ARY1_RAT
ID ARY1_RAT Reviewed; 290 AA.
AC P50297;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Arylamine N-acetyltransferase 1;
DE EC=2.3.1.5 {ECO:0000269|PubMed:7882993, ECO:0000269|PubMed:8761433};
DE AltName: Full=Arylamide acetylase 1;
DE AltName: Full=N-acetyltransferase type 1;
DE Short=AT-1;
DE Short=NAT-1;
GN Name=Nat1; Synonyms=Aac1;
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], FUNCTION, AND CATALYTIC ACTIVITY.
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 [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RA Jones R.F., Gott B., Land S.J., Park J., King C.M.;
RT "Recombinant rat and hamster acetyltransferases-1 and -2: relative rates of
RT N-acetylation of arylamines and N,O-acyltransfer with arylhydroxamic
RT acids.";
RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND 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 both arylamines and arylalkylamines.
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=0.64 uM for 4-aminoazobenzene {ECO:0000269|PubMed:8761433};
CC KM=0.18 uM for 2-aminofluorene {ECO:0000269|PubMed:8761433};
CC Vmax=47 nmol/min/mg enzyme toward 2-aminofluorene
CC {ECO:0000269|PubMed:8761433};
CC Vmax=41.8 nmol/min/mg enzyme toward 4-aminoazobenzene
CC {ECO:0000269|PubMed:8761433};
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the arylamine N-acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U01344; AAA70157.1; -; mRNA.
DR EMBL; U01343; AAA70156.1; -; mRNA.
DR EMBL; U17260; AAA56771.1; -; mRNA.
DR EMBL; U01345; AAA70158.1; -; mRNA.
DR EMBL; BC078765; AAH78765.1; -; mRNA.
DR PIR; I67465; I67465.
DR RefSeq; NP_001032392.1; NM_001037315.1.
DR RefSeq; NP_001032393.1; NM_001037316.1.
DR RefSeq; NP_446305.1; NM_053853.2.
DR RefSeq; XP_006253063.1; XM_006253001.2.
DR RefSeq; XP_006253064.1; XM_006253002.3.
DR RefSeq; XP_006253066.1; XM_006253004.3.
DR RefSeq; XP_017455467.1; XM_017599978.1.
DR AlphaFoldDB; P50297; -.
DR SMR; P50297; -.
DR STRING; 10116.ENSRNOP00000018854; -.
DR iPTMnet; P50297; -.
DR PhosphoSitePlus; P50297; -.
DR jPOST; P50297; -.
DR PaxDb; P50297; -.
DR DNASU; 116631; -.
DR Ensembl; ENSRNOT00000018854; ENSRNOP00000018854; ENSRNOG00000049498.
DR Ensembl; ENSRNOT00000090726; ENSRNOP00000070053; ENSRNOG00000049498.
DR Ensembl; ENSRNOT00000098891; ENSRNOP00000086542; ENSRNOG00000049498.
DR Ensembl; ENSRNOT00000107612; ENSRNOP00000086645; ENSRNOG00000049498.
DR GeneID; 116631; -.
DR KEGG; rno:116631; -.
DR UCSC; RGD:70490; rat.
DR CTD; 9; -.
DR RGD; 70490; Nat1.
DR eggNOG; ENOG502RD0D; Eukaryota.
DR GeneTree; ENSGT00390000012054; -.
DR HOGENOM; CLU_049918_3_0_1; -.
DR InParanoid; P50297; -.
DR OMA; IMYAMAQ; -.
DR OrthoDB; 1545569at2759; -.
DR PhylomeDB; P50297; -.
DR BRENDA; 2.3.1.56; 5301.
DR Reactome; R-RNO-156582; Acetylation.
DR Reactome; R-RNO-9753281; Paracetamol ADME.
DR SABIO-RK; P50297; -.
DR PRO; PR:P50297; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000014055; Expressed in liver and 19 other tissues.
DR ExpressionAtlas; P50297; baseline and differential.
DR Genevisible; P50297; RN.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0004060; F:arylamine N-acetyltransferase activity; IDA:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0097068; P:response to thyroxine; 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 Acetylation; Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..290
FT /note="Arylamine N-acetyltransferase 1"
FT /id="PRO_0000107911"
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 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 MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P18440"
SQ SEQUENCE 290 AA; 33437 MW; 2897CC1F84B7D72A CRC64;
MDIEAYFERI GYKNSVNKLD LATLTEVLQH QMRAVPFENL SMHCGEAMCL GLEATFDHIV
RKKRGGWCLQ VNHLLYWALT KMGFETTMLG GYVYITPVNK YSSEMVHLLV QVTISDRNYI
VDSAYGSSYQ MWEPLELTSG KDQPQVPAIF RLTEENGTWY LDQIRREQDV PNQEFVNSDL
LEKSKYRKIY SFTLEPRTIE DFEYVNTYLQ TSPASVFVST SFCSLQTSEG VCCLIGSTLT
SRRFSYKDNV DLVEFKSLTE EEIEDVLKTT FGISLEKKFV PKHGELVFTI
