ER-resident protein

spinqualitylabelsall models Mouse ERp5 (PDB code 3apo) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function ER-resident proteins (ERp) are proteins which are retained by the endoplasmic reticulum. ERp18 monitors control ensuring optimal processing of ATF6alpha following its trafficking to the Golgi. ERp27 functions a a disulphide isomerase. ERp29 facilitates processing and transport of proteins in the early secretary pathway. ERp44 may be involved in the control of oxidative protein folding. ERp46 regulates the mannose-trimming of misfiled glycoproteins and thus their degradation. ERdj5 reduces disulfides in proteins to be dislocated to the cytosol for degradation. For details on ERdj5 see Molecular Playground/ERDj5. Structural insights The retention signal of ERp is the sequence KDEL at the C-terminal.

3D Structures of ER-resident protein

Updated on 19-June-2024

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• ERp18 or thioredoxin domain-containing protein 12
  • Molecular Playground/ERDj5 – hERp18 24-172 – human NMR
    
• ERp27
  • 2l4c – hERp27 B domain - NMR
    
  • 4f9z – hERp27 tryptic domain
    
• ERp29
  • 2qc7 – hERp29
    
  • 5v8z – hERp29 D domain + calmegin P domain
    
  • 5v90 – hERp29 D domain + calreticulin P domain
    
  • 2m66, 6o6i – rERp29 C terminal – rat - NMR
    
  • 1g7d – rERp29 C domain - NMR
    
  • 1g7e – rERp29 N domain - NMR
    
• ERp44 or thioredoxin domain-containing protein 4
  • [[[2r2j|2r2j]], [5hqp]] – hERp44 + peroxiredoxin-4
    
• ERp46 or thioredoxin domain-containing protein 5
  • 3uj1, 3uvt – hERp46 3rd catalytic domain 323-428
    
  • 3wgd – hERp46 1st catalytic domain 62-170
    
  • 3wge – hERp46 2nd catalytic domain 190-298
    
  • 3wgx – hERp46 2nd catalytic domain + peroxiredoxin-4
    
• ERdj5
  • 3apo – mErdj5 - mouse
    
  • 3apq – mErdj5 J-Trx1 domain
    
  • 3aps – mErdj5 Trx4 domain
    

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