2RAK,3DYT


Conserved Protein Domain Family
PX_SNX9

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cd07285: PX_SNX9 
Click on image for an interactive view with Cn3D
The phosphoinositide binding Phox Homology domain of Sorting Nexin 9
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. SNX9, also known as SH3PX1, is a cytosolic protein that interacts with proteins associated with clathrin-coated pits such as Cdc-42-associated tyrosine kinase 2 (ACK2). It contains an N-terminal Src Homology 3 (SH3) domain, a PX domain, and a C-terminal Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature. The PX-BAR structural unit helps determine specific membrane localization. Through its SH3 domain, SNX9 binds class I polyproline sequences found in dynamin 1/2 and the WASP/N-WASP actin regulators. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis. Its array of interacting partners suggests that SNX9 functions at the interface between endocytosis and actin cytoskeletal organization.
Statistics
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PSSM-Id: 132818
View PSSM: cd07285
Aligned: 5 rows
Threshold Bit Score: 269.201
Threshold Setting Gi: 203282517
Created: 11-Feb-2009
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
phosphoinosit..
Conserved site includes 5 residues -Click on image for an interactive view with Cn3D
Feature 1:phosphoinositide binding site [chemical binding site]
Evidence:
  • Structure:2RAK_A; Human SNX9 PX domain binds Phosphatidylinositol-3-Phosphate; defined at 3.5A contacts.
    View structure with Cn3D
  • 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:
Feature 1                                            ###                        #             #  
2RAK_A        47 FDCVVADPRkgsKMYGLKSYIEYQLTPTntNRSVNHRYKHFDWLYERLLVKFGsaIPIPSLPDKQVTGRFEEEFIKMRME 126 human
3DYT_A        21 FDCVVADPRkgsKXYGLKSYIEYQLTPTntNRSVNHRYKHFDWLYERLLVKFGsaIPIPSLPDKQVTGRFEEEFIKXRXE 100 human
XP_419693    255 FDCVVADPKkgsKMYGLKSYIEYQLTCTntNRSVNHRYKHFDWLYERLLVKFGlaIPIPSLPDKQVTGRFEEEFIKMRME 334 chicken
NP_001086616 239 FDCIVADPRkgtKMYGLKSYIEYQLTATntNRSVNHRYKHFDWLYERLLVKFGlaIPIPSLPDKQVTGRFEEEFIKMRME 318 African clawed ...
NP_001012313 213 LDCVVADPKkgsKMYGLKSYIEYQITPNttNRPVNHRYKHFDWLYERLVEKFAcaLPVPGLPDKQVTGRFEEEFIKMRME 292 zebrafish
Feature 1                                                      
2RAK_A       127 RLQAWMTRMCRHPVISESEVFQQFLNFRDEKEWKTGKRKAERDELA 172 human
3DYT_A       101 RLQAWXTRXCRHPVISESEVFQQFLNFRDEKEWKTGKRKAERDELA 146 human
XP_419693    335 RLQAWMTRMCRHPIVSESEVFQQFLNFRDEKEWKTGKRKAEKDETV 380 chicken
NP_001086616 319 RLQGWMSRMCRHPVISESDTFQQFLNFRDEKEWKTGKRKAEKDEIV 364 African clawed frog
NP_001012313 293 RLQGWMSRMCRHPVISNSEVFQLFLNYRDEKEWKLGKRKAEKDETV 338 zebrafish

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