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Information on EC 3.1.3.108 - nocturnin
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3.1.3.108 nocturninIUBMB Comments
The mammalian mitochondrial enzyme is a rhythmically expressed protein that regulates metabolism under the control of circadian clock. It has a slight preference for NADPH over NADP+. The archaeal enzyme, identified in Methanocaldococcus jannaschii, is bifunctional acting as NAD+ kinase (EC 2.7.1.23) and NADP+ phosphatase with a slight preference for NADP+ over NADPH.
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- 3.1.3.108
- hair
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straight
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chlorotic
-
deadenylase
-
woolly
-
curly
-
saccules
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abaxial
-
tenckhoff
- hypotrichosis
- tppase
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conidiophores
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phytopathological
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deadenylation
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exit-site
The expected taxonomic range for this enzyme is: Archaea, Eukaryota
Synonyms
curled, nocturnin, nadpase, nadp phosphatase, ccrn4l, nadp(h) phosphatase, noc-a, noc-b, nadphase, nocturnin-b, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AF2372
MJ0109
MJ0917
NADP phosphatase
NADPase
NADPHase
NOCT
nocturnin (curled)
-
-
-
-
MJ0109
-
-
-
-
NADP phosphatase
-
-
-
-
NOCT
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NADP+ + H2O = NAD+ + phosphate
(2)
-
-
-
NADPH + H2O = NADH + phosphate
(1)
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
, ,
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SYSTEMATIC NAME
IUBMB Comments
NADPH 2'-phosphohydrolase
The mammalian mitochondrial enzyme is a rhythmically expressed protein that regulates metabolism under the control of circadian clock. It has a slight preference for NADPH over NADP+. The archaeal enzyme, identified in Methanocaldococcus jannaschii, is bifunctional acting as NAD+ kinase (EC 2.7.1.23) and NADP+ phosphatase with a slight preference for NADP+ over NADPH.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NADP+ + H2O
NAD+ + phosphate
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
-
-
?
NADP+ + H2O
NAD+ + phosphate
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
-
-
?
NADP+ + H2O
NAD+ + phosphate
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
-
-
?
NADP+ + H2O
NAD+ + phosphate
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
-
-
?
NADPH + H2O
NADH + phosphate
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
-
-
?
NADPH + H2O
NADH + phosphate
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
-
-
?
NADPH + H2O
NADH + phosphate
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
-
-
?
NADPH + H2O
NADH + phosphate
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NADP+ + H2O
NAD+ + phosphate
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
-
-
?
NADP+ + H2O
NAD+ + phosphate
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
-
-
?
NADP+ + H2O
NAD+ + phosphate
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
-
-
?
NADP+ + H2O
NAD+ + phosphate
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
-
-
?
NADPH + H2O
NADH + phosphate
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
-
-
?
NADPH + H2O
NADH + phosphate
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
-
-
?
NADPH + H2O
NADH + phosphate
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
-
-
?
NADPH + H2O
NADH + phosphate
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
in the 2.41 A resolution structure, two Mg2+ ions occupy the active site and are directly coordinated via an octahedral geometry to Glu195 (Mg2+(1)) and Asp324 (Mg2+(2)), respectively. In the 1.48 A resolution structure, only a single Mg2+ ion is bound in the active site and is directly coordinated by Glu195
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ca2+
NOCT is inactive in the presence of Zn2+ and Ca2+ presumably due imperfect transition state formed due to a slight size mismatch of these ions
Zn2+
NOCT is inactive in the presence of Zn2+ and Ca2+ presumably due imperfect transition state formed due to a slight size mismatch of these ions
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.18
NADP+
pH and temperature not specified in the publication
0.54
NADP+
pH and temperature not specified in the publication
0.3
NADPH
pH and temperature not specified in the publication
0.77
NADPH
pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5
NADP+
pH and temperature not specified in the publication
212
NADP+
pH and temperature not specified in the publication
6.9
NADPH
pH and temperature not specified in the publication
236
NADPH
pH and temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9.2
NADP+
pH and temperature not specified in the publication
56.8
NADP+
pH and temperature not specified in the publication
8.9
NADPH
pH and temperature not specified in the publication
63.1
NADPH
pH and temperature not specified in the publication
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
highly expressed in differentiating adipocytes. When adipocyte differentiation is complete there is two fold increase in nocturnin protein compared to undifferentiated controls
brenda
expression of nocturnin mRNA is confined to the clock-containing photoreceptor cell layer within the retina
