We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC51137VM domain profile
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PURL: https://purl.expasy.org/prosite/documentation/PDOC51137
Description
In Drosophila melanogaster the vitelline membrane (VM) is the first layer of the eggshell produced by the follicular epithelium. It is composed of at least four different proteins. VM proteins are similarly organized with a central highly conserved 38-amino acid domain which is flanked by unrelated regions. Since the surrounding regions have diverged significantly, it is possible that the VM domain is of key importance in VM protein structure [1,2].
The profile we developed covers the entire VM domain.
Last update:June 2005 / First entry.
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Technical section
PROSITE method (with tools and information) covered by this documentation:
References
| 1 | Authors | Scherer L.J. Harris D.H. Petri W.H. |
| Title | Drosophila vitelline membrane genes contain a 114 base pair region of highly conserved coding sequence. | |
| Source | Dev. Biol. 130:786-788(1988). | |
| PubMed ID | 3143615 |
| 2 | Authors | Scherer L.J. Harris D.H. White M.K. Steel L.F. Jin J. Petri W.H. |
| Title | Comparative analysis of the sequence and structure of two Drosophila melanogaster genes encoding vitelline membrane proteins. | |
| Source | Gene 136:121-127(1993). | |
| PubMed ID | 8293994 |
Copyright
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