ID ARY1_HUMAN Reviewed; 290 AA. AC P18440; A8K4E7; O15159; O15300; Q546N1; Q96TE9; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 2. DT 27-MAR-2024, entry version 205. DE RecName: Full=Arylamine N-acetyltransferase 1; DE EC=2.3.1.5; DE AltName: Full=Arylamide acetylase 1; DE AltName: Full=Monomorphic arylamine N-acetyltransferase; DE Short=MNAT; DE AltName: Full=N-acetyltransferase type 1; DE Short=NAT-1; GN Name=NAT1; Synonyms=AAC1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE NAT1*4). RC TISSUE=Leukocyte; RX PubMed=2340091; DOI=10.1089/dna.1990.9.193; RA Blum M., Grant D.M., McBride W., Heim M., Meyer U.A.; RT "Human arylamine N-acetyltransferase genes: isolation, chromosomal RT localization, and functional expression."; RL DNA Cell Biol. 9:193-203(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS NAT1*5 THR-117 AND 166-ARG-GLU-167 RP DELINS THR-GLN. RC TISSUE=Liver; RX PubMed=1968463; DOI=10.1016/s0021-9258(19)39609-7; RA Ohsako S., Deguchi T.; RT "Cloning and expression of cDNAs for polymorphic and monomorphic arylamine RT N-acetyltransferases from human liver."; RL J. Biol. Chem. 265:4630-4634(1990). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS NAT1*11 ILE-149 AND RP ALA-214. RX PubMed=8442668; DOI=10.1006/abbi.1993.1116; RA Vatsis K.P., Weber W.W.; RT "Structural heterogeneity of Caucasian N-acetyltransferase at the NAT1 gene RT locus."; RL Arch. Biochem. Biophys. 301:71-76(1993). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS NAT1*11 ILE-149 AND RP ALA-214. RC TISSUE=Blood; RX PubMed=9168895; DOI=10.1006/bbrc.1997.6501; RA Doll M.A., Jiang W., Deitz A.C., Rustan T.D., Hein D.W.; RT "Identification of a novel allele at the human NAT1 acetyltransferase RT locus."; RL Biochem. Biophys. Res. Commun. 233:584-591(1997). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TRP-64 AND GLN-187. RX PubMed=9511183; DOI=10.1097/00008571-199802000-00009; RA Butcher N.J., Ilett K.F., Minchin R.F.; RT "Functional polymorphism of the human arylamine N-acetyltransferase type 1 RT gene caused by C190T and G560A mutations."; RL Pharmacogenetics 8:67-72(1998). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Deitz A.C., Fretland A.J., Leff M.A., Doll M.A., Hein D.W.; RT "Homo sapiens N-acetyltransferase-1 (NAT1) gene complete cds."; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10862520; DOI=10.1097/00008571-200006000-00003; RA Lo-Guidice J.-M., Allorge D., Chevalier D., Debuysere H., Fazio F., RA Lafitte J.-J., Broly F.; RT "Molecular analysis of the N-acetyltransferase 1 gene (NAT1*) using RT polymerase chain reaction-restriction fragment-single strand conformation RT polymorphism assay."; RL Pharmacogenetics 10:293-300(2000). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-149 AND ALA-214. RA Johnson N., Sim E.; RT "Homo sapiens arylamine N-acetyltransferase type 1 (NAT1) gene, allele RT NAT1*11B."; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE NAT1*4). RA Johnson N., Sim E.; RT "Homo sapiens arylamine N-acetyltransferase type 1 (NAT1) gene, NAT1*4 RT allele."