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PDOC00906

Anaphylatoxin domain signature and profile

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, PS01178Anaphylatoxin domain profile  (MATRIX)
Sequences known to belong to this class detected by the profile: ALL
Other sequence(s) detected in Swiss-Prot: NONE.
Domain architecture view of Swiss-Prot proteins matching PS01178
PS01178
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
Retrieve the sequence logo from the alignment
Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS01178
Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS01178
Scan Swiss-Prot/TrEMBL entries against PS01178
view ligand binding statistics
Matching PDB structures: 1C5A 1CFA 1KJS 2A73 ... [ALL]
ANAPHYLATOXIN_1, PS01177Anaphylatoxin domain signature  (PATTERN)
Consensus pattern: [CSH] - C - x(2) - [GAP] - x(7,8) - [GASTDEQR] - C - [GASTDEQL] - x(3,9) - [GASTDEQN] - x(2) - [CE] - x(6,7) - C - C
The 6 C's are involved in disulfide bonds
Sequences known to belong to this class detected by the pattern: ALL
Other sequence(s) detected in Swiss-Prot: NONE.
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
Retrieve the sequence logo from the alignment
Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS01177
Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS01177
Scan Swiss-Prot/TrEMBL entries against PS01177
view ligand binding statistics
Matching PDB structures: 1C5A 1CFA 1KJS 2A73 ... [ALL]

References:

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

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