title: Molecular cloning, sequence, function and structural basis of human heart 150 kDa oxygen-regulated protein, an ER chaperone.
abstract: Apoptosis of heart tissues followed by hypoxia and ischemia leads finally to cardiac insufficiency. The full-length coding sequence of 3301 bp including cDNA(s) of the ER chaperone ORP150, which was specifically induced by hypoxia stress, was cloned from human cardiac infarct. Phylogenetic analyses reveal that human heart ORP150 shares a highly conserved N-terminal ATPase domain among its related family members. Moreover, hydropathic profiling reveals that their ca. 70 N-terminal residues and unique C-terminal halves exhibit similar hydropathy profiles among members. These findings suggest that ORP150 is structurally and functionally well conserved in distant species.
authors.affiliation: Department of Protein Research, Hibergenome (formerly ProstaColon), 85 NE, Takamatsu, Kahoku, Ishikawa, 929-1215, Japan. prostacolon@yahoo.co.jp
authors.forename: Satoru
authors.initials: S
authors.lastname: Takeuchi
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry; D001483:Base Sequence; D001921:Brain / Q000378:metabolism; D003001:Cloning, Molecular; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D018840:HSP70 Heat-Shock Proteins; D006801:Humans; D018832:Molecular Chaperones / Q000737:chemistry* / Q000235:genetics; D008969:Molecular Sequence Data; D009203:Myocardial Infarction / Q000378:metabolism; D009206:Myocardium / Q000737:chemistry* / Q000378:metabolism; D010802:Phylogeny; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
chemical_list: D018840:HSP70 Heat-Shock Proteins; D018832:Molecular Chaperones; D011506:Proteins; C050087:oxygen-regulated proteins; D000251:Adenosine Triphosphatases