brenda
additional information
almost no changes of noc-b mRNAs are observed after a meal
brenda
noc-a mRNAs rise sharply after a meal
brenda
almost no changes of noc-b mRNAs are observed after a meal in intestinal bulb
brenda
noc-a mRNAs rise sharply after a meal in intestinal bulb
brenda
almost no changes of noc-b mRNAs are observed after a meal
brenda
noc-a shows a considerable higher expression compared with noc-b. noc-a mRNAs rise sharply after a meal
brenda
noc-a shows a considerable higher expression compared with noc-b
brenda
additional information
mRNAs show a similar widespread distribution in central and peripheral tissues, with higher levels detected for noc-a compared with noc-b
brenda
additional information
mRNAs show a similar widespread distribution in central and peripheral tissues, with higher levels detected for noc-a compared with noc-b
brenda
additional information
-
mRNAs show a similar widespread distribution in central and peripheral tissues, with higher levels detected for noc-a compared with noc-b
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the cytoplasmic form of nocturnin is constitutively expressed and associates externally with membranes of other organelles, including the endoplasmic reticulum, via N-terminal glycine myristoylation
brenda
nocturnin is expressed in the cytoplasm of rod and cone photoreceptor cells
brenda
based on the presence of a mitochondrial target sequence in NOCT, it is determined that mouse NOCT protein localizes to the mitochondria
brenda
mitochondrial form of nocturnin possesses high-amplitude circadian rhythmicity with peak expression level during the early dark phase
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
NOCT-deficient mice are resistant to high fat diet induced weight gain, and exhibit dysregulation of bone formation
malfunction
knockdown of Nocturnin by injection of Nocturnin antisense expression vector into 1-cell embryos results in the delay of early embryonic development to the early blastocyst stage. Nocturnin-overexpressed embryos by injection of Nocturnin expression vector impair their development from the 1-cell to 2-cell or 4-cell stages
malfunction
mice lacking Nocturnin (Noct-/-) display significantly increased amplitudes of mRNA expression of hepatic genes encoding key metabolic enzymes regulating lipid and cholesterol synthesis, both over the daily circadian cycle and in response to fasting and refeeding. Noct-/- mice have increased plasma triglyceride throughout the night and increased amplitude of hepatic cholesterol levels. Posttranscriptional control by Nocturnin regulates the amplitude of these critical metabolic pathways, and loss of this activity results in increased metabolic flux and reduced obesity. Loss of Noct has a significant effect on epididymal white adipose tissue weight (eWAT), resulting in an overall reduced eWAT as a percentage of total body weight in KO mice
malfunction
mice lacking the Noc gene display resistance to diet-induced obesity and hepatic steatosis, due in part to reduced lipid trafficking in the small intestine
malfunction
Noc knock-out (Noc-/-) mice exhibit no obvious abnormalities in development or reproduction, however, they exhibit striking metabolic phenotypes when fed a High-Fat Diet (HFD). This diet causes wild-type mice to become obese, but the Noc-/- mice remain lean although they do not exhibit increased activity or reduced food intake
malfunction
NOCT knockout mice exhibit normal circadian behaviors, indicating that NOCT may function as a downstream effector of circadian signals in vertebrates
malfunction
NOCT knockout mice exhibit normal circadian behaviors, indicating that NOCT may function as a downstream effector of circadian signals in vertebrates
malfunction
nocturnin (Noc-/- mice) are resistant to diet-induced obesity and hepatic steatosis, yet are not hyperactive or hypophagic
metabolism
high dependence of its expression on feeding and nutritional status. Differential responses to feeding of the two nocturnins raise the possibility that they might be underlying different physiological mechanisms (e.g., food intake, lipid mobilization, energy homeostasis) in fish
metabolism
NOCT overexpression leads to a significant increase in the preadipocytes ability to utilize oxidative phosphorylation for ATP (adenosine triphosphate) generation
physiological function
NOCT represses translation and causes degradation of reporter mRNAs in vivo
physiological function
rhythmically expressed protein that regulates metabolism under the control of circadian clock
physiological function
rhythmically expressed protein that regulates metabolism under the control of circadian clock
physiological function
the enzyme helps the circadian clock to adjust metabolism according to day and night activity
physiological function
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
physiological function
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
physiological function
function for the circadian deadenylase nocturnin as a regulator of metabolic amplitude across the day/night cycle and in response to nutrient challenge. Posttranscriptional control by Nocturnin regulates the amplitude of lipid and cholesterol synthesis pathways
physiological function
Noct is crucial for maintaining metabolic homeostasis. Constitutively increased expression of Noct, wild type form, leads to lower fat mass and transiently disrupts bone mass
