ID ARY2_HUMAN Reviewed; 290 AA. AC P11245; O43637; O60654; O60655; Q13146; Q16697; Q2MLE4; Q2MLF5; Q2MLG8; AC Q2MLJ6; Q2MLK4; Q2MLK6; Q2MLN7; Q6LET4; Q86XS0; Q86XS1; Q96KY8; Q96T64; AC Q96T65; Q9H220; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 23-FEB-2022, sequence version 2. DT 02-SEP-2026, entry version 210. DE RecName: Full=Arylamine N-acetyltransferase 2 {ECO:0000305|PubMed:7915226}; DE EC=2.3.1.5 {ECO:0000269|PubMed:12222688, ECO:0000269|PubMed:7915226}; DE AltName: Full=Arylamide acetylase 2; DE AltName: Full=N-acetyltransferase type 2; DE Short=NAT-2; DE AltName: Full=N-hydroxyarylamine O-acetyltransferase {ECO:0000305|PubMed:7915226}; DE EC=2.3.1.118 {ECO:0000269|PubMed:12222688, ECO:0000269|PubMed:7915226}; DE AltName: Full=Polymorphic arylamine N-acetyltransferase; DE Short=PNAT; GN Name=NAT2; Synonyms=AAC2; 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 NAT2*4), AND VARIANT LYS-268. RX PubMed=2734109; DOI=10.1093/nar/17.10.3978; RA Grant D.M., Blum M., Demierre A., Meyer U.A.; RT "Nucleotide sequence of an intronless gene for a human arylamine N- RT acetyltransferase related to polymorphic drug acetylation."; RL Nucleic Acids Res. 17:3978-3978(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-268. 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS LYS-268 AND GLU-286. 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 [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES NAT2*4; NAT2*6A AND NAT2*7B), RP AND VARIANTS GLN-197; LYS-268 AND GLU-286. RC TISSUE=Liver; RX PubMed=1381364; DOI=10.1016/s0021-9258(19)37164-9; RA Deguchi T.; RT "Sequences and expression of alleles of polymorphic arylamine N- RT acetyltransferase of human liver."; RL J. Biol. Chem. 267:18140-18147(1992). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES NAT2*5C AND NAT2*14A), VARIANTS RP GLN-64; THR-114 AND LYS-268, FUNCTION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, AND CHARACTERIZATION OF VARIANTS GLN-64; RP THR-114 AND LYS-268. RX PubMed=7915226; DOI=10.1016/s0090-9556(25)08385-0; RA Ferguson R.J., Doll M.A., Rustan T.D., Gray K., Hein D.W.; RT "Cloning, expression, and functional characterization of two mutant RT (NAT2(191) and NAT2(341/803)) and wild-type human polymorphic N- RT acetyltransferase (NAT2) alleles."; RL Drug Metab. Dispos. 22:371-376(1994). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-24; GLN-64; THR-114; RP MET-193; GLN-197; HIS-208; LYS-268 AND GLU-286. 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 [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE NAT2*12A). RA Doll M.A., Satran S.L., Hein D.W.; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES NAT2*5D; NAT2*6D; NAT2*14G), AND RP VARIANTS GLN-64; THR-114; GLN-197 AND LYS-268. RA Leff M.A., Doll M.A., Feng Y., Fretland A.J., Hein D.W.; RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-114 AND LYS-268. RA Banerjee M., Anitha A.; RT "A novel linkage of two NAT2 mutations."; RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-114. RA Pillai A.A., Banerjee M.; RT "A novel allele showing linkage with 282, 341, 481, 803 point mutations in RT the NAT2 gene."; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-114. RA Pillai A.A., Banerjee M.; RT "A novel NAT2 allele with point mutations 341, 481, 803, 859 in the ethnic RT populations of Kerala."; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES NAT2*5I AND NAT2*12D), AND RP VARIANTS THR-114; ASN-122 AND PHE-137. RA Doll M.A., Zang Y., Yeager M., Welch R., Chanock S., Hein D.W.; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-268. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-24; GLN-64; THR-114; RP GLN-197; LEU-228; LYS-268 AND GLU-286. RG NIEHS SNPs program; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [15] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [16] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLN-197 AND LYS-268. RC TISSUE=Liver; 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 [17] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22. 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 [18] RP PROTEIN SEQUENCE OF 18-33 AND 189-197. RX PubMed=2924904; DOI=10.1016/0014-5793(89)81193-7; RA Grant D.M., Lottspeich F., Meyer U.A.; RT "Evidence for two closely related isozymes of arylamine N-acetyltransferase RT in human liver."; RL FEBS Lett. 244:203-207(1989). RN [19] RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) IN COMPLEX WITH COENZYME A. 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 [20] RP VARIANTS. RX PubMed=2068113; DOI=10.1073/pnas.88.14.6333; RA Vatsis K.P., Martell K.J., Weber W.W.; RT "Diverse point mutations in the human gene for polymorphic N- RT acetyltransferase."; RL Proc. Natl. Acad. Sci. U.S.A. 88:6333-6337(1991). RN [21] RP VARIANTS. RX PubMed=8466518; DOI=10.1006/bbrc.1993.1289; RA Abe M., Deguchi T., Suzuki T.; RT "The structure and characteristics of a fourth allele of polymorphic N- RT acetyltransferase gene found in the Japanese population."; RL Biochem. Biophys. Res. Commun. 191:811-816(1993). RN [22] RP VARIANTS PRO-145 AND THR-282. RX PubMed=7920692; DOI=10.1097/00008571-199406000-00003; RA Lin H.J., Han C.Y., Lin B.K., Hardy S.; RT "Ethnic distribution of slow acetylator mutations in the polymorphic N- RT acetyltransferase (NAT2) gene."; RL Pharmacogenetics 4:125-134(1994). RN [23] RP VARIANT TRP-64. RX PubMed=10970160; RX DOI=10.1002/1098-1004(200006)15:6<581::aid-humu17>3.0.co;2-v; RA Shishikura K., Hohjoh H., Tokunaga K.; RT "Novel allele containing a 190C>T nonsynonymous substitution in the N- RT acetyltransferase (NAT2) gene."; RL Hum. Mutat. 15:581-581(2000). RN [24] RP CHARACTERIZATION OF VARIANTS GLN-64; THR-114; PRO-145; GLN-197; LYS-268; RP THR-282 AND GLU-286. RX PubMed=11337936; DOI=10.1097/00008571-200104000-00004; RA Fretland A.J., Leff M.A., Doll M.A., Hein D.W.; RT "Functional characterization of human N-acetyltransferase 2 (NAT2) single RT nucleotide polymorphisms."; RL Pharmacogenetics 11:207-215(2001). RN [25] RP CHARACTERIZATION OF VARIANTS TRP-64 AND LYS-268, FUNCTION, CATALYTIC RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=12222688; DOI=10.1515/bc.2002.105; RA Zhu Y., Doll M.A., Hein D.W.; RT "Functional genomics of C190T single nucleotide polymorphism in human N- RT acetyltransferase 2."; RL Biol. Chem. 383:983-987(2002). RN [26] RP CHARACTERIZATION OF VARIANTS THR-114; ASN-122; PHE-137 AND LYS-268. RX PubMed=17264801; DOI=10.1097/01.fpc.0000236325.73186.2c; RA Zang Y., Zhao S., Doll M.A., States J.C., Hein D.W.; RT "Functional characterization of the A411T (L137F) and G364A (D122N) genetic RT polymorphisms in human N-acetyltransferase 2."; RL Pharmacogenet. Genomics 17:37-45(2007). RN [27] RP VARIANTS GLN-64; THR-114; VAL-135; GLN-197; ASP-203; LEU-213; LYS-268; RP MET-280 AND GLU-286. RX PubMed=18304320; DOI=10.1186/1471-2156-9-21; RA Sabbagh A., Langaney A., Darlu P., Gerard N., Krishnamoorthy R., RA Poloni E.S.; RT "Worldwide distribution of NAT2 diversity: implications for NAT2 RT evolutionary history."; RL BMC Genet. 9:21-21(2008). CC -!- FUNCTION: Catalyzes the N- or O-acetylation of various arylamine and CC heterocyclic amine substrates (PubMed:12222688, PubMed:7915226). CC Participates in the detoxification of a plethora of hydrazine and CC arylamine drugs, and is able to bioactivate several known carcinogens. CC {ECO:0000269|PubMed:12222688, ECO:0000269|PubMed:7915226}. CC -!- CATALYTIC ACTIVITY: CC Reaction=an arylamine + acetyl-CoA = 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:12222688, ECO:0000269|PubMed:7915226}; CC -!- CATALYTIC ACTIVITY: CC Reaction=an N-hydroxyarylamine + acetyl-CoA = an N-acetoxyarylamine + CC CoA; Xref=Rhea:RHEA:20277, ChEBI:CHEBI:13792, ChEBI:CHEBI:21494, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.118; CC Evidence={ECO:0000269|PubMed:12222688, ECO:0000269|PubMed:7915226}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=8.21 uM for 2-aminofluorene (measured with the enzyme encoded by CC allele NAT2*4) {ECO:0000269|PubMed:7915226}; CC KM=15.9 uM for 4-aminobiphenyl (measured with the enzyme encoded by CC allele NAT2*4) {ECO:0000269|PubMed:7915226}; CC KM=28.6 uM for 3,2-dimethyl-4-aminobiphenyl (measured with the enzyme CC encoded by allele NAT2*4) {ECO:0000269|PubMed:7915226}; CC KM=355 uM for acetyl-CoA (measured with the enzyme encoded by allele CC NAT2*4) {ECO:0000269|PubMed:7915226}; CC KM=483 uM for sulfamethazine (measured with the enzyme encoded by CC allele NAT2*4) {ECO:0000269|PubMed:12222688}; CC Vmax=1545 nmol/min/mg enzyme for N-acetyltransferase activity toward CC sulfamethazine (measured with the enzyme encoded by allele NAT2*4) CC {ECO:0000269|PubMed:12222688}; CC -!- INTERACTION: CC P11245; Q13315: ATM; NbExp=2; IntAct=EBI-9057228, EBI-495465; CC P11245; O95243-2: MBD4; NbExp=3; IntAct=EBI-9057228, EBI-6448717; CC P11245; Q06609: RAD51; NbExp=4; IntAct=EBI-9057228, EBI-297202; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- POLYMORPHISM: Genetic variations in NAT2 determine the rate of CC acetylation of various arylamine and heterocyclic amine substrates that CC include therapeutic and carcinogenic agents. They influence drug CC therapy response and susceptibility to chemical toxicity [MIM:243400]. CC Different alleles are known, whose combination defines the rapid, CC intermediate and slow acetylator phenotypes. Allele NAT2*4 sequence is CC historically considered as the reference in most publications. The CC sequence shown in this entry corresponds to the translation of allele CC NAT2*12A, which is the one represented in the human reference genome CC (GRCh38/hg38 assembly) and has an arginine at position 268 (Ref.7). The CC enzyme encoded by allele NAT2*4 differs by the variant p.Arg268Lys CC (PubMed:2734109). The two alloenzymes have comparable arylamine N- CC acetyltransferase activity (PubMed:11337936). CC {ECO:0000269|PubMed:10970160, ECO:0000269|PubMed:11337936, CC ECO:0000269|PubMed:12222688, ECO:0000269|PubMed:1381364, CC ECO:0000269|PubMed:16416399, ECO:0000269|PubMed:17264801, CC ECO:0000269|PubMed:18304320, ECO:0000269|PubMed:2734109, CC ECO:0000269|PubMed:7915226, ECO:0000269|Ref.10, ECO:0000269|Ref.11, CC ECO:0000269|Ref.12, ECO:0000269|Ref.14, ECO:0000269|Ref.7, CC ECO:0000269|Ref.8}. CC -!- SIMILARITY: Belongs to the arylamine N-acetyltransferase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAK51711.1; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/41498/NAT2"; CC -!- WEB RESOURCE: Name=NAT; Note=NAT alleles; CC URL="https://nat.mbg.duth.gr/"; 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; X14672; CAA32802.1; -; Genomic_DNA. DR EMBL; D90040; BAA14094.1; -; mRNA. DR EMBL; D90042; BAA14096.1; -; mRNA. DR EMBL; D10870; BAA01640.1; -; Genomic_DNA. DR EMBL; D10871; BAA01641.1; -; Genomic_DNA. DR EMBL; D10872; BAA01642.1; -; Genomic_DNA. DR EMBL; U23052; AAA64584.1; -; Genomic_DNA. DR EMBL; U23434; AAA64585.1; -; Genomic_DNA. DR EMBL; DQ305496; ABC26032.1; -; Genomic_DNA. DR EMBL; DQ305497; ABC26033.1; -; Genomic_DNA. DR EMBL; DQ305498; ABC26034.1; -; Genomic_DNA. DR EMBL; DQ305499; ABC26035.1; -; Genomic_DNA. DR EMBL; DQ305500; ABC26036.1; -; Genomic_DNA. DR EMBL; DQ305501; ABC26037.1; -; Genomic_DNA. DR EMBL; DQ305502; ABC26038.1; -; Genomic_DNA. DR EMBL; DQ305503; ABC26039.1; -; Genomic_DNA. DR EMBL; DQ305504; ABC26040.1; -; Genomic_DNA. DR EMBL; DQ305505; ABC26041.1; -; Genomic_DNA. DR EMBL; DQ305506; ABC26042.1; -; Genomic_DNA. DR EMBL; DQ305507; ABC26043.1; -; Genomic_DNA. DR EMBL; DQ305508; ABC26044.1; -; Genomic_DNA. DR EMBL; DQ305509; ABC26045.1; -; Genomic_DNA. DR EMBL; DQ305510; ABC26046.1; -; Genomic_DNA. DR EMBL; DQ305511; ABC26047.1; -; Genomic_DNA. DR EMBL; DQ305512; ABC26048.1; -; Genomic_DNA. DR EMBL; DQ305513; ABC26049.1; -; Genomic_DNA. DR EMBL; DQ305514; ABC26050.1; -; Genomic_DNA. DR EMBL; DQ305515; ABC26051.1; -; Genomic_DNA. DR EMBL; DQ305516; ABC26052.1; -; Genomic_DNA. DR EMBL; DQ305517; ABC26053.1; -; Genomic_DNA. DR EMBL; DQ305518; ABC26054.1; -; Genomic_DNA. DR EMBL; DQ305519; ABC26055.1; -; Genomic_DNA. DR EMBL; DQ305520; ABC26056.1; -; Genomic_DNA. DR EMBL; DQ305521; ABC26057.1; -; Genomic_DNA. DR EMBL; DQ305522; ABC26058.1; -; Genomic_DNA. DR EMBL; DQ305523; ABC26059.1; -; Genomic_DNA. DR EMBL; DQ305524; ABC26060.1; -; Genomic_DNA. DR EMBL; DQ305525; ABC26061.1; -; Genomic_DNA. DR EMBL; DQ305526; ABC26062.1; -; Genomic_DNA. DR EMBL; DQ305527; ABC26063.1; -; Genomic_DNA. DR EMBL; DQ305528; ABC26064.1; -; Genomic_DNA. DR EMBL; DQ305529; ABC26065.1; -; Genomic_DNA. DR EMBL; DQ305530; ABC26066.1; -; Genomic_DNA. DR EMBL; DQ305531; ABC26067.1; -; Genomic_DNA. DR EMBL; DQ305532; ABC26068.1; -; Genomic_DNA. DR EMBL; DQ305533; ABC26069.1; -; Genomic_DNA. DR EMBL; DQ305534; ABC26070.1; -; Genomic_DNA. DR EMBL; DQ305535; ABC26071.1; -; Genomic_DNA. DR EMBL; DQ305536; ABC26072.1; -; Genomic_DNA. DR EMBL; DQ305537; ABC26073.1; -; Genomic_DNA. DR EMBL; DQ305538; ABC26074.1; -; Genomic_DNA. DR EMBL; DQ305539; ABC26075.1; -; Genomic_DNA. DR EMBL; DQ305540; ABC26076.1; -; Genomic_DNA. DR EMBL; DQ305541; ABC26077.1; -; Genomic_DNA. DR EMBL; DQ305542; ABC26078.1; -; Genomic_DNA. DR EMBL; DQ305543; ABC26079.1; -; Genomic_DNA. DR EMBL; DQ305544; ABC26080.1; -; Genomic_DNA. DR EMBL; DQ305545; ABC26081.1; -; Genomic_DNA. DR EMBL; DQ305546; ABC26082.1; -; Genomic_DNA. DR EMBL; DQ305547; ABC26083.1; -; Genomic_DNA. DR EMBL; DQ305548; ABC26084.1; -; Genomic_DNA. DR EMBL; DQ305549; ABC26085.1; -; Genomic_DNA. DR EMBL; DQ305550; ABC26086.1; -; Genomic_DNA. DR EMBL; DQ305551; ABC26087.1; -; Genomic_DNA. DR EMBL; DQ305552; ABC26088.1; -; Genomic_DNA. DR EMBL; DQ305553; ABC26089.1; -; Genomic_DNA. DR EMBL; DQ305554; ABC26090.1; -; Genomic_DNA. DR EMBL; DQ305555; ABC26091.1; -; Genomic_DNA. DR EMBL; DQ305556; ABC26092.1; -; Genomic_DNA. DR EMBL; DQ305557; ABC26093.1; -; Genomic_DNA. DR EMBL; DQ305558; ABC26094.1; -; Genomic_DNA. DR EMBL; DQ305559; ABC26095.1; -; Genomic_DNA. DR EMBL; DQ305560; ABC26096.1; -; Genomic_DNA. DR EMBL; DQ305561; ABC26097.1; -; Genomic_DNA. DR EMBL; DQ305562; ABC26098.1; -; Genomic_DNA. DR EMBL; DQ305563; ABC26099.1; -; Genomic_DNA. DR EMBL; DQ305564; ABC26100.1; -; Genomic_DNA. DR EMBL; DQ305565; ABC26101.1; -; Genomic_DNA. DR EMBL; DQ305566; ABC26102.1; -; Genomic_DNA. DR EMBL; DQ305567; ABC26103.1; -; Genomic_DNA. DR EMBL; DQ305568; ABC26104.1; -; Genomic_DNA. DR EMBL; DQ305569; ABC26105.1; -; Genomic_DNA. DR EMBL; DQ305570; ABC26106.1; -; Genomic_DNA. DR EMBL; DQ305571; ABC26107.1; -; Genomic_DNA. DR EMBL; DQ305572; ABC26108.1; -; Genomic_DNA. DR EMBL; DQ305573; ABC26109.1; -; Genomic_DNA. DR EMBL; DQ305574; ABC26110.1; -; Genomic_DNA. DR EMBL; DQ305575; ABC26111.1; -; Genomic_DNA. DR EMBL; DQ305576; ABC26112.1; -; Genomic_DNA. DR EMBL; DQ305577; ABC26113.1; -; Genomic_DNA. DR EMBL; DQ305578; ABC26114.1; -; Genomic_DNA. DR EMBL; DQ305579; ABC26115.1; -; Genomic_DNA. DR EMBL; DQ305580; ABC26116.1; -; Genomic_DNA. DR EMBL; DQ305581; ABC26117.1; -; Genomic_DNA. DR EMBL; DQ305582; ABC26118.1; -; Genomic_DNA. DR EMBL; DQ305583; ABC26119.1; -; Genomic_DNA. DR EMBL; DQ305584; ABC26120.1; -; Genomic_DNA. DR EMBL; DQ305585; ABC26121.1; -; Genomic_DNA. DR EMBL; DQ305586; ABC26122.1; -; Genomic_DNA. DR EMBL; DQ305587; ABC26123.1; -; Genomic_DNA. DR EMBL; DQ305588; ABC26124.1; -; Genomic_DNA. DR EMBL; DQ305589; ABC26125.1; -; Genomic_DNA. DR EMBL; DQ305590; ABC26126.1; -; Genomic_DNA. DR EMBL; DQ305591; ABC26127.1; -; Genomic_DNA. DR EMBL; DQ305592; ABC26128.1; -; Genomic_DNA. DR EMBL; DQ305593; ABC26129.1; -; Genomic_DNA. DR EMBL; DQ305594; ABC26130.1; -; Genomic_DNA. DR EMBL; DQ305595; ABC26131.1; -; Genomic_DNA. DR EMBL; DQ305596; ABC26132.1; -; Genomic_DNA. DR EMBL; DQ305597; ABC26133.1; -; Genomic_DNA. DR EMBL; DQ305598; ABC26134.1; -; Genomic_DNA. DR EMBL; DQ305599; ABC26135.1; -; Genomic_DNA. DR EMBL; DQ305600; ABC26136.1; -; Genomic_DNA. DR EMBL; DQ305601; ABC26137.1; -; Genomic_DNA. DR EMBL; DQ305602; ABC26138.1; -; Genomic_DNA. DR EMBL; DQ305603; ABC26139.1; -; Genomic_DNA. DR EMBL; DQ305604; ABC26140.1; -; Genomic_DNA. DR EMBL; DQ305605; ABC26141.1; -; Genomic_DNA. DR EMBL; DQ305606; ABC26142.1; -; Genomic_DNA. DR EMBL; DQ305607; ABC26143.1; -; Genomic_DNA. DR EMBL; DQ305608; ABC26144.1; -; Genomic_DNA. DR EMBL; DQ305609; ABC26145.1; -; Genomic_DNA. DR EMBL; DQ305610; ABC26146.1; -; Genomic_DNA. DR EMBL; DQ305611; ABC26147.1; -; Genomic_DNA. DR EMBL; DQ305612; ABC26148.1; -; Genomic_DNA. DR EMBL; DQ305613; ABC26149.1; -; Genomic_DNA. DR EMBL; DQ305614; ABC26150.1; -; Genomic_DNA. DR EMBL; DQ305615; ABC26151.1; -; Genomic_DNA. DR EMBL; DQ305616; ABC26152.1; -; Genomic_DNA. DR EMBL; DQ305617; ABC26153.1; -; Genomic_DNA. DR EMBL; DQ305618; ABC26154.1; -; Genomic_DNA. DR EMBL; DQ305619; ABC26155.1; -; Genomic_DNA. DR EMBL; DQ305620; ABC26156.1; -; Genomic_DNA. DR EMBL; DQ305621; ABC26157.1; -; Genomic_DNA. DR EMBL; DQ305622; ABC26158.1; -; Genomic_DNA. DR EMBL; DQ305623; ABC26159.1; -; Genomic_DNA. DR EMBL; DQ305624; ABC26160.1; -; Genomic_DNA. DR EMBL; DQ305625; ABC26161.1; -; Genomic_DNA. DR EMBL; DQ305626; ABC26162.1; -; Genomic_DNA. DR EMBL; DQ305627; ABC26163.1; -; Genomic_DNA. DR EMBL; DQ305628; ABC26164.1; -; Genomic_DNA. DR EMBL; DQ305629; ABC26165.1; -; Genomic_DNA. DR EMBL; DQ305630; ABC26166.1; -; Genomic_DNA. DR EMBL; DQ305631; ABC26167.1; -; Genomic_DNA. DR EMBL; DQ305632; ABC26168.1; -; Genomic_DNA. DR EMBL; DQ305633; ABC26169.1; -; Genomic_DNA. DR EMBL; DQ305634; ABC26170.1; -; Genomic_DNA. DR EMBL; DQ305635; ABC26171.1; -; Genomic_DNA. DR EMBL; DQ305636; ABC26172.1; -; Genomic_DNA. DR EMBL; DQ305637; ABC26173.1; -; Genomic_DNA. DR EMBL; DQ305638; ABC26174.1; -; Genomic_DNA. DR EMBL; DQ305639; ABC26175.1; -; Genomic_DNA. DR EMBL; DQ305640; ABC26176.1; -; Genomic_DNA. DR EMBL; DQ305641; ABC26177.1; -; Genomic_DNA. DR EMBL; DQ305642; ABC26178.1; -; Genomic_DNA. DR EMBL; DQ305643; ABC26179.1; -; Genomic_DNA. DR EMBL; DQ305644; ABC26180.1; -; Genomic_DNA. DR EMBL; DQ305645; ABC26181.1; -; Genomic_DNA. DR EMBL; DQ305646; ABC26182.1; -; Genomic_DNA. DR EMBL; DQ305647; ABC26183.1; -; Genomic_DNA. DR EMBL; DQ305648; ABC26184.1; -; Genomic_DNA. DR EMBL; DQ305649; ABC26185.1; -; Genomic_DNA. DR EMBL; DQ305650; ABC26186.1; -; Genomic_DNA. DR EMBL; DQ305651; ABC26187.1; -; Genomic_DNA. DR EMBL; DQ305652; ABC26188.1; -; Genomic_DNA. DR EMBL; DQ305653; ABC26189.1; -; Genomic_DNA. DR EMBL; DQ305654; ABC26190.1; -; Genomic_DNA. DR EMBL; DQ305655; ABC26191.1; -; Genomic_DNA. DR EMBL; U53473; AAA98976.1; -; Genomic_DNA. DR EMBL; AF042740; AAC03773.1; -; Genomic_DNA. DR EMBL; AF055874; AAC14117.1; -; Genomic_DNA. DR EMBL; AF055875; AAC14118.1; -; Genomic_DNA. DR EMBL; AF320309; AAG34181.1; -; Genomic_DNA. DR EMBL; AF348074; AAK51710.1; -; Genomic_DNA. DR EMBL; AF348075; AAK51711.1; ALT_FRAME; Genomic_DNA. DR EMBL; AY230251; AAO73561.1; -; Genomic_DNA. DR EMBL; AY230252; AAO73562.1; -; Genomic_DNA. DR EMBL; CR407631; CAG28559.1; -; mRNA. DR EMBL; AY331807; AAP81164.1; -; Genomic_DNA. DR EMBL; AC025062; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC120051; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC015878; AAH15878.1; -; mRNA. DR EMBL; BC067218; AAH67218.1; -; mRNA. DR EMBL; M75163; AAA59906.1; -; Genomic_DNA. DR CCDS; CCDS6008.1; -. DR PIR; B34585; B34585. DR PIR; S02788; S02788. DR RefSeq; NP_000006.2; NM_000015.3. DR RefSeq; XP_016868427.1; XM_017012938.2. DR PDB; 2PFR; X-ray; 1.92 A; A/B=2-290. DR AlphaFoldDB; P11245; -. DR SMR; P11245; -. DR BioGRID; 106528; 23. DR FunCoup; P11245; 115. DR IntAct; P11245; 22. DR MINT; P11245; -. DR NDEx; IQUERY-CP-NAT2; 4 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000286479; -. DR ChEMBL; CHEMBL2194; -. DR DrugBank; DB00316; Acetaminophen. DR DrugBank; DB00945; Acetylsalicylic acid. DR DrugBank; DB11640; Amifampridine. DR DrugBank; DB01068; Clonazepam. DR DrugBank; DB00250; Dapsone. DR DrugBank; DB04953; Ezogabine. DR DrugBank; DB00951; Isoniazid. DR DrugBank; DB12612; Ozanimod. DR DrugBank; DB09288; Propacetamol. DR DrugBank; DB01015; Sulfamethoxazole. DR GlyGen; P11245; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P11245; -. DR PhosphoSitePlus; P11245; -. DR BioMuta; NAT2; -. DR DMDM; 114238; -. DR MassIVE; P11245; -. DR PaxDb; 9606-ENSP00000286479; -. DR PeptideAtlas; P11245; -. DR ProteomicsDB; 52728; -. DR Antibodypedia; 22356; 254 antibodies from 30 providers. DR DNASU; 10; -. DR Ensembl; ENST00000286479.4; ENSP00000286479.3; ENSG00000156006.6. DR Ensembl; ENST00000893781.1; ENSP00000563840.1; ENSG00000156006.6. DR Ensembl; ENST00000893782.1; ENSP00000563841.1; ENSG00000156006.6. DR Ensembl; ENST00000893783.1; ENSP00000563842.1; ENSG00000156006.6. DR GeneID; 10; -. DR KEGG; hsa:10; -. DR MANE-Select; ENST00000286479.4; ENSP00000286479.3; NM_000015.3; NP_000006.2. DR UCSC; uc003wyw.2; human. DR AGR; HGNC:7646; -. DR ClinPGx; PA18; -. DR CTD; 10; -. DR DisGeNET; 10; -. DR GeneCards; NAT2; -. DR HGNC; HGNC:7646; NAT2. DR HPA; ENSG00000156006; Group enriched (intestine, liver). DR MalaCards; NAT2; -. DR MIM; 243400; phenotype. DR MIM; 612182; gene. DR OpenTargets; ENSG00000156006; -. DR VEuPathDB; HostDB:ENSG00000156006; -. DR eggNOG; ENOG502RD0D; Eukaryota. DR GeneTree; ENSGT00390000012054; -. DR HOGENOM; CLU_049918_3_0_1; -. DR InParanoid; P11245; -. DR OMA; HCGQAME; -. DR OrthoDB; 9479791at2759; -. DR PAN-GO; P11245; 1 GO annotation based on evolutionary models. DR PhylomeDB; P11245; -. DR BRENDA; 2.3.1.5; 2681. DR BRENDA; 2.3.1.57; 2681. DR PathwayCommons; P11245; -. DR Reactome; R-HSA-156582; Acetylation. DR Reactome; R-HSA-9753281; Paracetamol ADME. DR SignaLink; P11245; -. DR Agora; ENSG00000156006; -. DR BioGRID-ORCS; 10; 12 hits in 1145 CRISPR screens. DR ChiTaRS; NAT2; human. DR EvolutionaryTrace; P11245; -. DR GeneWiki; N-acetyltransferase_2; -. DR GenomeRNAi; 10; -. DR Pharos; P11245; Tbio. DR PRO; PR:P11245; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; P11245; protein. DR Bgee; ENSG00000156006; Expressed in right lobe of liver and 89 other cell types or tissues. DR ExpressionAtlas; P11245; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0004060; F:arylamine N-acetyltransferase activity; EXP:UniProtKB. DR GO; GO:0046990; F:N-hydroxyarylamine O-acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0019707; F:protein-cysteine S-acyltransferase activity; TAS:Reactome. DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome. DR FunFam; 3.30.2140.20:FF:000001; Arylamine N-acetyltransferase 1; 1. DR Gene3D; 3.30.2140.20; -; 1. DR InterPro; IPR001447; Arylamine_N-AcTrfase. DR InterPro; IPR053710; Arylamine_NAT_domain_sf. DR InterPro; IPR038765; Papain-like_cys_pep_sf. DR PANTHER; PTHR11786:SF6; ARYLAMINE N-ACETYLTRANSFERASE 2; 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 PDBsum; 2PFR; -. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Cytoplasm; Direct protein sequencing; KW Proteomics identification; Reference proteome; Transferase. FT CHAIN 1..290 FT /note="Arylamine N-acetyltransferase 2" FT /id="PRO_0000107905" FT ACT_SITE 68 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000305|PubMed:17656365" FT ACT_SITE 107 FT /evidence="ECO:0000305|PubMed:17656365" FT ACT_SITE 122 FT /evidence="ECO:0000305|PubMed:17656365" FT BINDING 103 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000269|PubMed:17656365" FT BINDING 104 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000269|PubMed:17656365" FT BINDING 106..107 FT /ligand="substrate" FT /evidence="ECO:0000305" FT BINDING 208 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000269|PubMed:17656365" FT BINDING 214 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000269|PubMed:17656365" FT BINDING 287 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000269|PubMed:17656365" FT VARIANT 24 FT /note="L -> I (in allele NAT2*5L; dbSNP:rs45477599)" FT /evidence="ECO:0000269|PubMed:16416399, ECO:0000269|Ref.14" FT /id="VAR_018853" FT VARIANT 64 FT /note="R -> Q (in allele NAT2*14A, allele NAT2*14B, allele FT NAT2*14C, allele NAT2*14D, allele NAT2*14E, allele NAT2*14F FT and allele NAT2*14G; 5 to 6-fold lower Vmax and decreased FT arylamine N-acetyltransferase activity when associated in FT cis with K-268; dbSNP:rs1801279)" FT /evidence="ECO:0000269|PubMed:11337936, FT