2FNE


Conserved Protein Domain Family
PDZ13_MUPP1-like

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cd06676: PDZ13_MUPP1-like 
Click on image for an interactive view with Cn3D
PDZ domain 13 of multi-PDZ-domain protein 1 (MUPP1) and related domains
PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 13 of MUPP1. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, PDZ9, and PDZ13. This MuPP1-like PDZ13 domain is therefore absent from PATJ. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ13 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Statistics
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PSSM-Id: 467164
Aligned: 18 rows
Threshold Bit Score: 140.939
Created: 10-Jul-2007
Updated: 27-Apr-2023
Structure
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Program:
Drawing:
Aligned Rows:
 
peptide binding
Conserved site includes 13 residues -Click on image for an interactive view with Cn3D
Feature 1:peptide binding site [polypeptide binding site]
Evidence:
  • Comment:based on canonical PDZ domains with structure
  • Comment:PDZ domains specifically recognize and bind to short C-terminal peptide motifs, but can also recognize internal peptide motifs and certain lipids

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                  #######              #  #                             #   #  ##        
2FNE_A         28 SITLERGPDGLGFSIVGGygsPHGDLPIYVKTVFAKGAASEDGrLKRGDQIIAVNGQSLEGVTHEEAVAILKRTKGTVTL 107  human
CAC95158      117 SITLEKGSEGLGFSIVGGfgsPHGDLPIYVKTVFGKGAAAVDGrLKRGDQLLSVNGESLEGVTHEQAVAILKKQRGSVTL 196  zebrafish
AAI27286     1592 IIHLEKGGDGLGFSIVGGygsPQGDLPIYVKTIFSKGAAAADGrLKRGDQILSVNGESLEGVTHDEAVAILKKQRGNVTL 1671 western clawe...
EEC10224      759 LVSLERGSEGLGFSIVGGagsQHGDLPIYVKTVFESGAAARDGrLRRGHAILSVNGRSLQGLTHQEAVELLRDARGTVTL 838  black-legged ...
ELU09933      369 SIQLARGTDGLGFSIVGGfgsPHGDLPIYVKTVFAKGAAADDGrLKRGDQILTVNGETLEGASHDEAVNMLKKARGHIEL 448  Capitella teleta
XP_012558951 1644 SIELERGSEGLGFSIVGGcgsPHGNLPIYVKTVFEKGAAAKDTrLKRGDQILDVNGISLEGVTHEVAVNILKKSKGSIKL 1723 Hydra vulgaris
XP_013073342 2150 QITLNRGPDGLGFSIIGGhgsPHGDLPIYVKNVFNKGAAFEEGrLRRGDQILTVNGQPLDGLTHEEAVNILKNTRGTVTL 2229 Biomphalaria ...
XP_006822177  909 TVELIRGVDGLGFSIVGGfgsPHGDLPIYVKTVFSRGAASESGqLKRGDQILAVNGDNLDGASHEQAVAILKRCRGKVVL 988  Saccoglossus ...
XP_018667523 1959 DIELNRGSDGLGFSIVGGhgsPHGDLPIYVKSVFSVGAAAVDGrLRRGDRIVSVNGEKLDGYTHEEAAEALKRRATRIIL 2038 vase tunicate
XP_002113893 1843 QVILERGVDGLGFSIVGGndsVQGNLPIFIKQVFPWGAASRSQeLKAGDQLISANGHSLLNVSHEEAVNILKGSKGSLVL 1922 Trichoplax ad...
Feature 1            
2FNE_A        108 MVL 110  human
CAC95158      197 SVL 199  zebrafish
AAI27286     1672 SVL 1674 western clawed frog
EEC10224      839 EVL 841  black-legged tick
ELU09933      449 TIL 451  Capitella teleta
XP_012558951 1724 TVL 1726 Hydra vulgaris
XP_013073342 2230 GIL 2232 Biomphalaria glabrata
XP_006822177  989 TIL 991  Saccoglossus kowalevskii
XP_018667523 2039 RVV 2041 vase tunicate
XP_002113893 1923 TIS 1925 Trichoplax adhaerens

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