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PROSITE documentation PDOC50900 [for PROSITE entry PS50900]

PLAC domain profile





Description

The PLAC (protease and lacunin) domain is a six cysteine region of about 40 residues which is present at or near the C-termini of:

  • Mammalian paired basic amino acid cleaving enzyme 4 (PACE4).
  • Mammalian proprotein convertase subtilisin/kexin type 5 (PCSK5).
  • Mammalian metalloproteases ADAMTS-2, -3, -10, -12, -14, -16, -17 and -19.
  • Manduca sexta lacunin, a matrix protein that is also dynamically expressed on basal surfaces of epithelial cells during embryonic and postembryonic and morphogenesis.

The PLAC domain is found associated with other domains such as the thrombospondin type I repeat (TSP1) (see <PDOC50092>), the Kunitz proteinase inhibitor domain (see <PDOC00252>), the Ig-like domain (see <PDOC50835>), the WAP domain, the subtilase domain (see <PDOC00125>), or the ADAM type metalloprotease domain (see <PDOC50215>). The function of the PLAC domain is not yet known [1,2].

The profile we developed covers the entire PLAC domain.

Last update:

October 2003 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

PLAC, PS50900; PLAC domain profile  (MATRIX)


References

1AuthorsNardi J.B. Martos R. Walden K.K.O. Lampe D.J. Robertson H.M.
TitleExpression of lacunin, a large multidomain extracellular matrix protein, accompanies morphogenesis of epithelial monolayers in Manduca sexta.
SourceInsect Biochem. Mol. Biol. 29:883-897(1999).
PubMed ID10528409

2AuthorsCal S. Obaya A.J. Llamazares M. Garabaya C. Quesada V. Lopez-Otin C.
TitleCloning, expression analysis, and structural characterization of seven novel human ADAMTSs, a family of metalloproteinases with disintegrin and thrombospondin-1 domains.
SourceGene 283:49-62(2002).
PubMed ID11867212



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