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PROSITE documentation PDOC51041EMI domain profile
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PURL: https://purl.expasy.org/prosite/documentation/PDOC51041
The EMI domain, first named after its presence in proteins of the EMILIN family, is a small cysteine-rich module of ~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 (see <PDOC00857>), laminin-type EGF-like, collagen-like, FN3 (see <PDOC50853>), WAP (see <PDOC00026>), ZP (see <PDOC00577>) or FAS1 (see <PDOC50213>) [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 cysteines residues, which likely form disulfide 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].
Some proteins known to contain a EMI domain are listed below:
- Vertebrate Emilins, extracellular matrix glycoproteins.
- Vertebrate Multimerins, extracellular matrix glycoproteins.
- Vetebrate Emu proteins. They could interact with several different extracellular matrix components and serve to connect and integrate the function of multiple partner molecules.
- Vertebrate β 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.
The profile we developed covers the entire EMI domain.
Last update:November 2004 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Doliana R. Bot S. Bonaldo P. Colombatti A. |
| Title | EMI, a novel cysteine-rich domain of EMILINs and other extracellular proteins, interacts with the gC1q domains and participates in multimerization. | |
| Source | FEBS Lett. 484:164-168(2000). | |
| PubMed ID | 11068053 |
| 2 | Authors | Callebaut I. Mignotte V. Souchet M. Mornon J.-P. |
| Title | EMI domains are widespread and reveal the probable orthologs of the Caenorhabditis elegans CED-1 protein. | |
| Source | Biochem. Biophys. Res. Commun. 300:619-623(2003). | |
| PubMed ID | 12507493 |
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