T-cell ecto-ADP-ribosyltransferase 2 precursor

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O35975 (NAR2B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 92. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
T-cell ecto-ADP-ribosyltransferase 2
EC=2.4.2.31

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

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 › 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. Ref.3
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
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	peptidyl-arginine ADP-ribosylation Inferred from direct assay. Source: MGI
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW 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

By similarity

Chain

21 – 260

240

T-cell ecto-ADP-ribosyltransferase 2

PRO_0000019321

Propeptide

261 – 289

Removed in mature form By similarity

PRO_0000019322

Sites

Active site

216

By similarity

Binding site

NAD By similarity

Binding site

146

NAD By similarity

Binding site

164

NAD By similarity

Binding site

202

NAD By similarity

Amino acid modifications

Lipidation

260

GPI-anchor amidated serine By similarity

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

249

N-linked (GlcNAc...) Potential

Disulfide bond

41 ↔ 246

By similarity

Disulfide bond

141 ↔ 193

By similarity

Experimental info

Sequence conflict

N → K in CAA60948. Ref.1

Sequence conflict

S → G in CAA60948. Ref.1

Sequence conflict

115

K → I in CAA60948. Ref.1

Sequence conflict

231

E → Q in CAA60948. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

O35975 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: C224B463EEDA1C3F
Show »

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

« Hide

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.
[3]	"ADP-ribosylation at R125 gates the P2X7 ion channel by presenting a covalent ligand to its nucleotide binding site." Adriouch S., Bannas P., Schwarz N., Fliegert R., Guse A.H., Seman M., Haag F., Koch-Nolte F. FASEB J. 22:861-869(2008) [PubMed: 17928361] [Abstract] Cited for: FUNCTION.
+	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. NM_019915.2.
UniGene	Mm.57008.
3D structure databases
ProteinModelPortal	O35975.
SMR	O35975. Positions 24-249.
ModBase	Search...
Protein-protein interaction databases
STRING	O35975.
Proteomic databases
PRIDE	O35975.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	11872.
KEGG	mmu:11872.
UCSC	uc009ioy.1. mouse.
Organism-specific databases
CTD	11872.
MGI	MGI:107545. Art2b.
Phylogenomic databases
eggNOG	maNOG23179.
GeneTree	ENSGT00530000062975.
HOGENOM	HBG443999.
HOVERGEN	HBG004464.
InParanoid	O35975.
OrthoDB	EOG4ZCT5K.
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]
KO	K00775.
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
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:	December 14, 2011
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents