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Q9D2R0 (AACS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetoacetyl-CoA synthetase
EC=6.2.1.16
Gene names
Name:Aacs
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length672 AA.
Sequence statusComplete.
Protein existenceEvidence 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 By similarity.

Catalytic activity

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

Subcellular location

Cytoplasm › cytosol By similarity.

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processfatty acid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

acetoacetate-CoA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 672672Acetoacetyl-CoA synthetase
PRO_0000315786

Amino acid modifications

Modified residue5241Phosphotyrosine Ref.5

Experimental info

Sequence conflict260 – 2612DD → EY in BAF44057. Ref.1
Sequence conflict4011L → P in BAF44057. Ref.1
Sequence conflict4271K → T in BAF44057. Ref.1
Sequence conflict5151F → S in BAE29423. Ref.3
Sequence conflict6491E → G in BAE41938. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9D2R0 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 547E7F9B14C8BF7E

FASTA67275,200
        10         20         30         40         50         60 
MSKLARLERE EIMECQVMWE PDSKKDTQMD RFRAAVGTAC GLALGNYNDL YHWSVRSYMD 

        70         80         90        100        110        120 
FWAEFWKFSG IVYSRMYDEV VDTSKGIADV PEWFRGSRLN YAENLLRHKE NDRVALYVAR 

       130        140        150        160        170        180 
EGREEIVKVT FEELRQQVAL FAAAMRKMGV KKGDRVVGYL PNSAHAVEAM LAAASIGAIW 

       190        200        210        220        230        240 
SSTSPDFGVN GVLDRFSQIQ PKLIFSVEAV VYNGKEHGHL EKLQRVVKGL PDLQRVVLIP 

       250        260        270        280        290        300 
YVLPREKIDI SKIPNSVFLD DFLASGTGAQ APQLEFEQLP FSHPLFIMFS SGTTGAPKCM 

       310        320        330        340        350        360 
VHSAGGTLIQ HLKEHMLHGN MTSSDILLYY TTVGWMMWNW MVSALATGAS LVLYDGSPLV 

       370        380        390        400        410        420 
PTPNVLWDLV DRIGITILGT GAKWLSVLEE KDMKPVETHN LHTLHTILST GSPLKAQSYE 

       430        440        450        460        470        480 
YVYRCIKSSV LLGSISGGTD IISCFMGQNS SIPVYKGEIQ ARNLGMAVEA WDEEGKAVWG 

       490        500        510        520        530        540 
ASGELVCTKP IPCQPTHFWN DENGSKYRKA YFSKFPGVWA HGDYCRINPK TGGIIMLGRS 

       550        560        570        580        590        600 
DGTLNPNGVR FGSSEIYNIV EAFDEVEDSL CVPQYNRDGE ERVVLFLKMA SGHTFQPDLV 

       610        620        630        640        650        660 
KRIRDAIRLG LSARHVPSLI LETRGIPYTL NGKKVEVAVK QVMAGRTVEH RGAFSNPETL 

       670 
DLYRDIPELQ DF

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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: 16141072] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Kidney.
[5]"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
J. Immunol. 179:5864-5876(2007) [PubMed: 17947660] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-524, MASS SPECTROMETRY.
Tissue: Mast cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00135189.
RefSeqNP_084486.1. NM_030210.1.
UniGeneMm.431573.

3D structure databases

ProteinModelPortalQ9D2R0.
SMRQ9D2R0. Positions 34-668.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9D2R0.

PTM databases

PhosphoSiteQ9D2R0.

Proteomic databases

PRIDEQ9D2R0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031445; ENSMUSP00000031445; ENSMUSG00000029482.
GeneID78894.
KEGGmmu:78894.
NMPDRfig|10090.3.peg.12481.
UCSCuc008zrs.1. mouse.

Organism-specific databases

CTD65985.
MGIMGI:1926144. Aacs.

Phylogenomic databases

GeneTreeENSGT00580000081632.
HOGENOMHBG547964.
HOVERGENHBG059947.
InParanoidQ9D2R0.
OMASSCAPEF.
OrthoDBEOG4HQDHT.
PhylomeDBQ9D2R0.

Gene expression databases

ArrayExpressQ9D2R0.
BgeeQ9D2R0.
CleanExMM_AACS.
GenevestigatorQ9D2R0.

Family and domain databases

InterProIPR005914. Acac_CoA_synth.
IPR024597. Acyl-CoA_synth_DUF3448.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
KOK01907.
PANTHERPTHR24095:SF40. PTHR24095:SF40. 1 hit.
PfamPF00501. AMP-binding. 1 hit.
PF11930. DUF3448. 1 hit.
[Graphical view]
TIGRFAMsTIGR01217. Ac_ac_CoA_syn. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio349694.
SOURCESearch...

Entry information

Entry nameAACS_MOUSE
AccessionPrimary (citable) accession number: Q9D2R0
Secondary accession number(s): A1IG47, Q3TCL8, Q3UD39
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 1, 2001
Last modified: November 16, 2011
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents