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TIG1
Tazarotene-induced gene-1 (TIG1) is a protein which has been implicated as a putative tumor suppressor. It is structurally similar to the protein latexin, which has also been shown to demonstrate some tumor suppression activity (Liang et al., 2007). TIG1 is thought to be a transmembrane protein, and its mechanism of tumor suppression is largely unknown.
== Structure ==
The amino acid sequence of the protein TIG1 is as follows:
N terminus-Met-Gln-Pro-Arg-Arg-Gln-Arg-Leu-Pro-Ala-Pro-Trp-Ser-Gly-Pro-Arg-Gly-Pro-Arg-Pro-Thr-Ala-Pro-Leu-Leu-Ala-Leu-Leu-Leu-Leu-Leu-Ala-Pro-Val-Ala-Ala-Pro-Ala-Gly-Ser-Gly-Gly-Pro-Asp-Asp-Pro-Gly-Gln-Pro-Gln-Asp-Ala-Gly-Val-Pro-Arg-Arg-Leu-Leu-Gln-Gln-Lys-Ala-Arg-Ala-Ala-Leu-His-Phe-Phe-Asn-Phe-Arg-Ser-Gly-Ser-Pro-Ser-Ala-Leu-Arg-Val-Leu-Ala-Glu-Val-Gln-Glu-Gly-Arg-Ala-Trp-Ile-Asn-Pro-Lys-Glu-Gly-Cys-Lys-Val-His-Val-Val-Phe-Ser-Thr-Glu-Arg-Tyr-Asn-Pro-Glu-Ser-Leu-Leu-Gln-Glu-Gly-Glu-Gly-Arg-Leu-Gly-Lys-Cys-Ser-Ala-Arg-Val-Phe-Phe-Lys-Asn-Gln-Lys-Pro-Arg-Pro-Thr-Ile-Asn-Val-Thr-Cys-Thr-Arg-Leu-Ile-Glu-Lys-Lys-Lys-Arg-Gln-Gln-Glu-Asp-Tyr-Leu-Leu-Tyr-Lys-Gln-Met-Lys-Gln-Leu-Lys-Asn-Pro-Leu-Glu-Ile-Val-Ser-Ile-Pro-Asp-Asn-His-Gly-His-Ile-Asp-Pro-Ser-Leu-Arg-Leu-Ile-Trp-Asp-Leu-Ala-Phe-Leu-Gly-Ser-Ser-Tyr-Val-Met-Trp-Glu-Met-Thr-Thr-Gln-Val-Ser-His-Tyr-Tyr-Leu-Ala-Gln-Leu-Thr-Ser-Val-Arg-Gln-Trp-Val-Arg-Lys-Thr-C terminus.
TIG1 is a transmembrane protein which contains a hyaluronic acid binding motif. This particular motif suggests that it may increase cell-to-cell contact in cells which express TIG1 (Jing et al., 2002). TIG1 is predicted to contain a membrane anchor at the N-terminus. TIG1 contains two faces: the first face contains homology to the protein latexin, and the second contains a broad basic patch. The basic face is thought to be an interaction surface. Supporting the idea of a protein interaction surface, TIG1 also contains a cis-peptide bond between isoleucine-122 and proline-123 on a protruding loop that lies on its basic face (Aagard et al., 2005). Latexin and TIG1 have approximately 30 percent homology based on primary structure; however, their three-dimensional structures are thought to be much more similar (Liang et al., 2007). Both latexin and TIG1 are thought to have descended from a common progenitor. TIG1 also shares homology with another protein, ovacalyxin-32, although the evolutionary and functional relationship between the two proteins is unclear (Gautron et al., 2001).
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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