ID E9Q9Q8_MOUSE Unreviewed; 192 AA. AC E9Q9Q8; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 13-SEP-2023, entry version 67. DE RecName: Full=NAD(P)(+)--arginine ADP-ribosyltransferase {ECO:0000256|RuleBase:RU361228}; DE EC=2.4.2.31 {ECO:0000256|RuleBase:RU361228}; DE AltName: Full=Mono(ADP-ribosyl)transferase {ECO:0000256|RuleBase:RU361228}; DE Flags: Fragment; GN Name=Art3 {ECO:0000313|Ensembl:ENSMUSP00000119113.2, GN ECO:0000313|MGI:MGI:1202729}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000119113.2, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000119113.2, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000119113.2, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] {ECO:0007829|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [3] {ECO:0000313|Ensembl:ENSMUSP00000119113.2} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000119113.2}; RG Ensembl; RL Submitted (MAY-2023) to UniProtKB. 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:0000256|ARBA:ARBA00000858, CC ECO:0000256|RuleBase:RU361228}; CC -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family. CC {ECO:0000256|ARBA:ARBA00009558, ECO:0000256|RuleBase:RU361228}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; E9Q9Q8; -. DR SMR; E9Q9Q8; -. DR MaxQB; E9Q9Q8; -. DR ProteomicsDB; 318608; -. DR Antibodypedia; 2182; 435 antibodies from 29 providers. DR Ensembl; ENSMUST00000124509.2; ENSMUSP00000119113.2; ENSMUSG00000034842.17. DR AGR; MGI:1202729; -. DR MGI; MGI:1202729; Art3. DR VEuPathDB; HostDB:ENSMUSG00000034842; -. DR GeneTree; ENSGT01030000234601; -. DR OMA; ANCVENM; -. DR ChiTaRS; Art3; mouse. DR Proteomes; UP000000589; Chromosome 5. DR Bgee; ENSMUSG00000034842; Expressed in spermatocyte and 164 other tissues. DR ExpressionAtlas; E9Q9Q8; baseline and differential. DR GO; GO:0106274; F:NAD+-protein-arginine ADP-ribosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW. DR InterPro; IPR000768; ART. DR PANTHER; PTHR10339; ADP-RIBOSYLTRANSFERASE; 1. DR PANTHER; PTHR10339:SF4; ECTO-ADP-RIBOSYLTRANSFERASE 3; 1. DR Pfam; PF01129; ART; 1. DR PRINTS; PR00970; RIBTRNSFRASE. DR SUPFAM; SSF56399; ADP-ribosylation; 1. PE 1: Evidence at protein level; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, KW ECO:0000256|RuleBase:RU361228}; NAD {ECO:0000256|RuleBase:RU361228}; KW NADP {ECO:0000256|RuleBase:RU361228}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695}; KW Proteomics identification {ECO:0007829|MaxQB:E9Q9Q8, KW ECO:0007829|ProteomicsDB:E9Q9Q8}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Signal {ECO:0000256|RuleBase:RU361228}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361228}. FT SIGNAL 1..26 FT /evidence="ECO:0000256|RuleBase:RU361228" FT CHAIN 27..192 FT /note="NAD(P)(+)--arginine ADP-ribosyltransferase" FT /evidence="ECO:0000256|RuleBase:RU361228" FT /id="PRO_5005128632" FT NON_TER 192 FT /evidence="ECO:0000313|Ensembl:ENSMUSP00000119113.2" SQ SEQUENCE 192 AA; 22489 MW; 50A4B9C148739954 CRC64; MKMGHFEMVT TLLAAAVLMD IFQVKAEVLD MAENAFDDEY LKCKSRMESK YIPQMKREEW ANDALLRMVW DNAEIQWEAR KAQLFLPRNF KDTYGIALTA YVNEAQEQTS FYHTFSSAVK MAGLSRRRYI YNFPFKAFHF YLVRALQLLR RPCEKSYKTV VYSTSPDISF TFGEQNQARL GNFTLAYSAK PE //