SMART: Pfam domain EMI

The domain within your query sequence starts at position 53 and ends at position 123; the E-value for the EMI domain shown below is 5.6e-21.

RHWCHHTVTRTVSCQVQNGSETVVQRVYQSCRWPGPCANLVSYRTLIRPTYRVSYRTVTA
LEWRCCPGFTG

EMI

PFAM accession number:	PF07546
Interpro abstract (IPR011489):	The EMI domain, first named after its presence in proteins of the EMILIN family, is a small cysteine-rich module 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 [ (PUBMED:11068053) ]. It is found in association with other domains, such as C1q, laminin-type EGF-like, collagen-like, FN3, WAP, ZP or FAS1 [ (PUBMED:12507493) ]. 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 [ (PUBMED:11068053) ]. The EMI domain possesses six highly conserved cysteines 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 [ (PUBMED:12507493) ]. Proteins known to contain a EMI domain include: Vertebrate Emilins, extracellular matrix glycoproteins. Vertebrate Multimerins, extracellular matrix glycoproteins. Vetebrate 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. The Pfam alignment for this domain is truncated at the C terminus and does not include the final cysteine [ (PUBMED:12507493) ]. This is to stop the family overlapping with other domains.
GO function:	protein binding (GO:0005515)

PFAM accession number:

PF07546

Interpro abstract (IPR011489):

The EMI domain, first named after its presence in proteins of the EMILIN family, is a small cysteine-rich module 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 [ (PUBMED:11068053) ]. It is found in association with other domains, such as C1q, laminin-type EGF-like, collagen-like, FN3, WAP, ZP or FAS1 [ (PUBMED:12507493) ]. 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 [ (PUBMED:11068053) ].

The EMI domain possesses six highly conserved cysteines 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 [ (PUBMED:12507493) ].

Proteins known to contain a EMI domain include:

Vertebrate Emilins, extracellular matrix glycoproteins.
Vertebrate Multimerins, extracellular matrix glycoproteins.
Vetebrate 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.

The Pfam alignment for this domain is truncated at the C terminus and does not include the final cysteine [ (PUBMED:12507493) ]. This is to stop the family overlapping with other domains.

GO function:

protein binding (GO:0005515)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry EMI