EMI domain

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

EMI domain
Identifiers
Symbol	EMI
Pfam	PF07546
InterPro	IPR011489
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

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

Doliana R, Bot S, Bonaldo P, Colombatti A (November 2000). "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. doi:10.1016/S0014-5793(00)02140-2. PMID 11068053. S2CID 38531447.
Callebaut I, Mignotte V, Souchet M, Mornon JP (January 2003). "EMI domains are widespread and reveal the probable orthologs of the Caenorhabditis elegans CED-1 protein". Biochem. Biophys. Res. Commun. 300 (3): 619–23. doi:10.1016/S0006-291X(02)02904-2. PMID 12507493.

This article incorporates text from the public domain Pfam and InterPro: IPR011489

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[pmid11068053-1] Doliana R, Bot S, Bonaldo P, Colombatti A (November 2000). "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. doi:10.1016/S0014-5793(00)02140-2. PMID 11068053. S2CID 38531447.

[pmid12507493-2] Callebaut I, Mignotte V, Souchet M, Mornon JP (January 2003). "EMI domains are widespread and reveal the probable orthologs of the Caenorhabditis elegans CED-1 protein". Biochem. Biophys. Res. Commun. 300 (3): 619–23. doi:10.1016/S0006-291X(02)02904-2. PMID 12507493.