physiological function
nocturnin plays an important role in the trafficking of dietary lipid in the intestinal enterocyes by optimizing efficient absorption of lipids
physiological function
on the phenotype of NOCT knockout mice, it is probable that NOCT regulates a subset of metabolically and developmentally important transcripts in relevant tissues including the digestive tract, liver, and adipose tissues
physiological function
on the phenotype of NOCT knockout mice, it is probable that NOCT regulates a subset of metabolically and developmentally important transcripts in relevant tissues including the digestive tract, liver, and adipose tissues
physiological function
PARN, nocturnin and Angel are three of the multiple deadenylases that have been described in eukaryotic cells. While each of these enzymes appears to target poly(A) tails for shortening and influence RNA gene expression levels and quality control, the enzymes differ in terms of enzymatic mechanisms, regulation and biological impact. Nocturnin functions in adipogenesis and lipid metabolism
physiological function
precise expression of nocturnin is critical to proper development of early mouse embryos. Possible role of the deadenylase at mouse maternal-to-zygotic transition
physiological function
the enzyme is a direct regulator of oxidative stress response through its NADPH 2' phosphatase activity. It regulates local intracellular concentrations of NADP(H) in a manner that changes over the course of the day
physiological function
the enzyme is a potential key post-transcriptional mediator in the circadian control of many metabolic processes. It appears to play important roles in other tissues and has been implicated in lipid metabolism, adipogenesis, glucose homeostasis, inflammation and osteogenesis
physiological function
the enzyme may play an important role in lineage allocation
physiological function
the gene is required at pupal stage for proper wing morphogenesis after eclosion of the fly
physiological function
-
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
-
physiological function
-
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NOCT_HUMAN
431
0
48196
Swiss-Prot
Mitochondrion (Reliability: 1)
NOCT_MOUSE
429
0
48301
Swiss-Prot
Mitochondrion (Reliability: 2)
NOCT_RAT
428
0
48122
Swiss-Prot
Mitochondrion (Reliability: 1)
BSUHB_ARCFU
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
252
0
27967
Swiss-Prot
-
BSUHB_METJA
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
252
0
28578
Swiss-Prot
-
NPPNK_METJA
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
574
0
64119
Swiss-Prot
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, 2.7 A crystal structure of the catalytic domain
hanging-drop vapor diffusion method, high resolution (2.41 A) crystal structures of the human NOCT catalytic domain
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Strep(II) pSumo vector in BL21 Rosetta2 (DE3) Escherichia coli cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
fasting induces decreases in noc-a transcripts in hypothalamus, intestinal bulb, and liver
mitochondrial form of nocturnin possesses high-amplitude circadian rhythmicity with peak expression level during the early dark phase
nocturin deadenylase shows rhythmic expression under circadian control. It is rapidly induced in response to serum shock, LPS and other stimuli
nocturnin is rhythmically expressed in the cytoplasm of the retinal retina photoreceptor cells, with peak mRNA levels in the early night
nocturnin mRNA levels exhibits a high amplitude circadian rhythm. It is controlled by the retinal circadian clock at the level of transcription
nocturnin-a mRNAs rise sharply after a meal in hypothalamus, intestinal bulb, and liver
the abundance of Nocturnin mRNA level is significantly decreased from the MII to 4-cell stages and slightly increased from the 8-cell to blastocyst stages, whereas the Nocturnin protein level is almost stable in all examined cells including GV and MII oocytes and early embryos
when adipocyte differentiation is complete there is two fold increase in nocturnin protein compared to undifferentiated controls. nocturnin is up-regulated by CLOCK, Bmal1 and Pparg2. Nocturnin is markedly up-regulated with activation of the master transcription factor Pparg in adipocytes and bone marrow stromal cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kawai, S.; Murata, K.
Structure and function of NAD kinase and NADP phosphatase key enzymes that regulate the intracellular balance of NAD(H) and NADP(H)
Biosci. Biotechnol. Biochem.
72
919-930
2008
Archaeoglobus fulgidus (O30298), Methanocaldococcus jannaschii (Q57573), Methanocaldococcus jannaschii (Q58327), Archaeoglobus fulgidus ATCC 49558 (O30298), Methanocaldococcus jannaschii ATCC 43067 (Q57573), Methanocaldococcus jannaschii ATCC 43067 (Q58327)
brenda
Estrella, M.A.; Du, J.; Chen, L.; Rath, S.; Prangley, E.; Chitrakar, A.; Aoki, T.; Schedl, P.; Rabinowitz, J.; Korennykh, A.
The metabolites NADP+ and NADPH are the targets of the circadian protein nocturnin (curled)
Nat. Commun.
10
2367
2019
Drosophila melanogaster (A8JQX3), Homo sapiens (Q9UK39), Homo sapiens
brenda
Abshire, E.T.; Chasseur, J.; Bohn, J.A.; Del Rizzo, P.A.; Freddolino, P.L.; Goldstrohm, A.C.; Trievel, R.C.
The structure of human nocturnin reveals a conserved ribonuclease domain that represses target transcript translation and abundance in cells
Nucleic Acids Res.
