NAR2B_RAT
ID NAR2B_RAT Reviewed; 275 AA.
AC P20974; P97912; Q4FZV8; Q95576; Q9EPH9;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=T-cell ecto-ADP-ribosyltransferase 2;
DE EC=2.4.2.31 {ECO:0000250|UniProtKB:O35975};
DE AltName: Full=ADP-ribosyltransferase C2 and C3 toxin-like 2;
DE Short=ARTC2;
DE AltName: Full=Alloantigen Rt6.2;
DE AltName: Full=Mono(ADP-ribosyl)transferase 2B;
DE AltName: Full=NAD(+) glycohydrolase;
DE EC=3.2.2.5 {ECO:0000250|UniProtKB:O35975};
DE AltName: Full=T-cell NAD(P)(+)--arginine ADP-ribosyltransferase 2;
DE AltName: Full=T-cell mono(ADP-ribosyl)transferase 2;
DE AltName: Full=T-cell surface protein Rt6.2;
DE Flags: Precursor;
GN Name=Art2b; Synonyms=Rt6-b;
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].
RX PubMed=2300588; DOI=10.1073/pnas.87.3.964;
RA Koch F., Haag F., Kashan A., Thiele H.-G.;
RT "Primary structure of rat RT6.2, a nonglycosylated phosphatidylinositol-
RT linked surface marker of postthymic T cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:964-967(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BH;
RX PubMed=11220625; DOI=10.1007/s002510000267;
RA Rothenburg S., Koch-Nolte F., Thiele H.-G., Haag F.;
RT "DNA methylation contributes to tissue- and allele-specific expression of
RT the T-cell differentiation marker RT6.";
RL Immunogenetics 52:231-241(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-201.
RC STRAIN=DA; TISSUE=Spleen;
RX PubMed=8757323;
RA Haag F., Kuhlenbaumer G., Koch-Nolte F., Wingender E., Thiele H.-G.;
RT "Structure of the gene encoding the rat T cell ecto-ADP-ribosyltransferase
RT RT6.";
RL J. Immunol. 157:2022-2030(1996).
RN [5]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=2632369; DOI=10.1016/0165-2478(89)90125-9;
RA Kashan A., Buck F., Haag F., Koch F., Thiele H.-G.;
RT "A single-step purification procedure and partial amino acid sequence
RT analysis of picomole amounts of the rat T cell alloantigen RT6.2.";
RL Immunol. Lett. 23:133-138(1989).
RN [6]
RP CHARACTERIZATION.
RX PubMed=8144525; DOI=10.1016/s0021-9258(17)36897-7;
RA Takada T., Iida K., Moss J.;
RT "Expression of NAD glycohydrolase activity by rat mammary adenocarcinoma
RT cells transformed with rat T cell alloantigen RT6.2.";
RL J. Biol. Chem. 269:9420-9423(1994).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF 21-246, AND DISULFIDE BONDS.
RX PubMed=12270706; DOI=10.1016/s0022-2836(02)00818-5;
RA Mueller-Dieckmann C., Ritter H., Haag F., Koch-Nolte F., Schulz G.E.;
RT "Structure of the ecto-ADP-ribosyl transferase ART2.2 from rat.";
RL J. Mol. Biol. 322:687-696(2002).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 21-246 OF WILD-TYPE AND MUTANTS
RP ILE-189 AND ALA-189 IN COMPLEX WITH NAD(+), ADP-RIBOSYLATION AT ARG-204,
RP AND DISULFIDE BONDS.
RX PubMed=12939142; DOI=10.1021/bi034625w;
RA Ritter H., Koch-Nolte F., Marquez V.E., Schulz G.E.;
RT "Substrate binding and catalysis of ecto-ADP-ribosyltransferase 2.2 from
RT rat.";
RL Biochemistry 42:10155-10162(2003).
CC -!- FUNCTION: Has both NAD(+) glycohydrolase and ADP-ribosyltransferase
CC activity (to a lesser extent).
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:O35975};
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:O35975};
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; M85193; AAA42085.1; -; mRNA.
DR EMBL; AJ297708; CAC20897.1; -; Genomic_DNA.
DR EMBL; BC099070; AAH99070.1; -; mRNA.
DR EMBL; X99123; CAA67566.1; -; mRNA.
DR EMBL; X99122; CAA67565.1; -; mRNA.
DR PIR; A34866; A34866.
DR RefSeq; NP_942030.1; NM_198735.2.
DR RefSeq; XP_017444448.1; XM_017588959.1.
DR PDB; 1GXY; X-ray; 1.71 A; A/B=21-246.
DR PDB; 1GXZ; X-ray; 2.10 A; A/B=21-246.
DR PDB; 1GY0; X-ray; 2.08 A; A=21-246.
DR PDB; 1OG1; X-ray; 2.00 A; A=21-246.
DR PDB; 1OG3; X-ray; 2.60 A; A=21-246.
DR PDB; 1OG4; X-ray; 2.60 A; A=21-246.
DR PDBsum; 1GXY; -.
DR PDBsum; 1GXZ; -.
DR PDBsum; 1GY0; -.
DR PDBsum; 1OG1; -.
DR PDBsum; 1OG3; -.
DR PDBsum; 1OG4; -.
DR AlphaFoldDB; P20974; -.
DR SMR; P20974; -.
DR STRING; 10116.ENSRNOP00000026644; -.
DR PhosphoSitePlus; P20974; -.
DR PaxDb; P20974; -.
DR Ensembl; ENSRNOT00000026644; ENSRNOP00000026644; ENSRNOG00000019687.
DR GeneID; 293152; -.
DR KEGG; rno:293152; -.
DR UCSC; RGD:3521; rat.
DR CTD; 11872; -.
DR RGD; 3521; Art2b.
DR eggNOG; ENOG502QUE9; Eukaryota.
DR GeneTree; ENSGT01030000234601; -.
DR HOGENOM; CLU_059744_0_0_1; -.
DR OrthoDB; 963174at2759; -.
DR PhylomeDB; P20974; -.
DR TreeFam; TF335356; -.
DR EvolutionaryTrace; P20974; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000019687; Expressed in spleen and 12 other tissues.
DR ExpressionAtlas; P20974; baseline and differential.
DR Genevisible; P20974; RN.
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; IBA:GO_Central.
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 3D-structure; ADP-ribosylation; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; GPI-anchor; Hydrolase;
KW Lipoprotein; Membrane; NAD; NADP; Nucleotidyltransferase;
KW Reference proteome; Signal; Transferase.
FT SIGNAL 1..20
FT CHAIN 21..246
FT /note="T-cell ecto-ADP-ribosyltransferase 2"
FT /id="PRO_0000019323"
FT PROPEP 247..275
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000019324"
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 BINDING 146
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 164
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 202
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT MOD_RES 204
FT /note="ADP-ribosylarginine; by autocatalysis"
FT /evidence="ECO:0000305|PubMed:12939142"
FT LIPID 246
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000250"
FT DISULFID 41..243
FT DISULFID 141..193
FT CONFLICT 29
FT /note="T -> K (in Ref. 2; CAC20897)"
FT /evidence="ECO:0000305"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1OG1"
FT HELIX 42..59
FT /evidence="ECO:0007829|PDB:1GXY"
FT HELIX 61..77
FT /evidence="ECO:0007829|PDB:1GXY"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:1OG1"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:1GXY"
FT TURN 99..102
FT /evidence="ECO:0007829|PDB:1OG1"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:1GXY"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:1GXY"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:1GXY"
FT HELIX 123..135
FT /evidence="ECO:0007829|PDB:1GXY"
FT STRAND 142..150
FT /evidence="ECO:0007829|PDB:1GXY"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:1OG1"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:1GXY"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:1OG1"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:1GXY"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:1GXY"
FT STRAND 185..194
FT /evidence="ECO:0007829|PDB:1GXY"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:1GXY"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:1GXY"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:1GXY"
FT STRAND 216..224
FT /evidence="ECO:0007829|PDB:1GXY"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:1GXY"
FT STRAND 228..236
FT /evidence="ECO:0007829|PDB:1GXY"
SQ SEQUENCE 275 AA; 31438 MW; B3361D4E6FF77FC4 CRC64;
MPSNICKFFL TWWLIQQVTG LTGPLMLDTA PNAFDDQYEG CVNKMEEKAP LLLQEDFNMN
AKLKVAWEEA KKRWNNIKPS RSYPKGFNDF HGTALVAYTG SIAVDFNRAV REFKENPGQF
HYKAFHYYLT RALQLLSNGD CHSVYRGTKT RFHYTGAGSV RFGQFTSSSL SKKVAQSQEF
FSDHGTLFII KTCLGVYIKE FSFRPDQEEV LIPGYEVYQK VRTQGYNEIF LDSPKRKKSN
YNCLYSSAGA RESCVSLFLV VLPSLLVQLL CLAEP
