PROSITE documentation PDOC00906Anaphylatoxin domain signature and profile
Anaphylatoxins [1] are mediators of local inflammatory process that act by inducing smooth muscle contraction. There are three different anaphylatoxins: C3a, C4a and C5a. They are peptides of about 75 amino-acid residues that are derived from the proteolytic degradation of complement C3, C4 and C5 and which contains six disulfide-bonded cysteines [2] (see the schematic representation below).
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xxxCCxxxxxxxxxxxxCxxxxxxxxxxxxCxxxxxxCCxxx
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'C': conserved cysteine involved in a disulfide bond.
This cysteine-rich region shares similarity with a three times repeated domain found in the mammalian extracellular matrix proteins fibulins 1 and 2 [3,4]. The three disulfide bonds are conserved in the first and last repeats, but the first disulfide bond is missing in the second repeat.
Our consensus pattern spans the entire cysteine-rich domain.
Last update:May 2004 / Text revised.
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PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Hugli T.E. |
| Title | Biochemistry and biology of anaphylatoxins. | |
| Source | Complement 3:111-127(1986). | |
| PubMed ID | 3542363 |
| 2 | Authors | Huber R. Scholze H. Paques E.P. Deisenhofer J. |
| Title | Crystal structure analysis and molecular model of human C3a anaphylatoxin. | |
| Source | Hoppe-Seyler's Z. Physiol. Chem. 361:1389-1399(1980). | |
| PubMed ID | 7439885 |
| 3 | Authors | Argraves W.S. Tran H. Burgess W.H. Dickerson K. |
| Title | Fibulin is an extracellular matrix and plasma glycoprotein with repeated domain structure. | |
| Source | J. Cell Biol. 111:3155-3164(1990). | |
| PubMed ID | 2269669 |
| 4 | Authors | Pan T.-C. Sasaki T. Zhang R.-Z. Faessler R. Timpl R. Chu M.L. |
| Title | Structure and expression of fibulin-2, a novel extracellular matrix protein with multiple EGF-like repeats and consensus motifs for calcium binding. | |
| Source | J. Cell Biol. 123:1269-1277(1993). | |
| PubMed ID | 8245130 |
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