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-149 AND ALA-214. RX PubMed=16416399; DOI=10.1086/500614; RA Patin E., Barreiro L.B., Sabeti P.C., Austerlitz F., Luca F., Sajantila A., RA Behar D.M., Semino O., Sakuntabhai A., Guiso N., Gicquel B., McElreavey K., RA Harding R.M., Heyer E., Quintana-Murci L.; RT "Deciphering the ancient and complex evolutionary history of human RT arylamine N-acetyltransferase genes."; RL Am. J. Hum. Genet. 78:423-436(2006). RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-149 AND ALA-214. RG NIEHS SNPs program; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; 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 [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22. RC TISSUE=Liver; RX PubMed=1676262; DOI=10.1016/0006-291x(91)90676-x; RA Ebisawa T., Deguchi T.; RT "Structure and restriction fragment length polymorphism of genes for human RT liver arylamine N-acetyltransferases."; RL Biochem. Biophys. Res. Commun. 177:1252-1257(1991). RN [15] RP MUTAGENESIS OF ARG-64. RX PubMed=9173883; DOI=10.1042/bj3230207; RA Delomenie C., Goodfellow G.H., Krishnamoorthy R., Grant D.M., Dupret J.-M.; RT "Study of the role of the highly conserved residues Arg9 and Arg64 in the RT catalytic function of human N-acetyltransferases NAT1 and NAT2 by site- RT directed mutagenesis."; RL Biochem. J. 323:207-215(1997). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [17] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF WILD-TYPE IN COMPLEX WITH RP 2-BROMOACETANILIDE AND OF MUTANT SER-125, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=17656365; DOI=10.1074/jbc.m704138200; RA Wu H., Dombrovsky L., Tempel W., Martin F., Loppnau P., Goodfellow G.H., RA Grant D.M., Plotnikov A.N.; RT "Structural basis of substrate-binding specificity of human arylamine N- RT acetyltransferases."; RL J. Biol. Chem. 282:30189-30197(2007). RN [18] RP ALLELE NAT1*10. RX PubMed=7585580; RA Bell D.A., Badawi A.F., Lang N.P., Ilett K.F., Kadlubar F.F., Hirvonen A.; RT "Polymorphism in the N-acetyltransferase 1 (NAT1) polyadenylation signal: RT association of NAT1*10 allele with higher N-acetylation activity in bladder RT and colon tissue."; RL Cancer Res. 55:5226-5229(1995). RN [19] RP VARIANT GLN-187. RX PubMed=9511182; DOI=10.1097/00008571-199802000-00008; RA Hughes N.C., Janezic S.A., McQueen K.L., Jewett M.A., Castranio T., RA Bell D.A., Grant D.M.; RT "Identification and characterization of variant alleles of human RT acetyltransferase NAT1 with defective function using p-aminosalicylate as RT an in-vivo and in-vitro probe."; RL Pharmacogenetics 8:55-66(1998). RN [20] RP VARIANTS NAT1*17; NAT1*21; NAT1*22; NAT1*24 AND NAT1*25. RX PubMed=9682272; DOI=10.1097/00008571-199806000-00009; RA Lin H.J., Probst-Hensch N.M., Hughes N.C., Sakamoto G.T., Louie A.D., RA Kau I.H., Lin B.K., Lee D.B., Lin J., Frankl H.D., Lee E.R., Hardy S., RA Grant D.M., Haile R.W.; RT "Variants of N-acetyltransferase NAT1 and a case-control study of RT colorectal adenomas."; RL Pharmacogenetics 8:269-281(1998). CC -!