ID   NAR2B_MOUSE             Reviewed;         289 AA.
AC   O35975; O35702;
DT   13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   24-NOV-2009, entry version 76.
DE   RecName: Full=T-cell ecto-ADP-ribosyltransferase 2;
DE            EC=2.4.2.31;
DE   AltName: Full=T-cell NAD(P)(+)--arginine ADP-ribosyltransferase 2;
DE   AltName: Full=T-cell mono(ADP-ribosyl)transferase 2;
DE   AltName: Full=T-cell differentiation marker Rt6 homolog 2;
DE   Flags: Precursor;
GN   Name=Art2b; Synonyms=Rt6-2, Rt6.2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Spleen;
RX   MEDLINE=96406989; PubMed=8811076; DOI=10.1016/0161-5890(96)00008-9;
RA   Hollmann C., Haag F., Schlott M., Damaske A., Bertuleit H.,
RA   Matthes M., Kuehl M., Thiele H.-G.;
RT   "Molecular characterization of mouse T-cell ecto-ADP-
RT   ribosyltransferase Rt6: cloning of a second functional gene and
RT   identification of the Rt6 gene products.";
RL   Mol. Immunol. 33:807-817(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c, and C57BL/6; TISSUE=Spleen;
RX   MEDLINE=97444163; PubMed=9300695;
RA   Kanaitsuka T., Bortell R., Stevens L.A., Moss J., Sardinha D.,
RA   Rajan T.V., 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
RT   is a natural transferase knockout.";
RL   J. Immunol. 159:2741-2749(1997).
CC   -!- FUNCTION: Has both NAD(+) glycohydrolase and ADP-
CC       ribosyltransferase activity (to a lesser extent) (By similarity).
CC   -!- CATALYTIC ACTIVITY: NAD(+) + protein-L-arginine = nicotinamide +
CC       N(omega)-(ADP-D-ribosyl)-protein-L-arginine.
CC   -!- CATALYTIC ACTIVITY: NADP(+) + protein-L-arginine = nicotinamide +
CC       N(omega)-((2'-phospho-ADP)-D-ribosyl)-protein-L-arginine.
CC   -!- CATALYTIC ACTIVITY: NAD(+) + H(2)O = nicotinamide + ADP-ribose.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase
CC       family.
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DR   EMBL; X87612; CAA60948.1; -; mRNA.
DR   EMBL; AF016463; AAB71683.1; -; mRNA.
DR   EMBL; AF016465; AAB71684.1; -; mRNA.
DR   IPI; IPI00136315; -.
DR   RefSeq; NP_064299.2; -.
DR   UniGene; Mm.57008; -.
DR   SMR; O35975; 24-249.
DR   STRING; O35975; -.
DR   PRIDE; O35975; -.
DR   Ensembl; ENSMUST00000063920; ENSMUSP00000065658; ENSMUSG00000030651; Mus musculus.
DR   GeneID; 11872; -.
DR   KEGG; mmu:11872; -.
DR   UCSC; uc009ioy.1; mouse.
DR   CTD; 11872; -.
DR   MGI; MGI:107545; Art2b.
DR   HOGENOM; O35975; -.
DR   HOVERGEN; O35975; -.
DR   BRENDA; 2.4.2.31; 244.
DR   NextBio; 279891; -.
DR   ArrayExpress; O35975; -.
DR   Bgee; O35975; -.
DR   CleanEx; MM_ART2B; -.
DR   Genevestigator; O35975; -.
DR   GermOnline; ENSMUSG00000030651; Mus musculus.
DR   GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019897; C:extrinsic to plasma membrane; TAS:MGI.
DR   GO; GO:0003956; F:NAD(P)+-protein-arginine ADP-ribosyltransfe...; IDA:MGI.
DR   GO; GO:0018120; P:peptidyl-arginine ADP-ribosylation; IDA:MGI.
DR   GO; GO:0051789; P:response to protein stimulus; IMP:MGI.
DR   InterPro; IPR000768; ART.
DR   PANTHER; PTHR10339; ART; 1.
DR   Pfam; PF01129; ART; 1.
DR   PRINTS; PR00970; RIBTRNSFRASE.
DR   PROSITE; PS01291; ART; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW   GPI-anchor; Lipoprotein; Membrane; NAD; NADP; Signal; Transferase.
FT   SIGNAL        1     20       By similarity.
FT   CHAIN        21    260       T-cell ecto-ADP-ribosyltransferase 2.
FT                                /FTId=PRO_0000019321.
FT   PROPEP      261    289       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000019322.
FT   ACT_SITE    216    216       By similarity.
FT   BINDING      98     98       NAD (By similarity).
FT   BINDING     146    146       NAD (By similarity).
FT   BINDING     164    164       NAD (By similarity).
FT   BINDING     202    202       NAD (By similarity).
FT   LIPID       260    260       GPI-anchor amidated serine (By
FT                                similarity).
FT   CARBOHYD     79     79       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    249    249       N-linked (GlcNAc...) (Potential).
FT   DISULFID     41    246       By similarity.
FT   DISULFID    141    193       By similarity.
FT   CONFLICT      4      4       N -> K (in Ref. 1; CAA60948).
FT   CONFLICT     40     40       S -> G (in Ref. 1; CAA60948).
FT   CONFLICT    115    115       K -> I (in Ref. 1; CAA60948).
FT   CONFLICT    231    231       E -> Q (in Ref. 1; CAA60948).
SQ   SEQUENCE   289 AA;  33090 MW;  C224B463EEDA1C3F CRC64;
     MPSNNFKFFL 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 VQQLTLAEP
//