Description

IPR002083 is a MATH/TRAF domain.

<p>Although apparently functionally unrelated, intracellular TRAFs and extracellular meprins share a conserved region of about 180 residues, the meprin and TRAF homology (MATH) domain [[cite:PUB00011812]]. 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:PDOC00604]), a MATH domain, an EGF-like domain (see [prositedoc:PDOC00021]) 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 [[cite:PUB00011813]].</p> <p>TRAF proteins were first isolated by their ability to interact with TNF receptors [[cite:PUB00011814]]. 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:PDOC00449]) in the N-terminal part of the protein, one to seven TRAF zinc fingers (see [prositedoc:PDOC50145]) in the middle and the MATH domain in the C-terminal part [[cite:PUB00011812]]. 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 [[cite:PUB00011815]].</p> <p>The structure of the TRAF2 protein reveals a trimeric self-association of the MATH domain [[cite:PUB00011816]]. The domain forms a new, light-stranded antiparallel β-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 β-strands 6 and 7 [[cite:PUB00011815]].</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on April 27, 2020, while the GO metadata was last updated on April 27, 2020.

Associated Lotus transcripts 72

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: