NAR2A_RAT
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 03-AUG-2022, entry version 138.
DE RecName: Full=T-cell ecto-ADP-ribosyltransferase 1;
DE EC=2.4.2.31 {ECO:0000250|UniProtKB:P17981};
DE AltName: Full=Alloantigen Rt6.1;
DE AltName: Full=Mono(ADP-ribosyl)transferase 2A;
DE AltName: Full=NAD(+) glycohydrolase;
DE EC=3.2.2.5 {ECO:0000250|UniProtKB:P17981};
DE AltName: Full=T-cell NAD(P)(+)--arginine ADP-ribosyltransferase 1;
DE AltName: Full=T-cell mono(ADP-ribosyl)transferase 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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Lewis A;
RX 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 alloantigen
RT RT6.1.";
RL Nucleic Acids Res. 18:1047-1047(1990).
RN [2]
RP MUTAGENESIS OF GLN-207.
RX 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:
CC Reaction=L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-
CC ribosyl)-L-arginyl-[protein] + nicotinamide; Xref=Rhea:RHEA:19149,
CC Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:15087, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29965, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142554; EC=2.4.2.31;
CC Evidence={ECO:0000250|UniProtKB:P17981};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.5;
CC Evidence={ECO:0000250|UniProtKB:P17981};
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- TISSUE SPECIFICITY: Postthymic T-cells.
CC -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; X52082; CAA36301.1; -; mRNA.
DR PIR; S08464; S08464.
DR AlphaFoldDB; P17982; -.
DR SMR; P17982; -.
DR GlyGen; P17982; 1 site.
DR RGD; 3521; Rt6.
DR InParanoid; P17982; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:RGD.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; ISS:UniProtKB.
DR GO; GO:0061810; F:NAD glycohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0106274; F:NAD+-protein-arginine ADP-ribosyltransferase activity; IMP:RGD.
DR GO; GO:0019677; P:NAD catabolic process; ISS:UniProtKB.
DR GO; GO:0018120; P:peptidyl-arginine ADP-ribosylation; ISS:UniProtKB.
DR InterPro; IPR000768; ART.
DR Pfam; PF01129; ART; 1.
DR PRINTS; PR00970; RIBTRNSFRASE.
DR PROSITE; PS01291; ART; 1.
DR PROSITE; PS51996; TR_MART; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; NAD; NADP;
KW Nucleotidyltransferase; Reference proteome; Signal; Transferase.
FT SIGNAL 1..20
FT CHAIN 21..246
FT /note="T-cell ecto-ADP-ribosyltransferase 1"
FT /id="PRO_0000019319"
FT PROPEP 247..275
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000019320"
FT DOMAIN 61..238
FT /note="TR mART core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT BINDING 98
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT LIPID 246
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..243
FT /evidence="ECO:0000250"
FT DISULFID 141..193
FT /evidence="ECO:0000250"
FT MUTAGEN 207
FT /note="Q->E: Increased ADP-ribosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:8690084"
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
