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Protein

Acetoacetyl-CoA synthetase

Gene

Aacs

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Activates acetoacetate to acetoacetyl-CoA. May be involved in utilizing ketone body for the fatty acid-synthesis during adipose tissue development (By similarity).By similarity

Catalytic activityi

ATP + acetoacetate + CoA = AMP + diphosphate + acetoacetyl-CoA.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-77111. Synthesis of Ketone Bodies.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetoacetyl-CoA synthetase (EC:6.2.1.16)
Gene namesi
Name:Aacs
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1926144. Aacs.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 672672Acetoacetyl-CoA synthetasePRO_0000315786Add
BLAST

Proteomic databases

EPDiQ9D2R0.
MaxQBiQ9D2R0.
PaxDbiQ9D2R0.
PRIDEiQ9D2R0.

PTM databases

iPTMnetiQ9D2R0.
PhosphoSiteiQ9D2R0.
SwissPalmiQ9D2R0.

Expressioni

Gene expression databases

BgeeiQ9D2R0.
CleanExiMM_AACS.
GenevisibleiQ9D2R0. MM.

Interactioni

Protein-protein interaction databases

BioGridi219689. 1 interaction.
IntActiQ9D2R0. 2 interactions.
MINTiMINT-4126762.
STRINGi10090.ENSMUSP00000031445.

Structurei

3D structure databases

ProteinModelPortaliQ9D2R0.
SMRiQ9D2R0. Positions 16-666.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1175. Eukaryota.
COG0365. LUCA.
GeneTreeiENSGT00820000127056.
HOGENOMiHOG000229992.
HOVERGENiHBG059947.
InParanoidiQ9D2R0.
KOiK01907.
OMAiVWDFCGI.
OrthoDBiEOG738043.
PhylomeDBiQ9D2R0.
TreeFamiTF354241.

Family and domain databases

InterProiIPR005914. Acac_CoA_synth.
IPR032387. ACAS_N.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. AMP-binding. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01217. ac_ac_CoA_syn. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9D2R0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKLARLERE EIMECQVMWE PDSKKDTQMD RFRAAVGTAC GLALGNYNDL
60 70 80 90 100
YHWSVRSYMD FWAEFWKFSG IVYSRMYDEV VDTSKGIADV PEWFRGSRLN
110 120 130 140 150
YAENLLRHKE NDRVALYVAR EGREEIVKVT FEELRQQVAL FAAAMRKMGV
160 170 180 190 200
KKGDRVVGYL PNSAHAVEAM LAAASIGAIW SSTSPDFGVN GVLDRFSQIQ
210 220 230 240 250
PKLIFSVEAV VYNGKEHGHL EKLQRVVKGL PDLQRVVLIP YVLPREKIDI
260 270 280 290 300
SKIPNSVFLD DFLASGTGAQ APQLEFEQLP FSHPLFIMFS SGTTGAPKCM
310 320 330 340 350
VHSAGGTLIQ HLKEHMLHGN MTSSDILLYY TTVGWMMWNW MVSALATGAS
360 370 380 390 400
LVLYDGSPLV PTPNVLWDLV DRIGITILGT GAKWLSVLEE KDMKPVETHN
410 420 430 440 450
LHTLHTILST GSPLKAQSYE YVYRCIKSSV LLGSISGGTD IISCFMGQNS
460 470 480 490 500
SIPVYKGEIQ ARNLGMAVEA WDEEGKAVWG ASGELVCTKP IPCQPTHFWN
510 520 530 540 550
DENGSKYRKA YFSKFPGVWA HGDYCRINPK TGGIIMLGRS DGTLNPNGVR
560 570 580 590 600
FGSSEIYNIV EAFDEVEDSL CVPQYNRDGE ERVVLFLKMA SGHTFQPDLV
610 620 630 640 650
KRIRDAIRLG LSARHVPSLI LETRGIPYTL NGKKVEVAVK QVMAGRTVEH
660 670
RGAFSNPETL DLYRDIPELQ DF
Length:672
Mass (Da):75,200
Last modified:June 1, 2001 - v1
Checksum:i547E7F9B14C8BF7E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti260 – 2612DD → EY in BAF44057 (Ref. 1) Curated
Sequence conflicti401 – 4011L → P in BAF44057 (Ref. 1) Curated
Sequence conflicti427 – 4271K → T in BAF44057 (Ref. 1) Curated
Sequence conflicti515 – 5151F → S in BAE29423 (PubMed:16141072).Curated
Sequence conflicti649 – 6491E → G in BAE41938 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB054122 mRNA. Translation: BAF44057.1.
AB056114 mRNA. Translation: BAB63403.1.
AK019063 mRNA. Translation: BAB31530.1.
AK034184 mRNA. Translation: BAC28621.1.
AK043848 mRNA. Translation: BAC31680.1.
AK044017 mRNA. Translation: BAC31740.1.
AK147189 mRNA. Translation: BAE27749.1.
AK150266 mRNA. Translation: BAE29423.1.
AK165418 mRNA. Translation: BAE38173.1.
AK165457 mRNA. Translation: BAE38197.1.
AK170120 mRNA. Translation: BAE41577.1.
AK170653 mRNA. Translation: BAE41938.1.
AK170856 mRNA. Translation: BAE42076.1.
BC026817 mRNA. Translation: AAH26817.1.
CCDSiCCDS19687.1.
RefSeqiNP_084486.1. NM_030210.1.
UniGeneiMm.431573.
Mm.478133.

Genome annotation databases

EnsembliENSMUST00000031445; ENSMUSP00000031445; ENSMUSG00000029482.
GeneIDi78894.
KEGGimmu:78894.
UCSCiuc008zrs.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB054122 mRNA. Translation: BAF44057.1.
AB056114 mRNA. Translation: BAB63403.1.
AK019063 mRNA. Translation: BAB31530.1.
AK034184 mRNA. Translation: BAC28621.1.
AK043848 mRNA. Translation: BAC31680.1.
AK044017 mRNA. Translation: BAC31740.1.
AK147189 mRNA. Translation: BAE27749.1.
AK150266 mRNA. Translation: BAE29423.1.
AK165418 mRNA. Translation: BAE38173.1.
AK165457 mRNA. Translation: BAE38197.1.
AK170120 mRNA. Translation: BAE41577.1.
AK170653 mRNA. Translation: BAE41938.1.
AK170856 mRNA. Translation: BAE42076.1.
BC026817 mRNA. Translation: AAH26817.1.
CCDSiCCDS19687.1.
RefSeqiNP_084486.1. NM_030210.1.
UniGeneiMm.431573.
Mm.478133.

3D structure databases

ProteinModelPortaliQ9D2R0.
SMRiQ9D2R0. Positions 16-666.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi219689. 1 interaction.
IntActiQ9D2R0. 2 interactions.
MINTiMINT-4126762.
STRINGi10090.ENSMUSP00000031445.

PTM databases

iPTMnetiQ9D2R0.
PhosphoSiteiQ9D2R0.
SwissPalmiQ9D2R0.

Proteomic databases

EPDiQ9D2R0.
MaxQBiQ9D2R0.
PaxDbiQ9D2R0.
PRIDEiQ9D2R0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031445; ENSMUSP00000031445; ENSMUSG00000029482.
GeneIDi78894.
KEGGimmu:78894.
UCSCiuc008zrs.1. mouse.

Organism-specific databases

CTDi65985.
MGIiMGI:1926144. Aacs.

Phylogenomic databases

eggNOGiKOG1175. Eukaryota.
COG0365. LUCA.
GeneTreeiENSGT00820000127056.
HOGENOMiHOG000229992.
HOVERGENiHBG059947.
InParanoidiQ9D2R0.
KOiK01907.
OMAiVWDFCGI.
OrthoDBiEOG738043.
PhylomeDBiQ9D2R0.
TreeFamiTF354241.

Enzyme and pathway databases

ReactomeiR-MMU-77111. Synthesis of Ketone Bodies.

Miscellaneous databases

PROiQ9D2R0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D2R0.
CleanExiMM_AACS.
GenevisibleiQ9D2R0. MM.

Family and domain databases

InterProiIPR005914. Acac_CoA_synth.
IPR032387. ACAS_N.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. AMP-binding. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01217. ac_ac_CoA_syn. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "mouse acetoacetyl-CoA synthetase."
    Takahashi N., Ohgami M., Yamasaki M., Fukui T.
    Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ddY.
    Tissue: Liver.
  2. "Murine acetoacetyl-coenzyme A synthetase."
    Sone H., Shimano H., Yamada N.
    Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Amnion, Bone marrow, Brain cortex, Diencephalon, Kidney and Stomach.
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Kidney.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas and Spleen.

Entry informationi

Entry nameiAACS_MOUSE
AccessioniPrimary (citable) accession number: Q9D2R0
Secondary accession number(s): A1IG47, Q3TCL8, Q3UD39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.