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   24-JAN-2024, entry version 143.
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}.
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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; 10090-ENSMUSP00000026677; -.
DR   PeptideAtlas; P50294; -.
DR   ProteomicsDB; 281806; -.
DR   DNASU; 17960; -.
DR   Ensembl; ENSMUST00000026677.4; ENSMUSP00000026677.4; ENSMUSG00000025588.5.
DR   GeneID; 17960; -.
DR   KEGG; mmu:17960; -.
DR   UCSC; uc009lvv.1; mouse.
DR   AGR; MGI:97279; -.
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; 2696539at2759; -.
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 76 CRISPR screens.
DR   PRO; PR:P50294; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; P50294; Protein.
DR   Bgee; ENSMUSG00000025588; Expressed in mesodermal cell in embryo and 37 other cell types or tissues.
DR   ExpressionAtlas; P50294; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004060; F:arylamine N-acetyltransferase activity; IDA:MGI.
DR   Gene3D; 3.30.2140.20; -; 1.
DR   InterPro; IPR001447; Arylamine_N-AcTrfase.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   PANTHER; PTHR11786:SF2; ARYLAMINE N-ACETYLTRANSFERASE 1; 1.
DR   PANTHER; PTHR11786; N-HYDROXYARYLAMINE O-ACETYLTRANSFERASE; 1.
DR   Pfam; PF00797; Acetyltransf_2; 1.
DR   PRINTS; PR01543; ANATRNSFRASE.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   Genevisible; P50294; MM.
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
//