1OIW,3BFK,3CPJ


Conserved Protein Domain Family
Rab11_like

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cd01868: Rab11_like 
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Rab GTPase family 11 (Rab11)-like includes Rab11a, Rab11b, and Rab25
Rab11a, Rab11b, and Rab25 are closely related, evolutionary conserved Rab proteins that are differentially expressed. Rab11a is ubiquitously synthesized, Rab11b is enriched in brain and heart and Rab25 is only found in epithelia. Rab11/25 proteins seem to regulate recycling pathways from endosomes to the plasma membrane and to the trans-Golgi network. Furthermore, Rab11a is thought to function in the histamine-induced fusion of tubulovesicles containing H+, K+ ATPase with the plasma membrane in gastric parietal cells and in insulin-stimulated insertion of GLUT4 in the plasma membrane of cardiomyocytes. Overexpression of Rab25 has recently been observed in ovarian cancer and breast cancer, and has been correlated with worsened outcomes in both diseases. In addition, Rab25 overexpression has also been observed in prostate cancer, transitional cell carcinoma of the bladder, and invasive breast tumor cells. 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: 206660
Aligned: 49 rows
Threshold Bit Score: 283.682
Created: 6-Jan-2012
Updated: 2-Oct-2020
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:
  • Structure:1OIW: Human Rab11a binds GTP-gamma-S, a GTP analog and Mg2+, defined using 3.5 A contacts

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                #######          #  #  #                             #               
1OIW_A     27 DYLFKVVLIGDSGVGKSNLLSRFTRNEFNlESKSTIGVEFATRSIQVD----GKTIKAQIWDTAGLERYRAITSAYYRGA 102 Homo sapiens
AAO49245    6 DHLYKLILIGDSAVGKSNILSRFTSNKFNaSSAATIGVEFTTKTLTVEvqgkMISTRLQCWDTAGQERYRSITSSYYRGA 85  Giardia intestinalis
CAI44535    9 DLLYKLVLIGDSGVGKTNILNQFTRGEFLqDSKTTIGVEFASKNIMID----DKTVKAQIWDTAGQERYRAITSAYYRGA 84  Paramecium tetraur...
CAI44537    9 DYLFKVVLSGDSGVGKSNLLLRFTKNQFNpDSKTTIGVEFATRSISIS----GKIIKAQIWDTAGQERYRAITSAYYRGA 84  Paramecium tetraur...
CAI39309   10 KHLFKIVLIGDSSVGKSNILSRFTKRQFNfDSQPTIGVEFATRSLTEN----GKIIQAQIWDTCGQERYKSITSAYYRGA 85  Paramecium tetraur...
CAI39320    8 DYQYKIVIIGDSGVGKTNIMTQFTRGEFSeETKTTVGVEFANKQLVID----DKIIKAQLWDTAGQERYRAIISSYYKGA 83  Paramecium tetraur...
CAI39337   10 DYLFKIVLIGDSGVGKTNILKRFINNEFQlESKPTIGVEFATKTFQQQ----GKSVKCQIWDTAGQERFRAITNAYYRGA 85  Paramecium tetraur...
CAI39292    8 DILMKIIIVGDSGVGKTNLVNRFAQQKFLdDSKPTVGVEFFFRHIDIM----GKTIKAQVWDTAGQEKFRAITYGYYRGA 83  Paramecium tetraur...
CAI44562    7 SYLFKIILIGDSGVGKTNLFNRLQNKEFQyDTRPTIGVEFINRTVRQD----GNLVKCQIWDTAGQEKFRAITNAYYRGA 82  Paramecium tetraur...
CAI44483   10 DFLFKIILIGDSGVGKTNILQRFVKNEFIlDSKPTIGVEFSTKTINVE----NKSVKCQIWDTAGQERYRAITNAYYRGA 85  Paramecium tetraur...
Feature 1                                              ## #                          ###      
1OIW_A    103 VGALLVYDIAKHLTYENVERWLKELRDHADs--nIVIMLVGNKSDLRHLRAVPTDEARAFAEKNgLSFIETSALdSTNVE 180 Homo sapiens
AAO49245   86 HGCLLVFDVTKRTSFEHCTEWLTELRNASAnstaCKVILVGNKVDLRHLREVTTEEATAFAQQQgLSYIETSASsGHGID 165 Giardia intestinalis
CAI44535   85 VGAMIIYDITKSLTFENVDKWMKELKENADp--sLQIMIVGNKTDQKHIRQVATDCAIAYAQRNgVAFIETSAKdGTNVE 162 Paramecium tetraur...
CAI44537   85 IGAVLVYDITNKQSFESVERWIQEVRENADk--dIVIMIIGNKSDLKHLRAIRTESGQDLAQMYkVAFMEASAQdGTNVD 162 Paramecium tetraur...
CAI39309   86 VGAMLIYDITKQKTFENIEKWIQELKEYAEt--nVVAMLIGNKADLKAQRKVPSDKAAQFAENHtMAFMEVSAFdGTNVD 163 Paramecium tetraur...
CAI39320   84 SGALIVFDITKQSTFDNVDRWMKVQESTSNe---ISIILVGNKSDLRHLRQVSSDVSSAYASKHkIAFLETSAKdGANVN 160 Paramecium tetraur...
CAI39337   86 VGAFICYDITREITFKNTEKWLSELKEHADg--nIVIIMIGNKIDAVDSRAVRTDEAQDYCESQkIGFIETSALdGTNID 163 Paramecium tetraur...
CAI39292   84 LGAMICYDITKEQSFLNVERWIEELREHGDs--nLVMMLIGTKSDLESKRVVRNEDGTQKALQHnMAFLETSALkAANVG 161 Paramecium tetraur...
CAI44562   83 KGVFVCYDVTKQGTYESTLRWMSEIKQFGDh--dIVIMLVGNKIDLAEQRIVRTDEVSQFCEQNkVGYIETSALnNINVE 160 Paramecium tetraur...
CAI44483   86 VGAFVCYDITREITFTNIEKWLSEIKEYAPk--nIVIMMIGNKIDQANDRMVRSVEAAKLCQQNkIGYIETSAQnGLNVE 163 Paramecium tetraur...
Feature 1                
1OIW_A    181 AAFQTILTEIY 191 Homo sapiens
AAO49245  166 DAFKQLVTELA 176 Giardia intestinalis
CAI44535  163 DAFKNILQQIY 173 Paramecium tetraurelia
CAI44537  163 QAFTQIIQQIY 173 Paramecium tetraurelia
CAI39309  164 LAFSRLINEIY 174 Paramecium tetraurelia
CAI39320  161 EAFNKLINGKA 171 Paramecium tetraurelia
CAI39337  164 VAFNKIVANIF 174 Paramecium tetraurelia
CAI39292  162 KAFSMLLESKS 172 Paramecium tetraurelia
CAI44562  161 MAFNQMVTEIY 171 Paramecium tetraurelia
CAI44483  164 EAFSNLVSEIF 174 Paramecium tetraurelia

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