ARY2_RAT
ID ARY2_RAT Reviewed; 290 AA.
AC P50298;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Arylamine N-acetyltransferase 2 {ECO:0000305};
DE EC=2.3.1.5 {ECO:0000269|PubMed:7882993, ECO:0000269|PubMed:8761433};
DE AltName: Full=Arylamide acetylase 2;
DE AltName: Full=N-acetyltransferase type 2;
DE Short=AT-2;
DE Short=NAT-2;
GN Name=Nat2; Synonyms=Aac2;
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], CATALYTIC ACTIVITY, AND FUNCTION.
RC STRAIN=Wistar; TISSUE=Pineal gland;
RX PubMed=7882993; DOI=10.1111/j.1432-1033.1995.tb20240.x;
RA Ebisawa T., Sasaki Y., Deguchi T.;
RT "Complementary DNAs for two arylamine N-acetyltransferases with identical
RT 5' non-coding regions from rat pineal gland.";
RL Eur. J. Biochem. 228:129-137(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALLELE NAT2*21.
RC STRAIN=WKY/NCRLBR; TISSUE=Heart;
RX PubMed=8528272; DOI=10.1097/00008571-199508000-00009;
RA Doll M.A., Hein D.W.;
RT "Cloning, sequencing and expression of NAT1 and NAT2 encoding genes from
RT rapid and slow acetylator inbred rats.";
RL Pharmacogenetics 5:247-251(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8761433; DOI=10.1093/carcin/17.8.1729;
RA Jones R.F., Land S.J., King C.M.;
RT "Recombinant rat and hamster N-acetyltransferases-1 and -2: relative rates
RT of N-acetylation of arylamines and N,O-acyltransfer with arylhydroxamic
RT acids.";
RL Carcinogenesis 17:1729-1733(1996).
CC -!- FUNCTION: Participates in the detoxification of a plethora of hydrazine
CC and arylamine drugs. Acetylates only arylamines.
CC {ECO:0000269|PubMed:7882993, ECO:0000269|PubMed:8761433}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + an arylamine = an N-acetylarylamine + CoA;
CC Xref=Rhea:RHEA:16613, ChEBI:CHEBI:13790, ChEBI:CHEBI:50471,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.5;
CC Evidence={ECO:0000269|PubMed:7882993, ECO:0000269|PubMed:8761433};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16614;
CC Evidence={ECO:0000305|PubMed:7882993, ECO:0000305|PubMed:8761433};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=32.2 uM for 2-aminofluorene {ECO:0000269|PubMed:8761433};
CC KM=138 uM for 4-aminoazobenzene {ECO:0000269|PubMed:8761433};
CC Vmax=59 nmol/min/mg enzyme toward 4-aminoazobenzene
CC {ECO:0000269|PubMed:8761433};
CC Vmax=833 nmol/min/mg enzyme toward 2-aminofluorene
CC {ECO:0000269|PubMed:8761433};
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- POLYMORPHISM: There are two forms of NAT2: a rapid isoform (NAT2*21A)
CC and a slow isoform (NAT2*21B).
CC -!- SIMILARITY: Belongs to the arylamine N-acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U01348; AAA70161.1; -; mRNA.
DR EMBL; U23418; AAB53956.1; -; Genomic_DNA.
DR EMBL; U19272; AAB60501.1; -; Genomic_DNA.
DR EMBL; U17261; AAA56772.1; -; mRNA.
DR PIR; I58425; I58425.
DR RefSeq; NP_446306.1; NM_053854.1.
DR AlphaFoldDB; P50298; -.
DR SMR; P50298; -.
DR STRING; 10116.ENSRNOP00000051430; -.
DR iPTMnet; P50298; -.
DR PhosphoSitePlus; P50298; -.
DR PaxDb; P50298; -.
DR GeneID; 116632; -.
DR KEGG; rno:116632; -.
DR UCSC; RGD:70492; rat.
DR CTD; 10; -.
DR RGD; 70492; Nat2.
DR eggNOG; ENOG502RD0D; Eukaryota.
DR InParanoid; P50298; -.
DR OrthoDB; 1545569at2759; -.
DR BRENDA; 2.3.1.56; 5301.
DR Reactome; R-RNO-156582; Acetylation.
DR Reactome; R-RNO-9753281; Paracetamol ADME.
DR SABIO-RK; P50298; -.
DR PRO; PR:P50298; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0004060; F:arylamine N-acetyltransferase activity; IDA:RGD.
DR GO; GO:0008080; F:N-acetyltransferase activity; IDA:RGD.
DR GO; GO:0048565; P:digestive tract development; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR InterPro; IPR001447; Arylamine_N-AcTrfase.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR PANTHER; PTHR11786; PTHR11786; 1.
DR Pfam; PF00797; Acetyltransf_2; 1.
DR PRINTS; PR01543; ANATRNSFRASE.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..290
FT /note="Arylamine N-acetyltransferase 2"
FT /id="PRO_0000107912"
FT ACT_SITE 68
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 107
FT /evidence="ECO:0000250"
FT ACT_SITE 122
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 106..107
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT VARIANT 121
FT /note="V -> I (in allele NAT2*21; slow acetylator)"
FT /evidence="ECO:0000269|PubMed:8528272"
FT VARIANT 266
FT /note="V -> I (in allele NAT2*21; slow acetylator)"
FT /evidence="ECO:0000269|PubMed:8528272"
SQ SEQUENCE 290 AA; 33756 MW; A02BF839A230F84D CRC64;
MDIEAYFERI GYQSSRNKLD LEELTEILQH QIRAIPFENL NIHCGESMEL NLEVIFDQVV
RKKRGGWCLQ VNHLLYWALT KMGFEATMLG GYVFNTPANK YSSGMIHLLV QVTLSGKDYI
VDAGFGRSYQ MWEPLELTSG KDQPQVPAIF RLTEENGTWY LDQIRREQYV PNQEFVNSDL
LEKNKYRKIY SFTLEPRTIE DFESINTYLQ TSPASLFTSK SFCSLQTLEG VHCLVGSTLT
YRRFSYKDNI DLVEFKSLTE EEIEDVLKTI FGVSLERKLV PKHGDRFFTI
