Summary: Frog skin active peptide family signal and propeptide
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This is the Wikipedia entry entitled "Amphibian antimicrobial peptides". More...
Amphibian antimicrobial peptides Edit Wikipedia article
Brevenin | |||||||||
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Identifiers | |||||||||
Symbol | Brevenin | ||||||||
Pfam | PF03032 | ||||||||
InterPro | IPR004275 | ||||||||
TCDB | 1.C.52 | ||||||||
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In addition to the highly specific cell immune system, vertebrates possess an efficient host-defence mechanism against invading microorganisms which involves the synthesis of highly potent antimicrobial peptides with a large spectrum of activity. A number of these defence peptides are secreted from the skin of frogs and other amphibians, including the opiate-like dermorphins and deltorphins, and antimicrobial dermaseptins and temporins.
References
This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Frog skin active peptide family signal and propeptide Provide feedback
This family contains a number of defence peptides secreted from the skin of amphibians, including the opiate-like dermorphins and deltorphins, and the antimicrobial dermoseptins and temporins. The alignment for this family consists of the signal peptide and propeptide regions and does not include the active peptides [1] [2].Family members such as the peptide leucine arginine (pLR) belongs to a class of cyclic peptides isolated from frog skin. Its primary sequence is similar to the reactive loop of plant Bowman-Birk inhibitors (BBI), and the circular sunflower trypsin inhibitor-1 (SFTI-1) and to HV-BBI, an isolated peptide from amphibian skin with trypsin-inhibitory activity. pLR is a highly potent trypsin inhibitor, with therapeutic potential. A study describing immunomodulatory properties of pLR showed that the peptide is a potent activator of histamine release [3]. Other members such as Phylloseptins are antimicrobial peptides of 19-20 residues and carry an amidated C-terminus [4].
Literature references
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Vignal E, Chavanieu A, Roch P, Chiche L, Grassy G, Calas B, Aumelas A; , Eur J Biochem 1998;253:221-228.: Solution structure of the antimicrobial peptide ranalexin and a study of its interaction with perdeuterated dodecylphosphocholine micelles. PUBMED:9578480 EPMC:9578480
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Mor A, Nicolas P; , Eur J Biochem 1994;219:145-154.: Isolation and structure of novel defensive peptides from frog skin. PUBMED:8306981 EPMC:8306981
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Rothemund S, Sonnichsen FD, Polte T;, J Med Chem. 2013;56:6732-6744.: Therapeutic potential of the peptide leucine arginine as a new nonplant bowman-birk-like serine protease inhibitor. PUBMED:23988198 EPMC:23988198
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Resende JM, Moraes CM, Prates MV, Cesar A, Almeida FC, Mundim NC, Valente AP, Bemquerer MP, Pilo-Veloso D, Bechinger B;, Peptides. 2008;29:1633-1644.: Solution NMR structures of the antimicrobial peptides phylloseptin-1, -2, and -3 and biological activity: the role of charges and hydrogen bonding interactions in stabilizing helix conformations. PUBMED:18656510 EPMC:18656510
External database links
Transporter classification: | 1.C.52 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR004275
In addition to the highly specific cell-mediated immune system, vertebrates possess an efficient host-defence mechanism against invading microorganisms which involves the synthesis of highly potent antimicrobial peptides with a large spectrum of activity.
This entry represents the signal peptide and propeptide regions found in a number of these defence peptides secreted from the skin of amphibians, including caerins, dermaseptins, brevinin, dermorphin, tryptophillin, pleurain and phylloseptin [ PUBMED:18983817 , PUBMED:19272309 ]. This domain does not include the active peptides.
Domain organisation
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Alignments
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Seed (18) |
Full (3) |
Representative proteomes | UniProt (2151) |
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RP15 (3) |
RP35 (3) |
RP55 (3) |
RP75 (5) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (18) |
Full (3) |
Representative proteomes | UniProt (2151) |
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RP15 (3) |
RP35 (3) |
RP55 (3) |
RP75 (5) |
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Raw Stockholm | |||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
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Trees
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Curation and family details
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Curation
Seed source: | Pfam-B_1232 (release 6.4) |
Previous IDs: | Brevenin; |
Type: | Family |
Sequence Ontology: | SO:0100021 |
Author: |
Griffiths-Jones SR |
Number in seed: | 18 |
Number in full: | 3 |
Average length of the domain: | 30.7 aa |
Average identity of full alignment: | 87 % |
Average coverage of the sequence by the domain: | 77.31 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 46 | ||||||||||||
Family (HMM) version: | 18 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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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 FSAP_sig_propep domain has been found. There are 2 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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