T-cell ecto-ADP-ribosyltransferase 2 precursor

Contribute

Send feedback

Read comments (?) or add your own

P20974 (NAR2B_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 113. History...

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

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

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):
ADP-ribosyltransferase C2 and C3 toxin-like 2
Short name=ARTC2
Alloantigen Rt6.2
Mono(ADP-ribosyl)transferase 2B
T-cell NAD(P)(+)--arginine ADP-ribosyltransferase 2
T-cell mono(ADP-ribosyl)transferase 2
T-cell surface protein Rt6.2

Gene names

Name:	Art2b
Synonyms:	Rt6-b

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	275 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (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. 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.
Tissue specificity	Postthymic T-cells.
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	ADP-ribosylation Disulfide bond GPI-anchor Glycoprotein Lipoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	NAD catabolic process Inferred from sequence or structural similarity. Source: UniProtKB peptidyl-arginine ADP-ribosylation Inferred from electronic annotation. Source: Compara
Cellular_component	anchored to external side of plasma membrane Inferred from electronic annotation. Source: Compara anchored to plasma membrane Inferred from direct assay PubMed 12649291. Source: RGD
Molecular_function	NAD(P)+-protein-arginine ADP-ribosyltransferase activity Inferred from mutant phenotype PubMed 12649291. Source: RGD hydrolase activity, acting on glycosyl bonds Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

Chain

21 – 246

226

T-cell ecto-ADP-ribosyltransferase 2

PRO_0000019323

Propeptide

247 – 275

Removed in mature form By similarity

PRO_0000019324

Sites

Active site

216

By similarity

Binding site

NAD

Binding site

146

NAD

Binding site

164

NAD

Binding site

202

NAD

Amino acid modifications

Modified residue

204

ADP-ribosylarginine; by autocatalysis Probable

Lipidation

246

GPI-anchor amidated serine By similarity

Disulfide bond

Disulfide bond

Experimental info

Sequence conflict

T → K in CAC20897. Ref.2

Secondary structure

275

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P20974 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: B3361D4E6FF77FC4
Show »

FASTA

275

31,438

        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

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of rat RT6.2, a nonglycosylated phosphatidylinositol-linked surface marker of postthymic T cells." Koch F., Haag F., Kashan A., Thiele H.-G. Proc. Natl. Acad. Sci. U.S.A. 87:964-967(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"DNA methylation contributes to tissue- and allele-specific expression of the T-cell differentiation marker RT6." Rothenburg S., Koch-Nolte F., Thiele H.-G., Haag F. Immunogenetics 52:231-241(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BH.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Spleen.
[4]	"Structure of the gene encoding the rat T cell ecto-ADP-ribosyltransferase RT6." Haag F., Kuhlenbaumer G., Koch-Nolte F., Wingender E., Thiele H.-G. J. Immunol. 157:2022-2030(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-201. Strain: DA. Tissue: Spleen.
[5]	"A single-step purification procedure and partial amino acid sequence analysis of picomole amounts of the rat T cell alloantigen RT6.2." Kashan A., Buck F., Haag F., Koch F., Thiele H.-G. Immunol. Lett. 23:133-138(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE.
[6]	"Expression of NAD glycohydrolase activity by rat mammary adenocarcinoma cells transformed with rat T cell alloantigen RT6.2." Takada T., Iida K., Moss J. J. Biol. Chem. 269:9420-9423(1994) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[7]	"Structure of the ecto-ADP-ribosyl transferase ART2.2 from rat." Mueller-Dieckmann C., Ritter H., Haag F., Koch-Nolte F., Schulz G.E. J. Mol. Biol. 322:687-696(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF 21-246, DISULFIDE BONDS.
[8]	"Substrate binding and catalysis of ecto-ADP-ribosyltransferase 2.2 from rat." Ritter H., Koch-Nolte F., Marquez V.E., Schulz G.E. Biochemistry 42:10155-10162(2003) [PubMed] [Europe PMC] [Abstract] Cited for: 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, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M85193 mRNA. Translation: AAA42085.1.
AJ297708 Genomic DNA. Translation: CAC20897.1.
BC099070 mRNA. Translation: AAH99070.1.
X99123 mRNA. Translation: CAA67566.1.
X99122 mRNA. Translation: CAA67565.1.

IPI

IPI00204526.

PIR

A34866.

RefSeq

NP_942030.1. NM_198735.2.

UniGene

Rn.107075.
Rn.214239.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GXY	X-ray	1.71	A/B	21-246	[»]
1GXZ	X-ray	2.10	A/B	21-246	[»]
1GY0	X-ray	2.08	A	21-246	[»]
1OG1	X-ray	2.00	A	21-246	[»]
1OG3	X-ray	2.60	A	21-246	[»]
1OG4	X-ray	2.60	A	21-246	[»]

ProteinModelPortal

P20974.

SMR

P20974. Positions 24-246.

ModBase

Search...

Proteomic databases

PRIDE

P20974.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000026644; ENSRNOP00000026644; ENSRNOG00000019687.

GeneID

293152.

KEGG

rno:293152.

UCSC

RGD:3521. rat.

Organism-specific databases

CTD

11872.

RGD

3521. Art2b.

Phylogenomic databases

GeneTree

ENSGT00530000062975.

HOVERGEN

HBG004464.

K00775.

Gene expression databases

ArrayExpress

P20974.

Genevestigator

P20974.

GermOnline

ENSRNOG00000019687. Rattus norvegicus.

Family and domain databases

InterPro

IPR000768. ART.
[Graphical view]

PANTHER

PTHR10339. PTHR10339. 1 hit.

Pfam

PF01129. ART. 1 hit.
[Graphical view]

PRINTS

PR00970. RIBTRNSFRASE.

PROSITE

PS01291. ART. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P20974.

NextBio

635465.

Entry information

Entry name

NAR2B_RAT

Accession

Primary (citable) accession number: P20974
Secondary accession number(s): P97912

Q9EPH9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	July 15, 1998
Last modified:	May 1, 2013
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure 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