Conserved Protein Domain Family
PX_SNX15

?
cd07288: PX_SNX15 
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15
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. SNX15 contains an N-terminal PX domain and a C-terminal Microtubule Interacting and Trafficking (MIT) domain. It plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein.
Statistics
?
PSSM-Id: 132821
View PSSM: cd07288
Aligned: 3 rows
Threshold Bit Score: 251.813
Threshold Setting Gi: 13124562
Created: 30-Jan-2009
Updated: 17-Jan-2013
Structure
?
Aligned Rows:
 
phosphoinosit..
Feature 1: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
?
Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                  ###                           ##      
gi 148226346  11 YERRYNVTDTRTnpkGYTEYKITAQfISKKNPQDVkEIVVWKRYSDLKKLHGELSYTHRnlfqrcqEFPPFPRAQVFGRF 90
gi 31418957   10 YYRFFSVTDPRThekGHTEYKVTARfVSKTQPENVkEVVVWKRYTELKKLHGELAYTHRnlfrrqeEFPPFPRAQVFGRF 89
gi 13124562    9 FLRHYTVSDPRThpkGYTEYKVTAQfISKKDPEDVkEVVVWKRYSDFRKLHGDLAYTHRnlfrrleEFPAFPRAQVFGRF 88
                         90       100       110
                 ....*....|....*....|....*....|....*...
Feature 1               #                              
gi 148226346  91 EAAVIEERRQATEEMLQFTVNIpALYNSPQLKEFFREG 128
gi 31418957   90 DEAVIEERRNAAEAMLLFTTNIpALYNSPQLKEFFRDG 127
gi 13124562   89 EASVIEERRKGAEDLLRFTVHIpALNNSPQLKEFFRGG 126

| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap