Structural highlights
Function
[HRSL4_HUMAN] Exhibits PLA1/2 activity, catalyzing the calcium-independent hydrolysis of acyl groups in various phosphotidylcholines (PC) and phosphatidylethanolamine (PE). For most substrates, PLA1 activity is much higher than PLA2 activity. N- and O-acylation activity is hardly detectable.[1]
Publication Abstract from PubMed
Human TIG3 protein is a member of H-REV107 protein family which belongs to the type II tumor suppressor family. TIG3 can induce apoptosis in cancer cells, and it also possesses Ca(2+)-independent phospholipase A(1/2) activity. The NMR assignments of the N-terminal domain of TIG3 are essential for its solution structure determination.
(1)H, (13)C, and (15)N resonance assignments of the N-terminal domain of human TIG3.,Wang L, Yu W, Ren X, Lin J, Jin C, Xia B Biomol NMR Assign. 2012 Jan 31. PMID:22290676[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Uyama T, Jin XH, Tsuboi K, Tonai T, Ueda N. Characterization of the human tumor suppressors TIG3 and HRASLS2 as phospholipid-metabolizing enzymes. Biochim Biophys Acta. 2009 Dec;1791(12):1114-24. doi:, 10.1016/j.bbalip.2009.07.001. Epub 2009 Jul 14. PMID:19615464 doi:http://dx.doi.org/10.1016/j.bbalip.2009.07.001
- ↑ Wang L, Yu W, Ren X, Lin J, Jin C, Xia B. (1)H, (13)C, and (15)N resonance assignments of the N-terminal domain of human TIG3. Biomol NMR Assign. 2012 Jan 31. PMID:22290676 doi:http://dx.doi.org/10.1007/s12104-012-9357-2
