P13437 (THIM_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-ketoacyl-CoA thiolase, mitochondrial
EC=2.3.1.16

Alternative name(s):
Acetyl-CoA acyltransferase
Beta-ketothiolase
Mitochondrial 3-oxoacyl-CoA thiolase

Gene names

Name:

Acaa2

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	397 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Abolishes BNIP3-mediated apoptosis and mitochondrial damage By similarity.
Catalytic activity	Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.
Pathway	Lipid metabolism; fatty acid metabolism.
Subunit structure	Homotetramer. Interacts with BNIP3 By similarity.
Subcellular location	Mitochondrion By similarity. Note: Colocalizes with BNIP3 in the mitochondria By similarity.
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	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	acetyl-CoA metabolic process Inferred from direct assay PubMed 16476568. Source: RGD fatty acid beta-oxidation Inferred from direct assay PubMed 11879205. Source: RGD negative regulation of apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	mitochondrial matrix Inferred from direct assay PubMed 16476568. Source: RGD
Molecular_function	acetyl-CoA C-acyltransferase activity Inferred from direct assay PubMed 11879205PubMed 16476568. Source: RGD
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_0000223301
	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 By similarity
	Modified residue	121	1	Phosphoserine By similarity
	Modified residue	127	1	Phosphotyrosine By similarity
	Modified residue	137	1	N6-acetyllysine By similarity
	Modified residue	270	1	N6-acetyllysine By similarity
	Modified residue	344	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P13437 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: 8344FB7271C3E2E1	FASTA	397	41,871
	10 20 30 40 50 60 MALLRGVFIV AAKRTPFGAY GGLLKDFTAT DLTEFAARAA LSAGKVPPET IDSVIVGNVM 70 80 90 100 110 120 QSSSDAAYLA RHVGLRVGVP TETGALTLNR LCGSGFQSIV SGCQEICSKD AEVVLCGGTE 130 140 150 160 170 180 SMSQSPYSVR NVRFGTKFGL DLKLEDTLWA GLTDQHVKLP MGMTAENLAA KYNISREDCD 190 200 210 220 230 240 RYALQSQQRW KAANEAGYFN EEMAPIEVKT KKGKQTMQVD EHARPQTTLE QLQNLPPVFK 250 260 270 280 290 300 KEGTVTAGNA SGMSDGAGVV IIASEDAVKK HNFTPLARVV GYFVSGCDPA IMGIGPVPAI 310 320 330 340 350 360 TGALKKAGLS LKDMDLIDVN EAFAPQFLAV QKSLDLDPSK TNVSGGAIAL GHPLGGSGSR 370 380 390 ITAHLVHELR RRGGKYAVGS ACIGGGQGIS LIIQNTA

References

[1]	"cDNA-derived amino acid sequence of rat mitochondrial 3-oxoacyl-CoA thiolase with no transient presequence: structural relationship with peroxisomal isozyme." Arakawa H., Takiguchi M., Amaya Y., Nagata S., Hayashi H., Mori M. EMBO J. 6:1361-1366(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X05341 mRNA. Translation: CAA28952.1.
IPI	IPI00201413.
PIR	XURT. A29452.
RefSeq	NP_569117.1. NM_130433.1.
UniGene	Rn.3786.
3D structure databases
ProteinModelPortal	P13437.
ModBase	Search...
Protein-protein interaction databases
IntAct	P13437. 1 interaction.
STRING	10116.ENSRNOP00000060140.
Proteomic databases
PaxDb	P13437.
PRIDE	P13437.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	170465.
KEGG	rno:170465.
Organism-specific databases
CTD	10449.
RGD	620482. Acaa2.
Phylogenomic databases
eggNOG	COG0183.
HOGENOM	HOG000012238.
HOVERGEN	HBG003112.
InParanoid	P13437.
KO	K07508.
OrthoDB	EOG4H19VX.
Enzyme and pathway databases
SABIO-RK	P13437.
UniPathway	UPA00199.
Gene expression databases
ArrayExpress	P13437.
Genevestigator	P13437.
GermOnline	ENSRNOG00000013766. Rattus norvegicus.
Family and domain databases
Gene3D	3.40.47.10. 4 hits.
InterPro	IPR002155. Thiolase. IPR016039. Thiolase-like. IPR016038. Thiolase-like_subgr. IPR020615. Thiolase_acyl_enz_int_AS. IPR020610. Thiolase_AS. IPR020617. Thiolase_C. IPR020613. Thiolase_CS. IPR020616. Thiolase_N. [Graphical view]
PANTHER	PTHR18919. PTHR18919. 1 hit.
Pfam	PF02803. Thiolase_C. 1 hit. PF00108. Thiolase_N. 1 hit. [Graphical view]
PIRSF	PIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAM	SSF53901. Thiolase-like. 2 hits.
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
NextBio	620987.

Entry information

Entry name

THIM_RAT

Accession

Primary (citable) accession number: P13437

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	April 3, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program