ID   E9Q9Q8_MOUSE            Unreviewed;       192 AA.
AC   E9Q9Q8;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JUL-2024, entry version 72.
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|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {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 (APR-2024) 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}.
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DR   AlphaFoldDB; E9Q9Q8; -.
DR   SMR; E9Q9Q8; -.
DR   ProteomicsDB; 318608; -.
DR   Antibodypedia; 2182; 419 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 167 other cell types or 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; IPR050999; ADP-ribosyltransferase_ARG.
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|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
//