Multimerin 2 (MMRN2)

ENDOGLYX1, a 500-kD cell surface glycoprotein complex, and sequenced peptides derived from the component proteins. By searching databases using the peptide sequences, they obtained a full-length cDNA encoding MMRN2, which they called ENDOGLYX1. The deduced 949-amino acid protein has a calculated molecular mass of 104.4 kD. It contains an N-terminal signal sequence, followed by 2 major globular domains, an emilin (EM1) domain and a C-terminal C1q -like domain, which are separated by a large central coiled-coil-rich region. The EM1 domain contains 7 cysteines, 6 of which likely form disulfide bridges. The coiled-coil-rich region is divided into coiled-coil subdomains interrupted by noncoiled regions, allowing structural flexibility. An acidic region precedes the C1q region and is typically found in proteins that interact with glycosaminoglycans.