ARY3_MOUSE
ID ARY3_MOUSE Reviewed; 290 AA.
AC P50296;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Arylamine N-acetyltransferase 3;
DE EC=2.3.1.5;
DE AltName: Full=Arylamide acetylase 3;
DE AltName: Full=N-acetyltransferase type 3;
DE Short=NAT-3;
GN Name=Nat3; Synonyms=Aac3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=7545952; DOI=10.1042/bj3020347;
RA Kelly S.L., Sim E.;
RT "Arylamine N-acetyltransferase in Balb/c mice: identification of a novel
RT mouse isoenzyme by cloning and expression in vitro.";
RL Biochem. J. 302:347-353(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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 -!- SIMILARITY: Belongs to the arylamine N-acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; X72959; CAA51461.1; -; Genomic_DNA.
DR EMBL; AK077364; BAC36769.1; -; mRNA.
DR CCDS; CCDS22339.1; -.
DR PIR; S55276; S55276.
DR RefSeq; NP_032700.1; NM_008674.2.
DR AlphaFoldDB; P50296; -.
DR SMR; P50296; -.
DR STRING; 10090.ENSMUSP00000069359; -.
DR PhosphoSitePlus; P50296; -.
DR jPOST; P50296; -.
DR PaxDb; P50296; -.
DR PeptideAtlas; P50296; -.
DR PRIDE; P50296; -.
DR DNASU; 17962; -.
DR Ensembl; ENSMUST00000070514; ENSMUSP00000069359; ENSMUSG00000056426.
DR GeneID; 17962; -.
DR KEGG; mmu:17962; -.
DR UCSC; uc009lvy.1; mouse.
DR CTD; 17962; -.
DR MGI; MGI:102537; Nat3.
DR VEuPathDB; HostDB:ENSMUSG00000056426; -.
DR eggNOG; ENOG502RD0D; Eukaryota.
DR GeneTree; ENSGT00390000012054; -.
DR HOGENOM; CLU_049918_3_0_1; -.
DR InParanoid; P50296; -.
DR OMA; CKYSNTM; -.
DR OrthoDB; 1545569at2759; -.
DR PhylomeDB; P50296; -.
DR TreeFam; TF106311; -.
DR Reactome; R-MMU-156582; Acetylation.
DR Reactome; R-MMU-9753281; Paracetamol ADME.
DR BioGRID-ORCS; 17962; 3 hits in 71 CRISPR screens.
DR PRO; PR:P50296; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P50296; protein.
DR Bgee; ENSMUSG00000056426; Expressed in spermatocyte and 2 other tissues.
DR ExpressionAtlas; P50296; baseline and differential.
DR Genevisible; P50296; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0004060; F:arylamine N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IDA:MGI.
DR GO; GO:0015807; P:L-amino acid transport; IDA:MGI.
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 3"
FT /id="PRO_0000107910"
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 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"
SQ SEQUENCE 290 AA; 33686 MW; AB6477F3DA3B0A9E CRC64;
MDIEAYFERI GYQKSSNKLD LQTLTEILQH QIRAIPFENL NIHCGKTMEL SLEDTFHQIV
RKKRGGWCLQ VNHLLYWALA MIGFETTMLG GCVYVPSACK YSNTMIHLLL QVTISGKTYI
VDSAFPFSCQ LWEPLELTSG KDQPQVPAIF HLREENGTWY LEQTKRQEYV SNQEFIDSNF
LEKNTHRKIY SFTLEPRTIE DFWSISTYYQ VSRTSVMTNT SLCSLHTKDG VHGLMGTILA
YKKFNYKDNI DLVEFKTLKE EEIEEVLKSV FGIHLETKLV PKCGNVFFTI
