|Protein Name||Disintegrin and metalloproteinase domain-containing protein 10|
|Milk Fraction||Whey, Exosome|
|Ref Sequence Id||NP_776921.1|
|Amino Acid Lenth||748|
|Protein Existence Status||Reviewed: Experimental evidence at protein level|
|Presence in other biological fluids/tissue/cells||detected in secreted vesicles identified as exosomes;|
|Protein Function||metalloproteinases; regulate the bioavailability of adhesion molecules and ligands to various cellularsignaling receptors; functions include: (i) collagen processing as procollagen N-proteinase; (ii) cleavage of the matrix proteoglycans aggrecan, versican and brevican; (iii) inhibition of angiogenesis; and (iv) blood coagulation homoeostasis as the von Willebrand factor cleaving protease; involved in the intramembrane proteolysis process, whereby it mediates ectodomain shedding of various membrane-bound receptors, adhesion molecules, growth factors, and cytokines; involved in the regulation of the shedding of Notch, HER-2, CD44, IL-6 receptor, amyloid precursor protein, and cadherins; modulates the activation status of various cellularsignaling pathways that have an impact on cellular responses such as proliferation and migration;|
|Biochemical Properties||extracellular, multidomain enzymes; paired basic amino acid converting enzyme; secreted as a precursor protein and consists of multiple functional domains, including a prodomain, catalytic domain, cysteine-rich domain, transmembranous domain, and cytoplasmic domain|
|PTMs||As found in bovine ADAM 10, four potential N-glycosylation sites (N267, N278, N439 and N551); contain high-mannose and complex-type glycans; three located in the metalloprotease domain (N267, N278 and N439) and one in the disintegrin domain (N551)|
| Site(s) of PTM(s) |
|>sp|Q10741|ADA10_BOVIN Disintegrin and metalloproteinase domain-containing protein 10 OS=Bos taurus OX=9913 GN=ADAM10 PE=1 SV=1|
MVLLRVLILLLSWVAGLGGQYGNPLNKYIRHYEGLSYDVDSLHQKHQRAKRAVSHEDQFL RLDFHAHGRHFNLRMKRDTSLFSEEFRVETSNAVLDYDTSHIYTGHIYGEEGSFSHGSVI DGRFEGFIQTHGGTFYVEPAERYIKDRTLPFHSVIYHEDDIKYPHKYGPQGGCADHSVFE RMRKYQMTGVEEVTQTPQEKHAINGPELLRKKRTTVAEKNTCQLYIQTDHLFFKYYGTRE AVIAQISSHVKAIDTIYQTTDFSGIRNISFMVKRIRINTTADEKDPTNPFRFPNIGVEKF LELNSEQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPSGSSGGICEKSKLYSDGKKKSLNT GIITVQNYGSHVPPKVSHITFAHEVGHNFGSPHDSGTECTPGESKNLGQKENGNYIMYAR ATSGDKLNNNKFSLCSIRNISQVLEKKRNNCFVESGQPICGNGMVEQGEECDCGYSDQCK DECCYDANQPEGKKCKLKPGKQCSPSQGPCCTAHCAFKSKTEKCRDDSDCAKEGICNGIT ALCPASDPKPN*551FTDCNRHTQVCINGQCAGSICEKHGLEECTCASSDGKDDKELCHVCCMK KMEPSTCASTGSVQWNKYFLGRTITLQPGSPCNDFRGYCDVFMRCRLVDADGPLARLKKA IFSPELYENIAEWIVAYWWAVLLMGIALIMLMAGFIKICSVHTPSSNPKLPPPKPLPGTL KRRRPPQPIQQPQRQRPRESYQMGHMRR
|Significance of PTMs||role in processing, stability, activity and intracellular localization of ADAM 10; N278 are important for the folding of the protein probably mediating the interaction with calnexin; N439 glycosylation site resulted in increased susceptibility of bADAM10 to proteases|
|Bibliography||1. Armanious, H., Gelebart, P., Anand, M., Belch, A., & Lai, R. (2011). Constitutive activation of metalloproteinase ADAM10 in mantle cell lymphoma promotes cell growth and activates the TNFα/NFκB pathway. Blood, 117(23), 6237–6246. https://doi.org/10.1182/blood-2010-10-313940. |
2. Kuno, K., Kanada, N., Nakashima, E., Fujiki, F., Ichimura, F., & Matsushima, K. (1997). Molecular cloning of a gene encoding a new type of metalloproteinase-disintegrin family protein with thrombospondin motifs as an inflammation associated gene. The Journal of Biological Chemistry, 272(1), 556–562. https://doi.org/10.1074/jbc.272.1.556.
3. Escrevente, C., Morais, V. A., Keller, S., Soares, C. M., Altevogt, P., & Costa, J. (2008). Functional role of N-glycosylation from ADAM10 in processing, localization and activity of the enzyme. Biochimica et Biophysica Acta, 1780(6), 905–913. https://doi.org/10.1016/j.bbagen.2008.03.004.