NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/c;
TISSUE=Spleen;
DOI=10.1016/0161-5890(96)00008-9; PubMed=8811076 [NCBI, ExPASy, EBI, Israel, Japan]
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].
STRAIN=BALB/c, and C57BL/6;
TISSUE=Spleen;
PubMed=9300695 [NCBI, ExPASy, EBI, Israel, Japan]
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).

Comments

FUNCTION: Has both NAD(+) glycohydrolase and ADP-ribosyltransferase activity (to a lesser extent) (By similarity).
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 (By similarity).
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

X87612; CAA60948.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF016463; AAB71683.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF016465; AAB71684.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00136315; -.

NP_064299.2; -.

3D structure databases

HSSP

P20974; 1GXY. [HSSP ENTRY / PDB]

SMR

O35975; 24-249.

ModBase

O35975.

Enzyme and pathway databases

BRENDA

2.4.2.31; 244.

Organism-specific databases

MGI

MGI:107545; Art2b.

Gene expression databases

O35975; -.

O35975; -.

MM_ART2B; -.

ENSMUSG00000030651; Mus musculus.

Ontologies

GO:0031225;	Cellular component: anchored to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0019897;	Cellular component: extrinsic to plasma membrane (traceable author statement from MGI).
GO:0003956;	Molecular function: NAD(P)+-protein-arginine ADP-ribosyltransferase activity (inferred from direct assay from MGI).
GO:0018120;	Biological process: peptidyl-arginine ADP-ribosylation (inferred from direct assay from MGI).
GO:0051789;	Biological process: response to protein stimulus (inferred from mutant phenotype from MGI).
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

ENSMUSG00000030651; Mus musculus. [Contig view]

GeneID

11872; -.

KEGG

mmu:11872; -.

Phylogenomic databases

HOGENOM

O35975; -.

HOVERGEN

O35975; -.

Other

279891; -.

Art2b; Mus musculus.

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

Keywords

Cell membrane; 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`	`By similarity.`
`CHAIN`	`21 260`	`240`	`T-cell ecto-ADP-ribosyltransferase 2.`	`PRO_0000019321`
`PROPEP`	`261 289`	`29`	`Removed in mature form (By similarity).`	`PRO_0000019322`
`ACT_SITE`	`216 216`		`By similarity.`
`BINDING`	`98 98`		`NAD (By similarity).`
`BINDING`	`146 146`		`NAD (By similarity).`
`BINDING`	`164 164`		`NAD (By similarity).`
`BINDING`	`202 202`		`NAD (By similarity).`
`LIPID`	`260 260`		`GPI-anchor amidated serine (By similarity).`
`CARBOHYD`	`79 79`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`249 249`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`41 246`		`By similarity.`
`DISULFID`	`141 193`		`By similarity.`
`CONFLICT`	`4 4`		`N -> K (in Ref. 1; CAA60948).`
`CONFLICT`	`40 40`		`S -> G (in Ref. 1; CAA60948).`
`CONFLICT`	`115 115`		`K -> I (in Ref. 1; CAA60948).`
`CONFLICT`	`231 231`		`E -> Q (in Ref. 1; CAA60948).`

Sequence information

Length: 289 AA [This is the length of the unprocessed precursor]

Molecular weight: 33090 Da [This is the MW of the unprocessed precursor]

CRC64: C224B463EEDA1C3F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPSNNFKFFL TWWLTQQVTG LAVPFMLDMA PNAFDDQYES CVEDMEKKAP QLLQEDFNMN 

        70         80         90        100        110        120 
EELKLEWEKA EINWKEIKNS TSYPAGFHDF HGTALVAYTG NLAIDFNRAV RDFKKSPDNF 

       130        140        150        160        170        180 
HYKAFHYYLT RAVQLLNDQG CSLVYRGTKV MFEYTGKGSV RFGQFSSSSL TKRVALSSNF 

       190        200        210        220        230        240 
FSNHGTLFII RTCLGVNIKE FSSFPREEEV LIPGYEVYHK VTAQNDNGYN EIFLDSPERK 

       250        260        270        280 
KSNFNCFYNG SAQTVNIDFS ISGSRESCVS LFLVVLLGLL VQQLTLAEP

O35975 in FASTA format

View entry in raw text format (no links)
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	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