- FUNCTION: Participates in the detoxification of a plethora of hydrazine CC and arylamine drugs. Catalyzes the N- or O-acetylation of various CC arylamine and heterocyclic amine substrates and is able to bioactivate CC several known carcinogens. 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 -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- POLYMORPHISM: N-acetylation polymorphism is determined by a low or high CC NAT activity in liver and has been implicated in the action and CC toxicity of amine-containing drugs. Slow acetylation genotypes have CC been associated with significant lung cancer risk. Candidate risk CC factor for susceptibility to neural tube defects. The NAT1*10 allele CC has been associated with increased risk of colon and urinary bladder CC cancers and with higher levels of N-acetyltransferase activity and DNA CC adducts in aromatic amine tumor target organs such as colon and urinary CC bladder (PubMed:7585580). {ECO:0000269|PubMed:7585580}. CC -!- MISCELLANEOUS: NAT1 was historically considered to be monomorphic in CC nature but reports of allelic variations at the NAT1 locus suggest that CC it is a polymorphically expressed enzyme. CC -!- SIMILARITY: Belongs to the arylamine N-acetyltransferase family. CC {ECO:0000305}. CC -!- CAUTION: The allelic variation Ile-149 designated as NAT1*17 is part of CC the NAT1*11 allelic variation as reported by the nomenclature CC committee. {ECO:0000305}. CC -!- WEB RESOURCE: Name=NAT; Note=NAT alleles; CC URL="http://nat.mbg.duth.gr/"; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/nat1/"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/41497/NAT1"; 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; X17059; CAA34905.1; -; Genomic_DNA. DR EMBL; D90041; BAA14095.1; -; mRNA. DR EMBL; AF032677; AAB86878.1; -; Genomic_DNA. DR EMBL; AF032678; AAB86879.1; -; Genomic_DNA. DR EMBL; U80835; AAB62398.1; -; Genomic_DNA. DR EMBL; AF008204; AAB84384.1; -; Genomic_DNA. DR EMBL; AF071552; AAC24712.1; -; Genomic_DNA. DR EMBL; AF067408; AAC24707.1; -; Genomic_DNA. DR EMBL; AF082903; AAD13343.1; -; Genomic_DNA. DR EMBL; AF082904; AAC32388.1; -; Genomic_DNA. DR EMBL; AJ278017; CAC01128.1; -; Genomic_DNA. DR EMBL; AJ307007; CAC38345.1; -; Genomic_DNA. DR EMBL; DQ305816; ABC26192.1; -; Genomic_DNA. DR EMBL; DQ305817; ABC26193.1; -; Genomic_DNA. DR EMBL; DQ305818; ABC26194.1; -; Genomic_DNA. DR EMBL; DQ305819; ABC26195.1; -; Genomic_DNA. DR EMBL; DQ305820; ABC26196.1; -; Genomic_DNA. DR EMBL; DQ305821; ABC26197.1; -; Genomic_DNA. DR EMBL; DQ305822; ABC26198.1; -; Genomic_DNA. DR EMBL; DQ305823; ABC26199.1; -; Genomic_DNA. DR