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Reviewed, UniProtKB/Swiss-Prot Q9DBK0 (ACO12_MOUSE)

Last modified January 19, 2010. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Acyl-coenzyme A thioesterase 12
      Short name=Acyl-CoA thioesterase 12
    EC=3.1.2.1
Alternative name(s):
    Acyl-CoA thioester hydrolase 12
    Cytoplasmic acetyl-CoA hydrolase 1
      Short name=mCACH-1
      Short name=CACH-1
Gene names
Name: Acot12
Synonyms: Cach, Cach1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length556 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Hydrolyzes acetyl-CoA to acetate and CoA By similarity.

Catalytic activity

Acetyl-CoA + H2O = CoA + acetate.

Pathway

Carbohydrate metabolism; pyruvate metabolism.

Subunit structure

Homodimer or homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Contains 2 acyl coenzyme A hydrolase domains.

Contains 1 START domain.

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Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentCytoplasm
   DomainRepeat
   Molecular functionHydrolase
Serine esterase
Gene Ontology (GO)
   Biological processacetyl-CoA metabolic process Ref.1

Inferred from direct assay. Source: MGI

   Cellular componentcytosol Ref.1

Traceable author statement. Source: MGI

   Molecular functionATP binding Ref.1

Inferred from direct assay. Source: MGI

acetyl-CoA hydrolase activity Ref.1

Inferred from direct assay. Source: MGI

carboxylesterase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 556556Acyl-coenzyme A thioesterase 12
PRO_0000053810

Regions

Domain1 – 128128Acyl coenzyme A hydrolase 1
Domain162 – 302141Acyl coenzyme A hydrolase 2
Domain327 – 536210START
Region54 – 563Coenzyme A binding By similarity
Region83 – 853Coenzyme A binding By similarity
Region235 – 2373Coenzyme A binding By similarity

Sites

Binding site1451Coenzyme A By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q9DBK0-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 9FE9C487BBCBB812

FASTA55661,762
        10         20         30         40         50         60 
MESMVAPGEV LMSQAIQPAH ADSRGELSAG QLLKWMDTTA CLAAEKHAGI SCVTASMDDI 

        70         80         90        100        110        120 
LFEDTARIGQ IITIRAKVTR AFSTSMEISI KVIVQDKFTG IQKLLCVAFS TFVAKPVGKE 

       130        140        150        160        170        180 
KVHLKPVLLQ TEQEQVEHNL ASERRKVRLQ HENTFNNIMK ESSRFSDSIC NEEEGTATTM 

       190        200        210        220        230        240 
GTSVQSIELV LPPHANHHGN TFGGQIMAWM ETVATISASR LCHGHPFLKS VDMFKFRGPS 

       250        260        270        280        290        300 
TVGDRLVFSA IVNNTFQNSV EVGVRVEAFD CQEWAEGQGR HINSAFLIYN AVDDQEKLIT 

       310        320        330        340        350        360 
FPRIQPISKD DFRRYQGAIA RRRIRLGRKY VISHKKEVPL SAQWDISKKG SLSNTNVEAL 

       370        380        390        400        410        420 
KNLASKSGWE ITTTLEKIKI YTLEEQDAIS VKVEKLVGSP AHIAYHLLSD LTKRPLWDPH 

       430        440        450        460        470        480 
YISCEVIDQV SEDDQIYYIT CSVVNGDKPK DFVVLVSRRK PLKDNNTYTV ALRSVVLPSV 

       490        500        510        520        530        540 
PSSPQYIRSE VICAGFLIQA VDSNSCTVTY LNQMSDSILP YFAGNIGGWS KSIEEAAASC 

       550 
IKFIENATPD GLKSVL

« Hide

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References

« Hide 'large scale' references
[1]"Mouse cytosolic acetyl-CoA hydrolase, a novel candidate for a key enzyme involved in fat metabolism: cDNA cloning, sequencing and functional expression."
Suematsu N., Okamoto K., Isohashi F.
Acta Biochim. Pol. 49:937-945(2002) [PubMed: 12545200] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6J.
Tissue: Liver.
[2]"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.
Tissue: Embryo and Liver.
[3]"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] OF 14-556.
Tissue: Liver.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB078618 mRNA. Translation: BAB84021.1.
AK004905 mRNA. Translation: BAB23658.1.
AK034622 mRNA. Translation: BAC28775.1.
BC025852 mRNA. Translation: AAH25852.1.
IPIIPI00119810.
RefSeqNP_083066.1.
UniGeneMm.275963

3D structure databases

SMRQ9DBK0. Positions 8-299, 182-331, 355-529.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9DBK0.

Proteomic databases

PRIDEQ9DBK0.

Genome annotation databases

EnsemblENSMUST00000022120; ENSMUSP00000022120; ENSMUSG00000021620; Mus musculus. [Genome view]
GeneID74156.
KEGGmmu:74156.
UCSCuc007rka.1. mouse.

Organism-specific databases

CTD74156.
MGIMGI:1921406. Acot12.

Phylogenomic databases

HOGENOMHBG443629.
HOVERGENQ9DBK0.
InParanoidQ9DBK0.
OMAPYFAGNL.
OrthoDBEOG9CJZ2N.
PhylomeDBQ9DBK0.

Enzyme and pathway databases

BRENDA3.1.2.1. 244.

Gene expression databases

ArrayExpressQ9DBK0.
BgeeQ9DBK0.
CleanExMM_ACOT12.
GenevestigatorQ9DBK0.
GermOnlineENSMUSG00000021620. Mus musculus.

Family and domain databases

InterProIPR002913. START_lipid_bd.
IPR006683. Thioestr_supf.
[Graphical view]
PfamPF03061. 4HBT. 2 hits.
PF01852. START. 1 hit.
[Graphical view]
PROSITEPS50848. START. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio339934.
SOURCESearch...

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Entry information

Entry nameACO12_MOUSE
AccessionPrimary (citable) accession number: Q9DBK0
Secondary accession number(s): Q544M5, Q8R108
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: June 1, 2001
Last modified: January 19, 2010
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents