NAR2B_MOUSE
ID NAR2B_MOUSE Reviewed; 289 AA.
AC O35975; F8VQK8; O35702;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=T-cell ecto-ADP-ribosyltransferase 2;
DE EC=2.4.2.31 {ECO:0000269|PubMed:11011142, ECO:0000269|PubMed:9300695};
DE AltName: Full=ADP-ribosyltransferase C2 and C3 toxin-like 2;
DE Short=ARTC2;
DE AltName: Full=Mono(ADP-ribosyl)transferase 2B;
DE AltName: Full=NAD(+) glycohydrolase;
DE EC=3.2.2.5 {ECO:0000269|PubMed:11011142};
DE AltName: Full=T-cell NAD(P)(+)--arginine ADP-ribosyltransferase 2;
DE AltName: Full=T-cell differentiation marker Rt6 homolog 2;
DE AltName: Full=T-cell mono(ADP-ribosyl)transferase 2;
DE Flags: Precursor;
GN Name=Art2b; Synonyms=Rt6-2, Rt6.2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=8811076; DOI=10.1016/0161-5890(96)00008-9;
RA Hollmann C., Haag F., Schlott M., Damaske A., Bertuleit H., Matthes M.,
RA Kuehl M., Thiele H.-G.;
RT "Molecular characterization of mouse T-cell ecto-ADP-ribosyltransferase
RT Rt6: cloning of a second functional gene and identification of the Rt6 gene
RT products.";
RL Mol. Immunol. 33:807-817(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Spleen;
RX PubMed=9300695;
RA Kanaitsuka T., Bortell R., Stevens L.A., Moss J., Sardinha D., Rajan T.V.,
RA Zipris D., Mordes J.P., Greiner D.L., Rossini A.A.;
RT "Expression in BALB/c and C57BL/6 mice of Rt6-1 and Rt6-2 ADP-
RT ribosyltransferases that differ in enzymatic activity: C57BL/6 Rt6-1 is a
RT natural transferase knockout.";
RL J. Immunol. 159:2741-2749(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF SER-80 AND PHE-201.
RX PubMed=11011142; DOI=10.1093/oxfordjournals.jbchem.a022792;
RA Hara N., Terashima M., Shimoyama M., Tsuchiya M.;
RT "Mouse T-cell antigen rt6.1 has thiol-dependent NAD glycohydrolase
RT activity.";
RL J. Biochem. 128:601-607(2000).
RN [5]
RP FUNCTION.
RX PubMed=17928361; DOI=10.1096/fj.07-9294com;
RA Adriouch S., Bannas P., Schwarz N., Fliegert R., Guse A.H., Seman M.,
RA Haag F., Koch-Nolte F.;
RT "ADP-ribosylation at R125 gates the P2X7 ion channel by presenting a
RT covalent ligand to its nucleotide binding site.";
RL FASEB J. 22:861-869(2008).
CC -!- FUNCTION: Has both NAD(+) glycohydrolase and ADP-ribosyltransferase
CC activity. {ECO:0000269|PubMed:17928361, ECO:0000269|PubMed:9300695}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-
CC ribosyl)-L-arginyl-[protein] + nicotinamide; Xref=Rhea:RHEA:19149,
CC Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:15087, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29965, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142554; EC=2.4.2.31;
CC Evidence={ECO:0000269|PubMed:11011142, ECO:0000269|PubMed:9300695};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.5;
CC Evidence={ECO:0000269|PubMed:11011142};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in spleen, intestine and thymus.
CC {ECO:0000269|PubMed:9300695}.
CC -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; X87612; CAA60948.1; -; mRNA.
DR EMBL; AF016463; AAB71683.1; -; mRNA.
DR EMBL; AF016465; AAB71684.1; -; mRNA.
DR EMBL; AC129609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS21512.1; -.
DR RefSeq; NP_064299.2; NM_019915.2.
DR RefSeq; XP_006507319.1; XM_006507256.2.
DR AlphaFoldDB; O35975; -.
DR SMR; O35975; -.
DR STRING; 10090.ENSMUSP00000065658; -.
DR GlyGen; O35975; 2 sites.
DR iPTMnet; O35975; -.
DR PhosphoSitePlus; O35975; -.
DR SwissPalm; O35975; -.
DR PaxDb; O35975; -.
DR PRIDE; O35975; -.
DR ProteomicsDB; 287438; -.
DR DNASU; 11872; -.
DR Ensembl; ENSMUST00000063920; ENSMUSP00000065658; ENSMUSG00000030651.
DR GeneID; 11872; -.
DR KEGG; mmu:11872; -.
DR UCSC; uc009ioy.1; mouse.
DR CTD; 11872; -.
DR MGI; MGI:107545; Art2b.
DR VEuPathDB; HostDB:ENSMUSG00000030651; -.
DR eggNOG; ENOG502QUE9; Eukaryota.
DR GeneTree; ENSGT01030000234601; -.
DR HOGENOM; CLU_059744_4_0_1; -.
DR InParanoid; O35975; -.
DR OMA; KYKHCTE; -.
DR OrthoDB; 963174at2759; -.
DR PhylomeDB; O35975; -.
DR TreeFam; TF335356; -.
DR BioGRID-ORCS; 11872; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Art2b; mouse.
DR PRO; PR:O35975; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O35975; protein.
DR Bgee; ENSMUSG00000030651; Expressed in mesenteric lymph node and 35 other tissues.
DR ExpressionAtlas; O35975; baseline and differential.
DR Genevisible; O35975; MM.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0046658; C:anchored component of plasma membrane; ISO:MGI.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; TAS:MGI.
DR GO; GO:0016020; C:membrane; TAS:MGI.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IDA:UniProtKB.
DR GO; GO:0061810; F:NAD glycohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0106274; F:NAD+-protein-arginine ADP-ribosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0019677; P:NAD catabolic process; IDA:UniProtKB.
DR GO; GO:0018120; P:peptidyl-arginine ADP-ribosylation; IDA:UniProtKB.
DR InterPro; IPR000768; ART.
DR Pfam; PF01129; ART; 1.
DR PRINTS; PR00970; RIBTRNSFRASE.
DR PROSITE; PS01291; ART; 1.
DR PROSITE; PS51996; TR_MART; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; NAD; NADP;
KW Nucleotidyltransferase; Reference proteome; Signal; Transferase.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..260
FT /note="T-cell ecto-ADP-ribosyltransferase 2"
FT /id="PRO_0000019321"
FT PROPEP 261..289
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000019322"
FT DOMAIN 61..241
FT /note="TR mART core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT BINDING 98
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT LIPID 260
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..246
FT /evidence="ECO:0000250"
FT DISULFID 141..193
FT /evidence="ECO:0000250"
FT MUTAGEN 80
FT /note="S->C: Changes thiol-independent NADase activity to
FT thiol-dependent; when associated with C-201."
FT /evidence="ECO:0000269|PubMed:11011142"
FT MUTAGEN 201
FT /note="F->C: Changes thiol-independent NADase activity to
FT thiol-dependent; when associated with C-80."
FT /evidence="ECO:0000269|PubMed:11011142"
FT CONFLICT 2
FT /note="T -> P (in Ref. 1; CAA60948 and 2; AAB71683/
FT AAB71684)"
FT /evidence="ECO:0000305"
FT CONFLICT 4
FT /note="K -> N (in Ref. 2; AAB71683/AAB71684)"
FT /evidence="ECO:0000305"
FT CONFLICT 5
FT /note="I -> N (in Ref. 1; CAA60948 and 2; AAB71683/
FT AAB71684)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="S -> G (in Ref. 1; CAA60948)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="K -> I (in Ref. 1; CAA60948)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="E -> Q (in Ref. 1; CAA60948)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="L -> P (in Ref. 1; CAA60948 and 2; AAB71683/
FT AAB71684)"
FT /evidence="ECO:0000305"
SQ 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
