Reviewed, UniProtKB/Swiss-Prot Q8BWN8 (ACOT4_MOUSE)

Names and origin

Protein names

Recommended name:
    Acyl-coenzyme A thioesterase 4
      Short name=Acyl-CoA thioesterase 4
    EC=3.1.2.2
Alternative name(s):
    Peroxisomal acyl coenzyme A thioester hydrolase Ib
    Peroxisomal long-chain acyl-CoA thioesterase Ib
      Short name=PTE-Ib
    PTE-2b

Gene names

Name:	Acot4
Synonyms:	Pte1b, Pte2b

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

Protein attributes

Sequence length	421 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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 By similarity.
Catalytic activity	Palmitoyl-CoA + H2O = CoA + palmitate.
Subcellular location	Peroxisome Potential.
Tissue specificity	Expressed in liver, kidney, intestine, adrenal gland and white and brown tissues. Not detected in other tissues. Ref.1
Induction	In the liver, by peroxisome proliferator (Clofibrate) treatment, via the peroxisome proliferator-activated receptors (PPARs) or fasting for 24 hours. Ref.1
Sequence similarities	Belongs to the C/M/P thioester hydrolase family.

Ontologies

Keywords
Cellular component	Peroxisome
Molecular function	Hydrolase Serine esterase
Gene Ontology (GO)
Biological process	acyl-CoA metabolic process Inferred from direct assay. Source: HGNC dicarboxylic acid metabolic process Inferred from direct assay. Source: HGNC short-chain fatty acid metabolic process Inferred from direct assay. Source: HGNC succinyl-CoA metabolic process Inferred from direct assay. Source: HGNC
Cellular component	peroxisome Inferred from direct assay. Source: HGNC
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
	Chain	1 – 421	421	Acyl-coenzyme A thioesterase 4		PRO_0000202150
Regions
	Motif	419 – 421	3	Microbody targeting signal Potential
Sites
	Active site	232	1	Charge relay system By similarity
	Active site	326	1	Charge relay system By similarity
	Active site	360	1	Charge relay system By similarity
Experimental info
	Sequence conflict	87	1	D → N in BAC32814. Ref.2
	Sequence conflict	136	1	R → G in AAF13872. Ref.1
	Sequence conflict	215	1	M → K in BAC38060. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q8BWN8-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 93DB75F0191D49F7	FASTA	421	46,481
	10 20 30 40 50 60 MAATLSVEPT GRSCWDEPLS IAVRGLAPEQ PVTLRSVLRD EKGALFRAHA RYRADSHGEL 70 80 90 100 110 120 DLARVPALGG SFSGLEPMGL LWAMEPDRPF WRLIKRDVQT PFLVELEVLD GHEPDGGRRL 130 140 150 160 170 180 ARTVHERHFM APGVRRVPVR EGRVRATLFL PPGQGPFPGI IDVYGVGGGL LEYRAGLVAG 190 200 210 220 230 240 HGFATLALAF YDFEDLPKEL NVIEVDYFEE AVRYMLRHPK VKGPDIGLLG LSLGADVCLI 250 260 270 280 290 300 MASFLNNVSA TVSINGSAFS GNRHIKYKQT MIPPLGHDLR RMKVAFSGIL DIVDIRNDAV 310 320 330 340 350 360 GGCENPSMIP IEKAKGPILF VAGQDDHCWR SELYTQIASD RLQAHGKERP QVLSYPGTGH 370 380 390 400 410 420 YIEPPYFPMC PASLHKIVNE AVIWGGEVKA HSKAQIDAWK QILFFFGKHL GSTHSRASCR L

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, INDUCTION. Strain: C57BL/6.
[2]	"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: C57BL/6J. Tissue: Adipose tissue and Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF180801, AF180799, AF180800 Genomic DNA. Translation: AAF13872.1. AK046630 mRNA. Translation: BAC32814.1. AK050420 mRNA. Translation: BAC34246.1. AK080883 mRNA. Translation: BAC38060.1.
IPI	IPI00308769.
RefSeq	NP_599008.2.
UniGene	Mm.475660
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q8BWN8.
Genome annotation databases
Ensembl	ENSMUSG00000052392. Mus musculus. [Contig view]
GeneID	171282.
KEGG	mmu:171282.
Organism-specific databases
MGI	MGI:2159621. Acot4.
Phylogenomic databases
HOGENOM	Q8BWN8.
HOVERGEN	Q8BWN8.
OMA	Q8BWN8. PSMIPIE.
Enzyme and pathway databases
BRENDA	3.1.2.2. 244.
Gene expression databases
ArrayExpress	Q8BWN8.
Bgee	Q8BWN8.
CleanEx	MM_ACOT4.
GermOnline	ENSMUSG00000052392. Mus musculus.
Family and domain databases
InterPro	IPR016662. Acyl-CoA_thioEstase_long-chain. IPR014940. BAAT_C. IPR006862. Thio_Ohase/aa_AcTrfase. [Graphical view]
Pfam	PF08840. BAAT_C. 1 hit. PF04775. Bile_Hydr_Trans. 1 hit. [Graphical view]
PIRSF	PIRSF016521. Acyl-CoA_hydro. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	370951.
SOURCE	Search...

Entry information

Entry name

ACOT4_MOUSE

Accession

Primary (citable) accession number: Q8BWN8
Secondary accession number(s): Q8BJQ1, Q8BL20, Q9QYR8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	March 1, 2003
Last modified:	June 16, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)