Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Acyl-coenzyme A thioesterase 4

Gene

ACOT4

Organism
Homo sapiens (Human)
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 (By similarity). Succinyl-CoA thioesterase that also hydrolyzes long chain saturated and unsaturated monocarboxylic acyl-CoAs.By similarity

Catalytic activityi

Palmitoyl-CoA + H2O = CoA + palmitate.

Kineticsi

  1. KM=14 µM for succinyl-CoA1 Publication
  2. KM=147 µM for glutaryl-CoA1 Publication
  3. KM=3.4 µM for C14-acyl-CoA1 Publication
  1. Vmax=581 nmol/min/mg enzyme toward succinyl-CoA1 Publication
  2. Vmax=132 nmol/min/mg enzyme toward glutaryl-CoA1 Publication
  3. Vmax=137 nmol/min/mg enzyme toward C14-acyl-CoA1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei232Charge relay systemBy similarity1
Active sitei326Charge relay systemBy similarity1
Active sitei360Charge relay systemBy similarity1

GO - Molecular functioni

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

GO - Biological processi

  • acyl-CoA metabolic process Source: HGNC
  • dicarboxylic acid catabolic process Source: UniProtKB
  • dicarboxylic acid metabolic process Source: HGNC
  • long-chain fatty acid metabolic process Source: HGNC
  • long-chain fatty-acyl-CoA biosynthetic process Source: Reactome
  • saturated monocarboxylic acid metabolic process Source: HGNC
  • short-chain fatty acid metabolic process Source: HGNC
  • succinyl-CoA metabolic process Source: HGNC
  • unsaturated monocarboxylic acid metabolic process Source: HGNC
  • very long-chain fatty acid metabolic process Source: HGNC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

BioCyciMetaCyc:HS16863-MONOMER.
ZFISH:HS16863-MONOMER.
ReactomeiR-HSA-75105. Fatty Acyl-CoA Biosynthesis.
SABIO-RKQ8N9L9.

Protein family/group databases

ESTHERihuman-ACOT4. Acyl-CoA_Thioesterase.
MEROPSiS09.943.

Chemistry databases

SwissLipidsiSLP:000000592.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-coenzyme A thioesterase 4 (EC:3.1.2.2)
Short name:
Acyl-CoA thioesterase 4
Alternative name(s):
PTE-2b
Peroxisomal acyl coenzyme A thioester hydrolase Ib
Peroxisomal long-chain acyl-CoA thioesterase Ib
Short name:
PTE-Ib
Gene namesi
Name:ACOT4
Synonyms:PTE2B, PTEIB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:19748. ACOT4.

Subcellular locationi

GO - Cellular componenti

  • peroxisomal matrix Source: Reactome
  • peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Organism-specific databases

DisGeNETi122970.
OpenTargetsiENSG00000177465.
PharmGKBiPA142672654.

Polymorphism and mutation databases

BioMutaiACOT4.
DMDMi50401071.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002021491 – 421Acyl-coenzyme A thioesterase 4Add BLAST421

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei42N6-acetyllysineBy similarity1
Modified residuei313N6-succinyllysineBy similarity1
Modified residuei408N6-succinyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ8N9L9.
MaxQBiQ8N9L9.
PaxDbiQ8N9L9.
PeptideAtlasiQ8N9L9.
PRIDEiQ8N9L9.

PTM databases

PhosphoSitePlusiQ8N9L9.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000177465.
CleanExiHS_ACOT4.
GenevisibleiQ8N9L9. HS.

Organism-specific databases

HPAiHPA000779.

Interactioni

GO - Molecular functioni

  • receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi125809. 1 interactor.
STRINGi9606.ENSP00000323071.

Structurei

Secondary structure

1421
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 8Combined sources5
Beta strandi20 – 25Combined sources6
Beta strandi31 – 39Combined sources9
Beta strandi45 – 53Combined sources9
Turni62 – 64Combined sources3
Beta strandi69 – 72Combined sources4
Helixi79 – 82Combined sources4
Beta strandi85 – 88Combined sources4
Beta strandi102 – 112Combined sources11
Beta strandi119 – 130Combined sources12
Beta strandi135 – 141Combined sources7
Beta strandi144 – 150Combined sources7
Beta strandi152 – 154Combined sources3
Beta strandi159 – 163Combined sources5
Helixi173 – 179Combined sources7
Turni180 – 182Combined sources3
Beta strandi184 – 189Combined sources6
Beta strandi191 – 193Combined sources3
Helixi206 – 216Combined sources11
Beta strandi224 – 231Combined sources8
Helixi233 – 244Combined sources12
Beta strandi246 – 255Combined sources10
Beta strandi265 – 267Combined sources3
Beta strandi270 – 272Combined sources3
Helixi279 – 281Combined sources3
Helixi302 – 304Combined sources3
Helixi311 – 313Combined sources3
Beta strandi318 – 323Combined sources6
Beta strandi327 – 329Combined sources3
Helixi331 – 344Combined sources14
Beta strandi351 – 355Combined sources5
Beta strandi372 – 375Combined sources4
Turni376 – 379Combined sources4
Beta strandi380 – 383Combined sources4
Helixi388 – 409Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3K2IX-ray2.40A/B1-421[»]
ProteinModelPortaliQ8N9L9.
SMRiQ8N9L9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8N9L9.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi419 – 421Microbody targeting signalSequence analysis3

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410II3X. Eukaryota.
COG1073. LUCA.
GeneTreeiENSGT00390000001046.
HOGENOMiHOG000116219.
HOVERGENiHBG000331.
InParanoidiQ8N9L9.
KOiK01068.
OMAiCCWNEPV.
OrthoDBiEOG091G08KU.
PhylomeDBiQ8N9L9.
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.

Q8N9L9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSATLILEPP GRCCWNEPVR IAVRGLAPEQ RVTLRASLRD EKGALFRAHA
60 70 80 90 100
RYCADARGEL DLERAPALGG SFAGLEPMGL LWALEPEKPF WRFLKRDVQI
110 120 130 140 150
PFVVELEVLD GHDPEPGRLL CQAQHERHFL PPGVRRQSVR AGRVRATLFL
160 170 180 190 200
PPGPGPFPGI IDIFGIGGGL LEYRASLLAG HGFATLALAY YNFEDLPNNM
210 220 230 240 250
DNISLEYFEE AVCYMLQHPQ VKGPGIGLLG ISLGADICLS MASFLKNVSA
260 270 280 290 300
TVSINGSGIS GNTAINYKHS SIPPLGYDLR RIKVAFSGLV DIVDIRNALV
310 320 330 340 350
GGYKNPSMIP IEKAQGPILL IVGQDDHNWR SELYAQTVSE RLQAHGKEKP
360 370 380 390 400
QIICYPGTGH YIEPPYFPLC PASLHRLLNK HVIWGGEPRA HSKAQEDAWK
410 420
QILAFFCKHL GGTQKTAVPK L
Length:421
Mass (Da):46,327
Last modified:July 19, 2004 - v2
Checksum:i41BBE5AA826A9F2C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti130L → P in BAC04313 (PubMed:14702039).Curated1
Sequence conflicti187 – 190ALAY → DLQS in BAC04313 (PubMed:14702039).Curated4

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05230057R → C.1 PublicationCorresponds to variant rs3742819dbSNPEnsembl.1
Natural variantiVAR_052301187A → D.Corresponds to variant rs35724886dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK094223 mRNA. Translation: BAC04313.1.
AK055797 mRNA. Translation: BAB71017.1.
BX248023 mRNA. Translation: CAD62346.1.
BX248047 mRNA. Translation: CAD62354.1.
BC031799 mRNA. Translation: AAH31799.2.
BC090945 mRNA. Translation: AAH90945.1.
BC117341 mRNA. Translation: AAI17342.1.
BC117343 mRNA. Translation: AAI17344.1.
CCDSiCCDS9817.1.
RefSeqiNP_689544.3. NM_152331.3.
UniGeneiHs.49433.

Genome annotation databases

EnsembliENST00000326303; ENSP00000323071; ENSG00000177465.
GeneIDi122970.
KEGGihsa:122970.
UCSCiuc001xoo.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK094223 mRNA. Translation: BAC04313.1.
AK055797 mRNA. Translation: BAB71017.1.
BX248023 mRNA. Translation: CAD62346.1.
BX248047 mRNA. Translation: CAD62354.1.
BC031799 mRNA. Translation: AAH31799.2.
BC090945 mRNA. Translation: AAH90945.1.
BC117341 mRNA. Translation: AAI17342.1.
BC117343 mRNA. Translation: AAI17344.1.
CCDSiCCDS9817.1.
RefSeqiNP_689544.3. NM_152331.3.
UniGeneiHs.49433.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3K2IX-ray2.40A/B1-421[»]
ProteinModelPortaliQ8N9L9.
SMRiQ8N9L9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125809. 1 interactor.
STRINGi9606.ENSP00000323071.

Chemistry databases

SwissLipidsiSLP:000000592.

Protein family/group databases

ESTHERihuman-ACOT4. Acyl-CoA_Thioesterase.
MEROPSiS09.943.

PTM databases

PhosphoSitePlusiQ8N9L9.

Polymorphism and mutation databases

BioMutaiACOT4.
DMDMi50401071.

Proteomic databases

EPDiQ8N9L9.
MaxQBiQ8N9L9.
PaxDbiQ8N9L9.
PeptideAtlasiQ8N9L9.
PRIDEiQ8N9L9.

Protocols and materials databases

DNASUi122970.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000326303; ENSP00000323071; ENSG00000177465.
GeneIDi122970.
KEGGihsa:122970.
UCSCiuc001xoo.4. human.

Organism-specific databases

CTDi122970.
DisGeNETi122970.
GeneCardsiACOT4.
H-InvDBHIX0202062.
HGNCiHGNC:19748. ACOT4.
HPAiHPA000779.
MIMi614314. gene.
neXtProtiNX_Q8N9L9.
OpenTargetsiENSG00000177465.
PharmGKBiPA142672654.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410II3X. Eukaryota.
COG1073. LUCA.
GeneTreeiENSGT00390000001046.
HOGENOMiHOG000116219.
HOVERGENiHBG000331.
InParanoidiQ8N9L9.
KOiK01068.
OMAiCCWNEPV.
OrthoDBiEOG091G08KU.
PhylomeDBiQ8N9L9.
TreeFamiTF314911.

Enzyme and pathway databases

BioCyciMetaCyc:HS16863-MONOMER.
ZFISH:HS16863-MONOMER.
ReactomeiR-HSA-75105. Fatty Acyl-CoA Biosynthesis.
SABIO-RKQ8N9L9.

Miscellaneous databases

EvolutionaryTraceiQ8N9L9.
GeneWikiiACOT4.
GenomeRNAii122970.
PROiQ8N9L9.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000177465.
CleanExiHS_ACOT4.
GenevisibleiQ8N9L9. HS.

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 nameiACOT4_HUMAN
AccessioniPrimary (citable) accession number: Q8N9L9
Secondary accession number(s): Q17RF4
, Q5BKT6, Q86TX0, Q86TX1, Q96N88
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: November 2, 2016
This is version 121 of the entry and version 2 of the sequence. [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

Miscellaneous

Human ACOT4 may have acquired the combined activities of mouse ACOT3, ACOT4, and ACOT5.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.