The urotensin-II (U-II) receptor (UT) is activated by the endogenous dodecapeptide urotensin-II, originally isolated from the urophysis, the endocrine organ of the caudal neurosecretory system of teleost fish [1,2]. Several structural forms of U-II exist in fish and amphibians . The goby orthologue was used to identify U-II as the cognate ligand for the predicted receptor encoded by the rat gene gpr14 [4,5,6,7,8]. Human urotensin-II, an 11-amino-acid peptide , retains the cyclohexapeptide sequence of goby U-II that is thought to be important in ligand binding [9,10,11]. This sequence is also conserved in the deduced amino-acid sequence of rat urotensin-II (14 amino-acids) and mouse urotensin-II (14 amino-acids), although the N-terminal is more divergent from the human sequence . A second endogenous ligand for the UT has been discovered in rat . This is the urotensin II-related peptide, an octapeptide that is derived from a different gene, but shares the C-terminal sequence (CFWKYCV) common to U-II from other species. Identical sequences to rat urotensin II-related peptide are predicted for the mature mouse and human peptides . UT exhibits relatively high sequence identity with somatostatin, opioid and galanin receptors .
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