Summary: Allergen Fel d I-B chain
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Fel d 1 Edit Wikipedia article
| Major allergen I polypeptide chain 2 | |
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Crystallographic structure of the Fel d 1 dimer, the primary allergen present in cat saliva.[1] |
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| Identifiers | |
| Symbol | CH2 |
| Alt. symbols | Fel d I, AG4, Allergen Cat-1 |
| Entrez | 677879 |
| PDB | 1PUO |
| UniProt | P30440 |
| Allergen Fel d I-B chain | |||||||||
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structural characterization of the tetrameric form of the major cat allergen fel d 1 |
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| Identifiers | |||||||||
| Symbol | Feld-I_B | ||||||||
| Pfam | PF09252 | ||||||||
| Pfam clan | CL0370 | ||||||||
| InterPro | IPR015332 | ||||||||
| SCOP | 1puo | ||||||||
| SUPERFAMILY | 1puo | ||||||||
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Fel d 1 is a protein that in cats is encoded by the CH1 (chain 1/Fel d 1-A) and CH2 (chain 2/Fel d 1-B) genes.[2][3]
Fel d 1, produced largely in cat saliva and sebaceous glands, is the primary allergen present on cats and kittens.[1] The protein is of an unknown function to the animal but causes an IgG or IgE reaction in sensitive humans (either as an allergic or asthmatic response). Removal of soft surfaces in the home (carpet, furniture), frequent washings of bed linens, HEPA filters and even washing cats has been proven to reduce the amounts of Fel d 1 present in the home.
Neutered males produce Fel d 1 in levels similar to females (both intact and spayed females produce Fel d 1 in similar levels). Even though females and neutered males produce Fel d 1 in lower levels, they still produce enough to cause allergic symptoms in sensitive individuals.
[edit] Structure
The complete quaternary structure of Fel d 1 has been determined.[1] The allergen is a tetrameric glycoprotein consisting of two disulfide-linked heterodimers of [chains 1 and 2. Fel d 1 chains 1 and 2 share structural similarity with uteroglobin, a secretoglobin superfamily member; chain 2 is a glycoprotein with N-linked oligosaccharides. Both chains share an all alpha-helical structure.[1]
[edit] See also
[edit] References
- ^ a b c d PDB 1PUO; Kaiser L, Grönlund H, Sandalova T, Ljunggren HG, van Hage-Hamsten M, Achour A, Schneider G (September 2003). "The crystal structure of the major cat allergen Fel d 1, a member of the secretoglobin family". J. Biol. Chem. 278 (39): 37730–5. doi:10.1074/jbc.M304740200. PMID 12851385.
- ^ Morgenstern JP, Griffith IJ, Brauer AW, Rogers BL, Bond JF, Chapman MD, Kuo MC (November 1991). "Amino acid sequence of Fel dI, the major allergen of the domestic cat: protein sequence analysis and cDNA cloning". Proc. Natl. Acad. Sci. U.S.A. 88 (21): 9690–4. doi:10.1073/pnas.88.21.9690. PMC 52784. PMID 1946388.
- ^ Griffith IJ, Craig S, Pollock J, Yu XB, Morgenstern JP, Rogers BL (April 1992). "Expression and genomic structure of the genes encoding FdI, the major allergen from the domestic cat". Gene 113 (2): 263–8. doi:10.1016/0378-1119(92)90405-E. PMID 1572548.
This article incorporates text from the public domain Pfam and InterPro IPR015332
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Allergen Fel d I-B chain Provide feedback
Members of this family of cat allergens adopt a helical structure consisting of eight alpha helices, in a Uteroglobin-like fold. They are one of the most important causes of allergic asthma worldwide [1].
Literature references
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Kaiser L, Gronlund H, Sandalova T, Ljunggren HG, van Hage-Hamsten M, Achour A, Schneider G; , J Biol Chem. 2003;278:37730-37735.: The crystal structure of the major cat allergen Fel d 1, a member of the secretoglobin family. PUBMED:12851385 EPMC:12851385
External database links
| PANDIT: | PF09252 |
| Pseudofam: | PF09252 |
| SCOP: | 1puo |
| SYSTERS: | Feld-I_B |
This tab holds annotation information from the InterPro database.
InterPro entry IPR015332
Allergies are hypersensitivity reactions of the immune system to specific substances called allergens (such as pollen, stings, drugs, or food) that, in most people, result in no symptoms. A nomenclature system has been established for antigens (allergens) that cause IgE-mediated atopic allergies in humans. The nomenclature system uses the first three letters of the genus, followed by the first letter of the species name, followed by a number (additional letters can be added to the name as required to discriminate between similar designations).
Fel d 1 is allergen 1 from Felis silvestris catus (Cat), which is an important agent in human allergic reactions [PUBMED:17543334]. The protein is expressed in saliva and sebaceous glands. The complete primary structure of Fel d 1 has been determined [PUBMED:12851385]. The allergen is tetrameric glycoprotein consisting of two disulphide-linked heterodimers of chains 1 and 2, which have been shown to be encoded by different genes. Fel d 1 chains 1 and 2 share structural similarity with uteroglobin, a secretoglobin superfamily member; chain 2 is a glycoprotein with N-linked oligosaccharides.
This entry represents Fel d 1 chain 2.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Cellular component | extracellular space (GO:0005615) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan Uteroglobin (CL0370), which contains the following 2 members:
Feld-I_B UteroglobinAlignments
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| Seed (10) |
Full (38) |
Representative proteomes | NCBI (64) |
Meta (0) |
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| RP15 (0) |
RP35 (0) |
RP55 (0) |
RP75 (15) |
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| PP/heatmap | 1 | |||||||
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| Seed (10) |
Full (38) |
Representative proteomes | NCBI (64) |
Meta (0) |
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| RP15 (0) |
RP35 (0) |
RP55 (0) |
RP75 (15) |
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
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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.
Note: You can also download the data file for the tree.
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
| Seed source: | pdb_1puo |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Sammut SJ |
| Number in seed: | 10 |
| Number in full: | 38 |
| Average length of the domain: | 66.30 aa |
| Average identity of full alignment: | 42 % |
| Average coverage of the sequence by the domain: | 64.32 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 67 | ||||||||||||
| Family (HMM) version: | 5 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
There is 1 interaction for this family. More...
Feld-I_BStructures
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 Feld-I_B domain has been found. There are 6 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 seqence.
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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence