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Protein

Acyl-coenzyme A thioesterase 2, mitochondrial

Gene

Acot2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Most active on substrates with chain lengths ranging from C14-C20.1 Publication

Catalytic activityi

Palmitoyl-CoA + H2O = CoA + palmitate.1 Publication

Kineticsi

  1. KM=16 µM for C10-acyl-CoA1 Publication
  2. KM=5 µM for C12-acyl-CoA1 Publication
  3. KM=3 µM for C14-acyl-CoA1 Publication
  4. KM=6 µM for C16-acyl-CoA1 Publication
  5. KM=3 µM for C18-acyl-CoA1 Publication
  6. KM=2 µM for C20-acyl-CoA1 Publication
  1. Vmax=1 µmol/min/mg enzyme for C10-acyl-CoA1 Publication
  2. Vmax=2.2 µmol/min/mg enzyme for C12-acyl-CoA1 Publication
  3. Vmax=4.2 µmol/min/mg enzyme for C14-acyl-CoA1 Publication
  4. Vmax=4.5 µmol/min/mg enzyme for C16-acyl-CoA1 Publication
  5. Vmax=3.3 µmol/min/mg enzyme for C18-acyl-CoA1 Publication
  6. Vmax=3.1 µmol/min/mg enzyme for C20-acyl-CoA1 Publication

pH dependencei

Optimum pH is 8-9.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei273Charge relay systemBy similarity1
Active sitei365Charge relay systemBy similarity1
Active sitei399Charge relay systemBy similarity1

GO - Molecular functioni

  • acyl-CoA hydrolase activity Source: RGD
  • carboxylic ester hydrolase activity Source: UniProtKB-KW
  • myristoyl-CoA hydrolase activity Source: UniProtKB-EC
  • palmitoyl-CoA hydrolase activity Source: RGD

GO - Biological processi

  • acyl-CoA metabolic process Source: RGD
  • response to drug Source: RGD
  • response to epidermal growth factor Source: RGD
  • response to hormone Source: RGD
  • response to hypoxia Source: HGNC
  • response to nutrient levels Source: RGD
  • very long-chain fatty acid catabolic process Source: RGD

Keywordsi

Molecular functionHydrolase, Serine esterase

Enzyme and pathway databases

BRENDAi3.1.2.2 5301
3.1.2.20 5301

Protein family/group databases

ESTHERiratno-acot2 Acyl-CoA_Thioesterase

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-coenzyme A thioesterase 2, mitochondrial (EC:3.1.2.21 Publication)
Short name:
Acyl-CoA thioesterase 2
Alternative name(s):
ARTISt/p43
Acyl coenzyme A thioester hydrolase
MTE-I1 Publication
Very-long-chain acyl-CoA thioesterase1 Publication
Gene namesi
Name:Acot2
Synonyms:Mte1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621055 Acot2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 42MitochondrionSequence analysisAdd BLAST42
ChainiPRO_000003406643 – 453Acyl-coenzyme A thioesterase 2, mitochondrialAdd BLAST411

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei83N6-acetyllysineBy similarity1
Modified residuei447N6-succinyllysineBy similarity1

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiO55171
PRIDEiO55171

PTM databases

iPTMnetiO55171
PhosphoSitePlusiO55171

Expressioni

Tissue specificityi

Constitutively expressed in heart and brown fat. Strongly induced in liver, and weakly in kidney, in peroxisome proliferator treated rat.1 Publication

Inductioni

Regulated by peroxisome proliferator, via the peroxisome proliferator-activated receptors (PPARs).1 Publication

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000013515

Structurei

3D structure databases

ProteinModelPortaliO55171
SMRiO55171
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the C/M/P thioester hydrolase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410II3X Eukaryota
COG1073 LUCA
HOGENOMiHOG000116219
HOVERGENiHBG000331
InParanoidiO55171
PhylomeDBiO55171

Family and domain databases

Gene3Di3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR016662 Acyl-CoA_thioEstase_long-chain
IPR014940 BAAT_C
IPR006862 Thio_Ohase/aa_AcTrfase
PfamiView protein in Pfam
PF08840 BAAT_C, 1 hit
PF04775 Bile_Hydr_Trans, 1 hit
PIRSFiPIRSF016521 Acyl-CoA_hydro, 1 hit
SUPFAMiSSF53474 SSF53474, 2 hits

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O55171-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVASSFAVLR ASRLCQWGWK SWTQLSGPPP LSTGGRTTFA RTNATLSLEP
60 70 80 90 100
GSRSCWDEPL SITVRGLAPE QPVTLRAALR DEKGALFRAH ARYRADAGGE
110 120 130 140 150
LDLARAPALG GSFTGLEPMG LIWAMEPERP LWRLVKRDVQ KPYVVELEVL
160 170 180 190 200
DGHEPDGGQR LAQAVHERHF MAPGVRRVPV RDGRVRATLF LPPEPGPFPE
210 220 230 240 250
IIDLFGVGGG LLEYRASLLA GKGFAVMALA YYNYDDLPKT METMRIEYFE
260 270 280 290 300
EAVNYLRGHP EVKGPGIGLL GISKGGELGL AMASFLKGIT AAVVINGSVA
310 320 330 340 350
AVGNTVCYKD ETIPPVSLLR DKVKMTKDGL LDVVEALQSP LVDKKSFIPV
360 370 380 390 400
ERSDTTFLFL VGQDDHNWKS EFYAREASKR LQAHGKEKPQ IICYPEAGHY
410 420 430 440 450
IEPPYFPLCS AGMHLLVGAN ITFGGEPKPH SVAQLDAWQQ LQTFFHKQLS

GKS
Length:453
Mass (Da):49,701
Last modified:June 1, 1998 - v1
Checksum:iF48C2C61475072B2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti51 – 52GS → AG in BAA32539 (PubMed:9703974).Curated2
Sequence conflicti90 – 92HAR → RAL in BAA32539 (PubMed:9703974).Curated3
Sequence conflicti123W → R in BAA32539 (PubMed:9703974).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09333 mRNA Translation: CAA70513.1
AB010429 mRNA Translation: BAA32539.1
UniGeneiRn.37524

Genome annotation databases

UCSCiRGD:621055 rat

Similar proteinsi

Entry informationi

Entry nameiACOT2_RAT
AccessioniPrimary (citable) accession number: O55171
Secondary accession number(s): O88268
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: May 23, 2018
This is version 114 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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