{PDOC51041}
{PS51041; EMI}
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* EMI domain profile *
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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 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 profile we developed covers the entire EMI domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: November 2004 / First entry.

[ 1] Doliana R., Bot S., Bonaldo P., Colombatti A.
     "EMI, a novel cysteine-rich domain of EMILINs and other extracellular
     proteins, interacts with the gC1q domains and participates in
     multimerization."
     FEBS Lett. 484:164-168(2000).
     PubMed=11068053
[ 2] Callebaut I., Mignotte V., Souchet M., Mornon J.-P.
     "EMI domains are widespread and reveal the probable orthologs of the
     Caenorhabditis elegans CED-1 protein."
     Biochem. Biophys. Res. Commun. 300:619-623(2003).
     PubMed=12507493

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