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Reviewed, UniProtKB/Swiss-Prot Q86TX2 (ACOT1_HUMAN)

Last modified November 3, 2009. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Acyl-coenzyme A thioesterase 1
      Short name=Acyl-CoA thioesterase 1
    EC=3.1.2.2
Alternative name(s):
    Inducible cytosolic acyl-coenzyme A thioester hydrolase
    Long chain acyl-CoA thioester hydrolase
      Short name=Long chain acyl-CoA hydrolase
    CTE-I
    CTE-Ib
Gene names
Name: ACOT1
Synonyms: CTE1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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. Active towards fatty acyl-CoA with chain-lengths of C12-C16 By similarity.

Catalytic activity

Palmitoyl-CoA + H2O = CoA + palmitate.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm. Ref.1

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=35.8 µM for C10-acyl-CoA

KM=3.6 µM for C12-acyl-CoA

KM=2.8 µM for C14-acyl-CoA

KM=3.6 µM for C16-acyl-CoA

KM=2.4 µM for C18-acyl-CoA

KM=2 µM for C20-acyl-CoA

KM=2.4 µM for C16:1-acyl-CoA

KM=4.1 µM for C18:1-acyl-CoA

KM=2.1 µM for C18:1-trans-acyl-CoA

Vmax=224 nmol/min/mg enzyme toward C10-acyl-CoA

Vmax=700 nmol/min/mg enzyme toward C12-acyl-CoA

Vmax=912 nmol/min/mg enzyme toward C14-acyl-CoA

Vmax=691 nmol/min/mg enzyme toward C16-acyl-CoA

Vmax=597 nmol/min/mg enzyme toward C18-acyl-CoA

Vmax=520 nmol/min/mg enzyme toward C20-acyl-CoA

Vmax=577 nmol/min/mg enzyme toward C16:1-acyl-CoA

Vmax=258 nmol/min/mg enzyme toward C18:1-acyl-CoA

Vmax=309 nmol/min/mg enzyme toward C18:1-trans-acyl-CoA

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 421421Acyl-coenzyme A thioesterase 1
PRO_0000202155

Sites

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

Natural variations

Natural variant2661R → H: dbSNP rs1049568.
VAR_059830

Sequences

Sequence LengthMass (Da)Tools
Q86TX2-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 04675F28D9D53B97

FASTA42146,277
        10         20         30         40         50         60 
MAATLILEPA GRCCWDEPVR IAVRGLAPEQ PVTLRASLRD EKGALFQAHA RYRADTLGEL 

        70         80         90        100        110        120 
DLERAPALGG SFAGLEPMGL LWALEPEKPL VRLVKRDVRT PLAVELEVLD GHDPDPGRLL 

       130        140        150        160        170        180 
CRVRHERYFL PPGVRREPVR AGRVRGTLFL PPEPGPFPGI VDMFGTGGGL LEYRASLLAG 

       190        200        210        220        230        240 
KGFAVMALAY YNYEDLPKTM ETLHLEYFEE AVNYLLSHPE VKGPGVGLLG ISKGGELCLS 

       250        260        270        280        290        300 
MASFLKGITA AVVINGSVAN VGGTLRYKGE TLPPVGVNRN RIKVTKDGYA DIVDVLNSPL 

       310        320        330        340        350        360 
EGPDQKSFIP VERAESTFLF LVGQDDHNWK SEFYANEACK RLQAHGRRKP QIICYPETGH 

       370        380        390        400        410        420 
YIEPPYFPLC RASLHALVGS PIIWGGEPRA HAMAQVDAWK QLQTFFHKHL GGHEGTIPSK 


V 

« Hide

References

« Hide 'large scale' references
[1]"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: 16940157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
[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.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases

DQ082754 mRNA. Translation: AAZ31236.1.
BX161396 mRNA. Translation: CAD61883.1.
BC127748 mRNA. Translation: AAI27749.1.
BC132889 mRNA. Translation: AAI32890.1.
BC132891 mRNA. Translation: AAI32892.1.
BC143042 mRNA. Translation: AAI43043.1.
IPIIPI00333838.
RefSeqNP_001032238.1.
UniGeneHs.568046

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ86TX2.

PTM databases

PhosphoSiteQ86TX2.

Proteomic databases

PRIDEQ86TX2.

Genome annotation databases

EnsemblENST00000311148; ENSP00000311224; ENSG00000184227; Homo sapiens. [Genome view]
GeneID641371.
KEGGhsa:641371.
UCSCuc001xol.1. human.

Organism-specific databases

CTD641371.
GeneCardsGC14P073074.
HGNCHGNC:33128. ACOT1.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ86TX2.
HOVERGENQ86TX2.
OMALEPAGGC.

Enzyme and pathway databases

BRENDA3.1.2.2. 247.

Gene expression databases

BgeeQ86TX2.
CleanExHS_ACOT1.
GenevestigatorQ86TX2.
GermOnlineENSG00000184227. Homo sapiens.

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 Resources

NextBio113125.

Entry information

Entry nameACOT1_HUMAN
AccessionPrimary (citable) accession number: Q86TX2
Secondary accession number(s): A1L173, Q3I5F9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: June 1, 2003
Last modified: November 3, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 14

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents