Please use this identifier to cite or link to this item: https://doi.org/10.1017/S0003480097006295
Title: Alpha coat protein COPA (HEP-COP): Presence of an Alu repeat in cDNA and identity of the amino terminus to xenin
Authors: Chow, V.T.K.
Quek, H.H. 
Issue Date: Jul-1997
Citation: Chow, V.T.K., Quek, H.H. (1997-07). Alpha coat protein COPA (HEP-COP): Presence of an Alu repeat in cDNA and identity of the amino terminus to xenin. Annals of Human Genetics 61 (4) : 369-373. ScholarBank@NUS Repository. https://doi.org/10.1017/S0003480097006295
Abstract: We previously sequenced the 4333-nucleotide cDNA of the COPA (HEP-COP) gene which encodes the human homologue of the α-subunit of the coatomer protein complex, involved in intracellular protein transport. Within the 3' untranslated region at nucleotides 4049-4333 was observed an Alu repeat containing conserved A and B block elements, and showing high homology to the human Alu-Sx subfamily consensus sequence. Upstream of the Alu repeat were noted a TATA box, a CAAT motif and two activating transcription factor (ATF)-like binding sites, which represent putative regulatory elements directing Alu transcription. In addition, the 25 and 35 N-terminal amino acid residues of COPA and its bovine homologue were identical to xenin-25 and proxenin, respectively. Xenin-25 is a gastrointestinal hormone that stimulates exocrine pancreatic secretion. This peptide is related to xenopsin, neurotensin and neuromedin N which are bioactive peptides derived from larger precursors via proteolytic cleavage by cathepsin E at processing sites determined by conserved C-terminal sequences, i.e. proline/valine-X-X-hydrophobic amino acid. Given the conformity of the C-terminal residues of xenin-25 (PWIL) and of its progenitor molecule, proxenin (VIQL), it is proposed that these peptides are generated by a similar mechanism of post-translational modification involving a parent precursor represented by the α-subunit of coatomer.
Source Title: Annals of Human Genetics
URI: http://scholarbank.nus.edu.sg/handle/10635/113353
ISSN: 00034800
DOI: 10.1017/S0003480097006295
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