ID NAR2A_RAT Reviewed; 275 AA. AC P17982; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 13-OCT-2009, entry version 85. DE RecName: Full=T-cell ecto-ADP-ribosyltransferase 1; DE EC=2.4.2.31; DE AltName: Full=T-cell NAD(P)(+)--arginine ADP-ribosyltransferase 1; DE AltName: Full=T-cell mono(ADP-ribosyl)transferase 1; DE AltName: Full=Alloantigen Rt6.1; DE AltName: Full=T-cell surface protein Rt6.1; DE Flags: Precursor; GN Name=Art2a; Synonyms=Rt6, Rt6-a; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Lewis A; RX MEDLINE=90192088; PubMed=2129547; DOI=10.1093/nar/18.4.1047; RA Haag F., Koch F., Thiele H.-G.; RT "Nucleotide and deduced amino acid sequence of the rat T-cell RT alloantigen RT6.1."; RL Nucleic Acids Res. 18:1047-1047(1990). RN [2] RP MUTAGENESIS OF GLN-207. RX MEDLINE=96275529; PubMed=8690084; DOI=10.1016/0014-5793(96)00568-6; RA Maehama T., Hoshino S., Katada T.; RT "Increase in ADP-ribosyltransferase activity of rat T lymphocyte RT alloantigen RT6.1 by a single amino acid mutation."; RL FEBS Lett. 388:189-191(1996). CC -!- FUNCTION: Has NAD+ glycohydrolase activity and extremely low ADP- CC ribosyltransferase activity. CC -!- CATALYTIC ACTIVITY: NAD(+) + protein-L-arginine = nicotinamide + CC N(omega)-(ADP-D-ribosyl)-protein-L-arginine. CC -!- CATALYTIC ACTIVITY: NADP(+) + protein-L-arginine = nicotinamide + CC N(omega)-((2'-phospho-ADP)-D-ribosyl)-protein-L-arginine. CC -!- CATALYTIC ACTIVITY: NAD(+) + H(2)O = nicotinamide + ADP-ribose. CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. CC -!- TISSUE SPECIFICITY: Postthymic T-cells. CC -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X52082; CAA36301.1; -; mRNA. DR IPI; IPI00193034; -. DR PIR; S08464; S08464. DR UniGene; Rn.107075; -. DR UniGene; Rn.214239; -. DR HSSP; P20974; 1GXY. DR SMR; P17982; 24-246. DR STRING; P17982; -. DR Ensembl; ENSRNOT00000026644; ENSRNOP00000026644; ENSRNOG00000019687; Rattus norvegicus. DR Ensembl; ENSRNOT00000055260; ENSRNOP00000052135; ENSRNOG00000019687; Rattus norvegicus. DR RGD; 3521; Rt6. DR HOVERGEN; P17982; -. DR BRENDA; 2.4.2.31; 248. DR ArrayExpress; P17982; -. DR Genevestigator; P17982; -. DR GermOnline; ENSRNOG00000019687; Rattus norvegicus. DR GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0003956; F:NAD(P)+-protein-arginine ADP-ribosyltransfe...; IEA:EC. DR GO; GO:0006471; P:protein amino acid ADP-ribosylation; IEA:InterPro. DR InterPro; IPR000768; ART. DR PANTHER; PTHR10339; ART; 1. DR Pfam; PF01129; ART; 1. DR PRINTS; PR00970; RIBTRNSFRASE. DR PROSITE; PS01291; ART; 1. PE 1: Evidence at protein level; KW Cell membrane; Disulfide bond; Glycoprotein; Glycosyltransferase; KW GPI-anchor; Lipoprotein; Membrane; NAD; NADP; Signal; Transferase. FT SIGNAL 1 20 FT CHAIN 21 246 T-cell ecto-ADP-ribosyltransferase 1. FT /FTId=PRO_0000019319. FT PROPEP 247 275 Removed in mature form (By similarity). FT /FTId=PRO_0000019320. FT ACT_SITE 216 216 By similarity. FT BINDING 98 98 NAD (By similarity). FT BINDING 146 146 NAD (By similarity). FT BINDING 164 164 NAD (By similarity). FT BINDING 202 202 NAD (By similarity). FT LIPID 246 246 GPI-anchor amidated serine (By FT similarity). FT CARBOHYD 58 58 N-linked (GlcNAc...) (Potential). FT DISULFID 41 243 By similarity. FT DISULFID 141 193 By similarity. FT MUTAGEN 207 207 Q->E: Increased ADP-ribosyltransferase FT activity. SQ SEQUENCE 275 AA; 31388 MW; D84CBE8A4704031E CRC64; MPSNICKFFL TWWLIQQVTG LTGPLMLDTA PNAFDDQYEG CVNKMEEKAP LLLKEDFNKS EKLKVAWEEA KKRWNNIKPS MSYPKGFNDF HGTALVAYTG SIGVDFNRAV REFKENPGQF HYKAFHYYLT RALQLLSNGD CHSVYRGTKT RFHYTGAGSV RFGQFTSSSL SKTVAQSPEF FSDDGTLFII KTCLGVYIKE FSFYPDQEEV LIPGYEVYQK VRTQGYNEIF LDSPKRKKSN YNCLYSSAGT RESCVSLFLV VLTSLLVQLL CLAEP //