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Adenomatous polyposis coli
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Adenomatous polyposis coli : ウィキペディア英語版
Adenomatous polyposis coli

''This article refers to the tumor suppressor APC, in which mutations lead to colon cancer. For the cell-cycle regulatory complex, APC/C, see Anaphase-promoting complex.''
Adenomatous polyposis coli (APC) also known as deleted in polyposis 2.5 (DP2.5) is a protein that in humans is encoded by the ''APC'' gene. The APC protein is a negative regulator that controls beta-catenin concentrations and interacts with E-cadherin, which are involved in cell adhesion. Mutations in the ''APC'' gene may result in colorectal cancer.
''APC'' is classified as a tumor suppressor gene. Tumor suppressor genes prevent the uncontrolled growth of cells that may result in cancerous tumors. The protein made by the ''APC'' gene plays a critical role in several cellular processes that determine whether a cell may develop into a tumor. The APC protein helps control how often a cell divides, how it attaches to other cells within a tissue, or whether a cell moves within or away from a tissue. This protein also helps ensure that the chromosome number in cells produced through cell division is correct. The APC protein accomplishes these tasks mainly through association with other proteins, especially those that are involved in cell attachment and signaling. The activity of one protein in particular, beta-catenin, is controlled by the APC protein (see: Wnt signaling pathway). Regulation of beta-catenin prevents genes that stimulate cell division from being turned on too often and prevents cell overgrowth.
The human ''APC'' gene is located on the long (q) arm of chromosome 5 in band q22.2 The ''APC'' gene has been shown to contain an internal ribosome entry site. ''APC'' orthologs have also been identified in all mammals for which complete genome data are available.
== Structure ==

The full-length human protein comprises 2843 amino acids with a (predicted) molecular mass of 311646 Da. Several N-terminal domains have been structurally elucidated in unique atomistic high-resolution complex structures. Most of the protein is predicted to be intrinsically disordered. It is not known if this large predicted unstructured region from amino acid 800 to 2843 persists ''in vivo'' or would form stabilised complexes - possibly with yet unidentified interacting proteins. Recently, it has been experimentally confirmed that the mutation cluster region around the center of APC is intrinsically disordered ''in vitro''.

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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