P17982 (NAR2A_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
T-cell ecto-ADP-ribosyltransferase 1
EC=2.4.2.31

Alternative name(s):
Alloantigen Rt6.1
Mono(ADP-ribosyl)transferase 2A
T-cell NAD(P)(+)--arginine ADP-ribosyltransferase 1
T-cell mono(ADP-ribosyl)transferase 1
T-cell surface protein Rt6.1

Gene names

Name:	Art2a
Synonyms:	Rt6, Rt6-a

Organism

Rattus norvegicus (Rat)

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 NAD+ glycohydrolase activity and extremely low ADP-ribosyltransferase activity.
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	Disulfide bond GPI-anchor Glycoprotein Lipoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein ADP-ribosylation Inferred from electronic annotation. Source: InterPro
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAD(P)+-protein-arginine ADP-ribosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20
	Chain	21 – 246	226	T-cell ecto-ADP-ribosyltransferase 1		PRO_0000019319
	Propeptide	247 – 275	29	Removed in mature form By similarity		PRO_0000019320
Sites
	Active site	216	1	By similarity
	Binding site	98	1	NAD By similarity
	Binding site	146	1	NAD By similarity
	Binding site	164	1	NAD By similarity
	Binding site	202	1	NAD By similarity
Amino acid modifications
	Lipidation	246	1	GPI-anchor amidated serine By similarity
	Glycosylation	58	1	N-linked (GlcNAc...) Potential
	Disulfide bond	41 ↔ 243		By similarity
	Disulfide bond	141 ↔ 193		By similarity
Experimental info
	Mutagenesis	207	1	Q → E: Increased ADP-ribosyltransferase activity. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P17982 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: D84CBE8A4704031E	FASTA	275	31,388
	10 20 30 40 50 60 MPSNICKFFL TWWLIQQVTG LTGPLMLDTA PNAFDDQYEG CVNKMEEKAP LLLKEDFNKS 70 80 90 100 110 120 EKLKVAWEEA KKRWNNIKPS MSYPKGFNDF HGTALVAYTG SIGVDFNRAV REFKENPGQF 130 140 150 160 170 180 HYKAFHYYLT RALQLLSNGD CHSVYRGTKT RFHYTGAGSV RFGQFTSSSL SKTVAQSPEF 190 200 210 220 230 240 FSDDGTLFII KTCLGVYIKE FSFYPDQEEV LIPGYEVYQK VRTQGYNEIF LDSPKRKKSN 250 260 270 YNCLYSSAGT RESCVSLFLV VLTSLLVQLL CLAEP

References

[1]	"Nucleotide and deduced amino acid sequence of the rat T-cell alloantigen RT6.1." Haag F., Koch F., Thiele H.-G. Nucleic Acids Res. 18:1047-1047(1990) [PubMed: 2129547] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Lewis A.
[2]	"Increase in ADP-ribosyltransferase activity of rat T lymphocyte alloantigen RT6.1 by a single amino acid mutation." Maehama T., Hoshino S., Katada T. FEBS Lett. 388:189-191(1996) [PubMed: 8690084] [Abstract] Cited for: MUTAGENESIS OF GLN-207.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X52082 mRNA. Translation: CAA36301.1.
IPI	IPI00193034.
PIR	S08464.
UniGene	Rn.107075. Rn.214239.
3D structure databases
ProteinModelPortal	P17982.
SMR	P17982. Positions 24-246.
ModBase	Search...
Protein-protein interaction databases
STRING	P17982.
Proteomic databases
PRIDE	P17982.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
RGD	3521. Rt6.
Phylogenomic databases
eggNOG	maNOG23179.
HOVERGEN	HBG004464.
OrthoDB	EOG4ZCT5K.
Gene expression databases
ArrayExpress	P17982.
Genevestigator	P17982.
GermOnline	ENSRNOG00000019687. Rattus norvegicus.
Family and domain databases
InterPro	IPR000768. ART. [Graphical view]
PANTHER	PTHR10339. ART. 1 hit.
Pfam	PF01129. ART. 1 hit. [Graphical view]
PRINTS	PR00970. RIBTRNSFRASE.
PROSITE	PS01291. ART. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NAR2A_RAT

Accession

Primary (citable) accession number: P17982

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	October 19, 2011
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program