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Information on EC 2.4.2.31 - NAD+-protein-arginine ADP-ribosyltransferase and Organism(s) Mus musculus and UniProt Accession P70352
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2.4.2.31 NAD+-protein-arginine ADP-ribosyltransferaseIUBMB Comments
Protein mono-ADP-ribosylation is a reversible post-translational modification that plays a role in the regulation of cellular activities . Arginine residues in proteins act as acceptors. Free arginine, agmatine [(4-aminobutyl)guanidine], arginine methyl ester and guanidine can also do so. The enzyme from some, but not all, species can also use NADP+ as acceptor (giving rise to Nomega-[(2'-phospho-ADP)-D-ribosyl]-protein-L-arginine as the product), but more slowly [1,5]. The enzyme catalyses the NAD+-dependent activation of EC 4.6.1.1, adenylate cyclase. Some bacterial enterotoxins possess similar enzymic activities. (cf. EC 2.4.2.36 NAD+---diphthamide ADP-ribosyltransferase).
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Word Map
- 2.4.2.31
- angiotensin
- losartan
- arterial
-
renin-angiotensin
- hypertension
- subtype
-
blocker
- cardiovascular
- cardiac
- ventricular
- renin
- hypertrophy
-
ii-induced
-
angiotensin-converting
- agonist
-
hemodynamic
-
vasoconstriction
- valsartan
- bradykinin
-
angii
- candesartan
-
sympathetic
- angiotensinogen
-
antihypertensive
- aldosterone
-
nonpeptide
-
pressor
- aortic
- myocardial
-
systolic
-
normotensive
-
angii-induced
- medicine
- agriculture
- saralasin
- enalapril
-
aceis
-
conscious
- captopril
-
wistar-kyoto
-
baroreflex
-
renin-angiotensin-aldosterone
-
subfornical
-
natriuresis
-
ii-stimulated
-
angiotensin-1-7
-
intrarenal
- telmisartan
- angiotensin-ii
- olmesartan
-
ii-mediated
- irbesartan
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
at1, at2, iota toxin, rt6.1, rt6.2, mono(adp-ribosyl)transferase, arginine-specific adp-ribosyltransferase, nad:arginine adp-ribosyltransferase, arginine-specific mono-adp-ribosyltransferase, xopai, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(adenosine diphosphoribose)transferase, nicotinamide adenine dinucleotide-arginine
-
-
-
-
ADP-ribosyltransferase
ADPRT
-
-
-
-
alloantigen Rt6.1
-
-
-
-
alloantigen Rt6.2
-
-
-
-
arginine ADP-ribosyltransferase 1
arginine specific ADP-ribosyltransferase
-
-
-
-
arginine specific mono-ADP-ribosyltransferase
-
-
-
-
arginine-specific mono-ADP-ribosyltransferase
ART
ART1
AT1
-
-
-
-
AT2
-
-
-
-
Dombrock blood group carrier molecule
-
-
-
-
mono(ADP-ribosyl)transferase
-
-
-
-
mono-ADP-ribosyltransferase
NAD(P)+-arginine ADP-ribosyltransferase
-
-
-
-
NAD+:arginine ADP-ribosyltransferase
-
-
-
-
NAD+:arginine ecto-mono(ADP-ribosyl)transferase
-
-
-
-
NAD+:L-arginine ADP-D-ribosyltransferase
-
-
-
-
NAD-arginine ADP-ribosyltransferase
-
-
-
-
NAD-arginine mono-ADP-ribosyltransferase B
-
-
-
-
NAD-dependent ADPribosyltransferase
-
-
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NAD:arginine ADP-ribosyltransferase B
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-
-
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RT6
-
-
-
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RT6.1
-
-
-
-
RT6.2
-
-
-
-
T-cell surface protein Rt6.1
-
-
-
-
T-cell surface protein Rt6.2
-
-
-
-
ADP-ribosyltransferase
-
-
-
-
arginine-specific mono-ADP-ribosyltransferase
-
-
-
-
ART
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pentosyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
NAD+:protein-L-arginine ADP-D-ribosyltransferase
Protein mono-ADP-ribosylation is a reversible post-translational modification that plays a role in the regulation of cellular activities [4]. Arginine residues in proteins act as acceptors. Free arginine, agmatine [(4-aminobutyl)guanidine], arginine methyl ester and guanidine can also do so. The enzyme from some, but not all, species can also use NADP+ as acceptor (giving rise to Nomega-[(2'-phospho-ADP)-D-ribosyl]-protein-L-arginine as the product), but more slowly [1,5]. The enzyme catalyses the NAD+-dependent activation of EC 4.6.1.1, adenylate cyclase. Some bacterial enterotoxins possess similar enzymic activities. (cf. EC 2.4.2.36 NAD+---diphthamide ADP-ribosyltransferase).
