The domain within your query sequence starts at position 25 and ends at position 134; the E-value for the MATH domain shown below is 6.01e-8.

CHKWTISNFSFCMDGIMETITSPKFSLKASDKVEWGLKVHPNGIDEESKNYLSVYLALLH
CQKSPVWAKYEFWIINSQGEKYQSRKSTKVVSFHKNKYRGFKKFILRDFL

MATH

meprin and TRAF homology

• SMART accession number: SM00061
• 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 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 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 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) ].

• GO function: protein binding (GO:0005515)

There are 16432 MATH domains in 14479 proteins in SMART's nrdb database.

Metabolism (metabolic pathways involving proteins which contain this domain)

% proteins involved	KEGG pathway ID	Description
45.45	map05222	Small cell lung cancer
18.18	map04620	Toll-like receptor signaling pathway
14.77	map04010	MAPK signaling pathway
10.23	map04120	Ubiquitin mediated proteolysis
5.68	map04210	Apoptosis
5.68	map04920	Adipocytokine signaling pathway

This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with MATH domain which could be assigned to a KEGG orthologous group, and not all proteins containing MATH domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.

Structure (3D structures containing this domain)

3D Structures of MATH domains in PDB

PDB code	Title
1ca4	STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 (TRAF2)
1ca9	STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A PEPTIDE FROM TNF-R2
1czy	CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE TRAF DOMAIN OF HUMAN TRAF2 AND AN LMP1 BINDING PEPTIDE
1czz	STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A 17-RESIDUE CD40 PEPTIDE
1d00	STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A 5-RESIDUE CD40 PEPTIDE
1d01	STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A HUMAN CD30 PEPTIDE
1d0a	STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 (TRAF2) IN COMPLEX WITH A HUMAN OX40 PEPTIDE
1d0j	STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A M4-1BB PEPTIDE
1f3v	Crystal structure of the complex between the N-terminal domain of TRADD and the TRAF domain of TRAF2
1flk	MOLECULAR BASIS FOR CD40 SIGNALING MEDIATED BY TRAF3
1fll	MOLECULAR BASIS FOR CD40 SIGNALING MEDIATED BY TRAF3
1kzz	DOWNSTREAM REGULATOR TANK BINDS TO THE CD40 RECOGNITION SITE ON TRAF3
1l0a	DOWNSTREAM REGULATOR TANK BINDS TO THE CD40 RECOGNITION SITE ON TRAF3
1lb4	TRAF6 apo structure
1lb5	TRAF6-RANK Complex
1lb6	TRAF6-CD40 Complex
1qsc	CRYSTAL STRUCTURE OF THE TRAF DOMAIN OF TRAF2 IN A COMPLEX WITH A PEPTIDE FROM THE CD40 RECEPTOR
1rf3	Structurally Distinct Recognition Motifs in Lymphotoxin-B Receptor and CD40 for TRAF-mediated Signaling
1yy6	The Crystal Strucure of the N-terminal domain of HAUSP/USP7 complexed with an EBNA1 peptide
1yze	Crystal structure of the N-terminal domain of USP7/HAUSP.
1zms	LMP1 Protein binds to TRAF3 as a structural CD40
2cr2	Solution structure of N-terminal domain of speckle-type POZ protein
2f1w	Crystal structure of the TRAF-like domain of HAUSP/USP7
2f1x	Crystal structure of the TRAF-like domain of HAUSP/USP7 bound to a p53 peptide
2f1y	Crystal structure of the TRAF-like domain of HAUSP/USP7 bound to a MDM2 peptide
2f1z	Crystal structure of HAUSP
2foj	The Crystal Strucure of the N-terminal domain of HAUSP/USP7 complexed with p53 peptide 364-367
2foo	The Crystal Strucure of the N-terminal domain of HAUSP/USP7 complexed with p53 peptide 359-362
2fop	The Crystal Strucure of the N-terminal domain of HAUSP/USP7 complexed with mdm2 peptide 147-150
2gkw	Key contacts promote recongnito of BAFF-R by TRAF3
2xxn	Structure of the vIRF4-HAUSP TRAF domain complex
3hqh	Structures of SPOP-Substrate Complexes: Insights into Molecular Architectures of BTB-Cul3 Ubiquitin Ligases: SPOPMATHx-MacroH2ASBCpep1
3hqi	Structures of SPOP-Substrate Complexes: Insights into Molecular Architectures of BTB-Cul3 Ubiquitin Ligases: SPOPMATHx/BTB/3-box-PucSBC1
3hql	Structures of SPOP-Substrate Complexes: Insights into Molecular Architectures of BTB-Cul3 Ubiquitin Ligases:SPOPMATHx-PucSBC1_pep2
3hqm	Structures of SPOP-Substrate Complexes: Insights into Molecular Architectures of BTB-Cul3 Ubiquitin Ligases: SPOPMATHx-CiSBC2
3hsv	Structures of SPOP-Substrate Complexes: Insights into Molecular Architectures of BTB-Cul3 Ubiquitin Ligases: SPOPMATHx-MacroH2ASBCpep2
3hu6	Structures of SPOP-Substrate Complexes: Insights into Molecular Architectures of BTB-Cul3 Ubiquitin Ligases: SPOPMATHx/BTB/3-box-PucSBC1
3ivb	Structures of SPOP-Substrate Complexes: Insights into Architectures of BTB-Cul3 Ubiquitin Ligases: SPOPMATH-MacroH2ASBCpep1
3ivq	Structures of SPOP-Substrate Complexes: Insights into Molecular Architectures of BTB-Cul3 Ubiquitin Ligases: SPOPMATH-CiSBC2
3ivv	Structures of SPOP-Substrate Complexes: Insights into Molecular Architectures of BTB-Cul3 Ubiquitin Ligases: SPOPMATH-PucSBC1_pep1
3mqr	Crystal Structure of the USP7:HdmX(AHSS) complex
3mqs	Crystal Structure of the USP7:Hdm2(PSTS) complex
3zjb	The structure of the TRAF domain of human TRAF4
4ghu	Crystal structure of TRAF3/Cardif
4gjh	Crystal Structure of the TRAF domain of TRAF5
4gwm	Crystal structure of human promeprin beta
4gwn	Crystal structure of human mature meprin beta
4jjq	Crystal structure of usp7-ntd with an e2 enzyme
4k8u	Crystal structure of TRAF4 TRAF domain
4kg9	Crystal Structure Of USP7-NTD with MCM-BP
4m4e	TRAF domain of human TRAF4
4o1v	SPOP Promotes Tumorigenesis by Acting as a Key Regulatory Hub in Kidney Cancer
4ysi	4YSI
4z8m	4Z8M

Links (links to other resources describing this domain)

• PFAM: MATH
• INTERPRO: IPR002083