MMP27

MMP27
Identifiers
Gene ontology
Molecular function	zinc ion binding peptidase activity metalloendopeptidase activity hydrolase activity metallopeptidase activity metal ion binding
Cellular component	extracellular matrix extrinsic component of endoplasmic reticulum membrane endoplasmic reticulum membrane endoplasmic reticulum membrane extracellular space
Biological process	collagen catabolic process proteolysis extracellular matrix organization
Sources:Amigo / QuickGO

Ensembl				ENSG00000137675	ENSMUSG00000070323
UniProt	Q9H306	n/a
RefSeq (mRNA)	NM_022122	NM_001030289 NM_001310717
RefSeq (protein)	NP_071405	n/a
Location (UCSC)	Chr 11: 102.69 – 102.71 Mb	Chr 9: 7.57 – 7.58 Mb
PubMed search	[3]	[4]

Wikidata

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Matrix metallopeptidase 27 also known as MMP-27 is an enzyme which in humans is encoded by the MMP27 gene.^[5]

Structure

MMP-27 was discovered and cloned in 1998 by Yang and Kurkinen.

(99-263) containing the typical HEXXHXXGXXH motif of the metzincins (M10 and M12 families of the MEROPS[2] database), (iv) a proline-rich hinge region (264-278) and (v) a hemopexin-like domain (279-465) folded as a four-bladed β-propeller through disulfide bond formation between the two flanking Cys residues (Cys279 and Cys465). MMP-27 could be classified in the stromelysin group of MMPs, since MMP-27 shows 51,6% homology with stromelysin-2 (MMP-10) and localizes in the cluster of MMPs located on chromosome 11.

Like the six known MT-MMPs, human MMP-27 is prolonged by an additional C-terminal domain (466-513). The Spoctopus algorithm for topological prediction^[7] suggests that this C-terminal extension (CTE) includes a potential transmembrane domain (490-510). However, this sequence is less hydrophobic than in transmembrane MT-MMPs (MMP-14, -15, -16 and -24) as it contains hydrophilic/charged residues, in particular His492, Lys493, His504 and Lys507.

Function

Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases.^[8]

Cominelli A. and colleagues demonstrated that MMP-27 is an unusual protease which is not secreted and is efficiently retained in the

Deletion mutants and swapping with recombinant MMP-10 demonstrate that the unique MMP-27 C-terminal extension (CTE) is necessary and sufficient for endoplasmic reticulum retention but does not provide a stable membrane anchorage. Despite sequence homology with MT-MMPs, the CTE is not a transmembrane domain and does not interact permanently with membrane. This unique feature for an MMP raises important questions about potential functions of MMP-27, which remains to be investigated.

Clinical significance

Sparse information about MMP-27 expression was found in studies of gene expression profiling (

A recent investigation of the transcriptome from distinct tissue compartments of the menstrual

References

External links

• The MEROPS online database for peptidases and their inhibitors: M10.027

This article incorporates text from the United States National Library of Medicine, which is in the public domain.