CAS REGISTRY NUMBER
COMMENTARY
81457-93-4
-
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
histone + NAD+
Nomega-[(2'-phospho-ADP)-D-ribosyl]-histone-L-arginine + nicotinamide + H+
-
isozyme ART2 is active with high and low molecular weight histones, membrane-bound and PI-PLC released ART2 preferentially ADP-ribosylate high or low MW histones, respectively
-
-
?
human neutrophil peptide-1 + NAD+
Nomega-(ADP-D-ribosyl)-L-arginine-human neutrophil peptide-1 + nicotinamide
-
human neutrophil peptide-1, HNP-1, from neutrophil cell surface, isozyme ART1 is active on Arg14 and Arg24
-
-
?
NAD+ + human neutrophil peptide-1
nicotinamide + Nomega-(ADP-D-ribosyl)-human neutrophil peptide-1
-
the enzyme ADP-ribosylates human neutrophil peptide-1 on arginine 14 and 24
-
-
?
P2X7 purinoceptor protein + NAD+
Nomega-[(2'-phospho-ADP)-D-ribosyl]-P2X7 purinoceptor protein-L-arginine + nicotinamide
-
isozyme ART2
-
-
?
NAD+ + protein L-arginine
nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine
-
-
-
-
?
NAD+ + protein L-arginine
nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine
-
-
-
?
additional information
?
-
-
in contrast to Yac-1, the Yac-2 enzyme has significant NAD glycohydrolase activity and may preferentially hydrolyze NAD+
-
-
?
additional information
?
-
-
the enzyme might be involved in regulating T cell and immune system activity
-
-
?
additional information
?
-
-
enzyme is involved in posttranslational modification of proteins
-
-
?
additional information
?
-
-
protein mono-ADP-ribosylation is a reversible post-translational modification that plays a role in regulation of cellular activities specific amino acid of the acceptor protein, overview
-
-
?
additional information
?
-
-
ART2, in the absence of histone acceptor, has NAD+ glycohydrolase activity, overview, serum proteins are ADP-ribosylated in a thiol-specific manner, soluble recombinant ART2 lacking the GPI anchor shows a different histone specificity than does native cell-bound ART2, the membrane or solution environment of ART2 plays a pivotal role in determining its substrate specificity
-
-
?
additional information
?
-
-
CD38, a potent ecto-NAD-glycohydrolase, controls ADP-ribosyltransferase-2-catalyzed ADP-ribosylation of T cell surface proteins, overview, the enzyme is a a GPI-anchored, toxin-related ADP-ribosylating ectoenzyme, ART2 can sense and translate the local concentration of ecto-NAD into corresponding levels of ADP-ribosylated cell surface proteins, whereas CD38 controls the level of cell surface protein ADP-ribosylation by limiting the substrate availability for ART2
-
-
?
additional information
?
-
-
substrate specificity, human neutrophil peptide-1 is a poor substrate of isozymes ART2.2 and ART5, overview
-
-
?
additional information
?
-
-
among the three ARTs being expressed at the myotube stage ADP-ribosylation of surface proteins can only be attributed to ART1
-
-
?
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
histone + NAD+
Nomega-[(2'-phospho-ADP)-D-ribosyl]-histone-L-arginine + nicotinamide + H+
-
isozyme ART2 is active with high and low molecular weight histones, membrane-bound and PI-PLC released ART2 preferentially ADP-ribosylate high or low MW histones, respectively
-
-
?
NAD+ + protein L-arginine
nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine
-
-
-
-
?
NAD+ + protein L-arginine
nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine
-
-
-
?
additional information
?
-
-
the enzyme might be involved in regulating T cell and immune system activity
-
-
?
additional information
?
-
-
enzyme is involved in posttranslational modification of proteins
-
-
?
additional information
?
-
-
protein mono-ADP-ribosylation is a reversible post-translational modification that plays a role in regulation of cellular activities specific amino acid of the acceptor protein, overview
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CD38
-
CD38, a potent ecto-NAD-glycohydrolase, controls ADP-ribosyltransferase-2-catalyzed ADP-ribosylation of T cell surface proteins, CD38 decreases ART2-catalyzed ADP-ribosylation in trans by reducing the amount of ART substrate NAD+
-
Triton X-100
-
detergent solubilization of cell membranes specifically abolishes ADP-ribosylation of high MW histones
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
-
activity of RT6.1 increases fivefold, no effect on activity of RT6.2. Cys201 confers thiol sensitivity
DTT
-
dependent on, the DTT cencentration influences the target specificity of ART2
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
ART1, ART3 and ART5 present in myotubes. Absent from mesenchymal progenitor cells and, with the exception of ART3, in myoblasts
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ART1, ART3 and ART5 present in myotubes, absent, with the exception of ART3, from myoblasts
-
splenic lymphocyte subpopulations, ART2 is a T-cell-specific transferase, expression of CD38 and ART2 is inversely correlated on murine lymphocytes
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
ART2 is attached to the cell surface by a glycosylphosphatidylinositol anchor in T-cells
additional information
Yac-2 enzyme is membrane-bound but appears not to be glycosylphosphatidylinositol-anchored
-
Yac-1 enzyme is anchored to membranes by glycosylphosphatidylinositol
-
Yac-2 enzyme is membrane-bound but appears not to be glycosylphosphatidylinositol-anchored
-
anchored to membranes by glycosylphosphatidylinositol
additional information
Yac-1 enzyme may have a signal peptide and may be secreted
-
additional information
-
Yac-1 enzyme may have a signal peptide and may be secreted
-
additional information
-
the enzyme displays a hydrophobic amino terminus consistent with a signal sequence, but lacks a hydrophobic signal sequence at its carboxyl terminus suggesting that the protein is destined for export
-
additional information
-
the membrane or solution environment of ART2 plays a pivotal role in determining its substrate specificity
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
enzyme knockdown increases apoptosis of CT-26 cells transplant tumor. Furthermore, the activity of Akt and Erk cell signal pathways and expression of an apoptosis biomarker, betaIIItubulin, decrease when the enzyme is silenced
malfunction
enzyme silencing inhibits PARP 1 expression by decreasing the expression of nuclear factor-kappaB, inhibiting ras homolog A
malfunction
-
enzyme gene silencing inhibits the growth of the spleen transplanted CT-26 colon carcinoma tumor and its ability to spread to the liver via metastasis
malfunction
-
enzyme silencing induces hypermethylation of the urokinase plasminogen activator gene
physiological function
high level of enzyme expression decreases the apoptosis rate of CT-26 cells induced by cisplatin
physiological function
-
the enzyme can regulate epithelial-mesenchymal transition by regulating the RhoA/ROCK1/AKT/beta-catenin pathway and its downstream factors (snail1, vimentin, N-cadherin and E-cadherin) and therefore plays an important role in the progression of colon carcinoma
physiological function
-
enzyme over-expression causes hypomethylation of the urokinase plasminogen activator gene. The enzyme is related to the expression and activity of DNA methyltransferase 1
physiological function
-
the enzyme plays a potential role in the proliferation and invasion of CT-26 colon carcinoma cells
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). NAR5_MOUSE
309
0
34333
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
depletion of CD38 cells results in enhanced levels of cell surface etheno-ADP-ribosylation on CD38 T cells
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant membrane-bound His-tagged ART2 maltose-binding fusion protein from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, anion echange chromatography, and amylose resin affnity chromataography, the maltose-binding protein is cleaved off
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Yac-1 and Yac-2 enzymes are expressed as glutathione S-transferase fusion proteins in Escherichia coli
expression of Art 1 in 293T cells as a recombinant fusion protein with the Fc portion of human IgG1
-
expression of His-tagged ART2 as maltose-binding fusion protein in Escherichia coli strain BL21(DE3), expression of the membrane-bound ART2 in COS1 cells
-
expression of isozymes ART1, ART5, ART2.2 in Escherichia coli, ART1 expressed endogenously on C2C12 myotubes modifies arginine 14 on HNP-1 with a secondary site on arginine 24
-
mutated amplification products transformed into the Escherichia coli DH 5alpha strain. HEK 293-T cells stably transfected with ART1 or ART3
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of ART1, ART3 and ART5 mRNA in myogenic cell lines during skeletal muscle differentiation in vitro. ART1 expression is restricted to myotube formation. ART5 similar to ART1 mRNA is strongly upregulated during muscle cell differentiation. Upregulation of ART3 mRNA only in C3H10T1/2 cells. Differentiation-dependent upregulation of ART1 mRNA is induced by the binding of myogenin to an E box and of MEF-2 to an A/T-rich element in the proximal promoter region of the ART1 gene
-
mutating the DNA consensus sequence of either the E box or the A/T-rich element results in a nearly complete loss of ART1 promoter inducibility
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
McMahon, K.K.; Piron, K.J.; Ha, V.T.; Fullerton, A.T.
Developmental and biochemical characteristics of the cardiac membrane-bound arginine-specific mono-ADP-ribosyltransferase
Biochem. J.
293
789-793
1993
Canis sp., Coturnix sp., Oryctolagus cuniculus, Mus musculus, Rattus norvegicus, Sus scrofa
-
Kanaitsuka, T.; Bortell, R.; Stevens, L.A.; Moss, J.; Sardinha, D.; Rajan, T.V.; Zipris, D.; Mordes, J.P.; Greiner, D.L.; Rossini, A.A.
Expression in BALB/c and C57BL/6 mice of Rt6-1 and Rt6-2 ADP-ribosyltransferases that differ in enzymic activity
J. Immunol.
159
2741-2749
1997
Mus musculus, Rattus norvegicus
Rigby, M.R.; Bortell, R.; Stevens, L.A.; Moss, J.; Kanaitsuka, T.; Shigeta, H.; Mordes, J.P.; Greiner, D.L.; Rossini, A.A.
Rat RT6.2 and mouse Rt6 locus 1 are NAD+:arginine ADP ribosyltransferases with auto-ADP ribosylation activity
J. Immunol.
156
4259-4265
1996
Mus musculus, Rattus norvegicus
Braren, R.; Glowacki, G.; Nissen, M.; Haag, F.; Koch-Nolte, F.
Molecular characterization and expression of the gene for mouse NAD+:arginine ecto-mono(ADP-ribosyl)transferase, Art1
Biochem. J.
336
561-568
1998
Mus musculus
-
Okazaki, I.J.; Kim, H.J.; Moss, J.
Cloning and characterization of a novel membrane-associated lymphocyte NAD:arginine ADP-ribosyltransferase
J. Biol. Chem.
271
22052-22057
1996
Gallus gallus, Oryctolagus cuniculus, Homo sapiens, Mus musculus (P70352), Mus musculus
Moss, J.; Balducci, E.; Cavanaugh, E.; Kim, H.J.; Konczalik, P.; Lesma, E.A.; Okazaki, I.J.; Park, M.; Shoemaker, M.; Stevens, L.A.; Zolkiewska, A.
Characterization of NAD:arginine ADP-ribosyltransferases
Mol. Cell. Biochem.
193
109-113
1999
Homo sapiens, Mus musculus, Rattus norvegicus
Wang, J.; Nemoto, E.; Dennert, G.
Regulation of cytotoxic T cell functions by a GPI-anchored ecto-ADP-ribosyltransferase
Adv. Exp. Med. Biol.
419
191-201
1997
Mus musculus
Okazaki, I.J.; Kim, H.J.; Moss, J.
Molecular cloning and characterization of lymphocyte and muscle ADP-ribosyltransferases
Adv. Exp. Med. Biol.
