[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Lewis A; DOI=10.1093/nar/18.4.1047; PubMed=2129547 [NCBI, ExPASy, EBI, Israel, Japan] Haag F., Koch F., Thiele H.-G.; "Nucleotide and deduced amino acid sequence of the rat T-cell alloantigen RT6.1."; Nucleic Acids Res. 18:1047-1047(1990).
[2]	MUTAGENESIS OF GLN-207. DOI=10.1016/0014-5793(96)00568-6; PubMed=8690084 [NCBI, ExPASy, EBI, Israel, Japan] Maehama T., Hoshino S., Katada T.; "Increase in ADP-ribosyltransferase activity of rat T lymphocyte alloantigen RT6.1 by a single amino acid mutation."; FEBS Lett. 388:189-191(1996).

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.
CATALYTIC ACTIVITY: NADP⁺ + protein-L-arginine = nicotinamide + N(omega)-((2'-phospho-ADP)-D-ribosyl)-protein-L-arginine.
CATALYTIC ACTIVITY: NAD⁺ + H₂O = nicotinamide + ADP-ribose.
SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
TISSUE SPECIFICITY: Postthymic T-cells.
SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X52082; CAA36301.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00193034; -.

S08464; S08464.

3D structure databases

HSSP

P20974; 1GXY. [HSSP ENTRY / PDB]

SMR

P17982; 24-246.

ModBase

P17982.

Enzyme and pathway databases

BRENDA

2.4.2.31; 248.

Organism-specific databases

RGD

3521; Rt6.

Gene expression databases

ArrayExpress

P17982; -.

GermOnline

ENSRNOG00000019687; Rattus norvegicus.

Ontologies

GO:0031225;	Cellular component: anchored to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0003956;	Molecular function: NAD(P)+-protein-arginine ADP-ribosyltransferase activity (inferred from electronic annotation from EC).
GO:0006471;	Biological process: protein amino acid ADP-ribosylation (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000768; ART.
Graphical view of domain structure.

PANTHER

PTHR10339; ART; 1.

Pfam

PF01129; ART; 1.
Pfam graphical view of domain structure.

PRINTS

PR00970; RIBTRNSFRASE.

PROSITE

PS01291; ART; 1.

Genome annotation databases

Ensembl

ENSRNOG00000019687; Rattus norvegicus. [Contig view]

Phylogenomic databases

HOVERGEN

P17982; -.

Other

ProtoNet

P17982.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cell membrane; Disulfide bond; Glycoprotein; Glycosyltransferase; GPI-anchor; Lipoprotein; Membrane; NAD; NADP; Signal; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 20`	`20`
`CHAIN`	`21 246`	`226`	`T-cell ecto-ADP-ribosyltransferase 1.`	`PRO_0000019319`
`PROPEP`	`247 275`	`29`	`Removed in mature form (By similarity).`	`PRO_0000019320`
`ACT_SITE`	`216 216`		`By similarity.`
`BINDING`	`98 98`		`NAD (By similarity).`
`BINDING`	`146 146`		`NAD (By similarity).`
`BINDING`	`164 164`		`NAD (By similarity).`
`BINDING`	`202 202`		`NAD (By similarity).`
`LIPID`	`246 246`		`GPI-anchor amidated serine (By similarity).`
`CARBOHYD`	`58 58`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`41 243`		`By similarity.`
`DISULFID`	`141 193`		`By similarity.`
`MUTAGEN`	`207 207`		`Q->E: Increased ADP-ribosyltransferase activity.`

Sequence information

Length: 275 AA [This is the length of the unprocessed precursor]

Molecular weight: 31388 Da [This is the MW of the unprocessed precursor]

CRC64: D84CBE8A4704031E [This is a checksum on the sequence]

        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

P17982 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools