ARY1_HUMAN
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 03-AUG-2022, entry version 196.
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
RP 166-THR-GLN-167.
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 NAT1*17 TRP-64 AND NAT1*14
RP 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 NAT1*11 ILE-149 AND
RP 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 NAT1*11 ILE-149 AND
RP 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 NAT1*14 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="http://atlasgeneticsoncology.org/Genes/NAT1ID41497ch8p22.html";
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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 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; P18440; -.
DR PeptideAtlas; P18440; -.
DR PRIDE; P18440; -.
DR ProteomicsDB; 53563; -.
DR Antibodypedia; 22350; 352 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 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; CYEHNTL; -.
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; 8 hits in 1042 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 157 other tissues.
DR ExpressionAtlas; P18440; baseline and differential.
DR Genevisible; P18440; HS.
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 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 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 N-
FT acetylation of aromatic amines and the O- and N,O-
FT acetylation of their N-hydroxylated metabolites at rates up
FT 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 /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
