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Q9DBK0 (ACO12_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

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=CACH-1
Short name=mCACH-1
Gene names
Name:Acot12
Synonyms:Cach, Cach1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

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

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.

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

Amino acid modifications

Modified residue341N6-succinyllysine Ref.4
Modified residue971N6-succinyllysine Ref.4
Modified residue1601N6-succinyllysine Ref.4
Modified residue2291N6-succinyllysine Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9DBK0 [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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-556.
Tissue: Liver.
[4]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-34; LYS-97; LYS-160 AND LYS-229, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

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.
RefSeqNP_083066.1. NM_028790.3.
UniGeneMm.275963.

3D structure databases

ProteinModelPortalQ9DBK0.
SMRQ9DBK0. Positions 8-544.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9DBK0. 3 interactions.
MINTMINT-4089645.

PTM databases

PhosphoSiteQ9DBK0.

Proteomic databases

PaxDbQ9DBK0.
PRIDEQ9DBK0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022120; ENSMUSP00000022120; ENSMUSG00000021620.
GeneID74156.
KEGGmmu:74156.
UCSCuc007rka.1. mouse.

Organism-specific databases

CTD134526.
MGIMGI:1921406. Acot12.

Phylogenomic databases

eggNOGCOG1607.
GeneTreeENSGT00750000117709.
HOGENOMHOG000232032.
HOVERGENHBG023847.
InParanoidQ9DBK0.
KOK01067.
OMAPLWDPHY.
OrthoDBEOG70CR6C.
PhylomeDBQ9DBK0.
TreeFamTF328368.

Enzyme and pathway databases

UniPathwayUPA00231.

Gene expression databases

BgeeQ9DBK0.
CleanExMM_ACOT12.
GenevestigatorQ9DBK0.

Family and domain databases

Gene3D3.30.530.20. 1 hit.
InterProIPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
IPR006683. Thioestr_supf.
[Graphical view]
PfamPF03061. 4HBT. 2 hits.
PF01852. START. 1 hit.
[Graphical view]
PROSITEPS50848. START. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio339934.
PROQ9DBK0.
SOURCESearch...

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: April 16, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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