ID   A9X854_HUMAN            Unreviewed;       290 AA.
AC   A9X854;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   14-DEC-2022, entry version 53.
DE   RecName: Full=arylamine N-acetyltransferase {ECO:0000256|ARBA:ARBA00012701};
DE            EC=2.3.1.5 {ECO:0000256|ARBA:ARBA00012701};
GN   Name=NAT2 {ECO:0000313|EMBL:ABK34716.1};
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 {ECO:0000313|EMBL:ABK34716.1};
RN   [1] {ECO:0000313|EMBL:ABK34716.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MAN80_N2 {ECO:0000313|EMBL:ABK34716.1}, MAN82_N2
RC   {ECO:0000313|EMBL:ABK34720.1}, MAN88_N2 {ECO:0000313|EMBL:ABK34732.1},
RC   and MAN92_N2 {ECO:0000313|EMBL:ABK34740.1};
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).
RN   [2] {ECO:0000313|EMBL:ALN12634.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26620671; DOI=10.1186/s12862-015-0543-6;
RA   Podgorna E., Diallo I., Vangenot C., Sanchez-Mazas A., Sabbagh A.,
RA   Cerny V., Poloni E.S.;
RT   "Variation in NAT2 acetylation phenotypes is associated with differences in
RT   food-producing subsistence modes and ecoregions in Africa.";
RL   BMC Evol. Biol. 15:263-263(2015).
CC   -!- SIMILARITY: Belongs to the arylamine N-acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00006547, ECO:0000256|RuleBase:RU003452}.
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DR   EMBL; DQ904199; ABK34716.1; -; Genomic_DNA.
DR   EMBL; DQ904203; ABK34720.1; -; Genomic_DNA.
DR   EMBL; DQ904215; ABK34732.1; -; Genomic_DNA.
DR   EMBL; DQ904223; ABK34740.1; -; Genomic_DNA.
DR   EMBL; KR231065; ALN12634.1; -; Genomic_DNA.
DR   EMBL; KR231094; ALN12663.1; -; Genomic_DNA.
DR   EMBL; KR231113; ALN12682.1; -; Genomic_DNA.
DR   EMBL; KR231115; ALN12684.1; -; Genomic_DNA.
DR   EMBL; KR231205; ALN12774.1; -; Genomic_DNA.
DR   EMBL; KR231215; ALN12784.1; -; Genomic_DNA.
DR   EMBL; KR231355; ALN12924.1; -; Genomic_DNA.
DR   EMBL; KR231541; ALN13110.1; -; Genomic_DNA.
DR   EMBL; KR231567; ALN13136.1; -; Genomic_DNA.
DR   EMBL; KR231572; ALN13141.1; -; Genomic_DNA.
DR   EMBL; KR231598; ALN13167.1; -; Genomic_DNA.
DR   EMBL; KR231600; ALN13169.1; -; Genomic_DNA.
DR   EMBL; KR231603; ALN13172.1; -; Genomic_DNA.
DR   EMBL; KR231606; ALN13175.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9X854; -.
DR   PeptideAtlas; A9X854; -.
DR   ChiTaRS; NAT2; human.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; N-HYDROXYARYLAMINE O-ACETYLTRANSFERASE; 1.
DR   Pfam; PF00797; Acetyltransf_2; 1.
DR   PRINTS; PR01543; ANATRNSFRASE.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003452};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000256|RuleBase:RU003452, ECO:0000313|EMBL:ABK34716.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        74..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   290 AA;  33556 MW;  FAFA8486EE9541B4 CRC64;
     MDIEAYFERI GYKNSRNKLD LETLTDILEH QIRAVPFENL NMHCGQAMEL GLEAIFDHIV
     RRNRGGWCLQ VNQLLYWALT TIGFQTTMLG GYFYIPPVNK YSTGMVHLLL QVTIDGRNYI
     VDAGSGSSSQ MWQPVELISG KDQPQVPCIF CLTEERGIWY LDQIRREQYI TNKEFLNSHL
     LPKKKHQKIY LFTLEPRTIE DFESMNTYLQ TSPTSSFITT SFCSLQTPEG VYCLVGFILT
     YRKFNYKDNT DLVEFKTLTE EEVEEVLRNI FKISLGRNLV PKPGDGSLTI
//