1Z0K


Conserved Protein Domain Family
Rab4

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cd04113: Rab4 
Click on image for an interactive view with Cn3D
Rab GTPase family 4 (Rab4)
Rab4 subfamily. Rab4 has been implicated in numerous functions within the cell. It helps regulate endocytosis through the sorting, recycling, and degradation of early endosomes. Mammalian Rab4 is involved in the regulation of many surface proteins including G-protein-coupled receptors, transferrin receptor, integrins, and surfactant protein A. Experimental data implicate Rab4 in regulation of the recycling of internalized receptors back to the plasma membrane. It is also believed to influence receptor-mediated antigen processing in B-lymphocytes, in calcium-dependent exocytosis in platelets, in alpha-amylase secretion in pancreatic cells, and in insulin-induced translocation of Glut4 from internal vesicles to the cell surface. Rab4 is known to share effector proteins with Rab5 and Rab11. 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. 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: 206696
View PSSM: cd04113
Aligned: 10 rows
Threshold Bit Score: 304.743
Threshold Setting Gi: 29336944
Created: 9-Aug-2005
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
  next features
Conserved site includes 17 residues -Click on image for an interactive view with Cn3D
Feature 1:GTP/Mg2+ binding site [chemical binding site]
Evidence:
  • 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
  • Structure:1Z0K: Human Rab4q67l binds GTP and Mg2+, defined using 3.5 A contacts
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1               #######         #   #  #                         #                      
1Z0K_A        9 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINvggkYVKLQIWDTAGLERFRSVTRSYYRGAAGALLVY 88
gi 71006432  17 LKFIIIGEAGTGKSCLLHHFIHNQFKEQSAHTIGVEFSSRLIKignkSVKLQLWDTAGQERFRSVTRSYYRGAAGALLVY 96
gi 13785146   9 FKYLIIGNSGTGKSCVLHQFLENKFKQDTAHTIGIEFGSKVVKiqdrSIKLQVWDTAGQERFRSLTKNYYNGAACALLVY 88
gi 45552705   9 FKFLIIGSAGSGKSCLLHHFIESKFKDDSSHTIGVEFGSRIVNvggkSVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 88
gi 27924185   9 FKFLVIGSAGTGKSCLLHQFIESKFKQDSNHTIGVEFGSRIVNvggkSVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 88
gi 57524538   9 FKFLVIGSAGTGKSCLLHQFIENKFKQDSNHTIGVEFGSRVVNvggkTVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 88
gi 66801327   8 VKFIIIGSQSVGKSCLLFRFIDNKFKSQSTHTIGVDFSSRVVDiqgkNVKLQIWDTAGQERFRSVVISYYRGSAGVALVY 87
gi 56753091  11 FKFLIIGAAGSGKTCILRRYTEGKFIHNMPHTIGAEFGSKIINvdgtTVKIQIWDTAGQERFRSMARSYYHDAVGALLVY 90
gi 57227453  16 FKFIVIGEAGTGKSCLLYQCIHEQFKENSSHTIGVEFSSKTLRigdkNIKLQLWDTAGQERFRSVTRSYYRGAAGAILVY 95
gi 29336944  10 FKFLIIGNAGTGKTCILRRYTERKFFPNTQHTIGAEFGSRVISvdgtHVKIQIWDTAGQERFRSMARSYYHDAVGTLLVY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                       ## ##                           ##              
1Z0K_A       89 DITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLda-dREVTFLEASRFAQENelMFLETSALTGEDVEEAFVQCAR 167
gi 71006432  97 DITKRSTFEPLSRWLTDARALASPDLVVVLVGNKTDRgddeREVGYLEASKWANENgvLFLETSSITGENVEAPFALAAR 176
gi 13785146  89 DITCRQSFNAIAQWLSDARSLASPQIIVILIGNKKDLed-rREVTFMEASQFAQENgmLFLETSALTGENIEETFLRCAR 167
gi 45552705  89 DATSRDSFNALTNWLNDARTLASPNIVILLVGNKKDLee-aRDVTFLEASTFAQENelIFLETSAKTGENVEEAFLKCSK 167
gi 27924185  89 DIASRETYNALTNWLTDARTLASPNIIIILCGNKKDLda-dREVTFLEASRFAQENelMFLETSALTGENVEEAFLKCAR 167
gi 57524538  89 DITSRETYNALTNWLTDARTLASPNIVIILCGNKKDLda-dREVTFLEASRFAQENelMFLETSALTGENVEEAFLKCAR 167
gi 66801327  88 DVTNRESYNHITNWLSDVKSLASPDVTIILVGNKADLte-qREVTFLEASRIAQENglLFMETSALTGEGVEEMFLKCTR 166
gi 56753091  91 DVTNRDSFNDLGYWLSDARTLASPDIMIVLVGNKKDLqdtdGQVTQWEASAFAQDNdlHFLETSALTGENVEEAFTECVR 170
gi 57227453  96 DITSRQSFVNLSRWLTDCRALASPHLVVVLVGNKLDKee-dREVEYTEGSRWAQENglLFVEVSSLTGKNVSTPFLLAGR 174
gi 29336944  90 DITNRTSFGAVEQWLGDARHLATPGVVVILVGNKKDLrdtdGQVTHWEANTFAQENglQFIETSALTGENIDDAFTSCVR 169

                ..
Feature 1         
1Z0K_A      168 KI 169
gi 71006432 177 SI 178
gi 13785146 168 SI 169
gi 45552705 168 TI 169
gi 27924185 168 TI 169
gi 57524538 168 SI 169
gi 66801327 167 TI 168
gi 56753091 171 SL 172
gi 57227453 175 TI 176
gi 29336944 170 VL 171

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