Reviewed, UniProtKB/Swiss-Prot P42765 (THIM_HUMAN)

Names and origin

Protein names

Recommended name:
    3-ketoacyl-CoA thiolase, mitochondrial
    EC=2.3.1.16
Alternative name(s):
    Beta-ketothiolase
    Acetyl-CoA acyltransferase
    Mitochondrial 3-oxoacyl-CoA thiolase
    T1

Gene names

Name:

ACAA2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	397 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.
Pathway	Lipid metabolism; fatty acid metabolism.
Subunit structure	Homotetramer.
Subcellular location	Mitochondrion.
Sequence similarities	Belongs to the thiolase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion
Domain	Transit peptide
Molecular function	Acyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cholesterol biosynthetic process Ref.1 Non-traceable author statement. Source: UniProtKB fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	acetyl-CoA C-acyltransferase activity Ref.1 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 397	397	3-ketoacyl-CoA thiolase, mitochondrial		PRO_0000223299
	Transit peptide	1 – 16	16	Mitochondrion; not cleaved
Sites
	Active site	92	1	Acyl-thioester intermediate By similarity
	Active site	352	1	Proton acceptor By similarity
	Active site	382	1	Proton acceptor By similarity
Amino acid modifications
	Modified residue	119	1	Phosphothreonine
	Modified residue	121	1	Phosphoserine
	Modified residue	127	1	Phosphotyrosine
	Modified residue	137	1	N6-acetyllysine By similarity
	Modified residue	270	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	2	1	A → R in BAA03800. Ref.1
	Sequence conflict	169	1	A → T in BAA03800. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P42765-1 [UniParc]. Last modified January 4, 2005. Version 2. Checksum: 380CC8262ACF6D01	FASTA	397	41,924
	10 20 30 40 50 60 MALLRGVFVV AAKRTPFGAY GGLLKDFTAT DLSEFAAKAA LSAGKVSPET VDSVIMGNVL 70 80 90 100 110 120 QSSSDAIYLA RHVGLRVGIP KETPALTINR LCGSGFQSIV NGCQEICVKE AEVVLCGGTE 130 140 150 160 170 180 SMSQAPYCVR NVRFGTKLGS DIKLEDSLWV SLTDQHVQLP MAMTAENLAV KHKISREECD 190 200 210 220 230 240 KYALQSQQRW KAANDAGYFN DEMAPIEVKT KKGKQTMQVD EHARPQTTLE QLQKLPPVFK 250 260 270 280 290 300 KDGTVTAGNA SGVADGAGAV IIASEDAVKK HNFTPLARIV GYFVSGCDPS IMGIGPVPAI 310 320 330 340 350 360 SGALKKAGLS LKDMDLVEVN EAFAPQYLAV ERSLDLDISK TNVNGGAIAL GHPLGGSGSR 370 380 390 ITAHLVHELR RRGGKYAVGS ACIGGGQGIA VIIQSTA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequence analysis of a full length cDNA encoding human mitochondrial 3-oxoacyl-CoA thiolase." Abe H., Ohtake A., Yamamoto S., Satoh Y., Takayanagi M., Amaya Y., Takiguchi M., Sakuraba H., Suzuki Y., Mori M., Niimi H. Biochim. Biophys. Acta 1216:304-306(1993) [PubMed: 8241273] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"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: Lung.
[3]	"Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes." Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V. Biochem. J. 383:237-248(2004) [PubMed: 15242332] [Abstract] Cited for: PROTEIN SEQUENCE OF 15-25; 46-71 AND 341-360. Tissue: Adipocyte.
[4]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-119; SER-121 AND TYR-127, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D16294 mRNA. Translation: BAA03800.1. BC001918 mRNA. Translation: AAH01918.1.
PIR	S43440.
RefSeq	NP_006102.2.
UniGene	Hs.200136
3D structure databases
HSSP	HSSP built from PDB template 1AFW based on UniProtKB P27796.
ModBase	Search...
PTM databases
PhosphoSite	P42765.
2-D gel databases
REPRODUCTION-2DPAGE	IPI00001539.
Proteomic databases
PeptideAtlas	P42765.
Genome annotation databases
Ensembl	ENSG00000167315. Homo sapiens. [Contig view]
GeneID	10449.
KEGG	hsa:10449.
NMPDR	fig|9606.3.peg.15023.
Organism-specific databases
HGNC	HGNC:83. ACAA2.
MIM	604770. gene.
PharmGKB	PA24420.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	P42765.
HOVERGEN	P42765.
Gene expression databases
ArrayExpress	P42765.
GermOnline	ENSG00000167315. Homo sapiens.
Family and domain databases
InterPro	IPR002155. Thiolase. IPR016038. Thiolase-like_subgr. [Graphical view]
Gene3D	G3DSA:3.40.47.10. Thiolase-like_subgr. 1 hit.
PANTHER	PTHR18919. Thiolase. 1 hit.
Pfam	PF02803. Thiolase_C. 1 hit. PF00108. Thiolase_N. 1 hit. [Graphical view]
PIRSF	PIRSF000429. Ac-CoA_Ac_transf. 1 hit.
TIGRFAMs	TIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITE	PS00098. THIOLASE_1. 1 hit. PS00737. THIOLASE_2. 1 hit. PS00099. THIOLASE_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	39605.
SOURCE	Search...

Entry information

Entry name

THIM_HUMAN

Accession

Primary (citable) accession number: P42765
Secondary accession number(s): Q9BUT6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 4, 2005
Last modified:	November 25, 2008
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)