EMBL; DQ305824; ABC26200.1; -; Genomic_DNA. DR EMBL; DQ305825; ABC26201.1; -; Genomic_DNA. DR EMBL; DQ305826; ABC26202.1; -; Genomic_DNA. DR EMBL; DQ305827; ABC26203.1; -; Genomic_DNA. DR EMBL; DQ305828; ABC26204.1; -; Genomic_DNA. DR EMBL; DQ305829; ABC26205.1; -; Genomic_DNA. DR EMBL; DQ305830; ABC26206.1; -; Genomic_DNA. DR EMBL; DQ305831; ABC26207.1; -; Genomic_DNA. DR EMBL; DQ305832; ABC26208.1; -; Genomic_DNA. DR EMBL; DQ305833; ABC26209.1; -; Genomic_DNA. DR EMBL; DQ305834; ABC26210.1; -; Genomic_DNA. DR EMBL; DQ305835; ABC26211.1; -; Genomic_DNA. DR EMBL; DQ305836; ABC26212.1; -; Genomic_DNA. DR EMBL; DQ305837; ABC26213.1; -; Genomic_DNA. DR EMBL; DQ305838; ABC26214.1; -; Genomic_DNA. DR EMBL; DQ305839; ABC26215.1; -; Genomic_DNA. DR EMBL; DQ305840; ABC26216.1; -; Genomic_DNA. DR EMBL; DQ305841; ABC26217.1; -; Genomic_DNA. DR EMBL; DQ305842; ABC26218.1; -; Genomic_DNA. DR EMBL; DQ305843; ABC26219.1; -; Genomic_DNA. DR EMBL; DQ305844; ABC26220.1; -; Genomic_DNA. DR EMBL; DQ305845; ABC26221.1; -; Genomic_DNA. DR EMBL; DQ305846; ABC26222.1; -; Genomic_DNA. DR EMBL; DQ305847; ABC26223.1; -; Genomic_DNA. DR EMBL; DQ305848; ABC26224.1; -; Genomic_DNA. DR EMBL; DQ305849; ABC26225.1; -; Genomic_DNA. DR EMBL; DQ305850; ABC26226.1; -; Genomic_DNA. DR EMBL; DQ305851; ABC26227.1; -; Genomic_DNA. DR EMBL; DQ305852; ABC26228.1; -; Genomic_DNA. DR EMBL; DQ305853; ABC26229.1; -; Genomic_DNA. DR EMBL; DQ305854; ABC26230.1; -; Genomic_DNA. DR EMBL; DQ305855; ABC26231.1; -; Genomic_DNA. DR EMBL; DQ305856; ABC26232.1; -; Genomic_DNA. DR EMBL; DQ305857; ABC26233.1; -; Genomic_DNA. DR EMBL; DQ305858; ABC26234.1; -; Genomic_DNA. DR EMBL; DQ305859; ABC26235.1; -; Genomic_DNA. DR EMBL; DQ305860; ABC26236.1; -; Genomic_DNA. DR EMBL; DQ305861; ABC26237.1; -; Genomic_DNA. DR EMBL; DQ305862; ABC26238.1; -; Genomic_DNA. DR EMBL; DQ305863; ABC26239.1; -; Genomic_DNA. DR EMBL; DQ305864; ABC26240.1; -; Genomic_DNA. DR EMBL; DQ305865; ABC26241.1; -; Genomic_DNA. DR EMBL; DQ305866; ABC26242.1; -; Genomic_DNA. DR EMBL; DQ305867; ABC26243.1; -; Genomic_DNA. DR EMBL; DQ305868; ABC26244.1; -; Genomic_DNA. DR EMBL; DQ305869; ABC26245.1; -; Genomic_DNA. DR EMBL; DQ305870; ABC26246.1; -; Genomic_DNA. DR EMBL; DQ305871; ABC26247.1; -; Genomic_DNA. DR EMBL; DQ305872; ABC26248.1; -; Genomic_DNA. DR EMBL; DQ305873; ABC26249.1; -; Genomic_DNA. DR EMBL; DQ305874; ABC26250.1; -; Genomic_DNA. DR EMBL; DQ305875; ABC26251.1; -; Genomic_DNA. DR EMBL; DQ305876; ABC26252.1; -; Genomic_DNA. DR EMBL; DQ305877; ABC26253.1; -; Genomic_DNA. DR EMBL; DQ305878; ABC26254.1; -; Genomic_DNA. DR EMBL; DQ305879; ABC26255.1; -; Genomic_DNA. DR EMBL; DQ305880; ABC26256.1; -; Genomic_DNA. DR EMBL; DQ305881; ABC26257.1; -; Genomic_DNA. DR EMBL; DQ305882; ABC26258.1; -; Genomic_DNA. DR EMBL; DQ305883; ABC26259.1; -; Genomic_DNA. DR EMBL; DQ305884; ABC26260.1; -; Genomic_DNA. DR EMBL; DQ305885; ABC26261.1; -; Genomic_DNA. DR EMBL; DQ305886; ABC26262.1; -; Genomic_DNA. DR EMBL; DQ305887; ABC26263.1; -; Genomic_DNA. DR EMBL; DQ305888; ABC26264.1; -; Genomic_DNA. DR EMBL; DQ305889; ABC26265.1; -; Genomic_DNA. DR EMBL; DQ305890; ABC26266.1; -; Genomic_DNA. DR EMBL; DQ305891; ABC26267.1; -; Genomic_DNA. DR EMBL; DQ305892; ABC26268.1; -; Genomic_DNA. DR EMBL; DQ305893; ABC26269.1; -; Genomic_DNA. DR EMBL; DQ305894; ABC26270.1; -; Genomic_DNA. DR EMBL; DQ305895; ABC26271.1; -; Genomic_DNA. DR EMBL; DQ305896; ABC26272.1; -; Genomic_DNA. DR EMBL; DQ305897; ABC26273.1; -; Genomic_DNA. DR EMBL; DQ305898; ABC26274.1; -; Genomic_DNA. DR EMBL; DQ305899; ABC26275.1; -; Genomic_DNA. DR EMBL; DQ305900; ABC26276.1; -; Genomic_DNA. DR EMBL; DQ305901; ABC26277.1; -; Genomic_DNA. DR EMBL; DQ305902; ABC26278.1; -; Genomic_DNA. DR EMBL; DQ305903; ABC26279.1; -; Genomic_DNA. DR EMBL; DQ305904; ABC26280.1; -; Genomic_DNA. DR EMBL; DQ305905; ABC26281.1; -; Genomic_DNA. DR EMBL; DQ305906; ABC26282.1; -; Genomic_DNA. DR EMBL; DQ305907; ABC26283.1; -; Genomic_DNA. DR EMBL; DQ305908; ABC26284.1; -; Genomic_DNA. DR EMBL; DQ305909; ABC26285.1; -; Genomic_DNA. DR EMBL; DQ305910; ABC26286.1; -; Genomic_DNA. DR EMBL; DQ305911; ABC26287.1; -; Genomic_DNA. DR EMBL; DQ305912; ABC26288.1; -; Genomic_DNA. DR EMBL; DQ305913; ABC26289.1; -; Genomic_DNA. DR EMBL; DQ305914; ABC26290.1; -; Genomic_DNA. DR EMBL; DQ305915; ABC26291.1; -; Genomic_DNA. DR EMBL; DQ305916; ABC26292.1; -; Genomic_DNA. DR EMBL; DQ305917; ABC26293.1; -; Genomic_DNA. DR EMBL; DQ305918; ABC26294.1; -; Genomic_DNA. DR EMBL; DQ305919; ABC26295.1; -; Genomic_DNA. DR EMBL; DQ305920; ABC26296.1; -; Genomic_DNA. DR EMBL; DQ305921; ABC26297.1; -; Genomic_DNA. DR EMBL; DQ305922; ABC26298.1; -; Genomic_DNA. DR EMBL; DQ305923; ABC26299.1; -; Genomic_DNA. DR EMBL; DQ305924; ABC26300.1; -; Genomic_DNA. DR EMBL; DQ305925; ABC26301.1; -; Genomic_DNA. DR EMBL; DQ305926; ABC26302.1; -; Genomic_DNA. DR EMBL; DQ305927; ABC26303.1; -; Genomic_DNA. DR EMBL; DQ305928; ABC26304.1; -; Genomic_DNA. DR EMBL; DQ305929; ABC26305.1; -; Genomic_DNA. DR EMBL; DQ305930; ABC26306.1; -; Genomic_DNA. DR EMBL; DQ305931; ABC26307.1; -; Genomic_DNA. DR EMBL; DQ305932; ABC26308.1; -; Genomic_DNA. DR EMBL; DQ305933; ABC26309.1; -; Genomic_DNA. DR EMBL; DQ305934; ABC26310.1; -; Genomic_DNA. DR EMBL; DQ305935; ABC26311.1; -; Genomic_DNA. DR EMBL; DQ305936; ABC26312.1; -; Genomic_DNA. DR EMBL; DQ305937; ABC26313.1; -; Genomic_DNA. DR EMBL; DQ305938; ABC26314.1; -; Genomic_DNA. DR EMBL; DQ305939; ABC26315.1; -; Genomic_DNA. DR EMBL; DQ305940; ABC26316.1; -; Genomic_DNA. DR EMBL; DQ305941; ABC26317.1; -; Genomic_DNA. DR EMBL; DQ305942; ABC26318.1; -; Genomic_DNA. DR EMBL; DQ305943; ABC26319.1; -; Genomic_DNA. DR EMBL; DQ305944; ABC26320.1; -; Genomic_DNA. DR EMBL; DQ305945; ABC26321.1; -; Genomic_DNA. DR EMBL; DQ305946; ABC26322.1; -; Genomic_DNA. DR EMBL; DQ305947; ABC26323.1; -; Genomic_DNA. DR