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Protein

Acyl-coenzyme A thioesterase 2, mitochondrial

Gene

ACOT2

Organism
Homo sapiens (Human)
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. Displays high levels of activity on medium- and long chain acyl CoAs.2 Publications

Caution

Was originally (PubMed:10944470) thought to be peroxisomal but was later shown (PubMed:16940157) to be mitochondrial.2 Publications

Catalytic activityi

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

Kineticsi

  1. KM=40.3 µM for C10-acyl-CoA1 Publication
  2. KM=8.9 µM for C12-acyl-CoA1 Publication
  3. KM=1.6 µM for C14-acyl-CoA1 Publication
  4. KM=2.0 µM for C16-acyl-CoA1 Publication
  5. KM=2.8 µM for C18-acyl-CoA1 Publication
  6. KM=4.8 µM for C20-acyl-CoA1 Publication
  7. KM=4.5 µM for C16:1-acyl-CoA1 Publication
  8. KM=6.1 µM for C18:1-acyl-CoA1 Publication
  9. KM=4.3 µM for C18:1-trans-acyl-CoA1 Publication
  1. Vmax=212 nmol/min/mg enzyme toward C10-acyl-CoA1 Publication
  2. Vmax=681 nmol/min/mg enzyme toward C12-acyl-CoA1 Publication
  3. Vmax=766 nmol/min/mg enzyme toward C14-acyl-CoA1 Publication
  4. Vmax=656 nmol/min/mg enzyme toward C16-acyl-CoA1 Publication
  5. Vmax=488 nmol/min/mg enzyme toward C18-acyl-CoA1 Publication
  6. Vmax=408 nmol/min/mg enzyme toward C20-acyl-CoA1 Publication
  7. Vmax=661 nmol/min/mg enzyme toward C16:1-acyl-CoA1 Publication
  8. Vmax=304 nmol/min/mg enzyme toward C18:1-acyl-CoA1 Publication
  9. Vmax=418 nmol/min/mg enzyme toward C18:1-trans-acyl-CoA1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei294Charge relay system1 Publication1
Active sitei388Charge relay system1 Publication1
Active sitei422Charge relay system1 Publication1

GO - Molecular functioni

  • acyl-CoA hydrolase activity Source: HGNC
  • carboxylic ester hydrolase activity Source: UniProtKB-KW
  • myristoyl-CoA hydrolase activity Source: UniProtKB-EC
  • palmitoyl-CoA hydrolase activity Source: UniProtKB-EC
  • receptor binding Source: UniProtKB

GO - Biological processi

  • acyl-CoA metabolic process Source: HGNC
  • long-chain fatty acid metabolic process Source: HGNC
  • very long-chain fatty acid metabolic process Source: HGNC

Keywordsi

Molecular functionHydrolase, Serine esterase

Enzyme and pathway databases

BioCyciMetaCyc:HS04318-MONOMER
BRENDAi3.1.2.2 2681
ReactomeiR-HSA-77289 Mitochondrial Fatty Acid Beta-Oxidation
SABIO-RKiP49753

Protein family/group databases

ESTHERihuman-ACOT2 Acyl-CoA_Thioesterase
MEROPSiS09.942

Chemistry databases

SwissLipidsiSLP:000000590

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):
Acyl-coenzyme A thioester hydrolase 2a
CTE-Ia
Long-chain acyl-CoA thioesterase 2
ZAP128
Gene namesi
Name:ACOT2
Synonyms:PTE2, PTE2A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

EuPathDBiHostDB:ENSG00000119673.14
HGNCiHGNC:18431 ACOT2
MIMi609972 gene
neXtProtiNX_P49753

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

Pathology & Biotechi

Organism-specific databases

DisGeNETi10965
OpenTargetsiENSG00000119673
PharmGKBiPA142672653

Chemistry databases

ChEMBLiCHEMBL2189135

Polymorphism and mutation databases

BioMutaiACOT2
DMDMi269849771

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000202147? – 483Acyl-coenzyme A thioesterase 2, mitochondrial
Transit peptidei1 – ?MitochondrionSequence analysis

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei104N6-acetyllysineBy similarity1
Modified residuei470N6-succinyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP49753
MaxQBiP49753
PaxDbiP49753
PeptideAtlasiP49753
PRIDEiP49753

PTM databases

CarbonylDBiP49753
iPTMnetiP49753
PhosphoSitePlusiP49753
SwissPalmiP49753

Expressioni

Tissue specificityi

Strongest expression in heart, liver, muscle and kidney. Weak in placenta and pancreas.1 Publication

Gene expression databases

BgeeiENSG00000119673
CleanExiHS_ACOT2
ExpressionAtlasiP49753 baseline and differential
GenevisibleiP49753 HS

Organism-specific databases

HPAiHPA043705

Interactioni

Subunit structurei

Monomer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
NLGN3Q9NZ94-22EBI-1052865,EBI-16423037

GO - Molecular functioni

  • receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi11616410 interactors.
IntActiP49753 2 interactors.
STRINGi9606.ENSP00000238651

