F
IPR000215

Serpin family

InterPro entry
Short nameSerpin_fam
Overlapping
homologous
superfamilies
 
Serpin superfamily (IPR036186)
family relationships

Description

Protein protease inhibitors constitute a very important mechanism for regulating proteolytic activity. 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, mechanism, and function. Gettins PG. Chem. Rev. 102, 4751-804, (2002). View articlePMID: 12475206

5. Serpins: structure, function and molecular evolution. van Gent D, Sharp P, Morgan K, Kalsheker N. Int. J. Biochem. Cell Biol. 35, 1536-47, (2003). View articlePMID: 12824063

6. Serpins in unicellular Eukarya, Archaea, and Bacteria: sequence analysis and evolution. Roberts TH, Hejgaard J, Saunders NF, Cavicchioli R, Curmi PM. J. Mol. Evol. 59, 437-47, (2004). View articlePMID: 15638455

7. The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature. Silverman GA, Bird PI, Carrell RW, Church FC, Coughlin PB, Gettins PG, Irving JA, Lomas DA, Luke CJ, Moyer RW, Pemberton PA, Remold-O'Donnell E, Salvesen GS, Travis J, Whisstock JC. J. Biol. Chem. 276, 33293-6, (2001). View articlePMID: 11435447

8. Serpin structure, function and dysfunction. Huntington JA. J. Thromb. Haemost. 9 Suppl 1, 26-34, (2011). View articlePMID: 21781239

9. Serpins in prokaryotes. Irving JA, Steenbakkers PJ, Lesk AM, Op den Camp HJ, Pike RN, Whisstock JC. Mol. Biol. Evol. 19, 1881-90, (2002). View articlePMID: 12411597

10. A serpin in the cellulosome of the anaerobic fungus Piromyces sp. strain E2. Steenbakkers PJ, Irving JA, Harhangi HR, Swinkels WJ, Akhmanova A, Dijkerman R, Jetten MS, van der Drift C, Whisstock JC, Op den Camp HJ. Mycol. Res. 112, 999-1006, (2008). View articlePMID: 18539447

11. Structural and inhibitory effects of hinge loop mutagenesis in serpin-2 from the malaria vector Anopheles gambiae. Zhang X, Meekins DA, An C, Zolkiewski M, Battaile KP, Kanost MR, Lovell S, Michel K. J Biol Chem 290, 2946-56, (2015). PMID: 25525260

GO terms

Cross References

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