MMP-28, a new human matrix metalloproteinase with an unusual cysteine-switch sequence is widely expressed in tumors.
We report the discovery, cloning, and characterization of a novel human matrix metalloproteinase (MMP-28) cDNA gene. The deduced 520-amino-acid sequence of MMP-28 includes a signal peptide, a prodomain with an unusual cysteine-switch PRCGVTD motif followed by the furin cleavage RRKKR site, a catalytic domain, a hinge-region and a hemopexin-like domain. On the basis of their structural characteristics, MMP-28 belongs to the MMP-19 subfamily. The genomic MMP-28 gene uniquely mapped to chromosome 17q11.2 includes eight exons and seven introns. The broad range of expression in carcinomas as well as normal adult and fetal tissues suggests an important functional role for MMP-28.
The Burnham Institute, 10901 North Torrey Pines Road, 92037, La Jolla, CA, USA.
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Marchenko
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Strongin
D017398:Alternative Splicing; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D002874:Chromosome Mapping; D002886:Chromosomes, Human, Pair 17 / Q000235:genetics; D003001:Cloning, Molecular; D003545:Cysteine / Q000235:genetics*; D018076:DNA, Complementary / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D019143:Evolution, Molecular; D005091:Exons; D005260:Female; D015971:Gene Expression Regulation, Enzymologic; D015972:Gene Expression Regulation, Neoplastic; D005796:Genes / Q000235:genetics; D006801:Humans; D007438:Introns; D008297:Male; D020782:Matrix Metalloproteinases / Q000737:chemistry / Q000235:genetics*; D053505:Matrix Metalloproteinases, Secreted; D008969:Molecular Sequence Data; D009369:Neoplasms / Q000201:enzymology / Q000235:genetics* / Q000473:pathology; D010802:Phylogeny; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D014018:Tissue Distribution
D018076:DNA, Complementary; C424663:MMP28 protein, human; D020782:Matrix Metalloproteinases; D053505:Matrix Metalloproteinases, Secreted; D003545:Cysteine