Conserved Protein Domain Family
PX_SNX20_21_like

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cd07279: PX_SNX20_21_like 
The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21
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. This subfamily consists of SNX20, SNX21, and similar proteins. SNX20 interacts with P-Selectin glycoprotein ligand-1 (PSGL-1), a surface-expressed mucin that acts as a ligand for the selectin family of adhesion proteins. It may function in the sorting and cycling of PSGL-1 into endosomes. SNX21, also called SNX-L, is distinctly and highly-expressed in fetal liver and may be involved in protein sorting and degradation during embryonic liver development.
Statistics
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PSSM-Id: 132812
Aligned: 8 rows
Threshold Bit Score: 169.816
Created: 14-Jan-2009
Updated: 2-Oct-2020
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:
Feature 1                                                              ###                       
NP_878274     76 LLFEIASARIEERKv-------------SKFVVYQIIVIqtg-sfDNNKAVLERRYSDFAKLQKALLKTFREEIEDVEFP 141 human
XP_001661060  57 LCFEIPHARVLPPAltsvdgcgasassgKKYVVYDVSVRqdtsepDPNPTSIERRYTHFLKLYDGLRKEHPLLVQTINFP 136 yellow fever mo...
EEB17424       3 TKFDIVSARTVDDKen-----------qKKYVVYDIKIYhqgsdnDTQAIFVERRYSDFLELFLNLRQNYPQLTTKISFP 71  human body louse
XP_002111499 106 LKFESVAARTVTEGk-------------KKFVLYALALVrtd-dtDEIPPIIERRYSQFATLHKALSSSHPQIVKKFNFP 171 Trichoplax adha...
NP_608709     71 LRFDILLAHIMPPDged--------vkiKRFVVYELTVKqdgateDTQPAKIERRYTDFRELYLGLKRQHPAEMANKYFP 142 fruit fly
JC7910       121 LLFEVTSANVVKDPp-------------SKYVLYTLAVIgpg-ppDCQPAQISRRYSDFERLHRNLQRQFRGPMAAISFP 186 human
XP_002202738   3 IVFEVMNARTVKEGh-------------SKYVVYQVHVVksp-glDTSPAFIEKRYSQFDKLNQCLRKRFPHLLESVAFP 68  Florida lancelet
XP_972525     12 LVFEILSARICDEGe------------eRKHVVYTLQVRhisgndDLSPSVVERRYTHFLNLYSALKKEHPNLMTNVTFP 79  red flour beetle
Feature 1        ##             #                                         
NP_878274    142 RKHLTGNFAEEMICERRRALQEYLGLLYAIrcvr-----------rsrEFLDFLTRP 187 human
XP_001661060 137 KKVLVGNFSTELIGERSMAFESFLDYIVSVpslr-----------dsdHFLEFLQGD 182 yellow fever mosquito
EEB17424      72 RKVLIGNFSSDLIQTRLSSLENFLRIISENvtll-----------eslGFKMFLIGN 117 human body louse
XP_002111499 172 RKVAMGNFSQSTIIKRSTAFQDYLNLILKSsnydrgdsvpyasvrytkAFEEFLYIS 228 Trichoplax adhaerens
NP_608709    143 AKVLMGNFKSELIGERSAAFEAFLTYVASQamlr-----------dseYFLRFLQHD 188 fruit fly
JC7910       187 RKRLRRNFTAETIARRSRAFEQFLGHLQAVpelr-----------hapDLQDFFVLP 232 human
XP_002202738  69 KKTLTGNFKTQTIAERSRAFEQYLQHLHSIpqva-----------tchEFLDFFYLE 114 Florida lancelet
XP_972525     80 KKVIIGNFDNELISTRSTGFESLLRHICTEsklr-----------askALVEFLQGV 125 red flour beetle

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