| First Author | Tian F | Year | 1999 |
| Journal | DNA Seq | Volume | 10 |
| Pages | 155-61 | PubMed ID | 10647817 |
| Abstract Text | Human platelet and T cell activation antigen 1 (PTA1) is a 67kDa type I transmembrane glycoprotein mainly expressed on the surface of activated T cells and platelets, and is involved in the development of human cytotoxic T cell (CTL) as well as platelet activation and aggregation. We have cloned and sequenced gibbon PTA1 (gPTA1) and monkey PTA1 (mPTA1) cDNAs by RT-PCR from gibbon leukemic cell line MLA 144 and PHA-induced Rhesus monkey PBMC respectively. The mature proteins of gPTA1, mPTA1 and human PTA1 (hPTA1) share 93-95% amino acid similarity with the highest similarity in domain 1 of extracellular region. All the important features of PTA1 molecule are conserved among these Primates: (1) the ORF encoding 336 amino acid residues including signal sequence (18aa), extracellular region (232aa), transmembrane sequence (25aa) and cytoplasmic region (61aa); (2) two conserved pairs of Cys (Cys19 to Cys90 and Cys134 to Cys204) forming disulfide bonds stabilizing the two immunoglobulin superfamily V-like domains; (3) eight putative N-linked glycosylation sites (except gPTA1 with nine sites) and three O-linked glycosylation sites in extracellular region; and (4) predicated protein kinase C phosphorylation sites (Thr275 and Ser311), casein kinase II sites (Ser295 and The299) and the potential tyrosine phosphorylation site (Tyr304). These data indicate that PTA1 molecule is highly conserved among the Primates and may play important roles in immune response. | Doi | 10.3109/10425179909033941 |
| Issue | 3 |