Structurei

Secondary structure

1483
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi66 – 71Combined sources6
Beta strandi82 – 87Combined sources6
Beta strandi93 – 101Combined sources9
Beta strandi107 – 115Combined sources9
Turni124 – 126Combined sources3
Beta strandi131 – 133Combined sources3
Helixi141 – 144Combined sources4
Beta strandi147 – 150Combined sources4
Beta strandi164 – 174Combined sources11
Beta strandi181 – 192Combined sources12
Beta strandi197 – 203Combined sources7
Beta strandi206 – 212Combined sources7
Beta strandi214 – 216Combined sources3
Beta strandi221 – 225Combined sources5
Helixi235 – 241Combined sources7
Turni242 – 244Combined sources3
Beta strandi246 – 250Combined sources5
Beta strandi253 – 255Combined sources3
Beta strandi263 – 266Combined sources4
Helixi267 – 278Combined sources12
Beta strandi286 – 293Combined sources8
Helixi295 – 306Combined sources12
Beta strandi310 – 317Combined sources8
Beta strandi324 – 329Combined sources6
Beta strandi332 – 334Combined sources3
Helixi341 – 343Combined sources3
Beta strandi348 – 350Combined sources3
Helixi364 – 369Combined sources6
Helixi373 – 375Combined sources3
Beta strandi378 – 385Combined sources8
Helixi393 – 406Combined sources14
Beta strandi413 – 417Combined sources5
Helixi450 – 471Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HLKX-ray2.10A/B46-483[»]
ProteinModelPortaliP49753
SMRiP49753
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49753

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi481 – 483Microbody targeting signalSequence analysis3

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
InParanoidiP49753
KOiK01068
OMAiISKPHAM
OrthoDBiEOG091G08KU
PhylomeDBiP49753
TreeFamiTF314911

Family and domain databases

Gene3Di3.40.50.18201 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

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P49753-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSNKLLSPHP HSVVLRSEFK MASSPAVLRA SRLYQWSLKS SAQFLGSPQL
60 70 80 90 100
RQVGQIIRVP ARMAATLILE PAGRCCWDEP VRIAVRGLAP EQPVTLRASL
110 120 130 140 150
RDEKGALFQA HARYRADTLG ELDLERAPAL GGSFAGLEPM GLLWALEPEK
160 170 180 190 200
PLVRLVKRDV RTPLAVELEV LDGHDPDPGR LLCQTRHERY FLPPGVRREP
210 220 230 240 250
VRVGRVRGTL FLPPEPGPFP GIVDMFGTGG GLLEYRASLL AGKGFAVMAL
260 270 280 290 300
AYYNYEDLPK TMETLHLEYF EEAMNYLLSH PEVKGPGVGL LGISKGGELC
310 320 330 340 350
LSMASFLKGI TAAVVINGSV ANVGGTLHYK GETLPPVGVN RNRIKVTKDG
360 370 380 390 400
YADIVDVLNS PLEGPDQKSF IPVERAESTF LFLVGQDDHN WKSEFYANEA
410 420 430 440 450
CKRLQAHGRR KPQIICYPET GHYIEPPYFP LCRASLHALV GSPIIWGGEP
460 470 480
RAHAMAQVDA WKQLQTFFHK HLGGHEGTIP SKV
Length:483
Mass (Da):53,218
Last modified:November 24, 2009 - v6
Checksum:iFAEDD42BBBD935E4
GO
Isoform 2 (identifier: P49753-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: Missing.
     53-214: Missing.

Show »
Length:301
Mass (Da):32,959
Checksum:iD157DF13EAF26EC6
GO

Sequence cautioni

The sequence AAC42007 differs from that shown. Reason: Frameshift at positions 215 and 226.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti167E → V in AAZ31237 (PubMed:16940157).Curated1
Sequence conflicti167E → V in BAA91989 (PubMed:14702039).Curated1
Sequence conflicti328H → R in AAZ31237 (PubMed:16940157).Curated1
Sequence conflicti328H → R in BAA91989 (PubMed:14702039).Curated1
Sequence conflicti328H → R in BAD97355 (Ref. 4) Curated1
Sequence conflicti328H → R in AAH04436 (PubMed:15489334).Curated1
Sequence conflicti328H → R in AAH06335 (PubMed:15489334).Curated1
Sequence conflicti328H → R in AAH06500 (PubMed:15489334).Curated1
Sequence conflicti328H → R in AAF97985 (PubMed:10944470).Curated1
Sequence conflicti454A → V in AAH06335 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05727116R → S. Corresponds to variant dbSNP:rs11545741Ensembl.1
Natural variantiVAR_016136475H → R4 PublicationsCorresponds to variant dbSNP:rs7494Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0122251 – 20Missing in isoform 2. 1 PublicationAdd BLAST20
Alternative sequenceiVSP_01222653 – 214Missing in isoform 2. 1 PublicationAdd BLAST162

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L40401 mRNA Translation: AAC42007.1 Frameshift.
DQ082755 mRNA Translation: AAZ31237.1
AK001939 mRNA Translation: BAA91989.1
AK223635 mRNA Translation: BAD97355.1
BC004436 mRNA Translation: AAH04436.2
BC006335 mRNA Translation: AAH06335.1
BC006500 mRNA Translation: AAH06500.4
AY005822 mRNA Translation: AAF97985.1
CCDSiCCDS9816.1 [P49753-1]
PIRiJC7367
RefSeqiNP_006812.3, NM_006821.5 [P49753-1]
UniGeneiHs.446685

Genome annotation databases

EnsembliENST00000238651; ENSP00000238651; ENSG00000119673 [P49753-1]
GeneIDi10965
KEGGihsa:10965
UCSCiuc001xon.6 human [P49753-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiACOT2_HUMAN
AccessioniPrimary (citable) accession number: P49753
Secondary accession number(s): Q3I5F8, Q53EK4, Q9NUX4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 24, 2009
Last modified: March 28, 2018
This is version 175 of the entry and version 6 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome