IPR023795
Serpin, conserved site
InterPro entry
Short name | Serpin_CS |
Description
This entry represents a conserved site for the Serpin family of proteins, centred on a well conserved Pro-Phe sequence which is found ten to fifteen residues on the C-terminal side of the reactive bond.
Serpins (SERine Proteinase INhibitors) belong to MEROPS inhibitor family I4, clan ID. Most serpin family members are indeed serine protease inhibitors, but several have additional cross-class inhibition functions and inhibit cysteine protease family members such as the caspases and cathepsins
[2, 1]. Others, such as ovalbumin, are incapable of protease inhibition and serve other functions
[3].
References
1.Squamous cell carcinoma antigen is a potent inhibitor of cysteine proteinase cathepsin L. Takeda A, Yamamoto T, Nakamura Y, Takahashi T, Hibino T. FEBS Lett. 359, 78-80, (1995). View articlePMID: 7851535
2.Inhibition of interleukin-1 beta converting enzyme by the cowpox virus serpin CrmA. An example of cross-class inhibition. Komiyama T, Ray CA, Pickup DJ, Howard AD, Thornberry NA, Peterson EP, Salvesen G. J. Biol. Chem. 269, 19331-7, (1994). View articlePMID: 8034697
3.The ovalbumin family of serpin proteins. Remold-O'Donnell E. FEBS Lett. 315, 105-8, (1993). View articlePMID: 8417965
Further reading
4. Serpin structure, function and dysfunction. Huntington JA. J. Thromb. Haemost. 9 Suppl 1, 26-34, (2011). View articlePMID: 21781239
Contributing Member Database Entry
- PROSITE patterns:PS00284