ARY1_BOVIN
ID ARY1_BOVIN Reviewed; 290 AA.
AC Q1JPA6;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Arylamine N-acetyltransferase 1;
DE EC=2.3.1.5;
DE AltName: Full=Arylamide acetylase 1;
DE AltName: Full=N-acetyltransferase type 1;
DE Short=NAT-1;
GN Name=NAT1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Participates in the detoxification of a plethora of hydrazine
CC and arylamine drugs. {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; BT025447; ABF57403.1; -; mRNA.
DR EMBL; BC123764; AAI23765.1; -; mRNA.
DR RefSeq; NP_001069040.1; NM_001075572.1.
DR RefSeq; XP_005226217.1; XM_005226160.3.
DR RefSeq; XP_005226218.1; XM_005226161.3.
DR RefSeq; XP_005226219.1; XM_005226162.3.
DR RefSeq; XP_005226220.1; XM_005226163.3.
DR RefSeq; XP_005226221.1; XM_005226164.3.
DR RefSeq; XP_010818673.1; XM_010820371.2.
DR RefSeq; XP_010818674.1; XM_010820372.1.
DR AlphaFoldDB; Q1JPA6; -.
DR SMR; Q1JPA6; -.
DR STRING; 9913.ENSBTAP00000045530; -.
DR PaxDb; Q1JPA6; -.
DR PRIDE; Q1JPA6; -.
DR Ensembl; ENSBTAT00000048506; ENSBTAP00000045530; ENSBTAG00000016473.
DR GeneID; 512603; -.
DR KEGG; bta:512603; -.
DR CTD; 9; -.
DR VEuPathDB; HostDB:ENSBTAG00000016473; -.
DR eggNOG; ENOG502RD0D; Eukaryota.
DR GeneTree; ENSGT00390000012054; -.
DR HOGENOM; CLU_049918_3_0_1; -.
DR InParanoid; Q1JPA6; -.
DR OMA; CYEHNTL; -.
DR OrthoDB; 1545569at2759; -.
DR TreeFam; TF106311; -.
DR Reactome; R-BTA-156582; Acetylation.
DR Reactome; R-BTA-9753281; Paracetamol ADME.
DR Proteomes; UP000009136; Chromosome 27.
DR Bgee; ENSBTAG00000016473; Expressed in rumen papilla and 104 other tissues.
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 2: Evidence at transcript level;
KW Acetylation; Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..290
FT /note="Arylamine N-acetyltransferase 1"
FT /id="PRO_0000284078"
FT BINDING 103
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 MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P18440"
SQ SEQUENCE 290 AA; 34199 MW; 72E4A2B7C0F70F4C CRC64;
MDIDAYFERI GYKNSRDKLD LETLTDILQH QIRAIPFENL NIHCGEAMEL DLEVIFDQIV
RRKRGGWCLQ VNHLLYWALT MIGFETTILG GYVYNTFNDK YSSAMIHLLL KVTIDGRDYI
ADAGFGRSYQ MWQPLELISG KYQPQTPCIF RLTEDRGTWY LDQIRREQYI PNQDFLDSDL
LEKNEYRKIY SFTLEPRTIK DFESVNTYLQ ESPASVFTSK SFCSLQTPEG VHCLVGFTLT
YRRFNYKDNT DLVEFKTLNE KEIEENLKNI FNISLEKKLT PKHGDKFFTI