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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei232 – 2321Charge relay systemBy similarity
Active sitei326 – 3261Charge relay systemBy similarity
Active sitei360 – 3601Charge relay systemBy similarity

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
  • 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.
SABIO-RKQ8N9L9.

Protein family/group databases

ESTHERihuman-ACOT4. Acyl-CoA_Thioesterase.
MEROPSiS09.029.

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
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:19748. ACOT4.

Subcellular locationi

  • Peroxisome 1 Publication

GO - Cellular componenti

  • peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142672654.

Polymorphism and mutation databases

BioMutaiACOT4.
DMDMi50401071.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 421420Acyl-coenzyme A thioesterase 4PRO_0000202149Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei313 – 3131N6-succinyllysineBy similarity

Proteomic databases

MaxQBiQ8N9L9.
PaxDbiQ8N9L9.
PRIDEiQ8N9L9.

PTM databases

PhosphoSiteiQ8N9L9.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ8N9L9.
CleanExiHS_ACOT4.
GenevisibleiQ8N9L9. HS.

Organism-specific databases

HPAiHPA000779.

Interactioni

Protein-protein interaction databases

BioGridi125809. 1 interaction.
STRINGi9606.ENSP00000323071.

Structurei

Secondary structure

1
421
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Beta strandi20 – 256Combined sources
Beta strandi31 – 399Combined sources
Beta strandi45 – 539Combined sources
Turni62 – 643Combined sources
Beta strandi69 – 724Combined sources
Helixi79 – 824Combined sources
Beta strandi85 – 884Combined sources
Beta strandi102 – 11211Combined sources
Beta strandi119 – 13012Combined sources
Beta strandi135 – 1417Combined sources
Beta strandi144 – 1507Combined sources
Beta strandi152 – 1543Combined sources
Beta strandi159 – 1635Combined sources
Helixi173 – 1797Combined sources
Turni180 – 1823Combined sources
Beta strandi184 – 1896Combined sources
Beta strandi191 – 1933Combined sources
Helixi206 – 21611Combined sources
Beta strandi224 – 2318Combined sources
Helixi233 – 24412Combined sources
Beta strandi246 – 25510Combined sources
Beta strandi265 – 2673Combined sources
Beta strandi270 – 2723Combined sources
Helixi279 – 2813Combined sources
Helixi302 – 3043Combined sources
Helixi311 – 3133Combined sources
Beta strandi318 – 3236Combined sources
Beta strandi327 – 3293Combined sources
Helixi331 – 34414Combined sources
Beta strandi351 – 3555Combined sources
Beta strandi372 – 3754Combined sources
Turni376 – 3794Combined sources
Beta strandi380 – 3834Combined sources
Helixi388 – 40922Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3K2IX-ray2.40A/B1-421[»]
ProteinModelPortaliQ8N9L9.
SMRiQ8N9L9. Positions 3-410.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8N9L9.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi419 – 4213Microbody targeting signalSequence Analysis

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1073.
GeneTreeiENSGT00390000001046.
HOGENOMiHOG000116219.
HOVERGENiHBG000331.
InParanoidiQ8N9L9.
KOiK01068.
OMAiCCWNEPV.
OrthoDBiEOG75TMC9.
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.

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

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti130 – 1301L → P in BAC04313 (PubMed:14702039).Curated
Sequence conflicti187 – 1904ALAY → DLQS in BAC04313 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti57 – 571R → C.1 Publication
Corresponds to variant rs3742819 [ dbSNP | Ensembl ].
VAR_052300
Natural varianti187 – 1871A → D.
Corresponds to variant rs35724886 [ dbSNP | Ensembl ].
VAR_052301

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.3. 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
EntryMethodResolution (Å)ChainPositionsPDBsum
3K2IX-ray2.40A/B1-421[»]
ProteinModelPortaliQ8N9L9.
SMRiQ8N9L9. Positions 3-410.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125809. 1 interaction.
STRINGi9606.ENSP00000323071.

Protein family/group databases

ESTHERihuman-ACOT4. Acyl-CoA_Thioesterase.
MEROPSiS09.029.

PTM databases

PhosphoSiteiQ8N9L9.

Polymorphism and mutation databases

BioMutaiACOT4.
DMDMi50401071.

Proteomic databases

MaxQBiQ8N9L9.
PaxDbiQ8N9L9.
PRIDEiQ8N9L9.

Protocols and materials databases

DNASUi122970.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000326303; ENSP00000323071; ENSG00000177465.
GeneIDi122970.
KEGGihsa:122970.
UCSCiuc001xoo.3. human.

Organism-specific databases

CTDi122970.
GeneCardsiGC14P074058.
H-InvDBHIX0202062.
HGNCiHGNC:19748. ACOT4.
HPAiHPA000779.
MIMi614314. gene.
neXtProtiNX_Q8N9L9.
PharmGKBiPA142672654.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1073.
GeneTreeiENSGT00390000001046.
HOGENOMiHOG000116219.
HOVERGENiHBG000331.
InParanoidiQ8N9L9.
KOiK01068.
OMAiCCWNEPV.
OrthoDBiEOG75TMC9.
PhylomeDBiQ8N9L9.
TreeFamiTF314911.

Enzyme and pathway databases

BioCyciMetaCyc:HS16863-MONOMER.
SABIO-RKQ8N9L9.

Miscellaneous databases

EvolutionaryTraceiQ8N9L9.
GeneWikiiACOT4.
GenomeRNAii122970.
NextBioi81045.
PROiQ8N9L9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8N9L9.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cerebellum and Kidney.
  2. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Neuroblastoma and Placenta.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT CYS-57.
    Tissue: Colon and Urinary bladder.
  4. "Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs."
    Hunt M.C., Rautanen A., Westin M.A.K., Svensson L.T., Alexson S.E.H.
    FASEB J. 20:1855-1864(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  5. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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: July 22, 2015
This is version 110 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

External Data

Dasty 3

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 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.