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

 NAR2B_MOUSE             Reviewed;         289 AA.
O35975; F8VQK8; O35702;
13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
13-JUN-2012, sequence version 2.
07-JUN-2017, entry version 131.
RecName: Full=T-cell ecto-ADP-ribosyltransferase 2;
EC=2.4.2.31 {ECO:0000269|PubMed:11011142, ECO:0000269|PubMed:9300695};
AltName: Full=ADP-ribosyltransferase C2 and C3 toxin-like 2;
Short=ARTC2;
AltName: Full=Mono(ADP-ribosyl)transferase 2B;
AltName: Full=NAD(+) glycohydrolase;
EC=3.2.2.5 {ECO:0000269|PubMed:11011142};
AltName: Full=T-cell NAD(P)(+)--arginine ADP-ribosyltransferase 2;
AltName: Full=T-cell differentiation marker Rt6 homolog 2;
AltName: Full=T-cell mono(ADP-ribosyl)transferase 2;
Flags: Precursor;
Name=Art2b; Synonyms=Rt6-2, Rt6.2;
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=8811076; DOI=10.1016/0161-5890(96)00008-9;
Hollmann C., Haag F., Schlott M., Damaske A., Bertuleit H.,
Matthes M., Kuehl M., Thiele H.-G.;
"Molecular characterization of mouse T-cell ecto-ADP-
ribosyltransferase Rt6: cloning of a second functional gene and
identification of the Rt6 gene products.";
Mol. Immunol. 33:807-817(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
SPECIFICITY.
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
CATALYTIC ACTIVITY, AND MUTAGENESIS OF SER-80 AND PHE-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).
[5]
FUNCTION.
PubMed=17928361; DOI=10.1096/fj.07-9294com;
Adriouch S., Bannas P., Schwarz N., Fliegert R., Guse A.H., Seman M.,
Haag F., Koch-Nolte F.;
"ADP-ribosylation at R125 gates the P2X7 ion channel by presenting a
covalent ligand to its nucleotide binding site.";
FASEB J. 22:861-869(2008).
-!- FUNCTION: Has both NAD(+) glycohydrolase and ADP-
ribosyltransferase activity. {ECO:0000269|PubMed:17928361,
ECO:0000269|PubMed:9300695}.
-!- CATALYTIC ACTIVITY: NAD(+) + protein-L-arginine = nicotinamide +
N(omega)-(ADP-D-ribosyl)-protein-L-arginine.
{ECO:0000269|PubMed:11011142, ECO:0000269|PubMed:9300695}.
-!- CATALYTIC ACTIVITY: NAD(+) + H(2)O = ADP-D-ribose + nicotinamide.
{ECO:0000269|PubMed:11011142}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor,
GPI-anchor {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in spleen, intestine and thymus.
{ECO:0000269|PubMed:9300695}.
-!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X87612; CAA60948.1; -; mRNA.
EMBL; AF016463; AAB71683.1; -; mRNA.
EMBL; AF016465; AAB71684.1; -; mRNA.
EMBL; AC129609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS21512.1; -.
RefSeq; NP_064299.2; NM_019915.2.
RefSeq; XP_006507319.1; XM_006507256.2.
UniGene; Mm.57008; -.
ProteinModelPortal; O35975; -.
SMR; O35975; -.
STRING; 10090.ENSMUSP00000065658; -.
iPTMnet; O35975; -.
PhosphoSitePlus; O35975; -.
SwissPalm; O35975; -.
PaxDb; O35975; -.
PRIDE; O35975; -.
DNASU; 11872; -.
Ensembl; ENSMUST00000063920; ENSMUSP00000065658; ENSMUSG00000030651.
GeneID; 11872; -.
KEGG; mmu:11872; -.
UCSC; uc009ioy.1; mouse.
CTD; 11872; -.
MGI; MGI:107545; Art2b.
eggNOG; ENOG410J95D; Eukaryota.
eggNOG; ENOG410ZKT4; LUCA.
GeneTree; ENSGT00530000062975; -.
HOGENOM; HOG000273888; -.
HOVERGEN; HBG004464; -.
InParanoid; O35975; -.
KO; K19980; -.
OMA; CFGANIS; -.
OrthoDB; EOG091G0BSN; -.
TreeFam; TF335356; -.
PRO; PR:O35975; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000030651; -.
CleanEx; MM_ART2B; -.
ExpressionAtlas; O35975; baseline and differential.
Genevisible; O35975; MM.
GO; GO:0031362; C:anchored component of external side of plasma membrane; IDA:UniProtKB.
GO; GO:0019897; C:extrinsic component of plasma membrane; TAS:MGI.
GO; GO:0016020; C:membrane; TAS:MGI.
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 {ECO:0000250}.
CHAIN 21 260 T-cell ecto-ADP-ribosyltransferase 2.
/FTId=PRO_0000019321.
PROPEP 261 289 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000019322.
ACT_SITE 216 216 {ECO:0000250}.
BINDING 98 98 NAD. {ECO:0000250}.
BINDING 146 146 NAD. {ECO:0000250}.
BINDING 164 164 NAD. {ECO:0000250}.
BINDING 202 202 NAD. {ECO:0000250}.
LIPID 260 260 GPI-anchor amidated serine.
{ECO:0000250}.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 249 249 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 41 246 {ECO:0000250}.
DISULFID 141 193 {ECO:0000250}.
MUTAGEN 80 80 S->C: Changes thiol-independent NADase
activity to thiol-dependent; when
associated with C-201.
{ECO:0000269|PubMed:11011142}.
MUTAGEN 201 201 F->C: Changes thiol-independent NADase
activity to thiol-dependent; when
associated with C-80.
{ECO:0000269|PubMed:11011142}.
CONFLICT 2 2 T -> P (in Ref. 1; CAA60948 and 2;
AAB71683/AAB71684). {ECO:0000305}.
CONFLICT 4 4 K -> N (in Ref. 2; AAB71683/AAB71684).
{ECO:0000305}.
CONFLICT 5 5 I -> N (in Ref. 1; CAA60948 and 2;
AAB71683/AAB71684). {ECO:0000305}.
CONFLICT 40 40 S -> G (in Ref. 1; CAA60948).
{ECO:0000305}.
CONFLICT 115 115 K -> I (in Ref. 1; CAA60948).
{ECO:0000305}.
CONFLICT 231 231 E -> Q (in Ref. 1; CAA60948).
{ECO:0000305}.
CONFLICT 289 289 L -> P (in Ref. 1; CAA60948 and 2;
AAB71683/AAB71684). {ECO:0000305}.
SEQUENCE 289 AA; 33124 MW; BA3748FA37636051 CRC64;
MTSKIFKFFL TWWLTQQVTG LAVPFMLDMA PNAFDDQYES CVEDMEKKAP QLLQEDFNMN
EELKLEWEKA EINWKEIKNS TSYPAGFHDF HGTALVAYTG NLAIDFNRAV RDFKKSPDNF
HYKAFHYYLT RAVQLLNDQG CSLVYRGTKV MFEYTGKGSV RFGQFSSSSL TKRVALSSNF
FSNHGTLFII RTCLGVNIKE FSSFPREEEV LIPGYEVYHK VTAQNDNGYN EIFLDSPERK
KSNFNCFYNG SAQTVNIDFS ISGSRESCVS LFLVVLLGLL VQQLTLAEL


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