[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1073/pnas.87.3.964; PubMed=2300588 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1007/s002510000267; PubMed=11220625 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1016/0165-2478(89)90125-9; PubMed=2632369 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1021/bi034625w; PubMed=12939142 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

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.
CATALYTIC ACTIVITY: NADP⁺ + protein-L-arginine = nicotinamide + N(omega)-((2'-phospho-ADP)-D-ribosyl)-protein-L-arginine.
CATALYTIC ACTIVITY: NAD⁺ + H₂O = nicotinamide + ADP-ribose.
SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
TISSUE SPECIFICITY: Postthymic T-cells.
SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M85193; AAA42085.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ297708; CAC20897.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC099070; AAH99070.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X99123; CAA67566.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X99122; CAA67565.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00204526; -.

A34866; A34866.

NP_942030.1; -.

3D structure databases

PDB

1GXY; X-ray; 1.71 A; A/B=21-246.	[ExPASy / RCSB / EBI]
1GXZ; X-ray; 2.10 A; A/B=21-246.	[ExPASy / RCSB / EBI]
1GY0; X-ray; 2.08 A; A=21-246.	[ExPASy / RCSB / EBI]
1OG1; X-ray; 2.00 A; A=21-246.	[ExPASy / RCSB / EBI]
1OG3; X-ray; 2.60 A; A=21-246.	[ExPASy / RCSB / EBI]
1OG4; X-ray; 2.60 A; A=21-246.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1GXY; -.
1GXZ; -.
1GY0; -.
1OG1; -.
1OG3; -.
1OG4; -.

ModBase

P20974.

Enzyme and pathway databases

BRENDA

2.4.2.31; 248.

Organism-specific databases

RGD

735218; Art2b.

Gene expression databases

ArrayExpress

P20974; -.

GermOnline

ENSRNOG00000019687; Rattus norvegicus.

Ontologies

GO:0031225;	Cellular component: anchored to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0003956;	Molecular function: NAD(P)+-protein-arginine ADP-ribosyltransferase activity (inferred from electronic annotation from EC).
GO:0006471;	Biological process: protein amino acid ADP-ribosylation (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000768; ART.
Graphical view of domain structure.

PANTHER

PTHR10339; ART; 1.

Pfam

PF01129; ART; 1.
Pfam graphical view of domain structure.

PRINTS

PR00970; RIBTRNSFRASE.

PROSITE

PS01291; ART; 1.

Genome annotation databases

Ensembl

ENSRNOG00000019687; Rattus norvegicus. [Contig view]

GeneID

293152; -.

KEGG

rno:293152; -.

Phylogenomic databases

HOVERGEN

P20974; -.

Other

635465; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; ADP-ribosylation; Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosyltransferase; GPI-anchor; Lipoprotein; Membrane; NAD; NADP; Signal; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 20`	`20`
`CHAIN`	`21 246`	`226`	`T-cell ecto-ADP-ribosyltransferase 2.`	`PRO_0000019323`
`PROPEP`	`247 275`	`29`	`Removed in mature form (By similarity).`	`PRO_0000019324`
`ACT_SITE`	`216 216`		`By similarity.`
`BINDING`	`98 98`		`NAD.`
`BINDING`	`146 146`		`NAD.`
`BINDING`	`164 164`		`NAD.`
`BINDING`	`202 202`		`NAD.`
`MOD_RES`	`204 204`		`ADP-ribosylarginine; by autocatalysis (Probable).`
`LIPID`	`246 246`		`GPI-anchor amidated serine (By similarity).`
`DISULFID`	`41 243`
`DISULFID`	`141 193`
`CONFLICT`	`29 29`		`T -> K (in Ref. 2; CAC20897).`
`HELIX`	`42 59`	`18`
`HELIX`	`61 77`	`17`
`HELIX`	`89 98`	`10`
`HELIX`	`103 111`	`9`
`TURN`	`112 115`	`4`
`HELIX`	`117 119`	`3`
`HELIX`	`123 135`	`13`
`STRAND`	`142 150`	`9`
`STRAND`	`156 158`	`3`
`HELIX`	`172 175`	`4`
`TURN`	`178 180`	`3`
`STRAND`	`185 194`	`10`
`HELIX`	`199 201`	`3`
`HELIX`	`205 207`	`3`
`STRAND`	`209 212`	`4`
`STRAND`	`216 224`	`9`
`TURN`	`225 227`	`3`
`STRAND`	`228 236`	`9`

Sequence information

Length: 275 AA [This is the length of the unprocessed precursor]

Molecular weight: 31438 Da [This is the MW of the unprocessed precursor]

CRC64: B3361D4E6FF77FC4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPSNICKFFL TWWLIQQVTG LTGPLMLDTA PNAFDDQYEG CVNKMEEKAP LLLQEDFNMN 

        70         80         90        100        110        120 
AKLKVAWEEA KKRWNNIKPS RSYPKGFNDF HGTALVAYTG SIAVDFNRAV REFKENPGQF 

       130        140        150        160        170        180 
HYKAFHYYLT RALQLLSNGD CHSVYRGTKT RFHYTGAGSV RFGQFTSSSL SKKVAQSQEF 

       190        200        210        220        230        240 
FSDHGTLFII KTCLGVYIKE FSFRPDQEEV LIPGYEVYQK VRTQGYNEIF LDSPKRKKSN 

       250        260        270 
YNCLYSSAGA RESCVSLFLV VLPSLLVQLL CLAEP

P20974 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools