Conserved Protein Domain Family
PX_SNX16

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cd07276: PX_SNX16 
The phosphoinositide binding Phox Homology domain of Sorting Nexin 16
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. SNX16 contains a central PX domain followed by a coiled-coil region. SNX16 is localized in early and recycling endosomes through the binding of its PX domain to phosphatidylinositol-3-phosphate (PI3P). It plays a role in epidermal growth factor (EGF) signaling by regulating EGF receptor membrane trafficking.
Statistics
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PSSM-Id: 132809
View PSSM: cd07276
Aligned: 9 rows
Threshold Bit Score: 206.491
Threshold Setting Gi: 189235024
Created: 3-Feb-2009
Updated: 17-Jan-2013
Structure
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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
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                ###                       ##            
gi 109940025 105 DRPSTPTILGYEVMEERAKFTVYKILVKKSp-eESWVVFRRYTDFSRLNDKLKEMFPg-fRLALPPKRWFKdNYNADFLE 182
gi 24654550  219 NAVLRVPIIGYEVMEERARFTAYKLRVENPetnDYWLVMRRYTDFVRLNSKLKQAFPn-lTLMLPRKKLFGdNFNAVFLD 297
gi 48097416   70 SDDLRIPIVGYEVMEERARFTVYKLRVELKn-gDCWFVFRRYTDFVRLLSQLRRQKIpisQLSLPRKKWLGdNFAPSFLE 148
gi 62859811   96 ERPSTPTVLGYEVMEERAKFTVYKILVRKSp-eENWVVFRRYTDFSRLNDKLKEMFPg-fRLALPPKRWFKdNYDYDFLE 173
gi 45387753   63 PRPATPTVLGYEVMEERAKFTVYKVLVRKNv-dESWVVFRRYTDFSRLNDKLKDMFPg-fRLSLPPKRWFKdNYETEFLE 140
gi 118087149 104 DRPSTPTILGYEVMEERAKFTVYKILVKRSp-eESWVVFRRYTDFSRLNDKLKDMFPg-fRLALPPKRWFKdNYNPDFLE 181
gi 156401667  60 DNGIRAPITGYEVVERREKFTVYKIQVLCQg--RSWFVFRRYTDFVRLNNKLRQAFSg-fIIKMPGKRFLRdNYDPEFLE 136
gi 189235024  91 LNNIQIPIVGYEIMEERARFTVYKLRIENKvsgDCWYVFRRYTDFVRLCNRIRNSHTh-iVQLLPRKRWLKnNFDPLFLE 169
gi 215495513  79 VPEYNTPIIGYEVMEERARFTVFKIRVEHVesgRYWFVFRRYTDFGRLSKKLKPLFPg-lQLSLPPKRWFGnNFDPMFLE 157
                         90       100       110
                 ....*....|....*....|....*....|..
Feature 1         #                              
gi 109940025 183 DRQLGLQAFLQNLVAHkDIANCLAVREFLCLD 214
gi 24654550  298 NRVQGLQIFVNSVMAKeELRKCKLVREFFCLD 329
gi 48097416  149 GRIRGLQAFVNGILSSpLLIGTACVREFFCLD 180
gi 62859811  174 ERQLGLQAFLQNLVAHkDIANCAPVRLFLCLD 205
gi 45387753  141 ERQLGLQTFLQNLVAHkDIASCVAVREFLCLD 172
gi 118087149 182 DRQLGLQAFLQNLVAHkDIANCIAVREFLCLD 213
gi 156401667 137 ERAHGLQMFMNSIMRHsKISRSKLLREFLCID 168
gi 189235024 170 ERVSGLQTLVNAILAEpSLITSQEIQDFFCLN 201
gi 215495513 158 DRLLGLQAFVKNIMGHrDISKSSPVREFFCLD 189

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