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The MATH domain, in molecular biology, is a binding domain that was defined originally by a region of homology between otherwise functionally unrelated domains, the intracellular TRAF-C domains of TRAF proteins and a C-terminal region of extracellular meprins A and B. MATH domains are found in a large number of Arabidopsis thaliana sequences, where they often lie alongside BTB/POZ domains, a structural domain that also promotes oligomerisation.

Attributes	Values
rdf:type	Thing Biomolecule Biomolecule Protein yago:Abstraction100002137 yago:Family108078020 yago:Group100031264 yago:Organization108008335 yago:YagoLegalActor yago:YagoLegalActorGeo yago:YagoPermanentlyLocatedEntity protein yago:SocialGroup107950920 yago:Unit108189659
rdfs:label	MATH domain (en)
rdfs:comment	The MATH domain, in molecular biology, is a binding domain that was defined originally by a region of homology between otherwise functionally unrelated domains, the intracellular TRAF-C domains of TRAF proteins and a C-terminal region of extracellular meprins A and B. MATH domains are found in a large number of Arabidopsis thaliana sequences, where they often lie alongside BTB/POZ domains, a structural domain that also promotes oligomerisation. (en)
name	MATH (en)
foaf:depiction
dct:subject	Protein domains
Wikipage page ID	32712224 (xsd:integer)
Wikipage revision ID	1059236795 (xsd:integer)
Link from a Wikipage to another Wikipage	Protein-protein interaction Proteins Endopeptidase Nuclear receptor Meprin A TRAF2 Antiparallel (biochemistry) MEP1B Proteolysis Consensus sequence Conserved sequence TNF receptor associated factor Apoptosis Arabidopsis thaliana Mammalia Pathology Substrate (biochemistry) Protein kinase BTB/POZ domain Cell (biology) Extracellular Cell growth Cell membrane Upstream and downstream (DNA) Transcription factor Protein Receptor (biochemistry) Protein domains Intracellular Binding domain Biological membrane Coiled coil Homology (biology) Zinc finger Astacin Cis-regulatory element Extracellular matrix Cell signalling Molecular biology Ligand binding Secondary structure Gene activation MATH Secreted
Link from a Wikipage to an external page	http://expasy.org/prosite/PDOC00021
sameAs	MATH domain MATH domain MATH domain
dbp:wikiPageUsesTemplate	dbt:Infobox_protein_family dbt:InterPro_content dbt:Reflist dbt:Short_description dbt:Use_dmy_dates
thumbnail	wiki-commons:Special:FilePath/PDB_2cr2_EBI.jpg?width=300
SCOP	1 (xsd:integer)
caption	solution structure of n-terminal domain of speckle-type poz protein (en)
InterPro	IPR002083 (en)
Pfam	PF00917 (en)
Pfam clan	CL0389 (en)
symbol	MATH (en)
has abstract	The MATH domain, in molecular biology, is a binding domain that was defined originally by a region of homology between otherwise functionally unrelated domains, the intracellular TRAF-C domains of TRAF proteins and a C-terminal region of extracellular meprins A and B. Although apparently functionally unrelated, intracellular TRAFs and extracellular meprins share a conserved region of about 180 residues, the meprin and TRAF homology (MATH) \|domain. 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, a MATH domain, an EGF-like domain and a C-terminal transmembrane region. Meprin A and B form membrane bound homo-tetramers whereas homo-oligomers of meprin A are secreted. A proteolytic site adjacent to the MATH domain, only present in meprin A, allows the release of the protein from the membrane. TRAF proteins were first isolated through their ability to interact with TNF receptors. They promote cell survival by the activation of downstream protein kinases and, ultimately, transcription factors of the NF-κB 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. The MATH domain is necessary and sufficient for self-association and receptor interaction. Through structural analysis, two consensus sequences recognised by the TRAF domain have been defined: a major one, [PSAT]x[QE]E and a minor one, PxQxxD. The structure of the TRAF2 protein reveals a trimeric self-association of the MATH domain. 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. MATH domains are found in a large number of Arabidopsis thaliana sequences, where they often lie alongside BTB/POZ domains, a structural domain that also promotes oligomerisation. (en)
CDD	cd00121 (en)
gold:hypernym	Domain
prov:wasDerivedFrom	wikipedia-en:MATH_domain?oldid=1059236795&ns=0
page length (characters) of wiki page	6109 (xsd:nonNegativeInteger)
Symbol	MATH
foaf:isPrimaryTopicOf	wikipedia-en:MATH_domain
is Link from a Wikipage to another Wikipage of	TRAF-C domain Tripartite motif family
is Wikipage redirect of	TRAF-C domain
is foaf:primaryTopic of	wikipedia-en:MATH_domain

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