NRT1_CHICK
ID NRT1_CHICK Reviewed; 312 AA.
AC P55806;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=NAD(P)(+)--arginine ADP-ribosyltransferase 1;
DE EC=2.4.2.31;
DE AltName: Full=Mono(ADP-ribosyl)transferase 1;
DE Short=AT1;
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], AND PARTIAL PROTEIN SEQUENCE.
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; D31864; BAA06664.1; -; mRNA.
DR PIR; A55461; A55461.
DR RefSeq; NP_990444.1; NM_205113.1.
DR AlphaFoldDB; P55806; -.
DR SMR; P55806; -.
DR GeneID; 396008; -.
DR VEuPathDB; HostDB:geneid_395661; -.
DR PhylomeDB; P55806; -.
DR PRO; PR:P55806; -.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycosyltransferase; NAD; NADP;
KW Nucleotidyltransferase; Reference proteome; Secreted; Signal; Transferase;
KW Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..31
FT /id="PRO_0000019335"
FT CHAIN 32..266
FT /note="NAD(P)(+)--arginine ADP-ribosyltransferase 1"
FT /id="PRO_0000019336"
FT PROPEP 267..312
FT /evidence="ECO:0000255"
FT /id="PRO_0000019337"
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; 35319 MW; B82980439BC904FC CRC64;
MELLALRWVL LAGTLLSTSA ASSALQEGDL GSITVIMDMA LNSFDDQYLL CEDRMRARLQ
MENITEFSTN IAYAVTWRQA AAEWQKRWGH LARPMQLIRE QAIALLAYSA SSRMCTLFNE
ATRQGGRSHQ DYIHSYHFKT LHFFLTQALF ALRASQPRCY YVYRGVRGIR FMTQRGKSVR
FGQFTSTSLR KEATVNFGQD TLFVVKTCYG VPIKQFSFFP SEDEVLIPPF EVFEVINFSN
DRGSVKIQLH SKGKMSTHNC ELLKPQGGQW GRGHQEVGLG LSPGLSLPVL PCRRRVWEGL
GHREGDPIPA AV