Biology:EMI domain

From HandWiki
EMI domain
Identifiers
SymbolEMI
PfamPF07546
InterProIPR011489

In molecular biology, the EMI domain, first named after its presence in proteins of the EMILIN family, is a small cysteine-rich protein domain of around 75 amino acids. The EMI domain is most often found at the N terminus of metazoan extracellular proteins that are forming or are compatible with multimer formation.[1] It is found in association with other domains, such as C1q, laminin-type EGF-like, collagen-like, FN3, WAP, ZP or FAS1.[2] It has been suggested that the EMI domain could be a protein-protein interaction module, as the EMI domain of EMILIN-1 was found to interact with the C1q domain of EMILIN-2.[1]

The EMI domain possesses six highly conserved cysteine residues, which likely form disulphide bonds. Other key features of the EMI domain are the C-C-x-G-[WYFH] pattern, a hydrophobic position just preceding the first cysteine (Cys1) of the domain and a cluster of hydrophobic residues between Cys3 and Cys4. The EMI domain could be made of two sub-domains, the fold of the second one sharing similarities with the C-terminal sub-module characteristic of EGF-like domains.[2]

Proteins known to contain an EMI domain include:

  • Vertebrate Emilins, extracellular matrix glycoproteins.
  • Vertebrate Multimerins, extracellular matrix glycoproteins.
  • Vertebrate Emu proteins, which could interact with several different extracellular matrix components and serve to connect and integrate the function of multiple partner molecules.
  • Vertebrate beta-IG-H3.
  • Vertebrate osteoblast-specific factor 2 (OSF-2).
  • Mammalian NEU1/NG3 proteins.
  • Drosophila midline fasciclin.
  • Caenorhabditis elegans ced-1, a transmembrane receptor that mediates cell corpse engulfment.

References

  1. 1.0 1.1 "EMI, a novel cysteine-rich domain of EMILINs and other extracellular proteins, interacts with the gC1q domains and participates in multimerization". FEBS Lett. 484 (2): 164–8. November 2000. doi:10.1016/S0014-5793(00)02140-2. PMID 11068053. 
  2. 2.0 2.1 "EMI domains are widespread and reveal the probable orthologs of the Caenorhabditis elegans CED-1 protein". Biochem. Biophys. Res. Commun. 300 (3): 619–23. January 2003. doi:10.1016/S0006-291X(02)02904-2. PMID 12507493. 
This article incorporates text from the public domain Pfam and InterPro: IPR011489