2I4K


Conserved Protein Domain Family
PX_SNX1_2_like

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cd06859: PX_SNX1_2_like 
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The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2
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 SNX1, SNX2, and similar proteins. They harbor a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. Both domains have been shown to determine the specific membrane-targeting of SNX1. SNX1 and SNX2 are components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex.
Statistics
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PSSM-Id: 132769
View PSSM: cd06859
Aligned: 30 rows
Threshold Bit Score: 153.889
Threshold Setting Gi: 220973237
Created: 10-Jul-2008
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
phosphoinosit..
Conserved site includes 4 residues -Click on image for an interactive view with Cn3D
Feature 1:phosphoinositide binding site [chemical binding site]
Evidence:
  • Comment:SNX1 binds phosphatidylinositol-3-phosphate (PI3P) and PI(3,5)P2, but does not bind PI(3,4,5)P3.
  • 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                                                             ###                         
2I4K_A          4 LTVGITDPEKIGDGMn-AYVAYKVTTQTslpl----------frskQFAVKRRFSDFLGLYEKLSEKHsqnGFIVPPPPE 72   human
XP_570117     519 FQISVSDPTRVGDAVr-GYTVYTIRTRTssph----------yqqsTFSCLRRFSDFLWLFEQLSHNNp--GVIVPPMPD 585  Cryptococcus ...
XP_001831344  290 FVITVDDPQKVGDPLr-PYIMYTVHTRTtspl----------fhksAFSVLRRYSDFVWLYEALCYNNp--GVVVPPVPE 356  Coprinopsis c...
XP_500143     252 FEISVGDPIKVGDITs-SHTVYTVSTKTnhpn----------fktdAGSVTRRYSDFRWLFHALENKHp--GIVVPPPPD 318  Yarrowia lipo...
XP_761434     681 FSIKVGDPQRIGDPIs-AHTVYTVRTTTdcph----------frssHFSSLRRYRDFRWLHAALVQNNp--GIIVPPVPE 747  Ustilago mayd...
EDP50637      125 FEITVGDPHKVGDLTs-SHIVYQVRTKTtska----------yrqpEFTVSRRYRDFLWLYNSMHNNNp--GVVVPPPPE 191  Aspergillus f...
XP_002175392  150 YEITIHDPHKVGELTs-AHTVYCVTSTVtypnaqs-----pteskeELQVERRYRDFLLLYQLLGATHp--GTIIPPAPE 221  Schizosacchar...
CAL53764       55 IIIEIGDPHRVGDGLs-KHIEYKVTYWTdaeay--------ggkgsSGCVTRRYSDFEWLSKQLEANCd--GVIIPVIPS 123  Ostreococcus ...
EED91568       14 AYATVSDPVQHTEGLkgKYTVYRIAYDPppptadgavhtsaalfpyATSCYRRYSDFSWLFDHLHKERp--GAIVPPLPE 91   Thalassiosira...
EED91418       12 DYITVSDPVIHADGMn-KYTSYRVDCPAdypfl--------qnnqsPSSVLRRYSDFLWLYERLQKERa--GSIVPPIPE 80   Thalassiosira...
Feature 1                                 #                              
2I4K_A         73 KSLIGMTKVKvgkedsssaeFLEKRRAALERYLQRIVNHpTMLQDPDVREFLEKE 127  human
XP_570117     586 KHSWGRFEDQ----------FVETRRLALEKCLKKITSNpILQLDPDLRLFLESD 630  Cryptococcus neoformans var. neoforman...
XP_001831344  357 KSSFGRFEDQ----------FVRQRRLGLEKCIQKMANHpVLAKDPDLRLFLESD 401  Coprinopsis cinerea okayama7#130
XP_500143     319 KQAVGRFNED----------FVEARRAALETMLQKVARHhLLQDDPDLQLFLQSE 363  Yarrowia lipolytica CLIB122
XP_761434     748 KVSIGRFAAE----------LVEARRVGLETCINKIANHpLLQQDDDFRLFLESE 792  Ustilago maydis 521
EDP50637      192 KQAVGRFDTN----------FVESRRAALERMLNKIAAHpILQHDADLKIFLESE 236  Aspergillus fumigatus A1163
XP_002175392  222 KQVVGRFDDE----------FVELRRASLEKMIRKIAQHpRLCQDDAFRYFLSAS 266  Schizosaccharomyces japonicus yFS275
CAL53764      124 KTILHMDDPSs--------rGIERRRTGLAMFAARVAAHpLMRKSQDLLAFLTQD 170  Ostreococcus tauri
EED91568       92 KQQVSRFSES----------FIEDRRFHLEIFLRRVVCNpELKDTECLLVFLGGG 136  Thalassiosira pseudonana CCMP1335
EED91418       81 KQAVSRFSPE----------FVEERRGALERFLRRVVIHpELQDTSCLQTFLRAD 125  Thalassiosira pseudonana CCMP1335

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