PROSITE logo
Black ribbon
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.
Amos Bairoch

PROSITE documentation PDOC00906
Anaphylatoxin domain signature and profile


View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC00906

Description

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).

                          +--------------------+
            +-------------|------------+       |
            |             |            |       |
         xxxCCxxxxxxxxxxxxCxxxxxxxxxxxxCxxxxxxCCxxx
             |                                |
             +--------------------------------+
'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.

-------------------------------------------------------------------------------


Technical section

PROSITE methods (with tools and information) covered by this documentation:

ANAPHYLATOXIN_2, PS01178; Anaphylatoxin domain profile  (MATRIX)

ANAPHYLATOXIN_1, PS01177; Anaphylatoxin domain signature  (PATTERN)


References

1AuthorsHugli T.E.
TitleBiochemistry and biology of anaphylatoxins.
SourceComplement 3:111-127(1986).
PubMed ID3542363

2AuthorsHuber R. Scholze H. Paques E.P. Deisenhofer J.
TitleCrystal structure analysis and molecular model of human C3a anaphylatoxin.
SourceHoppe-Seyler's Z. Physiol. Chem. 361:1389-1399(1980).
PubMed ID7439885

3AuthorsArgraves W.S. Tran H. Burgess W.H. Dickerson K.
TitleFibulin is an extracellular matrix and plasma glycoprotein with repeated domain structure.
SourceJ. Cell Biol. 111:3155-3164(1990).
PubMed ID2269669

4AuthorsPan T.-C. Sasaki T. Zhang R.-Z. Faessler R. Timpl R. Chu M.L.
TitleStructure and expression of fibulin-2, a novel extracellular matrix protein with multiple EGF-like repeats and consensus motifs for calcium binding.
SourceJ. Cell Biol. 123:1269-1277(1993).
PubMed ID8245130



PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.