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57  structures 120  species 3  interactions 651  sequences 95  architectures

Family: ANATO (PF01821)

Summary: Anaphylotoxin-like domain

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Anaphylotoxin-like domain Provide feedback

C3a, C4a and C5a anaphylatoxins are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to a three-fold repeat in fibulins.

Literature references

  1. Pan TC, Sasaki T, Zhang RZ, Fassler R, Timpl R, Chu ML; , J Cell Biol 1993;123:1269-1277.: Structure and expression of fibulin-2, a novel extracellular matrix protein with multiple EGF-like repeats and consensus motifs for calcium binding. PUBMED:8245130 EPMC:8245130

  2. Zuiderweg ER, Nettesheim DG, Mollison KW, Carter GW; , Biochemistry 1989;28:172-185.: Tertiary structure of human complement component C5a in solution from nuclear magnetic resonance data. PUBMED:2784981 EPMC:2784981


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000020

This entry represents C3a, C4a and C5a anaphylatoxins, which are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to a three-fold repeat in fibulins.

Complement components C3, C4 and C5 are large glycoproteins that have important functions in the immune response and host defence [PUBMED:1431125]. They have a wide variety of biological activities and are proteolytically activated by cleavage at a specific site, forming a- and b-fragments [PUBMED:2777798]. A-fragments form distinct structural domains of approximately 76 amino acids, coded for by a single exon within the complement protein gene. The C3a, C4a and C5a components are referred to as anaphylatoxins [PUBMED:2777798, PUBMED:3081348]: they cause smooth muscle contraction, histamine release from mast cells, and enhanced vascular permeability [PUBMED:3081348]. They also mediate chemotaxis, inflammation, and generation of cytotoxic oxygen radicals [PUBMED:3081348]. The proteins are highly hydrophilic, with a mainly alpha-helical structure held together by 3 disulphide bridges [PUBMED:3081348].

Fibulins are secreted glycoproteins that become incorporated into a fibrillar extracellular matrix when expressed by cultured cells or added exogenously to cell monolayers [PUBMED:2269669, PUBMED:12778127]. The five known members of the family share an elongated structure and many calcium-binding sites, owing to the presence of tandem arrays of epidermal growth factor-like domains. They have overlapping binding sites for several basement-membrane proteins, tropoelastin, fibrillin, fibronectin and proteoglycans, and they participate in diverse supramolecular structures. The amino-terminal domain I of fibulin consists of three anaphylatoxin-like (AT) modules, each approximately 40 residues long and containing four or six cysteines. The structure of an AT module was determined for the complement-derived anaphylatoxin C3a, and was found to be a compact alpha-helical fold that is stabilised by three disulphide bridges in the pattern Cys1-4, Cys2-5 and Cys3-6 (where Cys is cysteine). The bulk of the remaining portion of the fibulin molecule is a series of nine EGF-like repeats [PUBMED:8245130].

Gene Ontology

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Domain organisation

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Alignments

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(119)
Full
(651)
Representative proteomes UniProt
(1097)
NCBI
(2347)
Meta
(0)
RP15
(82)
RP35
(237)
RP55
(475)
RP75
(560)
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  Seed
(119)
Full
(651)
Representative proteomes UniProt
(1097)
NCBI
(2347)
Meta
(0)
RP15
(82)
RP35
(237)
RP55
(475)
RP75
(560)
Alignment:
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  Seed
(119)
Full
(651)
Representative proteomes UniProt
(1097)
NCBI
(2347)
Meta
(0)
RP15
(82)
RP35
(237)
RP55
(475)
RP75
(560)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download    
Gzipped Download   Download   Download   Download   Download   Download   Download   Download    

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Prosite
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Bateman A , SMART
Number in seed: 119
Number in full: 651
Average length of the domain: 35.80 aa
Average identity of full alignment: 40 %
Average coverage of the sequence by the domain: 2.64 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.4 21.4
Trusted cut-off 21.4 21.4
Noise cut-off 21.3 21.3
Model length: 36
Family (HMM) version: 18
Download: download the raw HMM for this family

Species distribution

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Interactions

There are 3 interactions for this family. More...

ANATO TED_complement A2M_recep

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the ANATO domain has been found. There are 57 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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