ID ARY2_RABIT Reviewed; 290 AA. AC P11246; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 02-SEP-2026, entry version 111. DE RecName: Full=Arylamine N-acetyltransferase 2; DE EC=2.3.1.5 {ECO:0000250|UniProtKB:P11245}; DE AltName: Full=Arylamide acetylase 2; DE AltName: Full=N-acetyltransferase type 2; DE Short=NAT-2; DE AltName: Full=N-hydroxyarylamine O-acetyltransferase; DE EC=2.3.1.118 {ECO:0000250|UniProtKB:P11245}; DE AltName: Full=Polymorphic arylamine N-acetyltransferase; DE Short=PNAT; GN Name=NAT2; Synonyms=AAC2; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=New Zealand white; TISSUE=Liver; RX PubMed=2726493; DOI=10.1093/nar/17.9.3589; RA Blum M., Grant D.M., Demierre A., Meyer U.A.; RT "Nucleotide sequence of a full-length cDNA for arylamine N- RT acetyltransferase from rabbit liver."; RL Nucleic Acids Res. 17:3589-3589(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=New Zealand white; RX PubMed=2402461; DOI=10.1093/nar/18.17.5295; RA Blum M., Heim M., Meyer U.A.; RT "Nucleotide sequence of rabbit NAT2 encoding polymorphic liver arylamine N- RT acetyltransferase (NAT)."; RL Nucleic Acids Res. 18:5295-5295(1990). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC STRAIN=New Zealand white; TISSUE=Liver; RX PubMed=2071601; DOI=10.1016/s0021-9258(18)98830-7; RA Sasaki Y., Ohsako S., Deguchi T.; RT "Molecular and genetic analyses of arylamine N-acetyltransferase RT polymorphism of rabbit liver."; RL J. Biol. Chem. 266:13243-13250(1991). RN [4] RP PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION. RX PubMed=3574290; DOI=10.1016/s0026-895x(25)10455-0; RA Andres H.H., Vogel R.S., Tarr G.E., Johnson L., Weber W.W.; RT "Purification, physicochemical, and kinetic properties of liver acetyl- RT CoA:arylamine N-acetyltransferase from rapid acetylator rabbits."; RL Mol. Pharmacol. 31:446-456(1987). CC -!- FUNCTION: Catalyzes the N- or O-acetylation of various arylamine and CC heterocyclic amine substrates, and participates in the detoxification CC of a plethora of hydrazine and arylamine drugs. CC {ECO:0000250|UniProtKB:P11245}. 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:0000250|UniProtKB:P11245}; 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:0000250|UniProtKB:P11245}; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- PTM: The N-terminus is blocked. CC -!- SIMILARITY: Belongs to the arylamine N-acetyltransferase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X14673; CAA32803.1; -; mRNA. DR EMBL; X53767; CAA37786.1; -; Genomic_DNA. DR EMBL; D10109; BAA00990.1; -; Genomic_DNA. DR EMBL; D10111; BAA00991.1; -; mRNA. DR PIR; A39870; XYRBPR. DR RefSeq; NP_001075655.1; NM_001082186.1. DR AlphaFoldDB; P11246; -. DR SMR; P11246; -. DR FunCoup; P11246; 49. DR GeneID; 100008974; -. DR KEGG; ocu:100008974; -. DR CTD; 9; -. DR InParanoid; P11246; -. DR OrthoDB; 10260017at2759; -. DR Proteomes; UP000001811; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004060; F:arylamine N-acetyltransferase activity; ISS:UniProtKB. DR GO; GO:0046990; F:N-hydroxyarylamine O-acetyltransferase activity; ISS:UniProtKB. 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: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. PE 1: Evidence at protein level; KW Acyltransferase; Cytoplasm; Direct protein sequencing; Reference proteome; KW Transferase. FT CHAIN 1..290 FT /note="Arylamine N-acetyltransferase 2" FT /id="PRO_0000107914" FT ACT_SITE 68 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000250|UniProtKB:P11245" FT ACT_SITE 107 FT /evidence="ECO:0000250|UniProtKB:P11245" FT ACT_SITE 122 FT /evidence="ECO:0000250|UniProtKB:P11245" FT BINDING 103 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000250|UniProtKB:P11245" FT BINDING 104 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000250|UniProtKB:P11245" FT BINDING 106..107 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11245" FT BINDING 208 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000250|UniProtKB:P11245" FT BINDING 214 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000250|UniProtKB:P11245" FT BINDING 287 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000250|UniProtKB:P11245" SQ SEQUENCE 290 AA; 33649 MW; CF0ECBED398C352A CRC64; MDIEAYYQRI GYKNPRNKLD LESLTDIFQH QIRTVPYENL SIHCGESMEL DLEAIFDQIV RRNRGGWCLQ VNYLLYWALT TTGFETTMLG GFVYGSNNDK YSTGMIHLIV QVTINGRNYI VDAGFGRSYQ MWQPVELISG KDQPQVPSIF RLREEGETWY LDQIRRQQHV PDQEFLNSEL LEKKIYQKLY CFTLQPRTIE EFESANTYLQ ESPSSVFLDK SICSLQTPEG VHCLVGLTLT SRTYNYKENT DLVEFKVLTE EEVEGVLKTI FNISLGKKLV SKNGHLSFTI //