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UniProtKB/Swiss-Prot entry Q8BWN8


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ACOT4_MOUSE
Primary accession number Q8BWN8
Secondary accession numbers Q8BJQ1 Q8BL20 Q9QYR8
Integrated into Swiss-Prot on July 19, 2004
Sequence was last modified on March 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 43)
Name and origin of the protein
Protein name Acyl-coenzyme A thioesterase 4
Synonyms Acyl-CoA thioesterase 4
EC 3.1.2.2
Peroxisomal acyl coenzyme A thioester hydrolase Ib
Peroxisomal long-chain acyl-CoA thioesterase Ib
PTE-Ib
PTE-2b
Gene name
Name: Acot4
Synonyms: Pte1b, Pte2b
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
STRAIN=C57BL/6;
DOI=10.1074/jbc.274.48.34317; PubMed=10567408 [NCBI, ExPASy, EBI, Israel, Japan]
Hunt M.C., Nousiainen S.E.B., Huttunen M.K., Orii K.E., Svensson L.T., Alexson S.E.H.;
"Peroxisome proliferator-induced long chain acyl-CoA thioesterases comprise a highly conserved novel multi-gene family involved in lipid metabolism.";
J. Biol. Chem. 274:34317-34326(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Adipose tissue, and Liver;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
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.
  • INDUCTION: In the liver, by peroxisome proliferator (Clofibrate) treatment, via the peroxisome proliferator-activated receptors (PPARs) or fasting for 24 hours.
  • SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF180801; AAF13872.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF180799; AAF13872.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF180800; AAF13872.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK046630; BAC32814.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK050420; BAC34246.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK080883; BAC38060.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_599008.2; -.
UniGene Mm.219001
3D structure databases
ModBase Q8BWN8.
PTM databases
PhosphoSite Q8BWN8; -.
Organism-specific databases
MGI MGI:2159621; Acot4.
Gene expression databases
ArrayExpress Q8BWN8; -.
CleanEx MM_ACOT4; -.
GermOnline ENSMUSG00000052392; Mus musculus.
Ontologies
GO
GO:0005777; Cellular component: peroxisome (inferred from direct assay from HGNC).
GO:0004091; Molecular function: carboxylesterase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0016290; Molecular function: palmitoyl-CoA hydrolase activity (inferred from electronic annotation from InterPro).
GO:0006637; Biological process: acyl-CoA metabolic process (inferred from direct assay from HGNC).
GO:0043648; Biological process: dicarboxylic acid metabolic process (inferred from direct assay from HGNC).
GO:0046459; Biological process: short-chain fatty acid metabolic process (inferred from direct assay from HGNC).
GO:0006104; Biological process: succinyl-CoA metabolic process (inferred from direct assay from HGNC).
QuickGo view.
Family and domain databases
InterPro IPR016662; Acyl-CoA_thioEstase_long-chain.
IPR014940; BAAT_C.
IPR006862; Thio_Ohase/aa_AcTrfase.
Graphical view of domain structure.
Pfam PF08840; BAAT_C; 1.
PF04775; Bile_Hydr_Trans; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF016521; Acyl-CoA_hydro; 1.
BLOCKS Q8BWN8.
ProtoNet Q8BWN8.
Genome annotation databases
Ensembl ENSMUSG00000052392; Mus musculus. [Contig view]
GeneID 171282; -.
KEGG mmu:171282; -.
Phylogenomic databases
HOGENOM Q8BWN8; -.
HOVERGEN Q8BWN8; -.
Other
NextBio 370951; -.
SOURCE Acot4; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Hydrolase; Peroxisome; Serine esterase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   421  421     Acyl-coenzyme A thioesterase 4. PRO_0000202150
MOTIF   419   421  3     Microbody targeting signal (Potential). 
ACT_SITE   232   232        Charge relay system (By similarity). 
ACT_SITE   326   326        Charge relay system (By similarity). 
ACT_SITE   360   360        Charge relay system (By similarity). 
CONFLICT   87    87        D -> N (in Ref. 2; BAC32814). 
CONFLICT   136   136        R -> G (in Ref. 1; AAF13872). 
CONFLICT   215   215        M -> K (in Ref. 2; BAC38060). 
Sequence information
Length: 421 AA [This is the length of the unprocessed precursor] Molecular weight: 46481 Da [This is the MW of the unprocessed precursor] CRC64: 93DB75F0191D49F7 [This is a checksum on the sequence]
        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 

Q8BWN8 in FASTA format

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