Q9JMI1 (AACS_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetoacetyl-CoA synthetase
EC=6.2.1.16

Gene names

Name:

Aacs

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	672 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Activates acetoacetate to acetoacetyl-CoA. May be involved in utilizing ketone body for the fatty acid-synthesis during adipose tissue development.
Catalytic activity	ATP + acetoacetate + CoA = AMP + diphosphate + acetoacetyl-CoA. Ref.1
Subcellular location	Cytoplasm › cytosol By similarity Ref.1.
Tissue specificity	Abundant in male subcutaneous white adipose tissue after weaning. In white adipose tissue, it is preferentially detected in mature adipocytes but not in preadipocytes. The expression in primary preadipocytes increases during the adipocyte differentiation. In brain, it is expressed in the midbrain, pons/medulla, cerebral cortex, hippocampus and cerebellum. The expression in the cerebellum is restricted primarily to glial cells, while in the cerebral cortex, it is restricted to neuronal cells. Ref.3 Ref.4
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	adipose tissue development Inferred from expression pattern Ref.4. Source: RGD cellular response to cholesterol Inferred from expression pattern. Source: RGD cellular response to glucose stimulus Inferred from mutant phenotype. Source: RGD cellular response to testosterone stimulus Inferred from expression pattern. Source: RGD fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW liver development Inferred from direct assay. Source: RGD positive regulation of insulin secretion Inferred from mutant phenotype. Source: RGD response to drug Inferred from direct assay. Source: RGD response to ethanol Inferred from direct assay. Source: RGD response to nutrient Inferred from direct assay. Source: RGD response to oleic acid Inferred from direct assay. Source: RGD response to organic nitrogen Inferred from direct assay. Source: RGD response to purine-containing compound Inferred from expression pattern. Source: RGD response to starvation Inferred from expression pattern. Source: RGD white fat cell differentiation Inferred from expression pattern Ref.4. Source: RGD
Cellular component	cytosol Inferred from direct assay. Source: RGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetoacetate-CoA ligase activity Inferred from direct assay. Source: RGD butyrate-CoA ligase activity Inferred from direct assay. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 672	672	Acetoacetyl-CoA synthetase		PRO_0000315787
Amino acid modifications
	Modified residue	524	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9JMI1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: FB6FD5C6D1A927A9	FASTA	672	75,040
	10 20 30 40 50 60 MSKLARLERE EIMECQVMWE PDSKKDTQMD RFRAAVGTAC GLALGNYDDL YHWSVRSYSD 70 80 90 100 110 120 FWAEFWKFSG IVCSRMYDEV VDTSKGIADV PEWFRGSRLN YAENLLRHKE NDRVALYVAR 130 140 150 160 170 180 EGREEIAKVT FEELRQQVAL FAAAMRKMGV KKGDRVVGYL PNSAHAVEAM LAAASIGAIW 190 200 210 220 230 240 SSTSPDFGVN GVLDRFSQIQ PKLIFSVEAV VYNGKEHGHL EKLQRVVKGL PDLQRVVLIP 250 260 270 280 290 300 YVLPREKIDI SKIPNSMFLD DFLASGTGAQ APQLEFEQLP FSHPLFIMFS SGTTGAPKCM 310 320 330 340 350 360 VHSAGGTLIQ HLKEHVLHGN MTSSDILLYY TTVGWMMWNW MVSALATGAS LVLYDGSPLV 370 380 390 400 410 420 PTPNVLWDLV DRIGITILGT GAKWLSVLEE KDMKPMETHN LHTLHTILST GSPLKAQSYE 430 440 450 460 470 480 YVYRCIKSTV LLGSISGGTD IISCFMGQNS SIPVYKGEIQ ARNLGMAVEA WDEEGKTVWG 490 500 510 520 530 540 ASGELVCTKP IPCQPTHFWN DENGSKYRKA YFSKYPGVWA HGDYCRINPK TGGIVMLGRS 550 560 570 580 590 600 DGTLNPNGVR FGSSEIYNIV EAFDEVEDSL CVPQYNRDGE ERVVLFLKMA SGHTFQPDLV 610 620 630 640 650 660 KHIRDAIRLG LSARHVPSLI LETQGIPYTI NGKKVEVAVK QVIAGKTVEH RGAFSNPESL 670 DLYRDIPELQ DF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA-derived amino acid sequence of acetoacetyl-CoA synthetase from rat liver." Iwahori A., Takahashi N., Nakamoto M., Iwama M., Fukui T. FEBS Lett. 466:239-243(2000) [PubMed: 10682835] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 87-94; 236-242; 258-267; 370-377; 533-539; 558-567; 583-588 AND 647-671, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION. Strain: Sprague-Dawley. Tissue: Liver.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Prostate.
[3]	"Different localization in rat brain of the novel cytosolic ketone body-utilizing enzyme, acetoacetyl-CoA synthetase, as compared to succinyl-CoA:3-oxoacid CoA-transferase." Ohnuki M., Takahashi N., Yamasaki M., Fukui T. Biochim. Biophys. Acta 1729:147-153(2005) [PubMed: 15992942] [Abstract] Cited for: TISSUE SPECIFICITY.
[4]	"Acetoacetyl-CoA synthetase gene is abundant in rat adipose, and related with fatty acid synthesis in mature adipocytes." Yamasaki M., Hasegawa S., Suzuki H., Hidai K., Saitoh Y., Fukui T. Biochem. Biophys. Res. Commun. 335:215-219(2005) [PubMed: 16055091] [Abstract] Cited for: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB026291 mRNA. Translation: BAA90828.1. BC061803 mRNA. Translation: AAH61803.1.
IPI	IPI00204738.
RefSeq	NP_075592.1. NM_023104.1.
UniGene	Rn.9215.
3D structure databases
ProteinModelPortal	Q9JMI1.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9JMI1.
PTM databases
PhosphoSite	Q9JMI1.
Proteomic databases
PRIDE	Q9JMI1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000001292; ENSRNOP00000001292; ENSRNOG00000000967.
GeneID	65984.
KEGG	rno:65984.
NMPDR	fig|10116.3.peg.8494.
UCSC	NM_023104. rat.
Organism-specific databases
CTD	65985.
RGD	708522. Aacs.
Phylogenomic databases
eggNOG	roNOG08354.
GeneTree	ENSGT00580000081632.
HOVERGEN	HBG059947.
InParanoid	Q9JMI1.
OMA	SSCAPEF.
OrthoDB	EOG4HQDHT.
PhylomeDB	Q9JMI1.
Gene expression databases
ArrayExpress	Q9JMI1.
Genevestigator	Q9JMI1.
Family and domain databases
InterPro	IPR005914. Acac_CoA_synth. IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. [Graphical view]
KO	K01907.
PANTHER	PTHR24095:SF40. PTHR24095:SF40. 1 hit.
Pfam	PF00501. AMP-binding. 1 hit. [Graphical view]
TIGRFAMs	TIGR01217. Ac_ac_CoA_syn. 1 hit.
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	614262.

Entry information

Entry name

AACS_RAT

Accession

Primary (citable) accession number: Q9JMI1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	October 1, 2000
Last modified:	November 16, 2011
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program