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   03-AUG-2022, entry version 101.
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;
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;
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   -!- 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   -!- 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   GeneID; 100008974; -.
DR   KEGG; ocu:100008974; -.
DR   CTD; 10; -.
DR   InParanoid; P11246; -.
DR   Proteomes; UP000001811; 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   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"
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"
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