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The AVIT protein family
Author(s) -
Kaser Alexandra,
Winklmayr Martina,
Lepperdinger Günther,
Kreil Günther
Publication year - 2003
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.embor830
Subject(s) - biology , frog skin , receptor , amino acid , protein family , peptide sequence , microbiology and biotechnology , biochemistry , gene , chemistry , organic chemistry , sodium
Homologues of a protein originally isolated from snake venom and frog skin secretions are present in many vertebrate species. They contain 80–90 amino acids, 10 of which are cysteines with identical spacing. Various names have been given to these proteins, such as mamba intestinal protein 1 (MIT1), Bv8 ( Bombina variegata molecular mass ∼8 kDa), prokineticins and endocrine‐gland vascular endothelial growth factor (EG‐VEGF). Their amino‐terminal sequences are identical, and so we propose that the sequence of their first four residues, AVIT, is used as a name for this family. From a comparison of the sequences, two types of AVIT proteins can be discerned. These proteins seem to be distributed widely in mammalian tissues and are known to bind to G‐protein‐coupled receptors. Members of this family have been shown to stimulate contraction of the guinea pig ileum, to cause hyperalgesia after injection into rats and to be active as specific growth factors. Moreover, the messenger RNA level of one of these AVIT proteins changes rhythmically in the region of the brain known as the suprachiasmatic nucleus. This shows that members of this new family of small proteins are involved in diverse biological processes.