ECO:0000269|PubMed:16416399, ECO:0000269|PubMed:18304320, FT ECO:0000269|PubMed:7915226, ECO:0000269|Ref.14, FT ECO:0000269|Ref.8" FT /id="VAR_004608" FT VARIANT 64 FT /note="R -> W (in allele NAT2*19; decreased arylamine FT N-acetyltransferase activity when associated in cis with FT K-268; decreased N-hydroxyarylamine O-acetyltransferase FT when associated in cis with K-268; dbSNP:rs1805158)" FT /evidence="ECO:0000269|PubMed:10970160, FT ECO:0000269|PubMed:12222688" FT /id="VAR_009075" FT VARIANT 114 FT /note="I -> T (in allele NAT2*5A, allele NAT2*5B, allele FT NAT2*5C, allele NAT2*5D, allele NAT2*5E, allele NAT2*5F, FT allele NAT2*5G, allele NAT2*5I, allele NAT2*5K, allele FT NAT2*5L, allele NAT2*5M, allele NAT2*14C and allele FT NAT2*14F; 7 to 12-fold lower Vmax; decreased arylamine FT N-acetyltransferase activity when associated in cis with FT K-268; loss of arylamine N-acetyltransferase activity when FT associated in cis with F-137; dbSNP:rs1801280)" FT /evidence="ECO:0000269|PubMed:11337936, FT ECO:0000269|PubMed:16416399, ECO:0000269|PubMed:17264801, FT ECO:0000269|PubMed:18304320, ECO:0000269|PubMed:7915226, FT ECO:0000269|Ref.10, ECO:0000269|Ref.11, ECO:0000269|Ref.12, FT ECO:0000269|Ref.14, ECO:0000269|Ref.8, ECO:0000269|Ref.9" FT /id="VAR_004609" FT VARIANT 122 FT /note="D -> N (in allele NAT2*12D; loss of arylamine FT N-acetyltransferase activity; loss of arylamine FT N-acetyltransferase activity when associated in cis with FT K-268; dbSNP:rs4986996)" FT /evidence="ECO:0000269|PubMed:17264801, ECO:0000269|Ref.12" FT /id="VAR_020385" FT VARIANT 135 FT /note="L -> V (in allele NAT2*12H; dbSNP:rs12720065)" FT /evidence="ECO:0000269|PubMed:18304320" FT /id="VAR_046905" FT VARIANT 137 FT /note="L -> F (in allele NAT2*5I; loss of arylamine FT N-acetyltransferase activity when associated in cis with FT T-114; severely decreased arylamine N-acetyltransferase FT activity when associated in cis with K-268; FT dbSNP:rs4986997)" FT /evidence="ECO:0000269|PubMed:17264801, ECO:0000269|Ref.12" FT /id="VAR_020386" FT VARIANT 145 FT /note="Q -> P (in allele NAT2*17; loss of arylamine FT N-acetyltransferase activity when associated in cis with FT K-268; dbSNP:rs72554616)" FT /evidence="ECO:0000269|PubMed:11337936, FT ECO:0000269|PubMed:7920692" FT /id="VAR_009076" FT VARIANT 193 FT /note="T -> M (in allele NAT2*12E; dbSNP:rs79050330)" FT /evidence="ECO:0000269|PubMed:16416399" FT /id="VAR_028781" FT VARIANT 197 FT /note="R -> Q (in allele NAT2*5E, allele NAT2*6A, allele FT NAT2*6B, allele NAT2*6C, allele NAT2*6D, allele NAT2*6J, FT allele NAT2*6K, allele NAT2*6L and allele NAT2*14D; FT decreased arylamine N-acetyltransferase activity when FT associated in cis with K-268; dbSNP:rs1799930)" FT /evidence="ECO:0000269|PubMed:11337936, FT ECO:0000269|PubMed:1381364, ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:16416399, ECO:0000269|PubMed:18304320, FT ECO:0000269|Ref.14, ECO:0000269|Ref.8" FT /id="VAR_004610" FT VARIANT 203 FT /note="E -> D (in allele NAT2*12G; dbSNP:rs45618543)" FT /evidence="ECO:0000269|PubMed:18304320" FT /id="VAR_089009" FT VARIANT 208 FT /note="Y -> H (in allele NAT2*12F; dbSNP:rs56387565)" FT /evidence="ECO:0000269|PubMed:16416399" FT /id="VAR_028782" FT VARIANT 213 FT /note="P -> L (in allele NAT2*6K; dbSNP:rs138707146)" FT /evidence="ECO:0000269|PubMed:18304320" FT /id="VAR_089010" FT VARIANT 228 FT /note="P -> L (in dbSNP:rs45518335)" FT /evidence="ECO:0000269|Ref.14" FT /id="VAR_018854" FT VARIANT 268 FT /note="R -> K (in allele NAT2*4, allele NAT2*5A, allele FT NAT2*5D, allele NAT2*5E, allele NAT2*5K, allele NAT2*6A, FT allele NAT2*6B, allele NAT2*6D, allele NAT2*6J, allele FT NAT2*6K, allele NAT2*6L, allele NAT2*7A, allele NAT2*7B, FT allele NAT2*13A, allele NAT2*14A, allele NAT2*14B, allele FT NAT2*14D, allele NAT2*17, allele NAT2*18 and allele FT NAT2*19; no effect on arylamine N-acetyltransferase FT activity; decreased arylamine N-acetyltransferase activity FT when associated in cis with W-64; decreased FT N-hydroxyarylamine O-acetyltransferase when