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Q8N9L9 (ACOT4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acyl-coenzyme A thioesterase 4

Short name=Acyl-CoA thioesterase 4
EC=3.1.2.2
Alternative name(s):
PTE-2b
Peroxisomal acyl coenzyme A thioester hydrolase Ib
Peroxisomal long-chain acyl-CoA thioesterase Ib
Short name=PTE-Ib
Gene names
Name:ACOT4
Synonyms:PTE2B, PTEIB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

Palmitoyl-CoA + H2O = CoA + palmitate.

Subcellular location

Peroxisome Ref.4.

Tissue specificity

Strongest expression in liver and kidney and weaker expression in placenta, heart, and muscle. Ref.4

Miscellaneous

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

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=14 µM for succinyl-CoA Ref.4

KM=147 µM for glutaryl-CoA

KM=3.4 µM for C14-acyl-CoA

Vmax=581 nmol/min/mg enzyme toward succinyl-CoA

Vmax=132 nmol/min/mg enzyme toward glutaryl-CoA

Vmax=137 nmol/min/mg enzyme toward C14-acyl-CoA

Ontologies

Keywords
   Cellular componentPeroxisome
   Coding sequence diversityPolymorphism
   Molecular functionHydrolase
Serine esterase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacyl-CoA metabolic process

Inferred from direct assay Ref.4. Source: HGNC

dicarboxylic acid catabolic process

Inferred from direct assay PubMed 16141203. Source: UniProtKB

dicarboxylic acid metabolic process

Inferred from direct assay Ref.4. Source: HGNC

long-chain fatty acid metabolic process

Inferred from direct assay Ref.4. Source: HGNC

saturated monocarboxylic acid metabolic process

Inferred from direct assay Ref.4. Source: HGNC

short-chain fatty acid metabolic process

Inferred from direct assay Ref.4. Source: HGNC

succinyl-CoA metabolic process

Inferred from direct assay Ref.4. Source: HGNC

unsaturated monocarboxylic acid metabolic process

Inferred from direct assay Ref.4. Source: HGNC

very long-chain fatty acid metabolic process

Inferred from direct assay Ref.4. Source: HGNC

   Cellular_componentperoxisome

Inferred from direct assay PubMed 16141203. Source: UniProtKB

   Molecular_functionacyl-CoA hydrolase activity

Inferred from direct assay PubMed 16141203. Source: UniProtKB

palmitoyl-CoA hydrolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

receptor binding

Inferred from physical interaction PubMed 20178365. Source: UniProtKB

succinyl-CoA hydrolase activity

Inferred from direct assay PubMed 16141203. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 421421Acyl-coenzyme A thioesterase 4
PRO_0000202149

Regions

Motif419 – 4213Microbody targeting signal Potential

Sites

Active site2321Charge relay system By similarity
Active site3261Charge relay system By similarity
Active site3601Charge relay system By similarity

Amino acid modifications

Modified residue3131N6-succinyllysine By similarity

Natural variations

Natural variant571R → C. Ref.3
Corresponds to variant rs3742819 [ dbSNP | Ensembl ].
VAR_052300
Natural variant1871A → D.
Corresponds to variant rs35724886 [ dbSNP | Ensembl ].
VAR_052301

Experimental info

Sequence conflict1301L → P in BAC04313. Ref.1
Sequence conflict187 – 1904ALAY → DLQS in BAC04313. Ref.1

Secondary structure

.................................................................... 421
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8N9L9 [UniParc].

Last modified July 19, 2004. Version 2.
Checksum: 41BBE5AA826A9F2C

FASTA42146,327
        10         20         30         40         50         60 
MSATLILEPP GRCCWNEPVR IAVRGLAPEQ RVTLRASLRD EKGALFRAHA RYCADARGEL 

        70         80         90        100        110        120 
DLERAPALGG SFAGLEPMGL LWALEPEKPF WRFLKRDVQI PFVVELEVLD GHDPEPGRLL 

       130        140        150        160        170        180 
CQAQHERHFL PPGVRRQSVR AGRVRATLFL PPGPGPFPGI IDIFGIGGGL LEYRASLLAG 

       190        200        210        220        230        240 
HGFATLALAY YNFEDLPNNM DNISLEYFEE AVCYMLQHPQ VKGPGIGLLG ISLGADICLS 

       250        260        270        280        290        300 
MASFLKNVSA TVSINGSGIS GNTAINYKHS SIPPLGYDLR RIKVAFSGLV DIVDIRNALV 

       310        320        330        340        350        360 
GGYKNPSMIP IEKAQGPILL IVGQDDHNWR SELYAQTVSE RLQAHGKEKP QIICYPGTGH 

       370        380        390        400        410        420 
YIEPPYFPLC PASLHRLLNK HVIWGGEPRA HSKAQEDAWK QILAFFCKHL GGTQKTAVPK 


L 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_689544.3. NM_152331.3.
UniGeneHs.49433.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3K2IX-ray2.40A/B1-421[»]
ProteinModelPortalQ8N9L9.
SMRQ8N9L9. Positions 3-410.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125809. 1 interaction.
STRING9606.ENSP00000323071.

Protein family/group databases

MEROPSS09.029.

PTM databases

PhosphoSiteQ8N9L9.

Polymorphism databases

DMDM50401071.

Proteomic databases

PaxDbQ8N9L9.
PRIDEQ8N9L9.

Protocols and materials databases

DNASU122970.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000326303; ENSP00000323071; ENSG00000177465.
GeneID122970.
KEGGhsa:122970.
UCSCuc001xoo.3. human.

Organism-specific databases

CTD122970.
GeneCardsGC14P074058.
H-InvDBHIX0202062.
HGNCHGNC:19748. ACOT4.
HPAHPA000779.
MIM614314. gene.
neXtProtNX_Q8N9L9.
PharmGKBPA142672654.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1073.
HOGENOMHOG000116219.
HOVERGENHBG000331.
InParanoidQ8N9L9.
KOK01068.
OMACPASLHR.
OrthoDBEOG75TMC9.
PhylomeDBQ8N9L9.
TreeFamTF314911.

Enzyme and pathway databases

BioCycMetaCyc:HS16863-MONOMER.
SABIO-RKQ8N9L9.

Gene expression databases

BgeeQ8N9L9.
CleanExHS_ACOT4.
GenevestigatorQ8N9L9.

Family and domain databases

InterProIPR016662. Acyl-CoA_thioEstase_long-chain.
IPR014940. BAAT_C.
IPR006862. Thio_Ohase/aa_AcTrfase.
[Graphical view]
PfamPF08840. BAAT_C. 1 hit.
PF04775. Bile_Hydr_Trans. 1 hit.
[Graphical view]
PIRSFPIRSF016521. Acyl-CoA_hydro. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ8N9L9.
GeneWikiACOT4.
GenomeRNAi122970.
NextBio81045.
PROQ8N9L9.
SOURCESearch...

Entry information

Entry nameACOT4_HUMAN
AccessionPrimary (citable) accession number: Q8N9L9
Secondary accession number(s): Q17RF4 expand/collapse secondary AC list , Q5BKT6, Q86TX0, Q86TX1, Q96N88
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: April 16, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM