PROSITE documentation PDOC51468
VIT domain profile


The inter-α-trypsin inhibitor (ITI) family is composed of protease inhibitors that are assembled from two precursor proteins: a light chain and different homologous heavy chains (ITIHs). Originally identified as plasma inhibitors, recent data indicate that ITI plays a role in extracellular matrix stabilization and in prevention of tumor metastasis [1].

Two domains are conserved in all known ITIHs, the vault protein inter-α-trypsin (VIT) domain and a von Willebrand type A (vWA) domain (see <PDOC50234>). The VIT domain is less widespread than the vWA domain and is not genetically mobile. Therefore, it can be regarded as the characteristic domain of the ITIH family. The VIT domain is approximately 135 amino acids long. Its N-terminal part contains a pattern of hydrophobic residues, interrupted by a conserved arginine. The C-terminus is best characterized by its conserved aromatic residues. In the central part, an acidic amino acid resides between two basic residues [1].

The profile we developed covers the entire VIT domain.

Last update:

October 2009 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

VIT, PS51468; VIT domain profile  (MATRIX)


1AuthorsHimmelfarb M. Klopocki E. Grube S. Staub E. Klaman I. Hinzmann B. Kristiansen G. Rosenthal A. Duerst M. Dahl E.
TitleITIH5, a novel member of the inter-alpha-trypsin inhibitor heavy chain family is downregulated in breast cancer.
SourceCancer Lett. 204:69-77(2004).
PubMed ID14744536

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