46
6257-6270
2018
Homo sapiens (Q9UK39), Homo sapiens
brenda
Estrella, M.A.; Du, J.; Korennykh, A.
Crystal structure of human nocturnin catalytic domain
Sci. Rep.
8
16294
2018
Homo sapiens (Q9UK39), Homo sapiens
brenda
Blanco, A.M.; Gomez-Boronat, M.; Madera, D.; Valenciano, A.I.; Alonso-Gomez, A.L.; Delgado, M.J.
First evidence of nocturnin in fish two isoforms in goldfish differentially regulated by feeding
Am. J. Physiol. Regul. Integr. Comp. Physiol.
314
R304-R312
2018
Carassius auratus (A0A2D1UJM4), Carassius auratus (A0A2D1UJM7), Carassius auratus
brenda
Kawai, M.; Green, C.B.; Horowitz, M.; Ackert-Bicknell, C.; Lecka-Czernik, B.; Rosen, C.J.
Nocturnin a circadian target of Pparg-induced adipogenesis
Ann. N. Y. Acad. Sci.
1192
131-138
2010
Mus musculus (O35710)
brenda
Godwin, A.; Kojima, S.; Green, C.; Wilusz, J.
Kiss your tail goodbye The role of PARN, Nocturnin, and Angel deadenylases in mRNA biology
Biochim. Biophys. Acta
1829
571-579
2013
Mus musculus (O35710)
brenda
Stubblefield, J.J.; Gao, P.; Kilaru, G.; Mukadam, B.; Terrien, J.; Green, C.B.
Temporal control of metabolic amplitude by nocturnin
Cell Rep.
22
1225-1235
2018
Mus musculus (O35710), Mus musculus
brenda
Baggs, J.E.; Green, C.B.
Nocturnin, a deadenylase in Xenopus laevis retina a mechanism for posttranscriptional control of circadian-related mRNA
Curr. Biol.
13
189-198
2003
Xenopus laevis (P79942), Xenopus laevis
brenda
Douris, N.; Kojima, S.; Pan, X.; Lerch-Gaggl, A.F.; Duong, S.Q.; Hussain, M.M.; Green, C.B.
Nocturnin regulates circadian trafficking of dietary lipid in intestinal enterocytes
Curr. Biol.
21
1347-1355
2011
Mus musculus (O35710)
brenda
Groenke, S.; Bickmeyer, I.; Wunderlich, R.; Jaeckle, H.; Kuehnlein, R.P.
Curled encodes the Drosophila homolog of the vertebrate circadian deadenylase Nocturnin
Genetics
183
219-232
2009
Drosophila melanogaster (A8JQX3), Drosophila melanogaster
brenda
Le, P.T.; Bornstein, S.A.; Motyl, K.J.; Tian, L.; Stubblefield, J.J.; Hong, H.K.; Takahashi, J.S.; Green, C.B.; Rosen, C.J.; Guntur, A.R.
A novel mouse model overexpressing Nocturnin results in decreased fat mass in male mice
J. Cell. Physiol.
234
20228-20239
2019
Mus musculus (O35710), Mus musculus
brenda
Nishikawa, S.; Hatanaka, Y.; Tokoro, M.; Shin, S.W.; Shimizu, N.; Nishihara, T.; Kato, R.; Takemoto, A.; Amano, T.; Anzai, M.; Kishigami, S.; Hosoi, Y.; Matsumoto, K.
Functional analysis of nocturnin, a circadian deadenylase, at maternal-to-zygotic transition in mice
J. Reprod. Dev.
59
258-265
2013
Mus musculus (O35710), Mus musculus
brenda
Laothamatas, I.; Gao, P.; Wickramaratne, A.; Quintanilla, C.G.; Dino, A.; Khan, C.A.; Liou, J.; Green, C.B.
Spatiotemporal regulation of NADP(H) phosphatase Nocturnin and its role in oxidative stress response
Proc. Natl. Acad. Sci. USA
117
993-999
2020
Mus musculus (O35710), Mus musculus
brenda
Green, C.B.; Besharse, J.C.
Identification of a novel vertebrate circadian clock-regulated gene encoding the protein nocturnin
Proc. Natl. Acad. Sci. USA
93
14884-14888
1996
Xenopus laevis (P79942), Xenopus laevis
brenda
Hughes, K.L.; Abshire, E.T.; Goldstrohm, A.C.
Regulatory roles of vertebrate Nocturnin insights and remaining mysteries
RNA Biol.
15
1255-1267
2018
Mus musculus (O35710), Homo sapiens (Q9UK39), Homo sapiens
brenda
Stubblefield, J.J.; Terrien, J.; Green, C.B.
Nocturnin at the crossroads of clocks and metabolism
Trends Endocrinol. Metab.
23
326-333
2012
Mus musculus (O35710)
brenda
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