ID   ARY2_MESAU              Reviewed;         290 AA.
AC   P50293;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=AT-2;
DE            Short=NAT-2;
DE   AltName: Full=Polymorphic arylamine N-acetyltransferase;
DE            Short=PNAT;
GN   Name=NAT2; Synonyms=AAC2;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Heart;
RX   PubMed=8144033; DOI=10.1016/0378-1119(94)90552-5;
RA   Ferguson R.J., Doll M.A., Baumstark B.R., Hein D.W.;
RT   "Polymorphic arylamine N-acetyltransferase encoding gene (NAT2) from
RT   homozygous rapid and slow acetylator congenic Syrian hamsters.";
RL   Gene 140:247-249(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Liver;
RX   PubMed=8055637; DOI=10.1093/carcin/15.8.1585;
RA   Land S.J., Jones R.F., King C.M.;
RT   "Biochemical and genetic analysis of two acetyltransferases from hamster
RT   tissues that can metabolize aromatic amine derivatives.";
RL   Carcinogenesis 15:1585-1595(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7915937; DOI=10.1097/00008571-199404000-00006;
RA   Nagata K., Ozawa S., Miyata M., Shimada M., Yamazoe Y., Kato R.;
RT   "Primary structure and molecular basis of polymorphic appearance of an
RT   acetyltransferase (AT-II)* in hamsters.";
RL   Pharmacogenetics 4:91-100(1994).
CC   -!- FUNCTION: Participates in the detoxification of a plethora of hydrazine
CC       and arylamine drugs.
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: There are two forms of NAT2: a rapid isoform and a slow
CC       isoform. {ECO:0000269|PubMed:8144033}.
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; U03468; AAB60524.1; -; Genomic_DNA.
DR   EMBL; U03467; AAB60523.1; -; Genomic_DNA.
DR   EMBL; L24912; AAA21829.1; -; mRNA.
DR   EMBL; S72005; AAB31917.1; -; Genomic_DNA.
DR   EMBL; S72007; AAB31918.1; -; Genomic_DNA.
DR   PIR; I78930; I78930.
DR   PIR; I78931; I78931.
DR   RefSeq; NP_001268752.1; NM_001281823.1.
DR   RefSeq; XP_012972609.1; XM_013117155.1.
DR   RefSeq; XP_012972610.1; XM_013117156.1.
DR   RefSeq; XP_012972611.1; XM_013117157.1.
DR   RefSeq; XP_012972612.1; XM_013117158.1.
DR   AlphaFoldDB; P50293; -.
DR   SMR; P50293; -.
DR   STRING; 10036.XP_005075251.1; -.
DR   BindingDB; P50293; -.
DR   ChEMBL; CHEMBL3259464; -.
DR   GeneID; 101840555; -.
DR   CTD; 10; -.
DR   eggNOG; ENOG502RD0D; Eukaryota.
DR   OrthoDB; 1545569at2759; -.
DR   BRENDA; 2.3.1.5; 3239.
DR   BRENDA; 2.3.1.56; 3239.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004060; F:arylamine N-acetyltransferase activity; IEA:UniProtKB-EC.
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   2: Evidence at transcript level;
KW   Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..290
FT                   /note="Arylamine N-acetyltransferase 2"
FT                   /id="PRO_0000107907"
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   VARIANT         243..290
FT                   /note="Missing (in slow isoform)"
SQ   SEQUENCE   290 AA;  33833 MW;  54C10F5F6990F6FD CRC64;
     MDIEAYFERI GYQNSRNKLD LQTLTEILQH QIRAIPFENL NIHCGESMEL SLETIFDQIV
     RKKRGGWCLQ VNHLLYWALT KMGFETTMLG GYVFNTPANK YSSGMIHLLV QVTISDRNYI
     VDAGFGRSLQ MWEPLELVSG KDHPQVPAIF RLTEENETWY LDQIRREQYV PNQAFVNSDL
     LEKNKYRKIY SFTLEPRTIE DFESMNTYLQ TSPASVFTSK SFCSLQTPEG VHCLVGCTLT
     YRRFSYKDNV DLVEFKSLKE EEIEDVLKTI FGISLEKKLV PKHGDRFFTI