Reviewed, UniProtKB/Swiss-Prot O35975 (NAR2B_MOUSE)

Names and origin

Protein names

Recommended name:
    T-cell ecto-ADP-ribosyltransferase 2
    EC=2.4.2.31
Alternative name(s):
    T-cell NAD(P)(+)--arginine ADP-ribosyltransferase 2
    T-cell mono(ADP-ribosyl)transferase 2
    T-cell differentiation marker Rt6 homolog 2
    Mono(ADP-ribosyl)transferase 2B

Gene names

Name:	Art2b
Synonyms:	Rt6-2, Rt6.2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	289 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (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. NADP+ + protein-L-arginine = nicotinamide + N(omega)-((2'-phospho-ADP)-D-ribosyl)-protein-L-arginine. NAD+ + H2O = nicotinamide + ADP-ribose.
Subcellular location	Cell membrane; Lipid-anchor › GPI-anchor By similarity.
Sequence similarities	Belongs to the Arg-specific ADP-ribosyltransferase family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Signal
Ligand	NAD NADP
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein
Gene Ontology (GO)
Biological process	peptidyl-arginine ADP-ribosylation Inferred from direct assay. Source: MGI response to protein stimulus Inferred from mutant phenotype. Source: MGI
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to plasma membrane Traceable author statement. Source: MGI
Molecular function	NAD(P)+-protein-arginine ADP-ribosyltransferase activity Inferred from direct assay. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	By similarity
	Chain	21 – 260	240	T-cell ecto-ADP-ribosyltransferase 2		PRO_0000019321
	Propeptide	261 – 289	29	Removed in mature form By similarity		PRO_0000019322
Sites
	Active site	216	1	By similarity
	Binding site	98	1	NAD By similarity
	Binding site	146	1	NAD By similarity
	Binding site	164	1	NAD By similarity
	Binding site	202	1	NAD By similarity
Amino acid modifications
	Lipidation	260	1	GPI-anchor amidated serine By similarity
	Glycosylation	79	1	N-linked (GlcNAc...) Potential
	Glycosylation	249	1	N-linked (GlcNAc...) Potential
	Disulfide bond	41 ↔ 246		By similarity
	Disulfide bond	141 ↔ 193		By similarity
Experimental info
	Sequence conflict	4	1	N → K in CAA60948. Ref.1
	Sequence conflict	40	1	S → G in CAA60948. Ref.1
	Sequence conflict	115	1	K → I in CAA60948. Ref.1
	Sequence conflict	231	1	E → Q in CAA60948. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O35975-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: C224B463EEDA1C3F	FASTA	289	33,090
	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

References

[1]	"Molecular characterization of mouse T-cell ecto-ADP-ribosyltransferase Rt6: cloning of a second functional gene and identification of the Rt6 gene products." Hollmann C., Haag F., Schlott M., Damaske A., Bertuleit H., Matthes M., Kuehl M., Thiele H.-G. Mol. Immunol. 33:807-817(1996) [PubMed: 8811076] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Spleen.
[2]	"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." 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. J. Immunol. 159:2741-2749(1997) [PubMed: 9300695] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c and C57BL/6. Tissue: Spleen.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X87612 mRNA. Translation: CAA60948.1. AF016463 mRNA. Translation: AAB71683.1. AF016465 mRNA. Translation: AAB71684.1.
IPI	IPI00136315.
RefSeq	NP_064299.2.
UniGene	Mm.57008
3D structure databases
SMR	O35975. Positions 24-249.
ModBase	Search...
Protein-protein interaction databases
STRING	O35975.
Proteomic databases
PRIDE	O35975.
Genome annotation databases
Ensembl	ENSMUST00000063920; ENSMUSP00000065658; ENSMUSG00000030651; Mus musculus. [Genome view]
GeneID	11872.
KEGG	mmu:11872.
UCSC	uc009ioy.1. mouse.
Organism-specific databases
CTD	11872.
MGI	MGI:107545. Art2b.
Phylogenomic databases
eggNOG	maNOG23179.
HOGENOM	HBG443999.
HOVERGEN	O35975.
InParanoid	O35975.
Enzyme and pathway databases
BRENDA	2.4.2.31. 244.
Gene expression databases
ArrayExpress	O35975.
Bgee	O35975.
CleanEx	MM_ART2B.
Genevestigator	O35975.
GermOnline	ENSMUSG00000030651. Mus musculus.
Family and domain databases
InterPro	IPR000768. ART. [Graphical view]
PANTHER	PTHR10339. ART. 1 hit.
Pfam	PF01129. ART. 1 hit. [Graphical view]
PRINTS	PR00970. RIBTRNSFRASE.
PROSITE	PS01291. ART. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	279891.
SOURCE	Search...

Entry information

Entry name

NAR2B_MOUSE

Accession

Primary (citable) accession number: O35975
Secondary accession number(s): O35702

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 2002
Last sequence update:	January 1, 1998
Last modified:	February 9, 2010
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)