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T-cell ecto-ADP-ribosyltransferase 1 (EC 2.4.2.31) (ADP-ribosyltransferase 2a pseudogene) (ADP-ribosyltransferase C2 and C3 toxin-like 2) (ARTC2) (Mono(ADP-ribosyl)transferase 2A) (NAD( ) glycohydrolase) (EC 3.2.2.5) (T-cell NAD(P)( )--arginine ADP-ribosyltransferase 1) (T-cell differentiation marker Rt6 homolog 1) (T-cell mono(ADP-ribosyl)transferase 1)

 NAR2A_MOUSE             Reviewed;         287 AA.
P17981; O35278; Q0VB79; Q64173;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
13-AUG-2002, sequence version 2.
10-MAY-2017, entry version 128.
RecName: Full=T-cell ecto-ADP-ribosyltransferase 1;
EC=2.4.2.31 {ECO:0000269|PubMed:11011142};
AltName: Full=ADP-ribosyltransferase 2a pseudogene;
AltName: Full=ADP-ribosyltransferase C2 and C3 toxin-like 2;
Short=ARTC2;
AltName: Full=Mono(ADP-ribosyl)transferase 2A;
AltName: Full=NAD(+) glycohydrolase;
EC=3.2.2.5 {ECO:0000269|PubMed:11011142};
AltName: Full=T-cell NAD(P)(+)--arginine ADP-ribosyltransferase 1;
AltName: Full=T-cell differentiation marker Rt6 homolog 1;
AltName: Full=T-cell mono(ADP-ribosyl)transferase 1;
Flags: Precursor;
Name=Art2a; Synonyms=Art2a-ps, Rt6-1, Rt6.1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Spleen;
PubMed=2362814; DOI=10.1093/nar/18.12.3636;
Koch F., Haag F., Thiele H.-G.;
"Nucleotide and deduced amino acid sequence for the mouse homologue of
the rat T-cell differentiation marker RT6.";
Nucleic Acids Res. 18:3636-3636(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
AND VARIANTS 22-THR--SER-24; THR-26 AND SER-40.
STRAIN=NZW/LacJ; TISSUE=Spleen;
PubMed=7547715; DOI=10.1093/intimm/7.5.883;
Koch-Nolte F., Klein J., Hollmann C., Kuehl M., Haag F., Gaskins H.R.,
Leiter E., Thiele H.-G.;
"Defects in the structure and expression of the genes for the T cell
marker Rt6 in NZW and (NZB x NZW)F1 mice.";
Int. Immunol. 7:883-890(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND VARIANTS
22-THR--SER-24; THR-26; SER-40 AND ARG-161--PRO-287 DEL.
STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Spleen;
PubMed=9300695;
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 enzymatic activity: C57BL/6 Rt6-1
is a natural transferase knockout.";
J. Immunol. 159:2741-2749(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISULFIDE
BOND, AND MUTAGENESIS OF CYS-80 AND CYS-201.
PubMed=11011142; DOI=10.1093/oxfordjournals.jbchem.a022792;
Hara N., Terashima M., Shimoyama M., Tsuchiya M.;
"Mouse T-cell antigen rt6.1 has thiol-dependent NAD glycohydrolase
activity.";
J. Biochem. 128:601-607(2000).
-!- FUNCTION: Has both ADP-ribosyltransferase activity and thiol-
dependent NAD(+) glycohydrolase activity.
{ECO:0000269|PubMed:11011142, ECO:0000269|PubMed:9300695}.
-!- CATALYTIC ACTIVITY: NAD(+) + protein-L-arginine = nicotinamide +
N(omega)-(ADP-D-ribosyl)-protein-L-arginine.
{ECO:0000269|PubMed:11011142}.
-!- CATALYTIC ACTIVITY: NAD(+) + H(2)O = ADP-D-ribose + nicotinamide.
