Q9QYR9 (ACOT2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acyl-coenzyme A thioesterase 2, mitochondrial
Short name=Acyl-CoA thioesterase 2
EC=3.1.2.2

Alternative name(s):
Acyl coenzyme A thioester hydrolase
MTE-I
Very-long-chain acyl-CoA thioesterase

Gene names

Name:	Acot2
Synonyms:	Mte1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	453 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Most active on substrates with chain lengths ranging from C14-C20 By similarity.
Catalytic activity	Palmitoyl-CoA + H2O = CoA + palmitate.
Subunit structure	Monomer.
Subcellular location	Mitochondrion matrix.
Tissue specificity	Highly expressed in brown and white adipose tissue, muscle, heart, kidney, lung, adrenal gland and spleen; weakly expressed in intestine, testis and brain. Ref.1 Ref.2
Induction	In the liver, by peroxisome proliferator (Clofibrate) treatment, via the peroxisome proliferator-activated receptors (PPARs) or fasting for 24 hours. Ref.2
Sequence similarities	Belongs to the C/M/P thioester hydrolase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Molecular function	Hydrolase Serine esterase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	acyl-CoA metabolic process Traceable author statement Ref.1. Source: MGI lipid metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	carboxylesterase activity Inferred from electronic annotation. Source: UniProtKB-KW palmitoyl-CoA hydrolase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 42	42	Mitochondrion Potential
	Chain	43 – 453	411	Acyl-coenzyme A thioesterase 2, mitochondrial		PRO_0000034065
Sites
	Active site	273	1	Charge relay system By similarity
	Active site	365	1	Charge relay system By similarity
	Active site	399	1	Charge relay system By similarity
Amino acid modifications
	Modified residue	83	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	163	1	Q → H in AAF13871. Ref.1
	Sequence conflict	319	1	L → V in AAF13871. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9QYR9 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 5687F2363B16284B	FASTA	453	49,657
	10 20 30 40 50 60 MVASSFAVLR ASRLCQQDWK SWARLFVPPP LSTGGRTTWA RTNATLSVEP EGRSCWDEPL 70 80 90 100 110 120 SIAVRGLAPE QPVTLRSALR DEKGALFRAH ARYRADAGGE LNLARAPALG GSFSGLEPMG 130 140 150 160 170 180 LLWAMEPERP LWRLIKRDVQ TPFLVELEVL DGHEPDGGQR LAQAVHERHF LAPGVRRVPV 190 200 210 220 230 240 REGRVRATLF LPPEPGPFPG IIDLFGVGGG LLEYRASLLA GKGFAVMALA YYNYDDLPKS 250 260 270 280 290 300 IETMHMEYFE EAVNYLRSHP EVKGPGIGLL GISKGGELGL AMASFLKGIT AAVVINGSVA 310 320 330 340 350 360 AVGNTISYKD ETIPPVSLLR NQVKMTKDGL LDVVEALQSP LVDKKSFIPV ERSDTTFLFL 370 380 390 400 410 420 VGQDDHNWKS EFYADEISKR LQAHGKEKPQ IICYPAAGHY IEPPYFPLCS AGMHLLVGAN 430 440 450 ITFGGEPRAH AVAQVDAWQQ LQTFFHKQLG SKS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Peroxisome proliferator-induced long chain acyl-CoA thioesterases comprise a highly conserved novel multi-gene family involved in lipid metabolism." Hunt M.C., Nousiainen S.E.B., Huttunen M.K., Orii K.E., Svensson L.T., Alexson S.E.H. J. Biol. Chem. 274:34317-34326(1999) [PubMed: 10567408] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY. Strain: C57BL/6.
[2]	"Acyl-CoA thioesterases belong to a novel gene family of peroxisome proliferator-regulated enzymes involved in lipid metabolism." Hunt M.C., Lindquist P.J.G., Nousiainen S.E.B., Huttunen M.K., Orii K.E., Svensson L.T., Aoyama T., Hashimoto T., Diczfalusy U., Alexson S.E.H. Cell Biochem. Biophys. 32:317-324(2000) [PubMed: 11330065] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, INDUCTION, TISSUE SPECIFICITY.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: NOD. Tissue: Spleen.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF180798, AF180796, AF180797 Genomic DNA. Translation: AAF13871.1. AK172617 mRNA. Translation: BAE43095.1. CH466590 Genomic DNA. Translation: EDL02755.1.
IPI	IPI00136683.
RefSeq	NP_598949.3. NM_134188.3.
UniGene	Mm.371675.
3D structure databases
ProteinModelPortal	Q9QYR9.
SMR	Q9QYR9. Positions 40-449.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9QYR9.
PTM databases
PhosphoSite	Q9QYR9.
Proteomic databases
PRIDE	Q9QYR9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000021649; ENSMUSP00000021649; ENSMUSG00000021226.
GeneID	171210.
KEGG	mmu:171210.
Organism-specific databases
CTD	10965.
MGI	MGI:2159605. Acot2.
Phylogenomic databases
GeneTree	ENSGT00390000001046.
HOGENOM	HBG713807.
HOVERGEN	HBG000331.
InParanoid	Q9QYR9.
OrthoDB	EOG4QC15F.
Gene expression databases
ArrayExpress	Q9QYR9.
Bgee	Q9QYR9.
Genevestigator	Q9QYR9.
GermOnline	ENSMUSG00000021226. Mus musculus.
Family and domain databases
InterPro	IPR016662. Acyl-CoA_thioEstase_long-chain. IPR014940. BAAT_C. IPR006862. Thio_Ohase/aa_AcTrfase. [Graphical view]
KO	K01068.
Pfam	PF08840. BAAT_C. 1 hit. PF04775. Bile_Hydr_Trans. 1 hit. [Graphical view]
PIRSF	PIRSF016521. Acyl-CoA_hydro. 1 hit.
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

ACOT2_MOUSE

Accession

Primary (citable) accession number: Q9QYR9
Secondary accession number(s): Q3T9C9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 8, 2000
Last sequence update:	July 27, 2011
Last modified:	December 14, 2011
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program