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P20974 (NAR2B_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length275 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

NAD+ + H2O = nicotinamide + ADP-ribose.

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor.

Tissue specificity

Postthymic T-cells.

Sequence similarities

Belongs to the Arg-specific ADP-ribosyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020
Chain21 – 246226T-cell ecto-ADP-ribosyltransferase 2
PRO_0000019323
Propeptide247 – 27529Removed in mature form By similarity
PRO_0000019324

Sites

Active site2161 By similarity
Binding site981NAD
Binding site1461NAD
Binding site1641NAD
Binding site2021NAD

Amino acid modifications

Modified residue2041ADP-ribosylarginine; by autocatalysis Probable
Lipidation2461GPI-anchor amidated serine By similarity
Disulfide bond41 ↔ 243 Ref.7 Ref.8
Disulfide bond141 ↔ 193 Ref.7 Ref.8

Experimental info

Sequence conflict291T → K in CAC20897. Ref.2

Secondary structure

......................................... 275
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20974 [UniParc].

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

FASTA27531,438
        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' 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.
PIRA34866.
RefSeqNP_942030.1. NM_198735.2.
XP_006229916.1. XM_006229854.1.
XP_006229917.1. XM_006229855.1.
UniGeneRn.107075.
Rn.214239.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GXYX-ray1.71A/B21-246[»]
1GXZX-ray2.10A/B21-246[»]
1GY0X-ray2.08A21-246[»]
1OG1X-ray2.00A21-246[»]
1OG3X-ray2.60A21-246[»]
1OG4X-ray2.60A21-246[»]
ProteinModelPortalP20974.
SMRP20974. Positions 24-246.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP20974.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000026644; ENSRNOP00000026644; ENSRNOG00000019687.
GeneID293152.
KEGGrno:293152.
UCSCRGD:3521. rat.

Organism-specific databases

CTD11872.
RGD3521. Art2b.

Phylogenomic databases

GeneTreeENSGT00530000062975.
HOVERGENHBG004464.
KOK00775.
OMAYNEIFLD.
OrthoDBEOG7D85WV.
PhylomeDBP20974.
TreeFamTF335356.

Gene expression databases

GenevestigatorP20974.

Family and domain databases

InterProIPR000768. ART.
[Graphical view]
PANTHERPTHR10339. PTHR10339. 1 hit.
PfamPF01129. ART. 1 hit.
[Graphical view]
PRINTSPR00970. RIBTRNSFRASE.
PROSITEPS01291. ART. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP20974.
NextBio635465.

Entry information

Entry nameNAR2B_RAT
AccessionPrimary (citable) accession number: P20974
Secondary accession number(s): P97912 expand/collapse secondary AC list , Q4FZV8, Q95576, Q9EPH9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 15, 1998
Last modified: May 14, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references