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Q9DBK0

- ACO12_MOUSE

UniProt

Q9DBK0 - ACO12_MOUSE

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Protein
Acyl-coenzyme A thioesterase 12
Gene
Acot12, Cach, Cach1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Hydrolyzes acetyl-CoA to acetate and CoA By similarity.

Catalytic activityi

Acetyl-CoA + H2O = CoA + acetate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei145 – 1451Coenzyme A By similarity

GO - Molecular functioni

  1. ATP binding Source: MGI
  2. acetyl-CoA hydrolase activity Source: MGI
  3. lipid binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. acetyl-CoA metabolic process Source: MGI
  2. fatty acid metabolic process Source: MGI
  3. pyruvate metabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

UniPathwayiUPA00231.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-coenzyme A thioesterase 12 (EC:3.1.2.1)
Short name:
Acyl-CoA thioesterase 12
Alternative name(s):
Acyl-CoA thioester hydrolase 12
Cytoplasmic acetyl-CoA hydrolase 1
Short name:
CACH-1
Short name:
mCACH-1
Gene namesi
Name:Acot12
Synonyms:Cach, Cach1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:1921406. Acot12.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytosol Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 556556Acyl-coenzyme A thioesterase 12
PRO_0000053810Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei34 – 341N6-succinyllysine1 Publication
Modified residuei97 – 971N6-succinyllysine1 Publication
Modified residuei160 – 1601N6-succinyllysine1 Publication
Modified residuei229 – 2291N6-succinyllysine1 Publication

Proteomic databases

MaxQBiQ9DBK0.
PaxDbiQ9DBK0.
PRIDEiQ9DBK0.

PTM databases

PhosphoSiteiQ9DBK0.

Expressioni

Gene expression databases

BgeeiQ9DBK0.
CleanExiMM_ACOT12.
GenevestigatoriQ9DBK0.

Interactioni

Subunit structurei

Homodimer or homotetramer By similarity.

Protein-protein interaction databases

IntActiQ9DBK0. 3 interactions.
MINTiMINT-4089645.

Structurei

3D structure databases

ProteinModelPortaliQ9DBK0.
SMRiQ9DBK0. Positions 8-544.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 128128Acyl coenzyme A hydrolase 1
Add
BLAST
Domaini162 – 302141Acyl coenzyme A hydrolase 2
Add
BLAST
Domaini327 – 536210START
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni54 – 563Coenzyme A binding By similarity
Regioni83 – 853Coenzyme A binding By similarity
Regioni235 – 2373Coenzyme A binding By similarity

Sequence similaritiesi

Contains 1 START domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1607.
GeneTreeiENSGT00750000117709.
HOGENOMiHOG000232032.
HOVERGENiHBG023847.
InParanoidiQ9DBK0.
KOiK01067.
OMAiPLWDPHY.
OrthoDBiEOG70CR6C.
PhylomeDBiQ9DBK0.
TreeFamiTF328368.

Family and domain databases

Gene3Di3.10.129.10. 2 hits.
3.30.530.20. 1 hit.
InterProiIPR029069. HotDog_dom.
IPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
IPR006683. Thioestr_supf.
[Graphical view]
PfamiPF03061. 4HBT. 2 hits.
PF01852. START. 1 hit.
[Graphical view]
SUPFAMiSSF54637. SSF54637. 2 hits.
PROSITEiPS50848. START. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9DBK0-1 [UniParc]FASTAAdd to Basket

« Hide

MESMVAPGEV LMSQAIQPAH ADSRGELSAG QLLKWMDTTA CLAAEKHAGI    50
SCVTASMDDI LFEDTARIGQ IITIRAKVTR AFSTSMEISI KVIVQDKFTG 100
IQKLLCVAFS TFVAKPVGKE KVHLKPVLLQ TEQEQVEHNL ASERRKVRLQ 150
HENTFNNIMK ESSRFSDSIC NEEEGTATTM GTSVQSIELV LPPHANHHGN 200
TFGGQIMAWM ETVATISASR LCHGHPFLKS VDMFKFRGPS TVGDRLVFSA 250
IVNNTFQNSV EVGVRVEAFD CQEWAEGQGR HINSAFLIYN AVDDQEKLIT 300
FPRIQPISKD DFRRYQGAIA RRRIRLGRKY VISHKKEVPL SAQWDISKKG 350
SLSNTNVEAL KNLASKSGWE ITTTLEKIKI YTLEEQDAIS VKVEKLVGSP 400
AHIAYHLLSD LTKRPLWDPH YISCEVIDQV SEDDQIYYIT CSVVNGDKPK 450
DFVVLVSRRK PLKDNNTYTV ALRSVVLPSV PSSPQYIRSE VICAGFLIQA 500
VDSNSCTVTY LNQMSDSILP YFAGNIGGWS KSIEEAAASC IKFIENATPD 550
GLKSVL 556
Length:556
Mass (Da):61,762
Last modified:June 1, 2001 - v1
Checksum:i9FE9C487BBCBB812
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB078618 mRNA. Translation: BAB84021.1.
AK004905 mRNA. Translation: BAB23658.1.
AK034622 mRNA. Translation: BAC28775.1.
BC025852 mRNA. Translation: AAH25852.1.
CCDSiCCDS26678.1.
RefSeqiNP_083066.1. NM_028790.3.
UniGeneiMm.275963.

Genome annotation databases

EnsembliENSMUST00000022120; ENSMUSP00000022120; ENSMUSG00000021620.
GeneIDi74156.
KEGGimmu:74156.
UCSCiuc007rka.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB078618 mRNA. Translation: BAB84021.1 .
AK004905 mRNA. Translation: BAB23658.1 .
AK034622 mRNA. Translation: BAC28775.1 .
BC025852 mRNA. Translation: AAH25852.1 .
CCDSi CCDS26678.1.
RefSeqi NP_083066.1. NM_028790.3.
UniGenei Mm.275963.

3D structure databases

ProteinModelPortali Q9DBK0.
SMRi Q9DBK0. Positions 8-544.
ModBasei Search...

Protein-protein interaction databases

IntActi Q9DBK0. 3 interactions.
MINTi MINT-4089645.

PTM databases

PhosphoSitei Q9DBK0.

Proteomic databases

MaxQBi Q9DBK0.
PaxDbi Q9DBK0.
PRIDEi Q9DBK0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000022120 ; ENSMUSP00000022120 ; ENSMUSG00000021620 .
GeneIDi 74156.
KEGGi mmu:74156.
UCSCi uc007rka.1. mouse.

Organism-specific databases

CTDi 134526.
MGIi MGI:1921406. Acot12.

Phylogenomic databases

eggNOGi COG1607.
GeneTreei ENSGT00750000117709.
HOGENOMi HOG000232032.
HOVERGENi HBG023847.
InParanoidi Q9DBK0.
KOi K01067.
OMAi PLWDPHY.
OrthoDBi EOG70CR6C.
PhylomeDBi Q9DBK0.
TreeFami TF328368.

Enzyme and pathway databases

UniPathwayi UPA00231 .

Miscellaneous databases

NextBioi 339934.
PROi Q9DBK0.
SOURCEi Search...

Gene expression databases

Bgeei Q9DBK0.
CleanExi MM_ACOT12.
Genevestigatori Q9DBK0.

Family and domain databases

Gene3Di 3.10.129.10. 2 hits.
3.30.530.20. 1 hit.
InterProi IPR029069. HotDog_dom.
IPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
IPR006683. Thioestr_supf.
[Graphical view ]
Pfami PF03061. 4HBT. 2 hits.
PF01852. START. 1 hit.
[Graphical view ]
SUPFAMi SSF54637. SSF54637. 2 hits.
PROSITEi PS50848. START. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiACO12_MOUSE
AccessioniPrimary (citable) accession number: Q9DBK0
Secondary accession number(s): Q544M5, Q8R108
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 114 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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