419
129-136
1997
Oryctolagus cuniculus, Homo sapiens, Mus musculus
Hara, N.; Badruzzaman, M.; Sugae, T.; Shimoyama, M.; Tsuchiya, M.
Mouse Rt6.1 is a thiol-dependent arginine-specific ADP-ribosyltransferase cysteine 201 confers thiol sensitivity on the enzyme
Eur. J. Biochem.
259
289-294
1999
Mus musculus
Krebs, C.; Adriouch, S.; Braasch, F.; Koestner, W.; Leiter, E.H.; Seman, M.; Lund, F.E.; Oppenheimer, N.; Haag, F.; Koch-Nolte, F.
CD38 controls ADP-ribosyltransferase-2-catalyzed ADP-ribosylation of T cell surface proteins
J. Immunol.
174
3298-3305
2005
Mus musculus
Paone, G.; Stevens, L.A.; Levine, R.L.; Bourgeois, C.; Steagall, W.K.; Gochuico, B.R.; Moss, J.
ADP-ribosyltransferase-specific modification of human neutrophil peptide-1
J. Biol. Chem.
281
17054-17060
2006
Homo sapiens, Mus musculus
Zheng, X.; Morrison, A.R.; Chung, A.S.; Moss, J.; Bortell, R.
Substrate specificity of soluble and membrane-associated ADP-ribosyltransferase ART2.1
J. Cell. Biochem.
98
851-860
2006
Mus musculus
Friedrich, M.; Boehlig, L.; Kirschner, R.D.; Engeland, K.; Hauschildt, S.
Identification of two regulatory binding sites which confer myotube specific expression of the mono-ADP-ribosyltransferase ART1 gene
BMC Mol. Biol.
9
91
2008
Mus musculus
Tang, Y.; Wang, Y.L.; Yang, L.; Xu, J.X.; Xiong, W.; Xiao, M.; Li, M.
Inhibition of arginine ADP-ribosyltransferase 1 reduces the expression of poly(ADP-ribose) polymerase-1 in colon carcinoma
Int. J. Mol. Med.
32
130-136
2013
Mus musculus (Q60935), Mus musculus
Song, G.L.; Jin, C.C.; Zhao, W.; Tang, Y.; Wang, Y.L.; Li, M.; Xiao, M.; Li, X.; Li, Q.S.; Lin, X.; Chen, W.W.; Kuang, J.
Regulation of the RhoA/ROCK/AKT/beta-catenin pathway by arginine-specific ADP-ribosytransferases 1 promotes migration and epithelial-mesenchymal transition in colon carcinoma
Int. J. Oncol.
49
646-656
2016
Mus musculus
Kuang, J.; Wang, Y.L.; Xiao, M.; Tang, Y.; Chen, W.W.; Song, G.L.; Yang, X.; Li, M.
Synergistic effect of arginine-specific ADP-ribosyltransferase 1 and poly(ADP-ribose) polymerase-1 on apoptosis induced by cisplatin in CT26 cells
Oncol. Rep.
31
2335-2343
2014
Mus musculus (Q60935)
Xiao, M.; Tang, Y.; Chen, W.W.; Wang, Y.L.; Yang, L.; Li, X.; Song, G.L.; Kuang, J.
Tubb3 regulation by the Erk and Akt signaling pathways: a mechanism involved in the effect of arginine ADP-ribosyltransferase 1 (Art1) on apoptosis of colon carcinoma CT26 cells
Tumour Biol.
37
2353-2363
2016
Mus musculus (Q60935)
Yang, X.; Li, M.; Tang, Y.; Wang, Y.; Threadgill, M.; Han, J.; Han, X.; Chen, L.; Chen, H.; Hu, W.; Lin, X.
ART1 induces aberrant methylation of uPA promoter A preliminary study
Int. J. Clin. Exp. Pathol.
9
4269-4282
2016
Mus musculus
-
Stevens, L.A.; Moss, J.
Mono-ADP-ribosylation catalyzed by arginine-specific ADP-ribosyltransferases
Methods Mol. Biol.
1813
149-165
2018
Mus musculus, Vibrio cholerae
EXTERNAL LINKS (specific for EC-Number 2.4.2.31)
Transporter Classification Database (TCDB): 1.C.106.4.2
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