MATHmeprin and TRAF homology |
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| SMART accession number: | SM00061 |
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| Description: | |
| Interpro abstract (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 hydrolyzing 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 a MATH domain, an EGF-like domain 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 in the N-terminal part of the protein, one to seven TRAF zinc fingers 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 recognized 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, eight-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 signaling complexes with TNF receptor-1. The ligand binding surface of TRAF proteins is located in beta-strands 6 and 7 (PUBMED:10518213). |
| Family alignment: |
There are 1101 MATH domains in 954 proteins in SMART's nrdb database.
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- Evolution (species in which this domain is found)
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