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A DISINTEGRIN-LIKE AND METALLOPROTEINASE WITH THROMBOSPONDIN TYPE 1 MOTIF, 18; ADAMTS18

TEXT

DESCRIPTION

ADAMTS18 is a member of the large ADAMTS family of zinc-dependent proteases.

CLONING

Using homology with the metalloprotease domain of ADAMTS proteins, Cal et al. (2002) identified ADAMTS18 within a genomic database. They obtained the full-length clone by PCR and 5-prime and 3-prime RACE of fetal tissue cDNA libraries. The deduced protein contains an N-terminal signal peptide, followed by a propeptide; a metalloprotease catalytic domain that includes the Zn-binding motif; a disintegrin-like domain; a central thrombospondin I (THBS1; 188060)-like motif; a cysteine-rich domain; a spacer region; and 3 C-terminal THBS1 repeats. There is a stop codon within the third THBS1-like repeat that generates a truncated motif. ADAMTS18 also has 6 N-glycosylation sites. ADAMTS18 shares 57% sequence identity with ADAMTS16 (607510), including 85% identity within the catalytic domains. PCR analysis revealed that ADAMTS18 is expressed in fetal lung, liver, and kidney and in adult brain, prostate, submaxillary gland, and endothelium. 30 PubMed Neighbors

MAPPING

By genomic sequence analysis, Cal et al. (2002) mapped the ADAMTS18 gene to chromosome 16q23.

REFERENCES

1. Cal, S.; Obaya, A. J.; Llamazares, M.; Garabaya, C.; Quesada, V.; Lopez-Otin, C. :
Cloning, expression analysis, and structural characterization of seven novel human ADAMTSs, a family of metalloproteinases with disintegrin and thrombospondin-1 domains. Gene 283: 49-62, 2002.
PubMed ID : 11867212

CREATION DATE

Patricia A. Hartz : 1/24/2003

EDIT HISTORY

mgross : 1/24/2003

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