ID   NRT2_CHICK              Reviewed;         312 AA.
AC   P55807;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=NAD(P)(+)--arginine ADP-ribosyltransferase 2;
DE            EC=2.4.2.31;
DE   AltName: Full=Mono(ADP-ribosyl)transferase 2;
DE            Short=AT2;
DE   Flags: Precursor;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=White leghorn; TISSUE=Bone marrow;
RX   PubMed=7961658; DOI=10.1016/s0021-9258(18)47006-8;
RA   Tsuchiya M., Hara N., Yamada K., Osago H., Shimoyama M.;
RT   "Cloning and expression of cDNA for arginine-specific ADP-
RT   ribosyltransferase from chicken bone marrow cells.";
RL   J. Biol. Chem. 269:27451-27457(1994).
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   -!- SUBCELLULAR LOCATION: Secreted, extracellular space. Note=The mature
CC       enzyme is probably secreted from granulocytes into the extracellular
CC       space.
CC   -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; D31865; BAA06665.1; -; mRNA.
DR   PIR; B55461; B55461.
DR   RefSeq; NP_990186.1; NM_204855.1.
DR   AlphaFoldDB; P55807; -.
DR   SMR; P55807; -.
DR   PaxDb; P55807; -.
DR   GeneID; 395661; -.
DR   KEGG; gga:395661; -.
DR   CTD; 395661; -.
DR   VEuPathDB; HostDB:geneid_395661; -.
DR   InParanoid; P55807; -.
DR   OrthoDB; 963174at2759; -.
DR   PhylomeDB; P55807; -.
DR   TreeFam; TF335356; -.
DR   PRO; PR:P55807; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0044194; C:cytolytic granule; IDA:AgBase.
DR   GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR   GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:AgBase.
DR   GO; GO:0106274; F:NAD+-protein-arginine ADP-ribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0018120; P:peptidyl-arginine ADP-ribosylation; IBA:GO_Central.
DR   GO; GO:0046677; P:response to antibiotic; IDA:AgBase.
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   2: Evidence at transcript level;
KW   Disulfide bond; Glycosyltransferase; NAD; NADP; Nucleotidyltransferase;
KW   Reference proteome; Secreted; Signal; Transferase; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..31
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000019338"
FT   CHAIN           32..266
FT                   /note="NAD(P)(+)--arginine ADP-ribosyltransferase 2"
FT                   /id="PRO_0000019339"
FT   PROPEP          267..312
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000019340"
FT   DOMAIN          71..256
FT                   /note="TR mART core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   ACT_SITE        186
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   ACT_SITE        224
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   BINDING         108
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         183
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   DISULFID        51..260
FT                   /evidence="ECO:0000250"
FT   DISULFID        159..208
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   312 AA;  34966 MW;  9E45A9B7A6BC4057 CRC64;
     MELLALRWVL LAGTLLSTSA ASSALQEGDL GSITVIMDMA PNSFDDQYVG CAHVMWANLQ
     KLKCTEFARN YAYAVGWRKA AAEWQKRWGY LAHPMQLRPE QAIALLAYSA ASNLYQQFNA
     ATRQGGCSHQ YYVHFYHFKT LHFLLTQALF ALRASQPRCY YVYRGVRGIR FMTQRGKSVR
     FGQFTSTSLR KDVAVNFGQD TFFVVKTCYG VPIKQFSFYP SEDEVLIPPF EVFEVTNFCT
     GNGRIQIYLR SKGKMSRHNC ELLKPRGGQW GRGHQEVGLG LSPGLALPVL PCSNCSCWGS
     GHRAGDPIPA AV