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Protein

Acyl-coenzyme A thioesterase 2, mitochondrial

Gene

Acot2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 (By similarity).By similarity

Catalytic activityi

Palmitoyl-CoA + H2O = CoA + palmitate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei273 – 2731Charge relay systemBy similarity
Active sitei365 – 3651Charge relay systemBy similarity
Active sitei399 – 3991Charge relay systemBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

ReactomeiR-MMU-75105. Fatty Acyl-CoA Biosynthesis.

Protein family/group databases

ESTHERimouse-acot2. Acyl-CoA_Thioesterase.
MEROPSiS09.A52.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-coenzyme A thioesterase 2, mitochondrial (EC:3.1.2.2)
Short name:
Acyl-CoA thioesterase 2
Alternative name(s):
Acyl coenzyme A thioester hydrolase
MTE-I
Very-long-chain acyl-CoA thioesterase
Gene namesi
Name:Acot2
Synonyms:Mte1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:2159605. Acot2.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3259488.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4242MitochondrionSequence analysisAdd
BLAST
Chaini43 – 453411Acyl-coenzyme A thioesterase 2, mitochondrialPRO_0000034065Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei83 – 831N6-acetyllysineCombined sources
Modified residuei447 – 4471N6-succinyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9QYR9.
MaxQBiQ9QYR9.
PaxDbiQ9QYR9.
PeptideAtlasiQ9QYR9.
PRIDEiQ9QYR9.

PTM databases

iPTMnetiQ9QYR9.
PhosphoSiteiQ9QYR9.

Expressioni

Tissue specificityi

Highly expressed in brown and white adipose tissue, muscle, heart, kidney, lung, adrenal gland and spleen; weakly expressed in intestine, testis and brain.2 Publications

Inductioni

In the liver, by peroxisome proliferator (Clofibrate) treatment, via the peroxisome proliferator-activated receptors (PPARs) or fasting for 24 hours.1 Publication

Gene expression databases

BgeeiENSMUSG00000021226.
GenevisibleiQ9QYR9. MM.

Interactioni

Subunit structurei

Monomer.

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ9QYR9. 2 interactions.
MINTiMINT-1855915.
STRINGi10090.ENSMUSP00000021649.

Structurei

3D structure databases

ProteinModelPortaliQ9QYR9.
SMRiQ9QYR9. Positions 40-449.
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.
GeneTreeiENSGT00390000001046.
HOGENOMiHOG000116219.
HOVERGENiHBG000331.
InParanoidiQ9QYR9.
KOiK01068.
OMAiAYRIVQC.
OrthoDBiEOG091G08KU.
TreeFamiTF314911.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR016662. Acyl-CoA_thioEstase_long-chain.
IPR014940. BAAT_C.
IPR006862. Thio_Ohase/aa_AcTrfase.
[Graphical view]
PfamiPF08840. BAAT_C. 1 hit.
PF04775. Bile_Hydr_Trans. 1 hit.
[Graphical view]
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.

Q9QYR9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVASSFAVLR ASRLCQQDWK SWARLFVPPP LSTGGRTTWA RTNATLSVEP
60 70 80 90 100
EGRSCWDEPL SIAVRGLAPE QPVTLRSALR DEKGALFRAH ARYRADAGGE
110 120 130 140 150
LNLARAPALG GSFSGLEPMG LLWAMEPERP LWRLIKRDVQ TPFLVELEVL
160 170 180 190 200
DGHEPDGGQR LAQAVHERHF LAPGVRRVPV REGRVRATLF LPPEPGPFPG
210 220 230 240 250
IIDLFGVGGG LLEYRASLLA GKGFAVMALA YYNYDDLPKS IETMHMEYFE
260 270 280 290 300
EAVNYLRSHP EVKGPGIGLL GISKGGELGL AMASFLKGIT AAVVINGSVA
310 320 330 340 350
AVGNTISYKD ETIPPVSLLR NQVKMTKDGL LDVVEALQSP LVDKKSFIPV
360 370 380 390 400
ERSDTTFLFL VGQDDHNWKS EFYADEISKR LQAHGKEKPQ IICYPAAGHY
410 420 430 440 450
IEPPYFPLCS AGMHLLVGAN ITFGGEPRAH AVAQVDAWQQ LQTFFHKQLG

SKS
Length:453
Mass (Da):49,657
Last modified:July 27, 2011 - v2
Checksum:i5687F2363B16284B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti163 – 1631Q → H in AAF13871 (PubMed:10567408).Curated
Sequence conflicti319 – 3191L → V in AAF13871 (PubMed:10567408).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF180798, AF180796, AF180797 Genomic DNA. Translation: AAF13871.1.
AK172617 mRNA. Translation: BAE43095.1.
CH466590 Genomic DNA. Translation: EDL02755.1.
CCDSiCCDS26034.1.
RefSeqiNP_598949.3. NM_134188.3.
UniGeneiMm.371675.

Genome annotation databases

EnsembliENSMUST00000021649; ENSMUSP00000021649; ENSMUSG00000021226.
GeneIDi171210.
KEGGimmu:171210.
UCSCiuc011yor.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF180798, AF180796, AF180797 Genomic DNA. Translation: AAF13871.1.
AK172617 mRNA. Translation: BAE43095.1.
CH466590 Genomic DNA. Translation: EDL02755.1.
CCDSiCCDS26034.1.
RefSeqiNP_598949.3. NM_134188.3.
UniGeneiMm.371675.

3D structure databases

ProteinModelPortaliQ9QYR9.
SMRiQ9QYR9. Positions 40-449.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9QYR9. 2 interactions.
MINTiMINT-1855915.
STRINGi10090.ENSMUSP00000021649.

Chemistry

ChEMBLiCHEMBL3259488.

Protein family/group databases

ESTHERimouse-acot2. Acyl-CoA_Thioesterase.
MEROPSiS09.A52.

PTM databases

iPTMnetiQ9QYR9.
PhosphoSiteiQ9QYR9.

Proteomic databases

EPDiQ9QYR9.
MaxQBiQ9QYR9.
PaxDbiQ9QYR9.
PeptideAtlasiQ9QYR9.
PRIDEiQ9QYR9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021649; ENSMUSP00000021649; ENSMUSG00000021226.
GeneIDi171210.
KEGGimmu:171210.
UCSCiuc011yor.1. mouse.

Organism-specific databases

CTDi10965.
MGIiMGI:2159605. Acot2.

Phylogenomic databases

eggNOGiENOG410II3X. Eukaryota.
COG1073. LUCA.
GeneTreeiENSGT00390000001046.
HOGENOMiHOG000116219.
HOVERGENiHBG000331.
InParanoidiQ9QYR9.
KOiK01068.
OMAiAYRIVQC.
OrthoDBiEOG091G08KU.
TreeFamiTF314911.

Enzyme and pathway databases

ReactomeiR-MMU-75105. Fatty Acyl-CoA Biosynthesis.

Miscellaneous databases

PROiQ9QYR9.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000021226.
GenevisibleiQ9QYR9. MM.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR016662. Acyl-CoA_thioEstase_long-chain.
IPR014940. BAAT_C.
IPR006862. Thio_Ohase/aa_AcTrfase.
[Graphical view]
PfamiPF08840. BAAT_C. 1 hit.
PF04775. Bile_Hydr_Trans. 1 hit.
[Graphical view]
PIRSFiPIRSF016521. Acyl-CoA_hydro. 1 hit.
SUPFAMiSSF53474. SSF53474. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiACOT2_MOUSE
AccessioniPrimary (citable) accession number: Q9QYR9
Secondary accession number(s): Q3T9C9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: July 27, 2011
Last modified: September 7, 2016
This is version 128 of the entry and version 2 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.