Summary: MATH domain
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MATH domain Provide feedback
This motif has been called the Meprin And TRAF-Homology (MATH) domain. This domain is hugely expanded in the nematode C. elegans .
McWhirter SM, Pullen SS, Holton JM, Crute JJ, Kehry MR, Alber T; , Proc Natl Acad Sci U S A 1999;96:8408-8413.: Crystallographic analysis of CD40 recognition and signaling by human TRAF2. PUBMED:10411888 EPMC:10411888
Chervitz SA, Aravind L, Sherlock G, Ball CA, Koonin EV, Dwight SS, Harris MA, Dolinski K, Mohr S, Smith T, Weng S, Cherry JM, Botstein D; , Science 1998;282:2022-2028.: Comparison of the complete protein sets of worm and yeast: orthology and divergence. PUBMED:9851918 EPMC:9851918
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002083
Although apparently functionally unrelated, intracellular TRAFs and extracellular meprins share a conserved region of about 180 residues, the meprin and TRAF homology (MATH) domain [PUBMED:12387856]. Meprins are mammalian tissue-specific metalloendopeptidases of the astacin family implicated in developmental, normal and pathological processes by hydrolysing a variety of proteins. Various growth factors, cytokines, and extracellular matrix proteins are substrates for meprins. They are composed of five structural domains: an N-terminal endopeptidase domain, a MAM domain (see PROSITEDOC), a MATH domain, an EGF-like domain (see PROSITEDOC) and a C-terminal transmembrane region. Meprin A and B form membrane bound homotetramer whereas homooligomers of meprin A are secreted. A proteolitic site adjacent to the MATH domain, only present in meprin A, allows the release of the protein from the membrane [PUBMED:7890660].
TRAF proteins were first isolated by their ability to interact with TNF receptors [PUBMED:8069916]. They promote cell survival by the activation of downstream protein kinases and, finally, transcription factors of the NF-kB and AP-1 family. The TRAF proteins are composed of 3 structural domains: a RING finger (see PROSITEDOC) in the N-terminal part of the protein, one to seven TRAF zinc fingers (see PROSITEDOC) in the middle and the MATH domain in the C-terminal part [PUBMED:12387856]. The MATH domain is necessary and sufficient for self-association and receptor interaction. From the structural analysis two consensus sequence recognised by the TRAF domain have been defined: a major one, [PSAT]x[QE]E and a minor one, PxQxxD [PUBMED:10518213].
The structure of the TRAF2 protein reveals a trimeric self-association of the MATH domain [PUBMED:10206649]. The domain forms a new, light-stranded antiparallel beta sandwich structure. A coiled-coil region adjacent to the MATH domain is also important for the trimerisation. The oligomerisation is essential for establishing appropriate connections to form signalling complexes with TNF receptor-1. The ligand binding surface of TRAF proteins is located in beta-strands 6 and 7 [PUBMED:10518213].
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|Molecular function||protein binding (GO:0005515)|
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Curation and family details
|Seed source:||Pfam-B_1602 (release 3.0)|
|Number in seed:||52|
|Number in full:||3261|
|Average length of the domain:||124.00 aa|
|Average identity of full alignment:||17 %|
|Average coverage of the sequence by the domain:||25.90 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||21|
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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 MATH domain has been found. There are 92 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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