Taxonomic distribution of proteins containing CRF domains

The tree below includes only several representative species and genera. The complete taxonomic breakdown of all proteins containing CRF domains can be accessed here. Click the counts or percentage values to display the corresponding proteins.

Evolutionary aspects of corticotropin releasing hormones.

Lederis KP, Okawara Y, Richter D, Morley SD
Prog Clin Biol Res. 1990; 342: 467-72

Cloning and sequence analysis of cDNA for rat corticotropin-releasing factor precursor.

Jingami H, Mizuno N, Takahashi H, Shibahara S, Furutani Y, Imura H, Numa S
FEBS Lett. 1985; 191: 63-6

DNA complementary to the rat hypothalamic mRNA coding for the corticotropin-releasing factor precursor (prepro-CRF) has been cloned by screening a cDNA library with a human genomic DNA probe. Nucleotide sequence analysis of the cloned cDNA has revealed that rat prepro-CRF consists of 187 amino acid residues including a putative signal peptide. The CRF and putative signal peptide regions are more highly conserved among rat, human and ovine prepro-CRF than is the cryptic portion.

Isolation, analysis of structure, synthesis, and biological actions of urotensin I neuropeptides.

Lederis K, Letter A, McMaster D, Ichikawa T, MacCannell KL, Kobayashi Y, Rivier J, Rivier C, Vale W, Fryer J
Can J Biochem Cell Biol. 1983; 61: 602-14

The 41-residue neuropeptide urotensin I (UI), from the urophyses of two teleost fish species (Cyprinus carpio and Catostomus commersoni), was isolated and purified, and its amino acid sequence was determined and confirmed by synthesis of a fully active peptide. The UI peptide was found to be a close structural and biological homologue of the ovine hypothalamic corticotropin-releasing factor (CRF) and the frog skin peptide sauvagine; UI is, therefore, a phylogenetic prototype of this group of peptides. Extraction of urophyses in hot acetic or hydrochloric acid cleaves an amino terminal tripeptide yielding a fully active UI(4-41). The UI peptides are equipotent with the other two naturally occurring peptides (CRF and sauvagine) in the release of mammalian pituitary corticotropin (ACTH), but UI is several times more potent than the mammalian homologue in the stimulation of release of fish pituitary ACTH. The UI peptide and its mammalian or amphibian homologues have a long-lasting hypotensive action in mammals, via a uniquely selective vasodilatation in the superior (anterior) mesenteric vascular bed only. The significantly lower hypotensive vasodilatory action of the mammalian homologue (CRF) suggests a change in the unknown physiological role of the haemodynamic actions of the UI peptides in the mammalian gastrointestinal tract during phylogenetic progression from fishes to mammals.