associated in FT cis with W-64; 5 to 6-fold lower Vmax and decreased FT arylamine N-acetyltransferase activity when associated in FT cis with Q-64; decreased arylamine N-acetyltransferase FT activity when associated in cis with T-114; loss of FT arylamine N-acetyltransferase activity when associated in FT cis with N-122; severely decreased arylamine FT N-acetyltransferase activity when associated in cis with FT F-137; decreased arylamine N-acetyltransferase activity FT when associated in cis with Q-197; loss of arylamine FT N-acetyltransferase activity when associated in cis with FT P-145; no effect on arylamine N-acetyltransferase activity FT when associated in cis with T-282; no effect on arylamine FT N-acetyltransferase activity when associated in cis with FT E-286; dbSNP:rs1208)" FT /evidence="ECO:0000269|PubMed:10970160, FT ECO:0000269|PubMed:11337936, ECO:0000269|PubMed:12222688, FT ECO:0000269|PubMed:16416399, ECO:0000269|PubMed:17264801, FT ECO:0000269|PubMed:18304320, ECO:0000269|PubMed:2340091, FT ECO:0000269|PubMed:2734109, ECO:0000269|PubMed:7915226, FT ECO:0000269|Ref.10, ECO:0000269|Ref.11, ECO:0000269|Ref.12, FT ECO:0000269|Ref.14, ECO:0000269|Ref.7, ECO:0000269|Ref.8" FT /id="VAR_004611" FT VARIANT 280 FT /note="V -> M (in allele NAT2*5M; dbSNP:rs56393504)" FT /evidence="ECO:0000269|PubMed:18304320" FT /id="VAR_061368" FT VARIANT 282 FT /note="K -> T (in allele NAT2*18; no effect on arylamine FT N-acetyltransferase activity when associated in cis with FT K-268; dbSNP:rs56054745)" FT /evidence="ECO:0000269|PubMed:11337936, FT ECO:0000269|PubMed:7920692" FT /id="VAR_009077" FT VARIANT 286 FT /note="G -> E (in allele NAT2*6J, allele NAT2*7A and allele FT NAT2*7B; no effect on arylamine N-acetyltransferase FT activity when associated in cis with K-268; FT dbSNP:rs1799931)" FT /evidence="ECO:0000269|PubMed:11337936, FT ECO:0000269|PubMed:1381364, ECO:0000269|PubMed:16416399, FT ECO:0000269|PubMed:18304320, ECO:0000269|PubMed:1968463, FT ECO:0000269|Ref.14" FT /id="VAR_004612" FT CONFLICT 6 FT /note="Y -> D (in Ref. 13; CAG28559)" FT /evidence="ECO:0000305" FT CONFLICT 30 FT /note="H -> T (in Ref. 18; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 286 FT /note="G -> R (in Ref. 9; AAG34181)" FT /evidence="ECO:0000305" FT HELIX 2..9 FT /evidence="ECO:0007829|PDB:2PFR" FT HELIX 21..34 FT /evidence="ECO:0007829|PDB:2PFR" FT HELIX 40..43 FT /evidence="ECO:0007829|PDB:2PFR" FT HELIX 52..56 FT /evidence="ECO:0007829|PDB:2PFR" FT HELIX 57..61 FT /evidence="ECO:0007829|PDB:2PFR" FT HELIX 68..82 FT /evidence="ECO:0007829|PDB:2PFR" FT STRAND 85..95 FT /evidence="ECO:0007829|PDB:2PFR" FT HELIX 96..98 FT /evidence="ECO:0007829|PDB:2PFR" FT STRAND 107..114 FT /evidence="ECO:0007829|PDB:2PFR" FT STRAND 117..121 FT /evidence="ECO:0007829|PDB:2PFR" FT HELIX 127..129 FT /evidence="ECO:0007829|PDB:2PFR" FT STRAND 142..144 FT /evidence="ECO:0007829|PDB:2PFR" FT STRAND 149..155 FT /evidence="ECO:0007829|PDB:2PFR" FT STRAND 158..164 FT /evidence="ECO:0007829|PDB:2PFR" FT STRAND 167..171 FT /evidence="ECO:0007829|PDB:2PFR" FT HELIX 173..175 FT /evidence="ECO:0007829|PDB:2PFR" FT STRAND 185..192 FT /evidence="ECO:0007829|PDB:2PFR" FT HELIX 199..202 FT /evidence="ECO:0007829|PDB:2PFR" FT HELIX 203..211 FT /evidence="ECO:0007829|PDB:2PFR" FT HELIX 216..219 FT /evidence="ECO:0007829|PDB:2PFR" FT STRAND 222..226 FT /evidence="ECO:0007829|PDB:2PFR" FT STRAND 228..235 FT /evidence="ECO:0007829|PDB:2PFR" FT STRAND 238..247 FT /evidence="ECO:0007829|PDB:2PFR" FT STRAND 250..257 FT /evidence="ECO:0007829|PDB:2PFR" FT HELIX 260..269 FT /evidence="ECO:0007829|PDB:2PFR" FT STRAND 285..288 FT /evidence="ECO:0007829|PDB:2PFR" SQ SEQUENCE 290 AA; 33571 MW; FAEE3BC2107F000E CRC64; MDIEAYFERI GYKNSRNKLD LETLTDILEH QIRAVPFENL NMHCGQAMEL GLEAIFDHIV RRNRGGWCLQ VNQLLYWALT TIGFQTTMLG GYFYIPPVNK YSTGMVHLLL QVTIDGRNYI VDAGSGSSSQ MWQPLELISG KDQPQVPCIF CLTEERGIWY LDQIRREQYI TNKEFLNSHL LPKKKHQKIY LFTLEPRTIE DFESMNTYLQ TSPTSSFITT SFCSLQTPEG VYCLVGFILT YRKFNYKDNT DLVEFKTLTE EEVEEVLRNI FKISLGRNLV PKPGDGSLTI //