Letunic et al. (2017) Nucleic Acids Res doi: 10.1093/nar/gkx922
Letunic et al. (2020) Nucleic Acids Res doi: 10.1093/nar/gkaa937

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MADS

SMART accession number:	SM00432
Description:	-
Interpro abstract (IPR002100):	Human serum response factor (SRF) is a ubiquitous nuclear protein important for cell proliferation and differentiation. SRF function is essential for transcriptional regulation of numerous growth-factor-inducible genes, such as c-fos oncogene and muscle-specific actin genes. A core domain of around 90 amino acids is sufficient for the activities of DNA-binding, dimerisation and interaction with accessory factors. Within the core is a DNA-binding region, designated the MADS box [ (PUBMED:7637780) ], that is highly similar to many eukaryotic regulatory proteins: among these are MCM1, the regulator of cell type-specific genes in fission yeast; DSRF, a Drosophila trachea development factor; the MEF2 family of myocyte-specific enhancer factors; and the Agamous and Deficiens families of plant homeotic proteins. In SRF, the MADS box has been shown to be involved in DNA-binding and dimerisation [ (PUBMED:3203386) ]. Proteins belonging to the MADS family function as dimers, the primary DNA-binding element of which is an anti-parallel coiled coil of two amphipathic alpha-helices, one from each subunit. The DNA wraps around the coiled coil allowing the basic N-termini of the helices to fit into the DNA major groove. The chain extending from the helix N-termini reaches over the DNA backbone and penetrates into the minor groove. A 4-stranded, anti-parallel beta-sheet packs against the coiled-coil face opposite the DNA and is the central element of the dimerisation interface. The MADS-box domain is commonly found associated with K-box region see ( IPR002487 ).
GO function:	DNA binding (GO:0003677), protein dimerization activity (GO:0046983)
Family alignment:	View or CHROMA formatHMM/Web logoCLUSTALW formatMSF formatFASTA formatPIR format

There are 21394 MADS domains in 21348 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Taxonomic distribution of proteins containing MADS domain.

  This tree includes only several representative species. The complete taxonomic breakdown of all proteins with MADS domain is also avaliable.

  Click on the protein counts, or double click on taxonomic names to display all proteins containing MADS domain in the selected taxonomic class.

• Cellular role (predicted cellular role)

• Binding / catalysis: DNA-binding

• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Pellegrini L, Tan S, Richmond TJ
  • Structure of serum response factor core bound to DNA.
  • Nature. 1995; 376: 490-8
  • Display abstract

  • The human serum response factor is a transcription factor belonging to the MADS domain protein family with members characterized from the plant and animal kingdoms. The X-ray crystal structure of the serum response factor core in a specific-recognition DNA complex shows that the functions of DNA binding, dimerization and accessory-factor interaction are compactly integrated into a novel protein unit. The intrinsic and induced conformation of the serum response element DNA is the principal DNA feature recognized in the specific complex.

• Metabolism (metabolic pathways involving proteins which contain this domain)

• % proteins involved KEGG pathway ID Description 100.00 map04010 MAPK 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 MADS domain which could be assigned to a KEGG orthologous group, and not all proteins containing MADS 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 MADS domains in PDB

  PDB code	Main view	Title
  1c7u		Complex of the DNA binding core domain of the transcription factor MEF2A with a 20mer oligonucleotide
  1egw		CRYSTAL STRUCTURE OF MEF2A CORE BOUND TO DNA
  1hbx		Ternary Complex of SAP-1 and SRF with specific SRE DNA
  1k6o		Crystal Structure of a Ternary SAP-1/SRF/c-fos SRE DNA Complex
  1mnm		YEAST MATALPHA2/MCM1/DNA TERNARY TRANSCRIPTION COMPLEX CRYSTAL STRUCTURE
  1n6j		Structural basis of sequence-specific recruitment of histone deacetylases by Myocyte Enhancer Factor-2
  1srs		SERUM RESPONSE FACTOR (SRF) CORE COMPLEXED WITH SPECIFIC SRE DNA
  1tqe		Mechanism of recruitment of class II histone deacetylases by myocyte enhancer factor-2
  3kov		Structure of MEF2A bound to DNA reveals a completely folded MADS-box/MEF2 domain that recognizes DNA and recruits transcription co-factors
  3mu6		Inhibiting the Binding of Class IIa Histone Deacetylases to Myocyte Enhancer Factor-2 by Small Molecules
  3p57		Crystal structure of the p300 TAZ2 domain bound to MEF2 on DNA
  5f28		5F28

• Links (links to other resources describing this domain)

• PROSITE	MADS_BOX_1
  INTERPRO	IPR002100
  PFAM	transcript_fact

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