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Q99NB7

- ACO12_RAT

UniProt

Q99NB7 - ACO12_RAT

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

Functioni

Hydrolyzes acetyl-CoA to acetate and CoA.

Catalytic activityi

Acetyl-CoA + H2O = CoA + acetate.

Enzyme regulationi

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

Pathwayi

Sites

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

GO - Molecular functioni

  1. ATP binding Source: BHF-UCL
  2. acetyl-CoA hydrolase activity Source: HGNC
  3. lipid binding Source: InterPro

GO - Biological processi

  1. acyl-CoA metabolic process Source: HGNC
  2. fatty acid metabolic process Source: UniProtKB-KW
  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

BRENDAi3.1.2.1. 5301.
SABIO-RKQ99NB7.
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:
rACH
Short name:
rCACH-1
Gene namesi
Name:Acot12
Synonyms:Cach, Cach1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi619752. Acot12.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 556556Acyl-coenzyme A thioesterase 12
PRO_0000053811Add
BLAST

Amino acid modifications

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

Proteomic databases

PRIDEiQ99NB7.

Expressioni

Inductioni

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

Gene expression databases

GenevestigatoriQ99NB7.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021675.

Structurei

3D structure databases

ProteinModelPortaliQ99NB7.
SMRiQ99NB7. Positions 8-299.

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
Domaini341 – 550210START
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.
HOGENOMiHOG000232032.
HOVERGENiHBG023847.
InParanoidiQ99NB7.
KOiK01067.
PhylomeDBiQ99NB7.

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.

Q99NB7-1 [UniParc]FASTAAdd to Basket

« Hide

MEPTVAPGEV LMSQAIQPAH ADSRGELSAG QLLKWMDTTA CLAAEKHAGI    50
SCVTASMDDI LFEDTARIGQ IVTIRAKVTR AFSTSMEISI KVRVQDKFTG 100
IQKLLCVAFS TFVVKPLGKE KVHLKPVLLQ TEQEQVEHRL ASERRKVRLQ 150
HENTFSNIMK ESNWLRDPVC NEEEGTATTM ATSVQSIELV LPPHANHHGN 200
TFGGQIMAWM ETVATISASR LCHGHPFLKS VDMFKFRGPS TVGDRLVFNA 250
IVNNTFQNSV EVGVRVEAFD CREWAEGQGR HINSAFLIYN AVDDQEELIT 300
FPRIQPISKD DFRRYQGAIA RRRIRLGRKY VISHKKEVPL GTQWDISKKG 350
SISNTNVEAL KNLASKSGWE ITTTLEKIKI YTLEEQDAIS VKVEKQVGSP 400
ARVAYHLLSD FTKRPLWDPH YISCEVIDQV SEDDQIYYIT CSVVNGDKPK 450
DFVVLVSQRK PLKDDNTYIV ALMSVVLPSV PPSPQYIRSQ VICAGFLIQP 500
VDSSSCTVAY LNQMSDSILP YFAGNIGGWS KSIEEAAASC IKFIENATHD 550
GLKSVL 556
Length:556
Mass (Da):62,018
Last modified:June 1, 2001 - v1
Checksum:i81E592F066AB0C9E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB040609 mRNA. Translation: BAB39852.1.
RefSeqiNP_570103.1. NM_130747.1.
UniGeneiRn.212205.

Genome annotation databases

GeneIDi170570.
KEGGirno:170570.
UCSCiRGD:619752. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB040609 mRNA. Translation: BAB39852.1 .
RefSeqi NP_570103.1. NM_130747.1.
UniGenei Rn.212205.

3D structure databases

ProteinModelPortali Q99NB7.
SMRi Q99NB7. Positions 8-299.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000021675.

Proteomic databases

PRIDEi Q99NB7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 170570.
KEGGi rno:170570.
UCSCi RGD:619752. rat.

Organism-specific databases

CTDi 134526.
RGDi 619752. Acot12.

Phylogenomic databases

eggNOGi COG1607.
HOGENOMi HOG000232032.
HOVERGENi HBG023847.
InParanoidi Q99NB7.
KOi K01067.
PhylomeDBi Q99NB7.

Enzyme and pathway databases

UniPathwayi UPA00231 .
BRENDAi 3.1.2.1. 5301.
SABIO-RK Q99NB7.

Miscellaneous databases

NextBioi 621056.

Gene expression databases

Genevestigatori Q99NB7.

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

  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.

Entry informationi

Entry nameiACO12_RAT
AccessioniPrimary (citable) accession number: Q99NB7
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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