ARY1_MOUSE
ID ARY1_MOUSE Reviewed; 290 AA.
AC P50294;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Arylamine N-acetyltransferase 1;
DE EC=2.3.1.5 {ECO:0000269|PubMed:7545952};
DE AltName: Full=Arylamide acetylase 1;
DE AltName: Full=N-acetyltransferase type 1;
DE Short=NAT-1;
GN Name=Nat1; Synonyms=Aac1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J;
RX PubMed=1875909;
RA Martell K.J., Vatsis K.P., Weber W.W.;
RT "Molecular genetic basis of rapid and slow acetylation in mice.";
RL Mol. Pharmacol. 40:218-227(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C3H/HeJ; TISSUE=Heart;
RA Hein D.W., Doll M.A.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE, AND CATALYTIC ACTIVITY.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=7545952; DOI=10.1042/bj3020347;
RA Kelly S.L., Sim E.;
RT "Arylamine N-acetyltransferase in Balb/c mice: identification of a novel
RT mouse isoenzyme by cloning and expression in vitro.";
RL Biochem. J. 302:347-353(1994).
RN [4]
RP CHARACTERIZATION.
RX PubMed=1513324;
RA Martell K.J., Levy G.N., Weber W.W.;
RT "Cloned mouse N-acetyltransferases: enzymatic properties of expressed Nat-1
RT and Nat-2 gene products.";
RL Mol. Pharmacol. 42:265-272(1992).
CC -!- FUNCTION: Participates in the detoxification of a plethora of hydrazine
CC and arylamine drugs. Isoniazid, 2-aminofluorene and anisidine are
CC preferred substrates for NAT-1. No activity with p-aminobenzoic acid
CC (PABA) nor SMZ.
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:7545952};
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the arylamine N-acetyltransferase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U35885; AAA78942.1; -; mRNA.
DR EMBL; U37119; AAA80667.1; -; Genomic_DNA.
DR CCDS; CCDS22337.1; -.
DR PIR; A61267; A61267.
DR RefSeq; NP_032699.1; NM_008673.1.
DR AlphaFoldDB; P50294; -.
DR SMR; P50294; -.
DR STRING; 10090.ENSMUSP00000026677; -.
DR ChEMBL; CHEMBL5723; -.
DR iPTMnet; P50294; -.
DR PhosphoSitePlus; P50294; -.
DR jPOST; P50294; -.
DR PaxDb; P50294; -.
DR PeptideAtlas; P50294; -.
DR PRIDE; P50294; -.
DR ProteomicsDB; 281806; -.
DR DNASU; 17960; -.
DR Ensembl; ENSMUST00000026677; ENSMUSP00000026677; ENSMUSG00000025588.
DR GeneID; 17960; -.
DR KEGG; mmu:17960; -.
DR UCSC; uc009lvv.1; mouse.
DR CTD; 9; -.
DR MGI; MGI:97279; Nat1.
DR VEuPathDB; HostDB:ENSMUSG00000025588; -.
DR eggNOG; ENOG502RD0D; Eukaryota.
DR GeneTree; ENSGT00390000012054; -.
DR HOGENOM; CLU_049918_3_0_1; -.
DR InParanoid; P50294; -.
DR OrthoDB; 1545569at2759; -.
DR PhylomeDB; P50294; -.
DR TreeFam; TF106311; -.
DR BRENDA; 2.3.1.5; 3474.
DR Reactome; R-MMU-156582; Acetylation.
DR Reactome; R-MMU-9753281; Paracetamol ADME.
DR BioGRID-ORCS; 17960; 2 hits in 71 CRISPR screens.
DR PRO; PR:P50294; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P50294; protein.
DR Bgee; ENSMUSG00000025588; Expressed in pineal body and 35 other tissues.
DR ExpressionAtlas; P50294; baseline and differential.
DR Genevisible; P50294; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0004060; F:arylamine N-acetyltransferase activity; IDA:MGI.
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_0000107908"
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; 33713 MW; 228C64130A2AD881 CRC64;
MDIEAYFERI GYKNSVNKLD LATLTEVLQH QMRAVPFENL NMHCGEAMHL DLQDIFDHIV
RKKRGGWCLQ VNHLLYWALT KMGFETTMLG GYVYITPVSK YSSEMVHLLV QVTISDRKYI
VDSAYGGSYQ MWEPLELTSG KDQPQVPAIF LLTEENGTWY LDQIRREQYV PNEEFVNSDL
LEKNKYRKIY SFTLEPRVIE DFEYVNSYLQ TSPASVFVST SFCSLQTSEG VHCLVGSTFT
SRRFSYKDDV DLVEFKYVNE EEIEDVLKTA FGISLERKFV PKHGELVFTI
