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Protein

T-cell ecto-ADP-ribosyltransferase 1

Gene

Art2a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has both ADP-ribosyltransferase activity and thiol-dependent NAD+ glycohydrolase activity.2 Publications

Catalytic activityi

NAD+ + protein-L-arginine = nicotinamide + N(omega)-(ADP-D-ribosyl)-protein-L-arginine.1 Publication
NAD+ + H2O = ADP-D-ribose + nicotinamide.1 Publication

Kineticsi

  1. KM=0.12 mM for NAD for the NADase activity (in the presence of 0.03 mM DTT)1 Publication
  2. KM=0.41 mM for NAD for the NADase activity (in the presence of 2 mM DTT)1 Publication
  3. KM=0.5 mM for NAD for the ADP-ribosyltransferase activity (in the presence of 0.02 mM DTT)1 Publication
  4. KM=0.41 mM for NAD for the ADP-ribosyltransferase activity (in the presence of 2 mM DTT)1 Publication
  5. KM=1.2 mM for L-arginine for the ADP-ribosyltransferase activity (in the presence of 0.02 mM DTT)1 Publication
  6. KM=0.59 mM for L-arginine for the ADP-ribosyltransferase activity (in the presence of 2 mM DTT)1 Publication
  1. Vmax=1.3 nmol/h/µg enzyme toward NAD for the NADase activity (in the presence of 0.03 mM DTT)1 Publication
  2. Vmax=9.7 nmol/h/µg enzyme toward NAD for the NADase activity (in the presence of 2 mM DTT)1 Publication
  3. Vmax=12.3 nmol/h/µg enzyme toward NAD for the ADP-ribosyltransferase activity (in the presence of 0.02 mM DTT)1 Publication
  4. Vmax=159 nmol/h/µg enzyme toward NAD for the ADP-ribosyltransferase activity (in the presence of 2 mM DTT)1 Publication
  5. Vmax=6.8 nmol/h/µg enzyme toward L-arginine for the ADP-ribosyltransferase activity (in the presence of 0.02 mM DTT)1 Publication
  6. Vmax=77 nmol/h/µg enzyme toward L-arginine for the ADP-ribosyltransferase activity (in the presence of 2 mM DTT)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei80Required for the thiol-dependency of NADase activity1
Binding sitei98NADBy similarity1
Binding sitei146NADBy similarity1
Sitei201Required for the thiol-dependency of NADase activity1
Binding sitei202NADBy similarity1
Active sitei216By similarity1

GO - Molecular functioni

  • hydrolase activity, acting on glycosyl bonds Source: UniProtKB
  • NAD(P)+-protein-arginine ADP-ribosyltransferase activity Source: UniProtKB
  • NAD glycohydrolase activity Source: UniProtKB-EC

GO - Biological processi

  • NAD catabolic process Source: UniProtKB
  • peptidyl-arginine ADP-ribosylation Source: UniProtKB

Keywordsi

Molecular functionGlycosyltransferase, Hydrolase, Transferase
LigandNAD, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
T-cell ecto-ADP-ribosyltransferase 1 (EC:2.4.2.311 Publication)
Alternative name(s):
ADP-ribosyltransferase 2a pseudogene
ADP-ribosyltransferase C2 and C3 toxin-like 2
Short name:
ARTC2
Mono(ADP-ribosyl)transferase 2A
NAD(+) glycohydrolase (EC:3.2.2.51 Publication)
T-cell NAD(P)(+)--arginine ADP-ribosyltransferase 1
T-cell differentiation marker Rt6 homolog 1
T-cell mono(ADP-ribosyl)transferase 1
Gene namesi
Name:Art2a
Synonyms:Art2a-ps, Rt6-1, Rt6.1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:107546. Art2a-ps.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

A subset of Rt6+ regulatory T-cells may confer protection to autoimmune disease, and failure to develop this subset may result in enhanced susceptibility for autoimmune disease.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi80C → S: Loss of thiol-dependency of NADase activity. 1 Publication1
Mutagenesisi201C → F: Loss of thiol-dependency of NADase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Add BLAST20
ChainiPRO_000001931721 – 258T-cell ecto-ADP-ribosyltransferase 1Add BLAST238
PropeptideiPRO_0000019318259 – 287Removed in mature formBy similarityAdd BLAST29

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi41 ↔ 246By similarity
Disulfide bondi80 ↔ 201Alternate; present in the absence of reducing agents1 Publication
Disulfide bondi141 ↔ 193By similarity
Glycosylationi171N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi256N-linked (GlcNAc...) asparagineSequence analysis1
Lipidationi258GPI-anchor amidated serineBy similarity1

Post-translational modificationi

It is proposed that in the absence of reducing agents, a disulfide bond is formed between Cys-80 and Cys-201, leading to a conformational change that reduces the catalytic rate of NAD glycohydrolysis.

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PRIDEiP17981.

PTM databases

iPTMnetiP17981.
PhosphoSitePlusiP17981.

Expressioni

Tissue specificityi

Expressed in spleen, intestine and thymus.2 Publications

Developmental stagei

In intestine, the expression levels are highest during neonatal stages and decrease towards adulthood. In spleen, the expression is lowest in neonatals and increases during further developmental stages.1 Publication

Gene expression databases

CleanExiMM_ART2A.

Structurei

3D structure databases

ProteinModelPortaliP17981.
SMRiP17981.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000273888.
HOVERGENiHBG004464.
InParanoidiP17981.
KOiK19980.

Family and domain databases

InterProiView protein in InterPro
IPR000768. ART.
PfamiView protein in Pfam
PF01129. ART. 1 hit.
PRINTSiPR00970. RIBTRNSFRASE.
PROSITEiView protein in PROSITE
PS01291. ART. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P17981-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSNNFKFFL TWWLTQQVTG LAVPFMLDMA PNAFDDQYEG CVEDMEKKAP
60 70 80 90 100
QLLQEDFNMN EELKLEWEKA EIKWKEIKNC MSYPAGFHDF HGTALVAYTG
110 120 130 140 150
NIHRSLNEAT REFKINPGNF HYKAFHYYLT RALQLLSDQG CRSVYRGTNV
160 170 180 190 200
RFRYTGKGSV RFGHFASSSL NRSVATSSPF FNGQGTLFII KTCLGAHIKH
210 220 230 240 250
CSYYTHEEEV LIPGYEVFHK VKTQSVERYI QISLDSPKRK KSNFNCFYSG
260 270 280
STQAANVSSL GSRESCVSLF LVVLLGLLVQ QLTLAEP
Length:287
Mass (Da):32,801
Last modified:August 13, 2002 - v2
Checksum:i606A7F69943E2692
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2 – 4PSN → TSK in AAI20754 (PubMed:15489334).Curated3
Sequence conflicti5N → K in AAB35402 (PubMed:7547715).Curated1
Sequence conflicti11T → A in AAB35402 (PubMed:7547715).Curated1
Sequence conflicti268S → P in CAA37181 (PubMed:2362814).Curated1
Sequence conflicti287P → L in AAI20754 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti22 – 24AVP → TGS in strain: NZW and C57BL/6. 3
Natural varianti26M → T in strain: NZW and C57BL/6. 2 Publications1
Natural varianti40G → S in strain: NZW and C57BL/6. 2 Publications1
Natural varianti161 – 287Missing in strain: C57BL/6. Add BLAST127

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52991 mRNA. Translation: CAA37181.1.
S79913 mRNA. Translation: AAB35402.1.
AF016462 mRNA. Translation: AAB71682.1.
BC120753 mRNA. Translation: AAI20754.1.
PIRiS12738.
RefSeqiNP_031516.1. NM_007490.1.
UniGeneiMm.439746.

Genome annotation databases

GeneIDi11871.
KEGGimmu:11871.

Similar proteinsi

Entry informationi

Entry nameiNAR2A_MOUSE
AccessioniPrimary (citable) accession number: P17981
Secondary accession number(s): O35278, Q0VB79, Q64173
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: August 13, 2002
Last modified: May 10, 2017
This is version 128 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Defined as a polymorphic pseudogene by MGI. In strain C57BL/6, a polymorphism creates a premature stop codon at position 161. PubMed:9300695 shows that the truncated protein is not functional.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families