EMBL; DQ305948; ABC26324.1; -; Genomic_DNA. DR EMBL; DQ305949; ABC26325.1; -; Genomic_DNA. DR EMBL; DQ305950; ABC26326.1; -; Genomic_DNA. DR EMBL; DQ305951; ABC26327.1; -; Genomic_DNA. DR EMBL; DQ305952; ABC26328.1; -; Genomic_DNA. DR EMBL; DQ305953; ABC26329.1; -; Genomic_DNA. DR EMBL; DQ305954; ABC26330.1; -; Genomic_DNA. DR EMBL; DQ305955; ABC26331.1; -; Genomic_DNA. DR EMBL; DQ305956; ABC26332.1; -; Genomic_DNA. DR EMBL; DQ305957; ABC26333.1; -; Genomic_DNA. DR EMBL; DQ305958; ABC26334.1; -; Genomic_DNA. DR EMBL; DQ305959; ABC26335.1; -; Genomic_DNA. DR EMBL; DQ305960; ABC26336.1; -; Genomic_DNA. DR EMBL; DQ305961; ABC26337.1; -; Genomic_DNA. DR EMBL; DQ305962; ABC26338.1; -; Genomic_DNA. DR EMBL; DQ305963; ABC26339.1; -; Genomic_DNA. DR EMBL; DQ305964; ABC26340.1; -; Genomic_DNA. DR EMBL; DQ305965; ABC26341.1; -; Genomic_DNA. DR EMBL; DQ305966; ABC26342.1; -; Genomic_DNA. DR EMBL; DQ305967; ABC26343.1; -; Genomic_DNA. DR EMBL; DQ305968; ABC26344.1; -; Genomic_DNA. DR EMBL; DQ305969; ABC26345.1; -; Genomic_DNA. DR EMBL; DQ305970; ABC26346.1; -; Genomic_DNA. DR EMBL; DQ305971; ABC26347.1; -; Genomic_DNA. DR EMBL; DQ305972; ABC26348.1; -; Genomic_DNA. DR EMBL; DQ305973; ABC26349.1; -; Genomic_DNA. DR EMBL; DQ305974; ABC26350.1; -; Genomic_DNA. DR EMBL; DQ305975; ABC26351.1; -; Genomic_DNA. DR EMBL; AK290912; BAF83601.1; -; mRNA. DR EMBL; AY338489; AAP88036.1; -; Genomic_DNA. DR EMBL; AY800271; AAV50002.1; -; Genomic_DNA. DR EMBL; BC047666; AAH47666.1; -; mRNA. DR EMBL; M75164; AAA59905.1; -; Genomic_DNA. DR CCDS; CCDS6007.1; -. DR PIR; A34585; A34585. DR RefSeq; NP_000653.3; NM_000662.7. DR RefSeq; NP_001153642.1; NM_001160170.3. DR RefSeq; NP_001153643.1; NM_001160171.3. DR RefSeq; NP_001153644.1; NM_001160172.3. DR RefSeq; NP_001153645.1; NM_001160173.3. DR RefSeq; NP_001153646.1; NM_001160174.2. DR RefSeq; NP_001153651.1; NM_001160179.2. DR RefSeq; XP_006716473.1; XM_006716410.3. DR RefSeq; XP_011542991.1; XM_011544689.2. DR PDB; 2IJA; X-ray; 1.70 A; A=2-290. DR PDB; 2PQT; X-ray; 1.78 A; A=2-290. DR PDBsum; 2IJA; -. DR PDBsum; 2PQT; -. DR AlphaFoldDB; P18440; -. DR SMR; P18440; -. DR BioGRID; 106527; 9. DR IntAct; P18440; 2. DR STRING; 9606.ENSP00000443194; -. DR BindingDB; P18440; -. DR ChEMBL; CHEMBL5101; -. DR DrugBank; DB11640; Amifampridine. DR DrugBank; DB00244; Mesalazine. DR DrugBank; DB01015; Sulfamethoxazole. DR GlyGen; P18440; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P18440; -. DR PhosphoSitePlus; P18440; -. DR SwissPalm; P18440; -. DR BioMuta; NAT1; -. DR DMDM; 114234; -. DR EPD; P18440; -. DR jPOST; P18440; -. DR MassIVE; P18440; -. DR MaxQB; P18440; -. DR PaxDb; 9606-ENSP00000443194; -. DR PeptideAtlas; P18440; -. DR ProteomicsDB; 53563; -. DR Pumba; P18440; -. DR Antibodypedia; 22350; 391 antibodies from 35 providers. DR DNASU; 9; -. DR Ensembl; ENST00000307719.9; ENSP00000307218.4; ENSG00000171428.15. DR Ensembl; ENST00000517492.5; ENSP00000429407.1; ENSG00000171428.15. DR