Conserved Protein Domain Family
PX_SNX5_like

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cd06892: PX_SNX5_like 
The phosphoinositide binding Phox Homology domain of Sorting Nexins 5 and 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. Members of this subfamily include SNX5, SNX6, and similar proteins. They contain 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. SNX5 and SNX6 may be components 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.
Statistics
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PSSM-Id: 132802
View PSSM: cd06892
Aligned: 12 rows
Threshold Bit Score: 196.885
Threshold Setting Gi: 119630668
Created: 10-Jul-2008
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 10720289   29 PSLQIDIPDALSERDKVKFTVHTKTTLPtfq--spEFSVTRQHEDFVWLHDTLIETTDYAGLI--------------IPP 92
gi 115803059  35 TSLQVDISDALSERDKVKFTVHTKTTLPefs--esEFSVQREHEEFIWLHTMYEENEDYGGII--------------IPP 98
gi 156400170  18 SSLNVDISDALSERDRVKFTVHTKTTLPdfk--esDFSVVREHEEFVWLHDRCVENEEYAGII--------------IPP 81
gi 193209152 102 EAICVDISDALSEREKVKYTVHTRTRLQem---kpETAVVREHEEFLWLHGTLEDNENYAGFI--------------IPP 164
gi 74869782   72 NALHVEISDALSEKEKVKFTVHTRTTLPgfs--kkDNNVVRQHEEFVWLHDRIEENDDYAGYI--------------IPP 135
gi 196006650  28 ACLVIEISDALSERDKVKFTIHTRTTLPefk--lhDFSVTRDHEEFIWLYDRYQDNENLEAYI--------------IPH 91
gi 167536760  26 DALQISIADALNEQDIVKFTVHTKTSLErfq--krDFQVTRQHEEFVWLHDRLVEDPDYAGLL--------------IPP 89
gi 198427415  31 NSLLVDISDALSEKDKVKFTVHTKTTMKefk--gnEFSVVRQHEEFVWLHDSYVDDERYAGLLdkgilvrmlkllkkIPP 108
gi 149249685  40 FTKFNADEFEDMVAEKQLIPDGCGTTLStfq--spEFSVTRQHEDFVWLHDTLTETTDYAGLI--------------IPP 103
gi 119630668  29 PSLQIDIPDALSERDKVKFTVHTKTTLPtfq--spEFSVTRQHEDFVWLHDTLIETTDYAGLI--------------LSV 92
gi 90080199   14 SCASVDLQGDSSLQVEISDAVSERDKVKftvqtktEFSVVRQHEEFIWLHDAYVENEEYAGLI--------------VRR 79
gi 4689252    30 AALQVDISDALSERDKVKFTVHTKSSLPnfk--qnEFSVVRQHEEFIWLHDSFVENEDYAGYI--------------IPP 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1          ##                                                #                           
gi 10720289   93 APTKPDFDGPREKMQKLGEGEGs------MTKEEFAKMKQELEAEYLAVFKKTVSSHEVFLQRLSSHP-------VLSKD 159
gi 115803059  99 APPRPDFDASREKLQKLGEGEGt------MTKEEFNKMKQELEAEYLATFKKTVAMHEVFLQRLAAHA-------ILRND 165
gi 156400170  82 APPKPDFDVSREKLQKLGEGEGn------MTKEEFQKMKQELEAEYLATFKKTVAMHEVFLTRLASHP-------SLRKD 148
gi 193209152 165 APPKPNFDSSREKLQKLGEGEAt------MTKEEFLKMKHDLEQDYLAQFKKTVAMHEVFLQRIAAHP-------VFKND 231
gi 74869782  136 CPPRPDFDASREKLQRLGEGEGn------MTKEEFKKMKSELEAEYLATFKKTVAMHEVFLRRLASHP-------VFRVD 202
gi 196006650  92 PPPKPDFDTAREKLQRLGESEGv------LTKEEFDKMKQELEAEYLATFKKTVAMHELFLTRLASHS-------VLRND 158
gi 167536760  90 CPPKPDFSQSHGKLAKLQAGDSs------MTPEEIEKLKQEIQGEYLAAFQKTVAMHEVFLLRLVTHP-------IFREN 156
gi 198427415 109 SPLRPDFEASRDKLAKLSEGEGs------MTKEEFSRMKQELEAEYLAIFKKTVAMHEIFLCRLASHP-------TLKNS 175
gi 149249685 104 APTKPDFDGPREKMQKLGEGEGs------MTKEEFAKMKQELEAKDRNFHVFLEYDQDLSVRRKNTKEmfggffkSVVKS 177
gi 119630668  93 RRKNTKEMFGGFFKSVVKSADEvlftgvkEVDDFFEQEKNFLINYYNRIKDSCVKADKMTRSHKNVADd------YIHTA 166
gi 90080199   80 GRAGAGRDRQSTWVRTKGYGGC-------LGSERSPSSVPPLSRSPQPLRGQTLRLQGKSYRNWARGRees--raCLVCL 150
gi 4689252    94 APPRPDFDASREKLQKLGEGEGs------MTKEEFTKMKQELEAEYLAIFKKTVAMHEVFLCRVAAHP-------ILRRD 160
                        170
                 ....*....|
Feature 1                  
gi 10720289  160 RNFHVFLEYD 169
gi 115803059 166 HNFRVFLEYK 175
gi 156400170 149 SNFKVFLEYK 158
gi 193209152 232 QNFRIFLQYE 241
gi 74869782  203 QHLKVFLEYD 212
gi 196006650 159 SNFRVFLEYN 168
gi 167536760 157 ARLQAFLEFQ 166
gi 198427415 176 HNFRVFLEYE 185
gi 149249685 178 ADEVLFSGVK 187
gi 119630668 167 ACLHSLALEE 176
gi 90080199  151 WPQAPGLDVQ 160
gi 4689252   161 LNFHVFLEYN 170

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