PubMed:10025962
Annnotations
{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/10025962","sourcedb":"PubMed","sourceid":"10025962","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/10025962","text":"Molecular cloning and characterization of a novel angiopoietin family protein, angiopoietin-3.\nUsing homology-based PCR, we have isolated cDNA encoding a novel member (491 amino acids) of the angiopoietin (Ang) family from human adult heart cDNA and have designated it angiopoietin-3 (Ang3). The NH2-terminal and COOH-terminal portions of Ang-3 contain the characteristic coiled-coil domain and fibrinogen-like domain that are conserved in other known Angs. Ang3 has a highly hydrophobic region at the N-terminus (approximately 21 amino acids) that is typical of a signal sequence for protein secretion. Ang3 mRNA is most abundant in adrenal gland, placenta, thyroid gland, heart and small intestine in human adult tissues. 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