EMI, a novel cysteine-rich domain of EMILINs and other extracellular proteins, interacts with the gC1q domains and participates in multimerization.
The N-terminal cysteine-rich domain (EMI domain) of EMILIN-1 is a new protein domain that is shared with two proteins (multimerin and EMILIN-2) and with four additional database entries. The EMI domains are always located at the N-terminus, have a common gene organization, and belong to proteins that are forming or are compatible with multimer formation. The potential role of the EMI domain in the assembly of EMILIN-1 was investigated by the two-hybrid system. No reporter gene activity was detected when EMI-1 was co-transformed with the C-terminal gC1q-1 domain excluding a head-to-tail multimerization; conversely, a strong interaction was detected when the EMI-1 domain was co-transformed with the gC1q-2 domain of EMILIN-2.
Doliana
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Divisione di Oncologia Sperimentale 2, CRO-IRCCS, National Cancer Institute, Aviano, Italy.
Bot
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Bonaldo
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Colombatti
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D000595:Amino Acid Sequence; D001704:Biopolymers / Q000378:metabolism; D002460:Cell Line; D015922:Complement C1q / Q000737:chemistry / Q000378:metabolism*; D005109:Extracellular Matrix / Q000378:metabolism; D006801:Humans; D008562:Membrane Glycoproteins / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae; D017386:Sequence Homology, Amino Acid
D001704:Biopolymers; D008562:Membrane Glycoproteins; C030340:elastin microfibril interface located protein; D015922:Complement C1q