Ensembl; ENST00000518029.5; ENSP00000428270.1; ENSG00000171428.15. DR Ensembl; ENST00000520546.1; ENSP00000429341.1; ENSG00000171428.15. DR GeneID; 9; -. DR KEGG; hsa:9; -. DR MANE-Select; ENST00000307719.9; ENSP00000307218.4; NM_000662.8; NP_000653.3. DR UCSC; uc003wyq.4; human. DR AGR; HGNC:7645; -. DR CTD; 9; -. DR DisGeNET; 9; -. DR GeneCards; NAT1; -. DR HGNC; HGNC:7645; NAT1. DR HPA; ENSG00000171428; Low tissue specificity. DR MIM; 108345; gene. DR neXtProt; NX_P18440; -. DR OpenTargets; ENSG00000171428; -. DR PharmGKB; PA17; -. DR VEuPathDB; HostDB:ENSG00000171428; -. DR eggNOG; ENOG502RD0D; Eukaryota. DR GeneTree; ENSGT00390000012054; -. DR HOGENOM; CLU_049918_3_0_1; -. DR InParanoid; P18440; -. DR OMA; WYTSTHP; -. DR PhylomeDB; P18440; -. DR BRENDA; 2.3.1.5; 2681. DR PathwayCommons; P18440; -. DR Reactome; R-HSA-156582; Acetylation. DR Reactome; R-HSA-9753281; Paracetamol ADME. DR SignaLink; P18440; -. DR SIGNOR; P18440; -. DR BioGRID-ORCS; 9; 9 hits in 1118 CRISPR screens. DR ChiTaRS; NAT1; human. DR EvolutionaryTrace; P18440; -. DR GeneWiki; N-acetyltransferase_1; -. DR GenomeRNAi; 9; -. DR Pharos; P18440; Tchem. DR PRO; PR:P18440; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; P18440; Protein. DR Bgee; ENSG00000171428; Expressed in bronchial epithelial cell and 158 other cell types or tissues. DR ExpressionAtlas; P18440; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0004060; F:arylamine N-acetyltransferase activity; IBA:GO_Central. DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome. DR Gene3D; 3.30.2140.20; -; 1. DR InterPro; IPR001447; Arylamine_N-AcTrfase. DR InterPro; IPR038765; Papain-like_cys_pep_sf. DR PANTHER; PTHR11786:SF8; 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; P18440; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Acyltransferase; Cytoplasm; Reference proteome; KW Transferase. FT CHAIN 1..290 FT /note="Arylamine N-acetyltransferase 1" FT /id="PRO_0000107904" FT ACT_SITE 68 FT /note="Acyl-thioester intermediate" FT ACT_SITE 107 FT ACT_SITE 122 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 BINDING 208 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000250" FT BINDING 214 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000250" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT VARIANT 64 FT /note="R -> W (in allele NAT1*17; a slow acetylator; has FT defective enzyme activity; dbSNP:rs56379106)" FT /evidence="ECO:0000269|PubMed:9511183" FT /id="VAR_004606" FT VARIANT 117 FT /note="R -> T (in allele NAT1*5; dbSNP:rs55641436)" FT /evidence="ECO:0000269|PubMed:1968463" FT /id="VAR_009510" FT VARIANT 149 FT /note="V -> I (in allele NAT1*11; catalyzes the FT N-acetylation of aromatic amines and the O- and FT N,O-acetylation of their N-hydroxylated metabolites at FT rates up to 2-fold higher; dbSNP:rs4987076)" FT /evidence="ECO:0000269|PubMed:16416399, FT