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P20974

- NAR2B_RAT

UniProt

P20974 - NAR2B_RAT

Protein

T-cell ecto-ADP-ribosyltransferase 2

Gene

Art2b

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (15 Jul 1998)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

    NAD+ + protein-L-arginine = nicotinamide + N(omega)-(ADP-D-ribosyl)-protein-L-arginine.
    NAD+ + H2O = nicotinamide + ADP-ribose.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei98 – 981NAD
    Binding sitei146 – 1461NAD
    Binding sitei164 – 1641NAD
    Binding sitei202 – 2021NAD
    Active sitei216 – 2161By similarity

    GO - Molecular functioni

    1. hydrolase activity, acting on glycosyl bonds Source: UniProtKB
    2. NAD(P)+-protein-arginine ADP-ribosyltransferase activity Source: RGD

    GO - Biological processi

    1. NAD catabolic process Source: UniProtKB
    2. protein ADP-ribosylation Source: InterPro

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Ligandi

    NAD, NADP

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:Art2b
    Synonyms:Rt6-b
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 1

    Organism-specific databases

    RGDi3521. Art2b.

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of plasma membrane Source: RGD

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Add
    BLAST
    Chaini21 – 246226T-cell ecto-ADP-ribosyltransferase 2PRO_0000019323Add
    BLAST
    Propeptidei247 – 27529Removed in mature formBy similarityPRO_0000019324Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi41 ↔ 243
    Disulfide bondi141 ↔ 193
    Modified residuei204 – 2041ADP-ribosylarginine; by autocatalysis1 Publication
    Lipidationi246 – 2461GPI-anchor amidated serineBy similarity

    Keywords - PTMi

    ADP-ribosylation, Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    PRIDEiP20974.

    Expressioni

    Tissue specificityi

    Postthymic T-cells.

    Gene expression databases

    GenevestigatoriP20974.

    Structurei

    Secondary structure

    1
    275
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi25 – 284
    Helixi42 – 5918
    Helixi61 – 7717
    Helixi78 – 803
    Helixi89 – 9810
    Turni99 – 1024
    Helixi103 – 1119
    Turni112 – 1154
    Helixi117 – 1193
    Helixi123 – 13513
    Beta strandi142 – 1509
    Beta strandi152 – 1543
    Beta strandi156 – 1583
    Beta strandi166 – 1705
    Helixi172 – 1754
    Turni178 – 1803
    Beta strandi185 – 19410
    Helixi199 – 2013
    Helixi205 – 2073
    Beta strandi209 – 2124
    Beta strandi216 – 2249
    Turni225 – 2273
    Beta strandi228 – 2369

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP20974.
    SMRiP20974. Positions 24-246.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20974.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    GeneTreeiENSGT00530000062975.
    HOVERGENiHBG004464.
    KOiK00775.
    OMAiYNEIFLD.
    OrthoDBiEOG7D85WV.
    PhylomeDBiP20974.
    TreeFamiTF335356.

    Family and domain databases

    InterProiIPR000768. ART.
    [Graphical view]
    PANTHERiPTHR10339. PTHR10339. 1 hit.
    PfamiPF01129. ART. 1 hit.
    [Graphical view]
    PRINTSiPR00970. RIBTRNSFRASE.
    PROSITEiPS01291. ART. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P20974-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPSNICKFFL TWWLIQQVTG LTGPLMLDTA PNAFDDQYEG CVNKMEEKAP    50
    LLLQEDFNMN AKLKVAWEEA KKRWNNIKPS RSYPKGFNDF HGTALVAYTG 100
    SIAVDFNRAV REFKENPGQF HYKAFHYYLT RALQLLSNGD CHSVYRGTKT 150
    RFHYTGAGSV RFGQFTSSSL SKKVAQSQEF FSDHGTLFII KTCLGVYIKE 200
    FSFRPDQEEV LIPGYEVYQK VRTQGYNEIF LDSPKRKKSN YNCLYSSAGA 250
    RESCVSLFLV VLPSLLVQLL CLAEP 275
    Length:275
    Mass (Da):31,438
    Last modified:July 15, 1998 - v2
    Checksum:iB3361D4E6FF77FC4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti29 – 291T → K in CAC20897. (PubMed:11220625)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiA34866.
    RefSeqiNP_942030.1. NM_198735.2.
    XP_006229916.1. XM_006229854.1.
    XP_006229917.1. XM_006229855.1.
    UniGeneiRn.107075.
    Rn.214239.

    Genome annotation databases

    EnsembliENSRNOT00000026644; ENSRNOP00000026644; ENSRNOG00000019687.
    GeneIDi293152.
    KEGGirno:293152.
    UCSCiRGD:3521. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi A34866.
    RefSeqi NP_942030.1. NM_198735.2.
    XP_006229916.1. XM_006229854.1.
    XP_006229917.1. XM_006229855.1.
    UniGenei Rn.107075.
    Rn.214239.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali P20974.
    SMRi P20974. Positions 24-246.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P20974.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000026644 ; ENSRNOP00000026644 ; ENSRNOG00000019687 .
    GeneIDi 293152.
    KEGGi rno:293152.
    UCSCi RGD:3521. rat.

    Organism-specific databases

    CTDi 11872.
    RGDi 3521. Art2b.

    Phylogenomic databases

    GeneTreei ENSGT00530000062975.
    HOVERGENi HBG004464.
    KOi K00775.
    OMAi YNEIFLD.
    OrthoDBi EOG7D85WV.
    PhylomeDBi P20974.
    TreeFami TF335356.

    Miscellaneous databases

    EvolutionaryTracei P20974.
    NextBioi 635465.

    Gene expression databases

    Genevestigatori P20974.

    Family and domain databases

    InterProi IPR000768. ART.
    [Graphical view ]
    PANTHERi PTHR10339. PTHR10339. 1 hit.
    Pfami PF01129. ART. 1 hit.
    [Graphical view ]
    PRINTSi PR00970. RIBTRNSFRASE.
    PROSITEi PS01291. ART. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiNAR2B_RAT
    AccessioniPrimary (citable) accession number: P20974
    Secondary accession number(s): P97912
    , Q4FZV8, Q95576, Q9EPH9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 124 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3