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

 NAR2B_RAT               Reviewed;         275 AA.
P20974; P97912; Q4FZV8; Q95576; Q9EPH9;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
10-MAY-2017, entry version 148.
RecName: Full=T-cell ecto-ADP-ribosyltransferase 2;
EC=2.4.2.31 {ECO:0000250|UniProtKB:O35975};
AltName: Full=ADP-ribosyltransferase C2 and C3 toxin-like 2;
Short=ARTC2;
AltName: Full=Alloantigen Rt6.2;
AltName: Full=Mono(ADP-ribosyl)transferase 2B;
AltName: Full=NAD(+) glycohydrolase;
EC=3.2.2.5 {ECO:0000250|UniProtKB:O35975};
AltName: Full=T-cell NAD(P)(+)--arginine ADP-ribosyltransferase 2;
AltName: Full=T-cell mono(ADP-ribosyl)transferase 2;
AltName: Full=T-cell surface protein Rt6.2;
Flags: Precursor;
Name=Art2b; Synonyms=Rt6-b;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2300588; DOI=10.1073/pnas.87.3.964;
Koch F., Haag F., Kashan A., Thiele H.-G.;
"Primary structure of rat RT6.2, a nonglycosylated
phosphatidylinositol-linked surface marker of postthymic T cells.";
Proc. Natl. Acad. Sci. U.S.A. 87:964-967(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BH;
PubMed=11220625; DOI=10.1007/s002510000267;
Rothenburg S., Koch-Nolte F., Thiele H.-G., Haag F.;
"DNA methylation contributes to tissue- and allele-specific expression
of the T-cell differentiation marker RT6.";
Immunogenetics 52:231-241(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Spleen;
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-201.
STRAIN=DA; TISSUE=Spleen;
PubMed=8757323;
Haag F., Kuhlenbaumer G., Koch-Nolte F., Wingender E., Thiele H.-G.;
"Structure of the gene encoding the rat T cell ecto-ADP-
ribosyltransferase RT6.";
J. Immunol. 157:2022-2030(1996).
[5]
PARTIAL PROTEIN SEQUENCE.
PubMed=2632369; DOI=10.1016/0165-2478(89)90125-9;
Kashan A., Buck F., Haag F., Koch F., Thiele H.-G.;
"A single-step purification procedure and partial amino acid sequence
analysis of picomole amounts of the rat T cell alloantigen RT6.2.";
Immunol. Lett. 23:133-138(1989).
[6]
CHARACTERIZATION.
PubMed=8144525;
Takada T., Iida K., Moss J.;
"Expression of NAD glycohydrolase activity by rat mammary
adenocarcinoma cells transformed with rat T cell alloantigen RT6.2.";
J. Biol. Chem. 269:9420-9423(1994).
[7]
X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF 21-246, AND DISULFIDE BONDS.
PubMed=12270706; DOI=10.1016/S0022-2836(02)00818-5;
Mueller-Dieckmann C., Ritter H., Haag F., Koch-Nolte F., Schulz G.E.;
"Structure of the ecto-ADP-ribosyl transferase ART2.2 from rat.";
J. Mol. Biol. 322:687-696(2002).
[8]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 21-246 OF WILD-TYPE AND
MUTANTS ILE-189 AND ALA-189 IN COMPLEX WITH NAD(+), ADP-RIBOSYLATION
AT ARG-204, AND DISULFIDE BONDS.
PubMed=12939142; DOI=10.1021/bi034625w;
Ritter H., Koch-Nolte F., Marquez V.E., Schulz G.E.;
"Substrate binding and catalysis of ecto-ADP-ribosyltransferase 2.2
from rat.";
Biochemistry 42:10155-10162(2003).
-!- FUNCTION: Has both NAD(+) glycohydrolase and ADP-
ribosyltransferase activity (to a lesser extent).
-!- CATALYTIC ACTIVITY: NAD(+) + protein-L-arginine = nicotinamide +
N(omega)-(ADP-D-ribosyl)-protein-L-arginine.
{ECO:0000250|UniProtKB:O35975}.
-!- CATALYTIC ACTIVITY: NAD(+) + H(2)O = ADP-D-ribose + nicotinamide.
{ECO:0000250|UniProtKB:O35975}.
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
-!- TISSUE SPECIFICITY: Postthymic T-cells.
-!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M85193; AAA42085.1; -; mRNA.
EMBL; AJ297708; CAC20897.1; -; Genomic_DNA.
EMBL; BC099070; AAH99070.1; -; mRNA.
EMBL; X99123; CAA67566.1; -; mRNA.
EMBL; X99122; CAA67565.1; -; mRNA.
PIR; A34866; A34866.
RefSeq; NP_942030.1; NM_198735.2.
RefSeq; XP_017444448.1; XM_017588959.1.
UniGene; Rn.107075; -.
UniGene; Rn.214239; -.
PDB; 1GXY; X-ray; 1.71 A; A/B=21-246.
PDB; 1GXZ; X-ray; 2.10 A; A/B=21-246.
PDB; 1GY0; X-ray; 2.08 A; A=21-246.
PDB; 1OG1; X-ray; 2.00 A; A=21-246.
PDB; 1OG3; X-ray; 2.60 A; A=21-246.
