Literature summary for 2.7.7.18 extracted from

Ma, X.; Zhu, Y.; Lu, J.; Xie, J.; Li, C.; Shin, W.; Qiang, J.; Liu, J.; Dou, S.; Xiao, Y.; Wang, C.; Jia, C.; Long, H.; Yang, J.; Fang, Y.; Jiang, L.; Zhang, Y.; Zhang, S.; Zhai, R.; Liu, C.; Li, D.
Nicotinamide mononucleotide adenylyl transferase uses its NAD+ substrate-binding site to chaperone phosphorylated TAU (2020), eLife, 9, e51859 .

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Mus musculus
expression in Escherichia coli	Drosophila melanogaster

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of isoform NMNAT3 to 2 A resolution	Mus musculus

Protein Variants

Protein Variants	Comment	Organism
E198P/L217R	mutation disrupts the dimer interface, leading to a mixture of dimer and monomer in solution	Mus musculus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
64000	-	gel filtration	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Drosophila melanogaster	Q9VC03	cf. EC 2.7.7.1	-
Mus musculus	Q99JR6	isoform NMNAT3, cf. EC 2.7.7.1	-

Subunits

Subunits	Comment	Organism
dimer	2 * 27700, calculated from sequence, and crystallization data	Mus musculus

Synonyms

Synonyms	Comment	Organism
NMNAT3	cf. EC 2.7.7.1	Mus musculus

General Information

General Information	Comment	Organism
physiological function	NMNAT serves as a chaperone of phosphorylated Tau to prevent its amyloid aggregation in vitro as well as mitigate its pathology in Drosophila tauopathy models overexpressing human Tau. NMNAT adopts its enzymatic pocket to specifically bind the phosphorylated sites of Tau, which can be competitively disrupted by the enzymatic substrates of NMNAT. NMNAT serves as a cochaperone of Hsp90 for the specific recognition of phosphorylated Tau over Tau	Drosophila melanogaster
physiological function	NMNAT shows strong interaction with phosphorylated truncated Tau protein. The binding affinity of NMNAT3 to phosphorylated Tau is about one order of magnitude higher than that to Tau.The phosphorylated Ser residues of Tau are the primary binding sites. Substrates (i.e. NMN and ATP) and the chaperone client phosphorylated Tau share the same binding pocket with a partial overlap at the phosphate-binding site	Mus musculus

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Release 2023.1 (January 2023)