Biochem. J. 334 ( Pt 1), 93-98 (1998)[PubMed:9693107]
Cellular disintegrins are a family of membrane-anchored proteins structurally related to snake venom disintegrins, and are potential regulators of cell-cell and cell-matrix interactions. The members of this protein family are also called ADAMs (a disintegrin and metalloproteinase) or MDC proteins (metalloproteinase-like disintegrin-like cysteine-rich), because they all contain disintegrin-like and metalloproteinase-like domains. In this paper, we report the cloning and sequence analysis of two novel additional members of this family, which we have termed MDC2 and MDC3. The deduced amino acid sequences reveal that the two proteins possess typical cellular disintegrin structures [that is, pro-, metalloproteinase-like, disintegrin-like, cysteine-rich, epidermal growth factor-like, transmembrane, and cytoplasmic domains] and exhibit high sequence similarity with human MDC/ADAM11 protein [Katagiri, Harada, Emi and Nakamura (1995) Cytogenet. Cell Genet. 68, 39-44]. A zinc-binding motif, which is critical for proteinase activity, is disrupted in the metalloproteinase-like domain of MDC2 and MDC3, as well as MDC/ADAM11. In the disintegrin-like domain of snake venom short disintegrins, the RDG-containing loops are critical for integrin binding. These three MDCs do not contain the RDG sequences, but the corresponding loops in these proteins are similar to each other. Northern blot analysis revealed that the mRNAs of MDC2, MDC3 and MDC/ADAM11 are highly expressed in the brain. These findings suggest that these proteins may function as integrin ligands in the brain.
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
Catalysis of the hydrolysis of peptide bonds by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
Biochem. J. 334 ( Pt 1), 93-98 (1998)[PubMed:9693107]
Cellular disintegrins are a family of membrane-anchored proteins structurally related to snake venom disintegrins, and are potential regulators of cell-cell and cell-matrix interactions. The members of this protein family are also called ADAMs (a disintegrin and metalloproteinase) or MDC proteins (metalloproteinase-like disintegrin-like cysteine-rich), because they all contain disintegrin-like and metalloproteinase-like domains. In this paper, we report the cloning and sequence analysis of two novel additional members of this family, which we have termed MDC2 and MDC3. The deduced amino acid sequences reveal that the two proteins possess typical cellular disintegrin structures [that is, pro-, metalloproteinase-like, disintegrin-like, cysteine-rich, epidermal growth factor-like, transmembrane, and cytoplasmic domains] and exhibit high sequence similarity with human MDC/ADAM11 protein [Katagiri, Harada, Emi and Nakamura (1995) Cytogenet. Cell Genet. 68, 39-44]. A zinc-binding motif, which is critical for proteinase activity, is disrupted in the metalloproteinase-like domain of MDC2 and MDC3, as well as MDC/ADAM11. In the disintegrin-like domain of snake venom short disintegrins, the RDG-containing loops are critical for integrin binding. These three MDCs do not contain the RDG sequences, but the corresponding loops in these proteins are similar to each other. Northern blot analysis revealed that the mRNAs of MDC2, MDC3 and MDC/ADAM11 are highly expressed in the brain. These findings suggest that these proteins may function as integrin ligands in the brain.
A series of molecular signals initiated by the binding of extracellular ligand to an integrin on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
From chromosomal region 17q21.3, where a tumour suppressor gene(s) for breast and ovarian cancers is thought to be present, we have isolated a novel gene from a cosmid clone that revealed somatic rearrangements in two breast cancers. The gene (MDC) encodes a 524-amino acid metalloprotease-like, disintegrin-like and cysteine-rich protein with sequence similarity to members of the snake-venom metalloprotease/disintegrin family and guinea-pig sperm-surface protein PH-30. These proteins have been implicated in cell-cell or cell-extracellular matrix interactions. Rearrangements in both tumours involve multiple exons and disrupt the coding region of the new MDC.
A reference proteome is a set of protein sequences derived from a complete proteome which constitutes a defined standard for a particular user community. Reference proteomes are manually defined according to a number of criteria. They cover the proteomes of well- studied model organisms and other proteomes of interest for biomedical and biotechnological research. Reference proteomes have been selected to provide broad coverage of the tree of life, and constitute a representative cross-section of the taxonomic diversity to be found within UniProtKB.
My favorites 
My labels 
Login
