2V14


Conserved Protein Domain Family
PX_KIF16B_SNX23

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cd06874: PX_KIF16B_SNX23 
Click on image for an interactive view with Cn3D
The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23
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. KIF16B, also called sorting nexin 23 (SNX23), is a family-3 kinesin which harbors an N-terminal kinesin motor domain containing ATP and microtubule binding sites, a ForkHead Associated (FHA) domain, and a C-terminal PX domain. The PX domain of KIF16B binds to phosphatidylinositol-3-phosphate (PI3P) in early endosomes and plays a role in the transport of early endosomes to the plus end of microtubules. By regulating early endosome plus end motility, KIF16B modulates the balance between recycling and degradation of receptors. 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.
Statistics
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PSSM-Id: 132784
View PSSM: cd06874
Aligned: 8 rows
Threshold Bit Score: 192.211
Threshold Setting Gi: 24650642
Created: 10-Jul-2008
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
phosphoinosit..
Conserved site includes 6 residues -Click on image for an interactive view with Cn3D
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                                             ###                        ##             # 
2V14_A          6 IKISIPRYVLCGQgkDAHFEFEVKITVldETWTVFRRYSRFREXHKTLKLKYAe-lAALEFPPKKLFgNKDER-VIAERR 83
gi 24650642  1131 HFITIPSFVMRGAgkQTHYEYEVRIALpdGKLNILRRYSRFRELHLCMKHCYGakiSALPFPRRELF-ASNSEpVAKHRR 1209
gi 118087588 1341 IKISIPRYVLCGQgkDEHYEFEIKITVldETWTVFRRYSRFREMHRTLKLKYPe-vATLEFPPKKLFgNKDER-VIAERR 1418
gi 156362192    6 IQVQIPRYILRGQgrDSYHVFEVKVTIagDTWSVYRRYRKFRELHNTMKRLYIe-vGELDFPHRRFFgNRAEE-FVRARR 83
gi 189239408 1012 SVVTISSYCIRGAgtKTHYEYEVRVCTsdDRWSILRRYSRFRDLHIAMKARYGdkvASIPFPAKQLF-ANSET-VAKSRK 1089
gi 219449122 1106 IKISIPRFVMRGYgkEEHFEFEVKTDVlgEVWTIFRRYSKFRELHEMMKGKYPe-vNALEFPPKKLFgNKSQK-LAEERR 1183
gi 115921009 1273 IQITLPRFMQRGHgwDSYFVFELHLKVlnESWIVFRRYRRFRELHDYMRRKYKe-vNALQFPPRRLFgNKSER-VVLRRR 1350
gi 220672773   18 VKICIPRYVLCGQgkDEHFEFEVKITVldETWTVFRRYSRFREMHKSMKLKYPe-lAALDFPPKKIFgNRDER-TIAERR 95
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
Feature 1                                                            
2V14_A         84 SHLEKYLRDFFSVXLQsatsplh-inkvgltLSKHTICEFSPFFKKGVFDY 133
gi 24650642  1210 RLLELYLRRLFVVCSKipqcpiy-egpggtgLTRASLVQLSSFFKKGLFEN 1259
gi 118087588 1419 SHLETYLRSFFTAMLQspssplh-idkvgstLSKHTICEFSPFFRKGVFDY 1468
gi 156362192   84 AQLETYLKSFISLCASlhdcpis--afsgrlIAKRDLCDFAPFFKQGIFEQ 132
gi 189239408 1090 RQLEFYLRRLIETCKNlpacpl----aygdtVTKAALISFSPFFRKGVFEN 1136
gi 219449122 1184 VQLEAYLNNFIAVCLRnkasply--prkdkpFSKRTLCDFAPFFRKGIFES 1232
gi 115921009 1351 MELERYLQNLMHVCMKipkcpia--pgpgrvLSKQVVCEWSPFFRKGAFDI 1399
gi 220672773   96 NQLEQYLRNFFRVMMStsssspistdefglnLSKHAVWDISPFFKKGVFDY 146

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