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Reviewed, UniProtKB/Swiss-Prot P09110 (THIK_HUMAN)

Last modified July 22, 2008. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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

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Names and origin

Protein namesRecommended name:
    3-ketoacyl-CoA thiolase, peroxisomal
    EC=2.3.1.16
Alternative name(s):
    Beta-ketothiolase
    Acetyl-CoA acyltransferase
    Peroxisomal 3-oxoacyl-CoA thiolase
Gene names
Name: ACAA1
Synonyms: ACAA, PTHIO
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.

Pathway

Lipid metabolism; fatty acid metabolism.

Subunit structure

Homodimer.

Subcellular location

Peroxisome.

Induction

Peroxisomal thiolase is markedly induced (at the level of transcription) by various hypolipidemic compounds in parallel with the other two enzymes of the peroxisomal beta-oxidation system.

Sequence similarities

Belongs to the thiolase family.

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Ontologies

Keywords

   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentPeroxisome
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   Molecular functionAcyltransferase
Transferase
   Technical term3D-structure

Gene Ontology (GO)

   Biological processgeneration of precursor metabolites and energy Ref.4

Traceable author statement. Source: ProtInc

   Cellular componentperoxisome Ref.4

Non-traceable author statement. Source: ProtInc

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Transit peptide1 – 2626Peroxisome
Chain27 – 4243983-ketoacyl-CoA thiolase, peroxisomal

Sites

Active site1231Acyl-thioester intermediate By similarity
Active site3771Proton acceptor By similarity
Active site4081Proton acceptor By similarity

Natural variations

Natural variant1721E → D: dbSNP rs156265.

Secondary structure

1 ................................................................... 424
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P09110-1 [UniParc].

Last modified October 1, 1989. Version 2.
Checksum: 71B2BBAFA06AE412

FASTA42444,292
        10         20         30         40         50         60 
MQRLQVVLGH LRGPADSGWM PQAAPCLSGA PQASAADVVV VHGRRTAICR AGRGGFKDTT 

        70         80         90        100        110        120 
PDELLSAVMT AVLKDVNLRP EQLGDICVGN VLQPGAGAIM ARIAQFLSDI PETVPLSTVN 

       130        140        150        160        170        180 
RQCSSGLQAV ASIAGGIRNG SYDIGMACGV ESMSLADRGN PGNITSRLME KEKARDCLIP 

       190        200        210        220        230        240 
MGITSENVAE RFGISREKQD TFALASQQKA ARAQSKGCFQ AEIVPVTTTV HDDKGTKRSI 

       250        260        270        280        290        300 
TVTQDEGIRP STTMEGLAKL KPAFKKDGST TAGNSSQVSD GAAAILLARR SKAEELGLPI 

       310        320        330        340        350        360 
LGVLRSYAVV GVPPDIMGIG PAYAIPVALQ KAGLTVSDVD IFEINEAFAS QAAYCVEKLR 

       370        380        390        400        410        420 
LPPEKVNPLG GAVALGHPLG CTGARQVITL LNELKRRGKR AYGVVSMCIG TGMGAAAVFE 


YPGN

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References

« Hide 'large scale' references
[1]"Nucleotide sequence of human peroxisomal 3-oxoacyl-CoA thiolase."
Bout A., Teunissen Y., Hashimoto T., Benne R., Tager J.M.
Nucleic Acids Res. 16:10369-10369(1988) [PubMed: 3194209] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]Bout A.
Submitted (AUG-1989) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 285-287.
[3]"Complete cDNA sequence of human foetal liver peroxisomal 3-oxoacyl-CoA thiolase."
Fairbairn L.J., Tanner M.J.A.
Nucleic Acids Res. 17:3588-3588(1989) [PubMed: 2726492] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[4]"Characterization of the gene encoding human peroxisomal 3-oxoacyl-CoA thiolase (ACAA). No large DNA rearrangement in a thiolase-deficient patient."
Bout A., Franse M.M., Collins J., Blonden L., Tager J.M., Benne R.
Biochim. Biophys. Acta 1090:43-51(1991) [PubMed: 1679347] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"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].
Tissue: Lymph and Ovary.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X12966 mRNA. Translation: CAA31412.1.
X14813 mRNA. Translation: CAA32918.1.
X65140 Genomic DNA. Translation: CAA46270.1.
X65148 Genomic DNA. Translation: CAA46271.1.
BC000635 mRNA. Translation: AAH00635.1.
BC011977 mRNA. Translation: AAH11977.1.
PIRXUHUAB. S17515.
RefSeqNP_001598.1.
UniGeneHs.643487

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2IIKX-ray2.55A/B28-424[»]
ModBaseSearch...

2-D gel databases

REPRODUCTION-2DPAGEIPI00012828.

Proteomic databases

PeptideAtlasP09110.

Genome annotation databases

EnsemblENSG00000060971. Homo sapiens. [Contig view]
GeneID30.
KEGGhsa:30.
NMPDRfig|9606.3.peg.22303.

Organism-specific databases

HGNCHGNC:82. ACAA1.
HPAHPA006764.
HPA007244.
MIM604054. gene.
Orphanet2981. Pseudo-Zellweger syndrome.
PharmGKBPA24419.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMP09110.
HOVERGENP09110.

Gene expression databases

ArrayExpressP09110.
CleanExHS_ACAA1.
GermOnlineENSG00000060971. Homo sapiens.

Family and domain databases

InterProIPR002155. Thiolase.
IPR016038. Thiolase-like_subgr.
[Graphical view]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 1 hit.
PANTHERPTHR18919. Thiolase. 1 hit.
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
TIGRFAMsTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProDomP09110.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

SOURCESearch...
ProtoNetSearch...

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Entry information

Entry nameTHIK_HUMAN
AccessionPrimary (citable) accession number: P09110
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1989
Last modified: July 22, 2008
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 3

Human chromosome 3: 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

MIM cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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