Conserved Protein Domain Family
PX_SNX6

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cd07292: PX_SNX6 
The phosphoinositide binding Phox Homology domain of Sorting Nexin 6
The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX6 forms a stable complex with SNX1 and may be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It interacts with the receptor serine/threonine kinases from the transforming growth factor-beta family. It also plays roles in enhancing the degradation of EGFR and in regulating the activity of Na,K-ATPase through its interaction with Translationally Controlled Tumor Protein (TCTP). SNX6 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs.
Statistics
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PSSM-Id: 132825
View PSSM: cd07292
Aligned: 4 rows
Threshold Bit Score: 280.063
Threshold Setting Gi: 148237580
Created: 23-Jan-2009
Updated: 17-Jan-2013
Structure
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Aligned Rows:
 
putative
Feature 1:putative phosphoinositide binding site [chemical binding site]
Evidence:
  • Comment:A majority of PX domain containing proteins binds phosphatidylinositol-3-phosphate (PI3P) at this site. In some cases, other phosphoinositides, such as PI4P or PI(3,4)P2, are the preferred substrates.
  • Comment:based on the structures of phosphatidylinositol-3-phosphate bound to other members of this superfamily
  • Comment:Two basic residues are key in binding with phosphoinositides: one forms hydrogen bonds with the 3-phosphate of PI(3)P and another forms hydrogen bonds with the 4-and 5-hydroxyl groups of PI(3)P.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                               ###                        ##            
gi 4689252    30 AALQVDISDALSERDKVKFTVHTKSSLPNFKQnEFSVVRQHEEFIWLHDSFVENEDYAGYIIPPAPPRPDFDASREKLQK 109
gi 119331150  30 AALQVDISDALSERDKVKFTVHTKSSLPNFKQsEFSVVRQHEEFIWLHDSFVENEDYAGYIIPPAPPRPDFDASREKLQK 109
gi 148237580  30 ATLQVDISDALSERDKVKFTVHTKSSLPNFKQnEFSVVRQHEEFIWLHDSFVENEEYAGYIIPPAPPRPDFDASREKLQK 109
gi 71834572   30 ATLQVDISDALSERDKVKFTVHTKSTLPNFKQnEFSVVRQHEEFIWLHDSFVENEEYAGYIIPPAPPRPDFDASREKLQK 109
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
Feature 1                                      #                              
gi 4689252   110 LGEGEGsMTKEEFTKMKQELEAEYLAIFKKTVAMHEVFLCRVAAHPILRRDLNFHVFLEYN 170
gi 119331150 110 LGEGEGsMTKEEFTKMKQELEAEYLAIFKKTVAMHEVFLCRVAAHPILRKDLNFHVFLEYN 170
gi 148237580 110 LGEGEGsMTKEEFTKMKQELEAEYLAIFKKTVAMHEVFLCRVAAHPILRKDLNFHVFLEYN 170
gi 71834572  110 LGEGEGsMTKEEFTKMKQELEAEYLAIFKKTVAMHEVFLCRVAAHPVLRKDLNFHVFLEYN 170

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