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0  structures 72  species 0  interactions 529  sequences 46  architectures

Family: EMI (PF07546)

Summary: EMI domain

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EMI domain Edit Wikipedia article

EMI domain
Identifiers
Symbol EMI
Pfam PF07546
InterPro IPR011489

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 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.

References[edit]

  1. ^ a b 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. 
  2. ^ a b 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

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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EMI domain Provide feedback

The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al [2]. This is to stop the family overlapping with other domains.

Literature references

  1. Doliana R, Bot S, Bonaldo P, Colombatti A; , FEBS Lett 2000;484:164-168.: EMI, a novel cysteine-rich domain of EMILINs and other extracellular proteins, interacts with the gC1q domains and participates in multimerization. PUBMED:11068053 EPMC:11068053

  2. Callebaut I, Mignotte V, Souchet M, Mornon JP; , Biochem Biophys Res Commun 2003;300:619-623.: EMI domains are widespread and reveal the probable orthologs of the Caenorhabditis elegans CED-1 protein. PUBMED:12507493 EPMC:12507493


External database links

This tab holds annotation information from the InterPro database.

InterPro entry 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.

Gene Ontology

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Domain organisation

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Alignments

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(43)
Full
(529)
Representative proteomes NCBI
(472)
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(28)
RP35
(49)
RP55
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RP75
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  Seed
(43)
Full
(529)
Representative proteomes NCBI
(472)
Meta
(0)
RP15
(28)
RP35
(49)
RP55
(116)
RP75
(259)
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  Seed
(43)
Full
(529)
Representative proteomes NCBI
(472)
Meta
(0)
RP15
(28)
RP35
(49)
RP55
(116)
RP75
(259)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

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Curation and family details

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Seed source: [2]
Previous IDs: none
Type: Domain
Author: Bateman A, Doliana R
Number in seed: 43
Number in full: 529
Average length of the domain: 70.40 aa
Average identity of full alignment: 32 %
Average coverage of the sequence by the domain: 10.79 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.8 21.8
Trusted cut-off 21.8 21.8
Noise cut-off 21.5 19.6
Model length: 72
Family (HMM) version: 8
Download: download the raw HMM for this family

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