Conserved Protein Domain Family
PX_RICS

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cd07298: PX_RICS 
The phosphoinositide binding Phox Homology domain of PX-RICS
The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. RICS is a Rho GTPase-activating protein for cdc42 and Rac1. It is implicated in the regulation of postsynaptic signaling and neurite outgrowth. An N-terminal splicing variant of RICS containing additional PX and Src Homology 3 (SH3) domains, also called PX-RICS, is the main isoform expressed during neural development. PX-RICS is involved in neural functions including axon and dendrite extension, postnatal remodeling, and fine-tuning of neural circuits during early brain development. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction. The PX domain of PX-RICS specifically binds phosphatidylinositol 3-phosphate (PI3P), PI4P, and PI5P.
Statistics
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PSSM-Id: 132831
View PSSM: cd07298
Aligned: 4 rows
Threshold Bit Score: 253.364
Threshold Setting Gi: 47216829
Created: 9-Feb-2009
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 206558298  127 NVEFGSIQLSLSEEQNEVMKNGcESKELVYLVQIACQGKsWIVKRSYEDFRVLDKHLHLCIYDRRFSQLTELPRSDVlkd 206
gi 118101866   88 NVDFGNIQLSLPEEQSEVMRNGcESKELVYLVQISCQGKsWIVKRSYEDFRVLDKHLHLCIYDRRFSQLAELPRSDVlrd 167
gi 47216829   148 NVDFGTLQLSLGDEQCEATRNGyESKELVYLVHIHCQGRsWIVKRTYEDFRVLDKHLHLCIYDRRFSKLPELPRLDSltd 227
gi 147904467  130 NVDFGSIQLTLTEDQNEVNRNGcESKELVFLVQIACQGRsWIVKRSYEDFRVLDKHLHLCIYDRRFSQLSELPRSDSvkd 209
                          90       100       110
                  ....*....|....*....|....*....|....*
Feature 1             #                              
gi 206558298  207 SPESVTQMLTAYLSRLSTIAGNKINCGPALTWMEI 241
gi 118101866  168 SPELVTHTLMAYLSRLSAIACNKINCGPALTWMEI 202
gi 47216829   228 QSESVSQMLLAYLSRFSAIADNKINCGPALTWMEV 262
gi 147904467  210 NPELVTQMLMAYLSRLSAIAGNKINCGPALTWMEI 244

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