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Q99NB7 (ACO12_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 87. 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

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=rACH
Short name=rCACH-1
Gene names
Name:Acot12
Synonyms:Cach, Cach1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

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

General annotation (Comments)

Function

Hydrolyzes acetyl-CoA to acetate and CoA.

Catalytic activity

Acetyl-CoA + H2O = CoA + acetate.

Enzyme regulation

Allosterically regulated by ATP (activator) and ADP (inhibitor).

Pathway

Carbohydrate metabolism; pyruvate metabolism.

Subunit structure

Active homodimer or homotetramer at room temperature and inactive monomer at low temperature.

Subcellular location

Cytoplasm.

Induction

By 2-(p-chlorophenoxy)isobutyric acid (CPIB).

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_0000053811

Regions

Domain1 – 128128Acyl coenzyme A hydrolase 1
Domain162 – 302141Acyl coenzyme A hydrolase 2
Domain341 – 550210START
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 By similarity
Modified residue971N6-succinyllysine By similarity
Modified residue1601N6-succinyllysine By similarity
Modified residue2291N6-succinyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q99NB7 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 81E592F066AB0C9E

FASTA55662,018
        10         20         30         40         50         60 
MEPTVAPGEV LMSQAIQPAH ADSRGELSAG QLLKWMDTTA CLAAEKHAGI SCVTASMDDI 

        70         80         90        100        110        120 
LFEDTARIGQ IVTIRAKVTR AFSTSMEISI KVRVQDKFTG IQKLLCVAFS TFVVKPLGKE 

       130        140        150        160        170        180 
KVHLKPVLLQ TEQEQVEHRL ASERRKVRLQ HENTFSNIMK ESNWLRDPVC NEEEGTATTM 

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

       250        260        270        280        290        300 
TVGDRLVFNA IVNNTFQNSV EVGVRVEAFD CREWAEGQGR HINSAFLIYN AVDDQEELIT 

       310        320        330        340        350        360 
FPRIQPISKD DFRRYQGAIA RRRIRLGRKY VISHKKEVPL GTQWDISKKG SISNTNVEAL 

       370        380        390        400        410        420 
KNLASKSGWE ITTTLEKIKI YTLEEQDAIS VKVEKQVGSP ARVAYHLLSD FTKRPLWDPH 

       430        440        450        460        470        480 
YISCEVIDQV SEDDQIYYIT CSVVNGDKPK DFVVLVSQRK PLKDDNTYIV ALMSVVLPSV 

       490        500        510        520        530        540 
PPSPQYIRSQ VICAGFLIQP VDSSSCTVAY LNQMSDSILP YFAGNIGGWS KSIEEAAASC 

       550 
IKFIENATHD GLKSVL 

« Hide

References

[1]"Molecular cloning and functional expression of rat liver cytosolic acetyl-CoA hydrolase."
Suematsu N., Okamoto K., Shibata K., Nakanishi Y., Isohashi F.
Eur. J. Biochem. 268:2700-2709(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 161-174 AND 352-364.
Strain: Donryu.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB040609 mRNA. Translation: BAB39852.1.
RefSeqNP_570103.1. NM_130747.1.
UniGeneRn.212205.

3D structure databases

ProteinModelPortalQ99NB7.
SMRQ99NB7. Positions 8-299.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000021675.

Proteomic databases

PRIDEQ99NB7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID170570.
KEGGrno:170570.
UCSCRGD:619752. rat.

Organism-specific databases

CTD134526.
RGD619752. Acot12.

Phylogenomic databases

eggNOGCOG1607.
HOGENOMHOG000232032.
HOVERGENHBG023847.
InParanoidQ99NB7.
KOK01067.
PhylomeDBQ99NB7.

Enzyme and pathway databases

BRENDA3.1.2.1. 5301.
SABIO-RKQ99NB7.
UniPathwayUPA00231.

Gene expression databases

GenevestigatorQ99NB7.

Family and domain databases

Gene3D3.10.129.10. 2 hits.
3.30.530.20. 1 hit.
InterProIPR029069. HotDog_dom.
IPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
IPR006683. Thioestr_supf.
[Graphical view]
PfamPF03061. 4HBT. 2 hits.
PF01852. START. 1 hit.
[Graphical view]
SUPFAMSSF54637. SSF54637. 2 hits.
PROSITEPS50848. START. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio621056.

Entry information

Entry nameACO12_RAT
AccessionPrimary (citable) accession number: Q99NB7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: June 1, 2001
Last modified: June 11, 2014
This is version 87 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