PROSITE documentation PDOC50856AMOP domain profile
The AMOP domain (for adhesion-associated domain in MUC4 and other proteins) is an ~100-residue long extracellular domain that occurs in putative cell adhesion molecules and in some splice variants of MUC4. It contains eight invariant cysteines residues that are predicted to be involved in disulfide bonds. The AMOP domain is found associated with extracellular domains involved in cell adhesion, such as NIDO, sushi (see <PDOC50923>), somatomedin B (see <PDOC00453>), VWFD, EGF (see <PDOC00021>), IPT, or TSP1 (see <PDOC50092>). The presence of the AMOP domain in cell adhesion molecules could be indicative of a role for this domain in adhesion [1].
Secondary structure prediction indicates an initial region rich in α helix followed by four β strands, suggesting a β-sheet organization for the C-terminus of the AMOP domain [1].
The profile we developed covers the entire AMOP domain.
Note:This profile contains an additional cut-off value, which only detects true full length AMOP domains. The traditional default cut-off value also allows the detection of truncated AMOP domains found in some MUC4 splice variants.
Last update:May 2004 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Ciccarelli F.D. Doerks T. Bork P. |
| Title | AMOP, a protein module alternatively spliced in cancer cells. | |
| Source | Trends Biochem. Sci. 27:113-115(2002). | |
| PubMed ID | 11893501 |
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