ECO:0000269|PubMed:8442668, ECO:0000269|PubMed:9168895, FT ECO:0000269|Ref.12, ECO:0000269|Ref.8" FT /id="VAR_004607" FT VARIANT 166..167 FT /note="RE -> TQ (in allele NAT1*5; dbSNP:rs72554608)" FT /evidence="ECO:0000269|PubMed:1968463" FT /id="VAR_009511" FT VARIANT 187 FT /note="R -> Q (in allele NAT1*14; a slow acetylator; FT dbSNP:rs4986782)" FT /evidence="ECO:0000269|PubMed:9511182, FT ECO:0000269|PubMed:9511183" FT /id="VAR_009069" FT VARIANT 205 FT /note="M -> V (in allele NAT1*21; dbSNP:rs72554609)" FT /id="VAR_009070" FT VARIANT 207 FT /note="T -> I (in dbSNP:rs4987195)" FT /id="VAR_020384" FT VARIANT 214 FT /note="S -> A (in allele NAT1*11; dbSNP:rs4986783)" FT /evidence="ECO:0000269|PubMed:16416399, FT ECO:0000269|PubMed:8442668, ECO:0000269|PubMed:9168895, FT ECO:0000269|Ref.12, ECO:0000269|Ref.8" FT /id="VAR_009071" FT VARIANT 251 FT /note="D -> V (in allele NAT1*22; dbSNP:rs56172717)" FT /id="VAR_009072" FT VARIANT 261 FT /note="E -> K (in allele NAT1*24; dbSNP:rs72554610)" FT /id="VAR_009073" FT VARIANT 263 FT /note="I -> V (in allele NAT1*25; dbSNP:rs72554611)" FT /id="VAR_009074" FT MUTAGEN 64 FT /note="R->A,M,Q,K: Reduced enzymatic activity." FT /evidence="ECO:0000269|PubMed:9173883" FT HELIX 2..9 FT /evidence="ECO:0007829|PDB:2IJA" FT HELIX 21..34 FT /evidence="ECO:0007829|PDB:2IJA" FT HELIX 42..44 FT /evidence="ECO:0007829|PDB:2IJA" FT HELIX 52..60 FT /evidence="ECO:0007829|PDB:2IJA" FT HELIX 68..82 FT /evidence="ECO:0007829|PDB:2IJA" FT STRAND 85..95 FT /evidence="ECO:0007829|PDB:2IJA" FT TURN 96..99 FT /evidence="ECO:0007829|PDB:2IJA" FT STRAND 107..114 FT /evidence="ECO:0007829|PDB:2IJA" FT STRAND 117..121 FT /evidence="ECO:0007829|PDB:2IJA" FT STRAND 123..125 FT /evidence="ECO:0007829|PDB:2PQT" FT HELIX 127..129 FT /evidence="ECO:0007829|PDB:2IJA" FT STRAND 142..144 FT /evidence="ECO:0007829|PDB:2IJA" FT STRAND 149..155 FT /evidence="ECO:0007829|PDB:2IJA" FT STRAND 158..164 FT /evidence="ECO:0007829|PDB:2IJA" FT STRAND 167..169 FT /evidence="ECO:0007829|PDB:2IJA" FT HELIX 173..175 FT /evidence="ECO:0007829|PDB:2IJA" FT STRAND 185..192 FT /evidence="ECO:0007829|PDB:2IJA" FT HELIX 199..202 FT /evidence="ECO:0007829|PDB:2IJA" FT HELIX 203..211 FT /evidence="ECO:0007829|PDB:2IJA" FT HELIX 216..219 FT /evidence="ECO:0007829|PDB:2IJA" FT STRAND 222..226 FT /evidence="ECO:0007829|PDB:2IJA" FT STRAND 228..235 FT /evidence="ECO:0007829|PDB:2IJA" FT STRAND 238..243 FT /evidence="ECO:0007829|PDB:2IJA" FT STRAND 247..257 FT /evidence="ECO:0007829|PDB:2IJA" FT HELIX 260..271 FT /evidence="ECO:0007829|PDB:2IJA" SQ SEQUENCE 290 AA; 33899 MW; C015F7F3D4830107 CRC64; MDIEAYLERI GYKKSRNKLD LETLTDILQH QIRAVPFENL NIHCGDAMDL GLEAIFDQVV RRNRGGWCLQ VNHLLYWALT TIGFETTMLG GYVYSTPAKK YSTGMIHLLL QVTIDGRNYI VDAGFGRSYQ MWQPLELISG KDQPQVPCVF RLTEENGFWY LDQIRREQYI PNEEFLHSDL LEDSKYRKIY SFTLKPRTIE DFESMNTYLQ TSPSSVFTSK SFCSLQTPDG VHCLVGFTLT HRRFNYKDNT DLIEFKTLSE EEIEKVLKNI FNISLQRKLV PKHGDRFFTI //