ID   ARY2_MACMU              Reviewed;         290 AA.
AC   Q7YRG5; Q7YRG6;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Arylamine N-acetyltransferase 2;
DE            EC=2.3.1.5;
DE   AltName: Full=Arylamide acetylase 2;
DE   AltName: Full=N-acetyltransferase type 2;
DE            Short=NAT-2;
DE   AltName: Full=Polymorphic arylamine N-acetyltransferase;
DE            Short=PNAT;
GN   Name=NAT2; Synonyms=AAC2, NAT;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-231.
RA   Fakis G., Boukouvala S., Sim E., Kennedy S.;
RT   "Cloning of a gene encoding for arylamine N-acetyltransferase in the rhezus
RT   monkey; description and functional analysis of two polymorphic alleles.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the arylamine N-acetyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ504439; CAD43197.1; -; Genomic_DNA.
DR   EMBL; AJ504440; CAD43198.1; -; Genomic_DNA.
DR   RefSeq; NP_001038201.1; NM_001044736.1.
DR   RefSeq; XP_015000281.1; XM_015144795.1.
DR   AlphaFoldDB; Q7YRG5; -.
DR   SMR; Q7YRG5; -.
DR   STRING; 9544.ENSMMUP00000028547; -.
DR   Ensembl; ENSMMUT00000030505; ENSMMUP00000028547; ENSMMUG00000021680.
DR   GeneID; 704357; -.
DR   KEGG; mcc:704357; -.
DR   CTD; 10; -.
DR   VEuPathDB; HostDB:ENSMMUG00000021680; -.
DR   VGNC; VGNC:84092; NAT2.
DR   eggNOG; ENOG502RD0D; Eukaryota.
DR   GeneTree; ENSGT00390000012054; -.
DR   HOGENOM; CLU_049918_3_0_1; -.
DR   InParanoid; Q7YRG5; -.
DR   OMA; THQKVYS; -.
DR   TreeFam; TF106311; -.
DR   BRENDA; 2.3.1.5; 3126.
DR   Proteomes; UP000006718; Chromosome 8.
DR   Bgee; ENSMMUG00000021680; Expressed in liver and 9 other tissues.
DR   ExpressionAtlas; Q7YRG5; baseline.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004060; F:arylamine N-acetyltransferase activity; IBA:GO_Central.
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   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..290
FT                   /note="Arylamine N-acetyltransferase 2"
FT                   /id="PRO_0000254005"
FT   ACT_SITE        68
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        107
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        122
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         106..107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         208
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         214
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         287
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   VARIANT         231
FT                   /note="V -> I (in allele 2)"
FT                   /evidence="ECO:0000269|Ref.1"
SQ   SEQUENCE   290 AA;  33429 MW;  36C686573BDC79A0 CRC64;
     MDIEAYFERI GYKNSRNKLD LETLTDILEH QIRAVPFENL NMHCGEAMEL GLETIFDHIV
     RRNRGGWCLQ VNQLLYWALT TIGFQTTMLG GYVYIPAANK YSTGMIHLLL QVTIDGRNYI
     ADAGFGSSSQ MWQPLELISG KDQPQMPSIF RLTEQKGIWY LDQIRREQYI PNTEFLNSDL
     LPKTTHQKVY SFTLEPRKIE DFESMNTYLQ TSPTSAFTTT SFCSLQTPEG VHCLVGFTLT
     YRIFNYKDNT DLIEFKTLIE EEVEEVLKNI FKISLGRKLV PKPGNGSFTI