AACS_RAT
ID AACS_RAT Reviewed; 672 AA.
AC Q9JMI1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Acetoacetyl-CoA synthetase;
DE EC=6.2.1.16 {ECO:0000269|PubMed:10682835, ECO:0000269|PubMed:3082367};
GN Name=Aacs;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 87-94; 236-242; 258-267;
RP 370-377; 533-539; 558-567; 583-588 AND 647-671, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=10682835; DOI=10.1016/s0014-5793(99)01794-9;
RA Iwahori A., Takahashi N., Nakamoto M., Iwama M., Fukui T.;
RT "cDNA-derived amino acid sequence of acetoacetyl-CoA synthetase from rat
RT liver.";
RL FEBS Lett. 466:239-243(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [3]
RP SUBCELLULAR LOCATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=3082367; DOI=10.1016/0005-2760(86)90285-7;
RA Ito M., Fukui T., Saito T., Tomita K.;
RT "Acetoacetyl-CoA synthetase specific activity and concentration in rat
RT tissues.";
RL Biochim. Biophys. Acta 876:280-287(1986).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=15992942; DOI=10.1016/j.bbaexp.2005.05.006;
RA Ohnuki M., Takahashi N., Yamasaki M., Fukui T.;
RT "Different localization in rat brain of the novel cytosolic ketone body-
RT utilizing enzyme, acetoacetyl-CoA synthetase, as compared to succinyl-
RT CoA:3-oxoacid CoA-transferase.";
RL Biochim. Biophys. Acta 1729:147-153(2005).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=16055091; DOI=10.1016/j.bbrc.2005.07.053;
RA Yamasaki M., Hasegawa S., Suzuki H., Hidai K., Saitoh Y., Fukui T.;
RT "Acetoacetyl-CoA synthetase gene is abundant in rat adipose, and related
RT with fatty acid synthesis in mature adipocytes.";
RL Biochem. Biophys. Res. Commun. 335:215-219(2005).
CC -!- FUNCTION: Converts acetoacetate to acetoacetyl-CoA in the cytosol.
CC Ketone body-utilizing enzyme, responsible for the synthesis of
CC cholesterol and fatty acids. {ECO:0000269|PubMed:10682835,
CC ECO:0000269|PubMed:3082367}.
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:0000269|PubMed:10682835, ECO:0000269|PubMed:3082367};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16118;
CC Evidence={ECO:0000305|PubMed:10682835};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10682835,
CC ECO:0000269|PubMed:3082367}.
CC -!- TISSUE SPECIFICITY: Abundant in male subcutaneous white adipose tissue
CC after weaning. In white adipose tissue, it is preferentially detected
CC in mature adipocytes but not in preadipocytes. The expression in
CC primary preadipocytes increases during the adipocyte differentiation.
CC In brain, it is expressed in the midbrain, pons/medulla, cerebral
CC cortex, hippocampus and cerebellum. The expression in the cerebellum is
CC restricted primarily to glial cells, while in the cerebral cortex, it
CC is restricted to neuronal cells. {ECO:0000269|PubMed:15992942,
CC ECO:0000269|PubMed:16055091}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme 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; AB026291; BAA90828.1; -; mRNA.
DR EMBL; BC061803; AAH61803.1; -; mRNA.
DR RefSeq; NP_075592.1; NM_023104.1.
DR AlphaFoldDB; Q9JMI1; -.
DR SMR; Q9JMI1; -.
DR STRING; 10116.ENSRNOP00000001292; -.
DR iPTMnet; Q9JMI1; -.
DR PhosphoSitePlus; Q9JMI1; -.
DR jPOST; Q9JMI1; -.
DR PaxDb; Q9JMI1; -.
DR PRIDE; Q9JMI1; -.
DR Ensembl; ENSRNOT00000001292; ENSRNOP00000001292; ENSRNOG00000000967.
DR GeneID; 65984; -.
DR KEGG; rno:65984; -.
DR UCSC; RGD:708522; rat.
DR CTD; 65985; -.
DR RGD; 708522; Aacs.
DR eggNOG; KOG1175; Eukaryota.
DR GeneTree; ENSGT00940000156044; -.
DR HOGENOM; CLU_000022_3_3_1; -.
DR InParanoid; Q9JMI1; -.
DR OMA; WYSSTGW; -.
DR OrthoDB; 899666at2759; -.
DR PhylomeDB; Q9JMI1; -.
DR TreeFam; TF354241; -.
DR BRENDA; 2.3.1.194; 5301.
DR BRENDA; 6.2.1.16; 5301.
DR Reactome; R-RNO-77111; Synthesis of Ketone Bodies.
DR SABIO-RK; Q9JMI1; -.
DR PRO; PR:Q9JMI1; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000000967; Expressed in thymus and 20 other tissues.
DR Genevisible; Q9JMI1; RN.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030729; F:acetoacetate-CoA ligase activity; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047760; F:butyrate-CoA ligase activity; IDA:RGD.
DR GO; GO:0060612; P:adipose tissue development; IEP:RGD.
DR GO; GO:0071397; P:cellular response to cholesterol; IEP:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IMP:RGD.
DR GO; GO:0071394; P:cellular response to testosterone stimulus; IEP:RGD.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0001889; P:liver development; IDA:RGD.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:RGD.
DR GO; GO:0045471; P:response to ethanol; IDA:RGD.
DR GO; GO:0007584; P:response to nutrient; IDA:RGD.
DR GO; GO:0034201; P:response to oleic acid; IDA:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IDA:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IDA:RGD.
DR GO; GO:0014074; P:response to purine-containing compound; IEP:RGD.
DR GO; GO:0042594; P:response to starvation; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:RGD.
DR GO; GO:0050872; P:white fat cell differentiation; IEP:RGD.
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; Direct protein sequencing; Fatty acid metabolism;
KW Ligase; Lipid metabolism; Nucleotide-binding; Reference proteome.
FT CHAIN 1..672
FT /note="Acetoacetyl-CoA synthetase"
FT /id="PRO_0000315787"
SQ SEQUENCE 672 AA; 75040 MW; FB6FD5C6D1A927A9 CRC64;
MSKLARLERE EIMECQVMWE PDSKKDTQMD RFRAAVGTAC GLALGNYDDL YHWSVRSYSD
FWAEFWKFSG IVCSRMYDEV VDTSKGIADV PEWFRGSRLN YAENLLRHKE NDRVALYVAR
EGREEIAKVT FEELRQQVAL FAAAMRKMGV KKGDRVVGYL PNSAHAVEAM LAAASIGAIW
SSTSPDFGVN GVLDRFSQIQ PKLIFSVEAV VYNGKEHGHL EKLQRVVKGL PDLQRVVLIP
YVLPREKIDI SKIPNSMFLD DFLASGTGAQ APQLEFEQLP FSHPLFIMFS SGTTGAPKCM
VHSAGGTLIQ HLKEHVLHGN MTSSDILLYY TTVGWMMWNW MVSALATGAS LVLYDGSPLV
PTPNVLWDLV DRIGITILGT GAKWLSVLEE KDMKPMETHN LHTLHTILST GSPLKAQSYE
YVYRCIKSTV LLGSISGGTD IISCFMGQNS SIPVYKGEIQ ARNLGMAVEA WDEEGKTVWG
ASGELVCTKP IPCQPTHFWN DENGSKYRKA YFSKYPGVWA HGDYCRINPK TGGIVMLGRS
DGTLNPNGVR FGSSEIYNIV EAFDEVEDSL CVPQYNRDGE ERVVLFLKMA SGHTFQPDLV
KHIRDAIRLG LSARHVPSLI LETQGIPYTI NGKKVEVAVK QVIAGKTVEH RGAFSNPESL
DLYRDIPELQ DF
