFDNCC 200
gi 46250042 168 VAEDYvnfnctqspte------ekgvdlnqnsAMYSCC 199

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