Isolation and sequencing of cDNAs for proteins with multiple domains of Gly-Xaa-Yaa repeats identify a distinct family of collagenous proteins

Document Type

Article

Abstract

We have isolated overlapping mouse cDNAs encoding a collagenous polypeptide that we have designated α1(XVIII) collagen. Nucleotide sequence analysis shows that α1(XVIII) collagen contains 10 triple-helical domains separated and flanked by non-triple-helical regions. Within the non-triple- helical regions, there are several Ser-Gly-containing sequences that conform to consensus sequences for glycosaminoglycan attachment sites in proteoglycan core proteins. Northern blots show that α1(XVIII) transcripts are present in multiple organs, with the highest levels in liver, lung, and kidney. We have also isolated overlapping cDNAs encoding human α1(XV) collagen, and their sequence extends a published partial α1(XV) sequence to the 3' end. Comparison of the α1(XV) and α1(XVIII) sequences reveals a striking similarity in the lengths of the six most carboxyl-terminal triple-helical domains. In addition, within the carboxyl non-triple-helical domain NC1 of the two chains, a region of 177 amino acid residues shows about 60% identity at the amino acid level. We suggest, therefore, that α1(XV) and α1(XVIII) collagens are structurally related. Their structure is different from that of other known collagen types. We conclude that they belong to a subfamily of extracellular matrix proteins and we suggest the designation multiplexins (for protein with multiple triple-helix domains and interruptions) for members of this subfamily.

Publication Date

5-10-1994

Publication Title

Proceedings of the National Academy of Sciences of the United States of America

ISSN

00278424

Volume

91

Issue

10

First Page

4229

Last Page

4233

PubMed ID

8183893

Digital Object Identifier (DOI)

10.1073/pnas.91.10.4229

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