Search by BoMiProt ID - Bomi210

Primary Information

BoMiProt ID Bomi210
Protein Name Disintegrin and metalloproteinase domain-containing protein 10
Organism Bos taurus
Uniprot IDQ10741
Milk FractionWhey, Exosome
Ref Sequence ID NP_776921.1
Aminoacid Length 748
Molecular Weight 84188
FASTA Sequence Download
Gene Name ADAM10
Gene ID 282132
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondary Information

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; Disintegrin And Metalloproteinase 10 (ADAM10), a zinc-dependent protease, was heavily invested in by the pharmaceutical industry
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)

N-glycosylation, O-glycosylation,
>sp|Q10741|ADA10_BOVIN Disintegrin and metalloproteinase domain-containing protein 10 OS=Bos taurus OX=9913 GN=ADAM10 PE=1 SV=1
CATH Matched CATH superfamily
Predicted Disorder Regions (704-748)
DisProt Annotation
TM Helix Prediction 1TMH; (674-696)
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.
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.
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. 4.Atapattu L, Saha N, Chheang C, Eissman MF, Xu K, Vail ME, Hii L, Llerena C, Liu Z, Horvay K, Abud HE, Kusebauch U, Moritz RL, Ding BS, Cao Z, Rafii S, Ernst M, Scott AM, Nikolov DB, Lackmann M, Janes PW. An activated form of ADAM10 is tumor selective and regulates cancer stem-like cells and tumor growth. J Exp Med. 2016 Aug 22;213(9):1741-57. doi: 10.1084/jem.20151095. Epub 2016 Aug 8. PMID: 27503072; PMCID: PMC4995075. 5.Smith TM Jr, Tharakan A, Martin RK. Targeting ADAM10 in Cancer and Autoimmunity. Front Immunol. 2020 Mar 24;11:499. doi: 10.3389/fimmu.2020.00499. PMID: 32265938; PMCID: PMC7105615.