Search by BoMiProt ID - Bomi284


Primary Information

BoMiProt ID Bomi284
Protein Name Deoxyribonuclease (Fragment)
Organism Bos taurus
Uniprot IdF1MW13
Milk FractionMFGM, Exosome
Amino Acid Lenth 316
Molecular Weight 35174
Fasta Sequence https://www.uniprot.org/uniprot/F1MW13.fasta
Gene Name DNASE1L1
Protein Existence Status Unreviewed: Protein inferred from homology

Secondry Information

Presence in other biological fluids/tissue/cells Pancreas, Kidney ,Liver ,Spleen ,Heart ,Lung ,Stomach ,Small intestine,Cerebrum ,Cerebellum ,Parotid gland ,Submaxillary gland ,Testis ,Epididymis
Protein Function perform a variety of important cellular roles by degrading DNA via hydrolysis of its phosphodiester backbone; cleave single or double-stranded DNA and require divalent metal ions to hydrolyze DNA yielding 3 -hydroxyl and 5 -phosphorylated products
Biochemical Properties divalent cation-dependent endonuclease originally isolated from bovine pancreas; G-actin is known to be a potent inhibitor of mammalian DNase I -the activity of mouse DNase I was inhibited as readily as that of human DNase I by G-actin; all DNase I family proteins contain hydrophobic precursor peptides in their N-termini, two essential histidine residues of DNase I are conserved in the other members, all are activated by Ca2+ and Mg2+ and are strongly inhibited by Zn2+, and members hydrolyse DNA endonucleolytically to produce 3' -OH/5' -P ends; DNase X has an extra hydrophobic stretch in its C-terminus; optimal activity at the low pH environment of lysosomes
Significance in milk protect against viruses in milk owing to the ability to inhibit the activity of RNAdependent DNA-polymerase
PTMs Glycosylated: In humans, N-linked glycosylation at Asn-243- conserved in the corresponding regions of monkey, porcine and bovine DNase X proteins
Bibliography 1. Takeshita, H. et al. (1997) ‘Mouse deoxyribonuclease I (DNase I): biochemical and immunological characterization, cDNA structure and tissue distribution.’, Biochemistry and molecular biology international, 42(1), pp. 65–75. Available at: http://www.ncbi.nlm.nih.gov/pubmed/9192086 (Accessed: 4 October 2019).
2. Shiokawa, D. et al. (2005) ‘Physical and biochemical properties of mammalian DNase X proteins: non-AUG translation initiation of porcine and bovine mRNAs for DNase X’, Biochemical Journal, 392(3), pp. 511–517. doi: 10.1042/BJ20051114.
3. Varela-Ramirez, A. et al. (2017) ‘Structure of acid deoxyribonuclease’, Nucleic Acids Research, 45(10), pp. 6217–6227. doi: 10.1093/nar/gkx222.