{ECO:0000269|PubMed:11011142}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.12 mM for NAD for the NADase activity (in the presence of
0.03 mM DTT) {ECO:0000269|PubMed:11011142};
KM=0.41 mM for NAD for the NADase activity (in the presence of 2
mM DTT) {ECO:0000269|PubMed:11011142};
KM=0.5 mM for NAD for the ADP-ribosyltransferase activity (in
the presence of 0.02 mM DTT) {ECO:0000269|PubMed:11011142};
KM=0.41 mM for NAD for the ADP-ribosyltransferase activity (in
the presence of 2 mM DTT) {ECO:0000269|PubMed:11011142};
KM=1.2 mM for L-arginine for the ADP-ribosyltransferase activity
(in the presence of 0.02 mM DTT) {ECO:0000269|PubMed:11011142};
KM=0.59 mM for L-arginine for the ADP-ribosyltransferase
activity (in the presence of 2 mM DTT)
{ECO:0000269|PubMed:11011142};
Vmax=1.3 nmol/h/ug enzyme toward NAD for the NADase activity (in
the presence of 0.03 mM DTT) {ECO:0000269|PubMed:11011142};
Vmax=9.7 nmol/h/ug enzyme toward NAD for the NADase activity (in
the presence of 2 mM DTT) {ECO:0000269|PubMed:11011142};
Vmax=12.3 nmol/h/ug enzyme toward NAD for the ADP-
ribosyltransferase activity (in the presence of 0.02 mM DTT)
{ECO:0000269|PubMed:11011142};
Vmax=159 nmol/h/ug enzyme toward NAD for the ADP-
ribosyltransferase activity (in the presence of 2 mM DTT)
{ECO:0000269|PubMed:11011142};
Vmax=6.8 nmol/h/ug enzyme toward L-arginine for the ADP-
ribosyltransferase activity (in the presence of 0.02 mM DTT)
{ECO:0000269|PubMed:11011142};
Vmax=77 nmol/h/ug enzyme toward L-arginine for the ADP-
ribosyltransferase activity (in the presence of 2 mM DTT)
{ECO:0000269|PubMed:11011142};
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
-!- TISSUE SPECIFICITY: Expressed in spleen, intestine and thymus.
{ECO:0000269|PubMed:7547715, ECO:0000269|PubMed:9300695}.
-!- DEVELOPMENTAL STAGE: In intestine, the expression levels are
highest during neonatal stages and decrease towards adulthood. In
spleen, the expression is lowest in neonatals and increases during
further developmental stages. {ECO:0000269|PubMed:7547715}.
-!- PTM: It is proposed that in the absence of reducing agents, a
disulfide bond is formed between Cys-80 and Cys-201, leading to a
conformational change that reduces the catalytic rate of NAD
glycohydrolysis.
-!- DISEASE: Note=A subset of Rt6+ regulatory T-cells may confer
protection to autoimmune disease, and failure to develop this
subset may result in enhanced susceptibility for autoimmune
disease.
-!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase
family. {ECO:0000305}.
-!- CAUTION: Defined as a polymorphic pseudogene by MGI. In strain
C57BL/6, a polymorphism creates a premature stop codon at position
161. PubMed:9300695 shows that the truncated protein is not
functional. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X52991; CAA37181.1; -; mRNA.
EMBL; S79913; AAB35402.1; -; mRNA.
EMBL; AF016462; AAB71682.1; -; mRNA.
EMBL; BC120753; AAI20754.1; -; mRNA.
PIR; S12738; S12738.
RefSeq; NP_031516.1; NM_007490.1.
UniGene; Mm.439746; -.
ProteinModelPortal; P17981; -.
SMR; P17981; -.
iPTMnet; P17981; -.
PhosphoSitePlus; P17981; -.
PRIDE; P17981; -.
GeneID; 11871; -.
KEGG; mmu:11871; -.
CTD; 11871; -.
MGI; MGI:107546; Art2a-ps.
HOGENOM; HOG000273888; -.
HOVERGEN; HBG004464; -.
InParanoid; P17981; -.
KO; K19980; -.
PRO; PR:P17981; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_ART2A; -.
GO; GO:0031362; C:anchored component of external side of plasma membrane; IDA:UniProtKB.
GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IDA:UniProtKB.
GO; GO:0061810; F:NAD glycohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0003956; F:NAD(P)+-protein-arginine ADP-ribosyltransferase activity; IDA:UniProtKB.
GO; GO:0019677; P:NAD catabolic process; IDA:UniProtKB.
GO; GO:0018120; P:peptidyl-arginine ADP-ribosylation; IDA:UniProtKB.
InterPro; IPR000768; ART.
Pfam; PF01129; ART; 1.
PRINTS; PR00970; RIBTRNSFRASE.
PROSITE; PS01291; ART; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
Glycosyltransferase; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
NAD; NADP; Reference proteome; Signal; Transferase.
SIGNAL 1 20
CHAIN 21 258 T-cell ecto-ADP-ribosyltransferase 1.
/FTId=PRO_0000019317.
PROPEP 259 287 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000019318.
ACT_SITE 216 216 {ECO:0000250}.
BINDING 98 98 NAD. {ECO:0000250}.
BINDING 146 146 NAD. {ECO:0000250}.
BINDING 202 202 NAD. {ECO:0000250}.
SITE 80 80 Required for the thiol-dependency of
NADase activity.
SITE 201 201 Required for the thiol-dependency of
NADase activity.
LIPID 258 258 GPI-anchor amidated serine.
{ECO:0000250}.
CARBOHYD 171 171 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 256 256 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 41 246 {ECO:0000250}.
DISULFID 80 201 Alternate; present in the absence of
reducing agents.
{ECO:0000305|PubMed:11011142}.
DISULFID 141 193 {ECO:0000250}.
VARIANT 22 24 AVP -> TGS (in strain: NZW and C57BL/6).
VARIANT 26 26 M -> T (in strain: NZW and C57BL/6).
{ECO:0000269|PubMed:7547715,
ECO:0000269|PubMed:9300695}.
VARIANT 40 40 G -> S (in strain: NZW and C57BL/6).
{ECO:0000269|PubMed:7547715,
ECO:0000269|PubMed:9300695}.
VARIANT 161 287 Missing (in strain: C57BL/6).
MUTAGEN 80 80 C->S: Loss of thiol-dependency of NADase
activity. {ECO:0000269|PubMed:11011142}.
MUTAGEN 201 201 C->F: Loss of thiol-dependency of NADase
activity. {ECO:0000269|PubMed:11011142}.
CONFLICT 2 4 PSN -> TSK (in Ref. 4; AAI20754).
{ECO:0000305}.
CONFLICT 5 5 N -> K (in Ref. 2; AAB35402).
{ECO:0000305}.
CONFLICT 11 11 T -> A (in Ref. 2; AAB35402).
{ECO:0000305}.
CONFLICT 268 268 S -> P (in Ref. 1; CAA37181).
{ECO:0000305}.
CONFLICT 287 287 P -> L (in Ref. 4; AAI20754).
{ECO:0000305}.
SEQUENCE 287 AA; 32801 MW; 606A7F69943E2692 CRC64;
MPSNNFKFFL TWWLTQQVTG LAVPFMLDMA PNAFDDQYEG CVEDMEKKAP QLLQEDFNMN
EELKLEWEKA EIKWKEIKNC MSYPAGFHDF HGTALVAYTG NIHRSLNEAT REFKINPGNF
HYKAFHYYLT RALQLLSDQG CRSVYRGTNV RFRYTGKGSV RFGHFASSSL NRSVATSSPF
FNGQGTLFII KTCLGAHIKH CSYYTHEEEV LIPGYEVFHK VKTQSVERYI QISLDSPKRK
KSNFNCFYSG STQAANVSSL GSRESCVSLF LVVLLGLLVQ QLTLAEP


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