PDB; 1OG4; X-ray; 2.60 A; A=21-246.
PDBsum; 1GXY; -.
PDBsum; 1GXZ; -.
PDBsum; 1GY0; -.
PDBsum; 1OG1; -.
PDBsum; 1OG3; -.
PDBsum; 1OG4; -.
ProteinModelPortal; P20974; -.
SMR; P20974; -.
STRING; 10116.ENSRNOP00000026644; -.
PhosphoSitePlus; P20974; -.
PaxDb; P20974; -.
PRIDE; P20974; -.
Ensembl; ENSRNOT00000026644; ENSRNOP00000026644; ENSRNOG00000019687.
GeneID; 293152; -.
KEGG; rno:293152; -.
UCSC; RGD:3521; rat.
CTD; 11872; -.
RGD; 3521; Art2b.
eggNOG; ENOG410J95D; Eukaryota.
eggNOG; ENOG410ZKT4; LUCA.
GeneTree; ENSGT00530000062975; -.
HOVERGEN; HBG004464; -.
KO; K19980; -.
PhylomeDB; P20974; -.
TreeFam; TF335356; -.
EvolutionaryTrace; P20974; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000019687; -.
ExpressionAtlas; P20974; baseline and differential.
Genevisible; P20974; RN.
GO; GO:0046658; C:anchored component of plasma membrane; IDA:RGD.
GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; ISS:UniProtKB.
GO; GO:0061810; F:NAD glycohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0003956; F:NAD(P)+-protein-arginine ADP-ribosyltransferase activity; IMP:RGD.
GO; GO:0019677; P:NAD catabolic process; ISS:UniProtKB.
GO; GO:0006471; P:protein ADP-ribosylation; IEA:InterPro.
InterPro; IPR000768; ART.
Pfam; PF01129; ART; 1.
PRINTS; PR00970; RIBTRNSFRASE.
PROSITE; PS01291; ART; 1.
1: Evidence at protein level;
3D-structure; ADP-ribosylation; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Glycosyltransferase; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
NAD; NADP; Reference proteome; Signal; Transferase.
SIGNAL 1 20
CHAIN 21 246 T-cell ecto-ADP-ribosyltransferase 2.
/FTId=PRO_0000019323.
PROPEP 247 275 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000019324.
ACT_SITE 216 216 {ECO:0000250}.
BINDING 98 98 NAD.
BINDING 146 146 NAD.
BINDING 164 164 NAD.
BINDING 202 202 NAD.
MOD_RES 204 204 ADP-ribosylarginine; by autocatalysis.
{ECO:0000305|PubMed:12939142}.
LIPID 246 246 GPI-anchor amidated serine.
{ECO:0000250}.
DISULFID 41 243
DISULFID 141 193
CONFLICT 29 29 T -> K (in Ref. 2; CAC20897).
{ECO:0000305}.
STRAND 25 28 {ECO:0000244|PDB:1OG1}.
HELIX 42 59 {ECO:0000244|PDB:1GXY}.
HELIX 61 77 {ECO:0000244|PDB:1GXY}.
HELIX 78 80 {ECO:0000244|PDB:1OG1}.
HELIX 89 98 {ECO:0000244|PDB:1GXY}.
TURN 99 102 {ECO:0000244|PDB:1OG1}.
HELIX 103 111 {ECO:0000244|PDB:1GXY}.
TURN 112 115 {ECO:0000244|PDB:1GXY}.
HELIX 117 119 {ECO:0000244|PDB:1GXY}.
HELIX 123 135 {ECO:0000244|PDB:1GXY}.
STRAND 142 150 {ECO:0000244|PDB:1GXY}.
STRAND 152 154 {ECO:0000244|PDB:1OG1}.
STRAND 156 158 {ECO:0000244|PDB:1GXY}.
STRAND 166 170 {ECO:0000244|PDB:1OG1}.
HELIX 172 175 {ECO:0000244|PDB:1GXY}.
TURN 178 180 {ECO:0000244|PDB:1GXY}.
STRAND 185 194 {ECO:0000244|PDB:1GXY}.
HELIX 199 201 {ECO:0000244|PDB:1GXY}.
HELIX 205 207 {ECO:0000244|PDB:1GXY}.
STRAND 209 212 {ECO:0000244|PDB:1GXY}.
STRAND 216 224 {ECO:0000244|PDB:1GXY}.
TURN 225 227 {ECO:0000244|PDB:1GXY}.
STRAND 228 236 {ECO:0000244|PDB:1GXY}.
SEQUENCE 275 AA; 31438 MW; B3361D4E6FF77FC4 CRC64;
MPSNICKFFL TWWLIQQVTG LTGPLMLDTA PNAFDDQYEG CVNKMEEKAP LLLQEDFNMN
AKLKVAWEEA KKRWNNIKPS RSYPKGFNDF HGTALVAYTG SIAVDFNRAV REFKENPGQF
HYKAFHYYLT RALQLLSNGD CHSVYRGTKT RFHYTGAGSV RFGQFTSSSL SKKVAQSQEF
FSDHGTLFII KTCLGVYIKE FSFRPDQEEV LIPGYEVYQK VRTQGYNEIF LDSPKRKKSN
YNCLYSSAGA RESCVSLFLV VLPSLLVQLL CLAEP


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