AACS_MOUSE
ID AACS_MOUSE Reviewed; 672 AA.
AC Q9D2R0; A1IG47; Q3TCL8; Q3UD39;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Acetoacetyl-CoA synthetase;
DE EC=6.2.1.16 {ECO:0000250|UniProtKB:Q9JMI1};
GN Name=Aacs;
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 [MRNA].
RC STRAIN=ddY; TISSUE=Liver;
RA Takahashi N., Ohgami M., Yamasaki M., Fukui T.;
RT "mouse acetoacetyl-CoA synthetase.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sone H., Shimano H., Yamada N.;
RT "Murine acetoacetyl-coenzyme A synthetase.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Amnion, Bone marrow, Brain cortex, Diencephalon, Kidney, and
RC Stomach;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, and
RC Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION.
RX PubMed=22985732; DOI=10.1016/j.ymgme.2012.08.017;
RA Hasegawa S., Noda K., Maeda A., Matsuoka M., Yamasaki M., Fukui T.;
RT "Acetoacetyl-CoA synthetase, a ketone body-utilizing enzyme, is controlled
RT by SREBP-2 and affects serum cholesterol levels.";
RL Mol. Genet. Metab. 107:553-560(2012).
CC -!- FUNCTION: Converts acetoacetate to acetoacetyl-CoA in the cytosol (By
CC similarity). Ketone body-utilizing enzyme, responsible for the
CC synthesis of cholesterol and fatty acids (PubMed:22985732).
CC {ECO:0000250|UniProtKB:Q9JMI1, ECO:0000269|PubMed:22985732}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetoacetate + ATP + CoA = acetoacetyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:16117, ChEBI:CHEBI:13705,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57286,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:456215; EC=6.2.1.16;
CC Evidence={ECO:0000250|UniProtKB:Q9JMI1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16118;
CC Evidence={ECO:0000250|UniProtKB:Q9JMI1};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9JMI1}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AB054122; BAF44057.1; -; mRNA.
DR EMBL; AB056114; BAB63403.1; -; mRNA.
DR EMBL; AK019063; BAB31530.1; -; mRNA.
DR EMBL; AK034184; BAC28621.1; -; mRNA.
DR EMBL; AK043848; BAC31680.1; -; mRNA.
DR EMBL; AK044017; BAC31740.1; -; mRNA.
DR EMBL; AK147189; BAE27749.1; -; mRNA.
DR EMBL; AK150266; BAE29423.1; -; mRNA.
DR EMBL; AK165418; BAE38173.1; -; mRNA.
DR EMBL; AK165457; BAE38197.1; -; mRNA.
DR EMBL; AK170120; BAE41577.1; -; mRNA.
DR EMBL; AK170653; BAE41938.1; -; mRNA.
DR EMBL; AK170856; BAE42076.1; -; mRNA.
DR EMBL; BC026817; AAH26817.1; -; mRNA.
DR CCDS; CCDS19687.1; -.
DR RefSeq; NP_084486.1; NM_030210.1.
DR AlphaFoldDB; Q9D2R0; -.
DR SMR; Q9D2R0; -.
DR BioGRID; 219689; 4.
DR IntAct; Q9D2R0; 1.
DR STRING; 10090.ENSMUSP00000031445; -.
DR iPTMnet; Q9D2R0; -.
DR PhosphoSitePlus; Q9D2R0; -.
DR SwissPalm; Q9D2R0; -.
DR EPD; Q9D2R0; -.
DR jPOST; Q9D2R0; -.
DR MaxQB; Q9D2R0; -.
DR PaxDb; Q9D2R0; -.
DR PeptideAtlas; Q9D2R0; -.
DR PRIDE; Q9D2R0; -.
DR ProteomicsDB; 286039; -.
DR Antibodypedia; 31900; 147 antibodies from 19 providers.
DR DNASU; 78894; -.
DR Ensembl; ENSMUST00000031445; ENSMUSP00000031445; ENSMUSG00000029482.
DR GeneID; 78894; -.
DR KEGG; mmu:78894; -.
DR UCSC; uc008zrs.1; mouse.
DR CTD; 65985; -.
DR MGI; MGI:1926144; Aacs.
DR VEuPathDB; HostDB:ENSMUSG00000029482; -.
DR eggNOG; KOG1175; Eukaryota.
DR GeneTree; ENSGT00940000156044; -.
DR HOGENOM; CLU_000022_3_3_1; -.
DR InParanoid; Q9D2R0; -.
DR OMA; WYSSTGW; -.
DR OrthoDB; 899666at2759; -.
DR PhylomeDB; Q9D2R0; -.
DR TreeFam; TF354241; -.
DR BRENDA; 6.2.1.16; 3474.
DR Reactome; R-MMU-77111; Synthesis of Ketone Bodies.
DR BioGRID-ORCS; 78894; 2 hits in 61 CRISPR screens.
DR PRO; PR:Q9D2R0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9D2R0; protein.
DR Bgee; ENSMUSG00000029482; Expressed in right kidney and 235 other tissues.
DR Genevisible; Q9D2R0; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030729; F:acetoacetate-CoA ligase activity; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047760; F:butyrate-CoA ligase activity; ISO:MGI.
DR GO; GO:0071333; P:cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0001889; P:liver development; ISO:MGI.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISO:MGI.
DR GO; GO:0045471; P:response to ethanol; ISO:MGI.
DR GO; GO:0007584; P:response to nutrient; ISO:MGI.
DR GO; GO:0034201; P:response to oleic acid; ISO:MGI.
DR GO; GO:0014070; P:response to organic cyclic compound; ISO:MGI.
DR GO; GO:0010243; P:response to organonitrogen compound; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR005914; Acac_CoA_synth.
DR InterPro; IPR032387; ACAS_N.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR TIGRFAMs; TIGR01217; ac_ac_CoA_syn; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..672
FT /note="Acetoacetyl-CoA synthetase"
FT /id="PRO_0000315786"
FT CONFLICT 260..261
FT /note="DD -> EY (in Ref. 1; BAF44057)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="L -> P (in Ref. 1; BAF44057)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="K -> T (in Ref. 1; BAF44057)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="F -> S (in Ref. 3; BAE29423)"
FT /evidence="ECO:0000305"
FT CONFLICT 649
FT /note="E -> G (in Ref. 3; BAE41938)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 672 AA; 75200 MW; 547E7F9B14C8BF7E CRC64;
MSKLARLERE EIMECQVMWE PDSKKDTQMD RFRAAVGTAC GLALGNYNDL YHWSVRSYMD
FWAEFWKFSG IVYSRMYDEV VDTSKGIADV PEWFRGSRLN YAENLLRHKE NDRVALYVAR
EGREEIVKVT FEELRQQVAL FAAAMRKMGV KKGDRVVGYL PNSAHAVEAM LAAASIGAIW
SSTSPDFGVN GVLDRFSQIQ PKLIFSVEAV VYNGKEHGHL EKLQRVVKGL PDLQRVVLIP
YVLPREKIDI SKIPNSVFLD DFLASGTGAQ APQLEFEQLP FSHPLFIMFS SGTTGAPKCM
VHSAGGTLIQ HLKEHMLHGN MTSSDILLYY TTVGWMMWNW MVSALATGAS LVLYDGSPLV
PTPNVLWDLV DRIGITILGT GAKWLSVLEE KDMKPVETHN LHTLHTILST GSPLKAQSYE
YVYRCIKSSV LLGSISGGTD IISCFMGQNS SIPVYKGEIQ ARNLGMAVEA WDEEGKAVWG
ASGELVCTKP IPCQPTHFWN DENGSKYRKA YFSKFPGVWA HGDYCRINPK TGGIIMLGRS
DGTLNPNGVR FGSSEIYNIV EAFDEVEDSL CVPQYNRDGE ERVVLFLKMA SGHTFQPDLV
KRIRDAIRLG LSARHVPSLI LETRGIPYTL NGKKVEVAVK QVMAGRTVEH RGAFSNPETL
DLYRDIPELQ DF
