Part:BBa_K4165093

Histocompatibility minor serpin domain (HMSD).

This basic part encodes Histocompatibility minor serpin domain which is predicted to be able to inhibit HtrA1 (BBa_K4165004).

Usage and Biology

This gene encodes a protein with a serpin-domain that may act as a serine protease inhibitor. This gene is predominantly expressed in myeloid cells. A splice variant encoding a minor histocompatibility antigen may be expressed as a result of a polymorphism in this gene. This type of inhibitor is predicted to have high affinity for trypsin-like proteases (serine proteases), and in our case it would act as an inhibitor for the trypsin-like catalytic domain of serine protease HtrA1[1]-[3].

Sequence and Features

Assembly Compatibility:

• 10
  INCOMPATIBLE WITH RFC[10]

  Illegal PstI site found at 400
  
• 12
  INCOMPATIBLE WITH RFC[12]

  Illegal PstI site found at 400
  
• 21
  COMPATIBLE WITH RFC[21]
• 23
  INCOMPATIBLE WITH RFC[23]

  Illegal PstI site found at 400
  
• 25
  INCOMPATIBLE WITH RFC[25]

  Illegal PstI site found at 400
  
• 1000
  COMPATIBLE WITH RFC[1000]

Functional Parameters

GC Content% 60.9%

Isoelectric point (PI) 4.993

Charge at pH 7 -2.188

Molecular Weight (Protein) 15.535 kDa

PDB Structure

The predicted structure (AlphaFold) is present.

AlphaFold https://alphafold.ebi.ac.uk/entry/A8MTL9 Q_Mean = Ramachandran Favoured = Ramachandran Outliers = Clash Score = C-beta Deviation = Rotamers outliers = Total Score =

References

1. Clauss, A., Lilja, H., & Lundwall, Å. (2005). The evolution of a genetic locus encoding small serine proteinase inhibitors. Biochemical and biophysical research communications, 333(2), 383-389. 2. Eigenbrot, C., Ultsch, M., Lipari, M. T., Moran, P., Lin, S. J., Ganesan, R., ... & Kirchhofer, D. (2012). Structural and functional analysis of HtrA1 and its subdomains. Structure, 20(6), 1040-1050. 3. Grau, S., Baldi, A., Bussani, R., Tian, X., Stefanescu, R., Przybylski, M., ... & Ehrmann, M. (2005). Implications of the serine protease HtrA1 in amyloid precursor protein processing. Proceedings of the National Academy of Sciences, 102(17), 6021-6026.