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Protein

Acyl-coenzyme A thioesterase 4

Gene

Acot4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Palmitoyl-CoA + H2O = CoA + palmitate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei232 – 2321Charge relay systemBy similarity
Active sitei326 – 3261Charge relay systemBy similarity
Active sitei360 – 3601Charge relay systemBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

ReactomeiR-MMU-75105. Fatty Acyl-CoA Biosynthesis.

Protein family/group databases

ESTHERimouse-acot4. Acyl-CoA_Thioesterase.
MEROPSiS09.A60.

Chemistry

SwissLipidsiSLP:000000593.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-coenzyme A thioesterase 4 (EC:3.1.2.2)
Short name:
Acyl-CoA thioesterase 4
Alternative name(s):
PTE-2b
Peroxisomal acyl coenzyme A thioester hydrolase Ib
Peroxisomal long-chain acyl-CoA thioesterase Ib
Short name:
PTE-Ib
Gene namesi
Name:Acot4
Synonyms:Pte1b, Pte2b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:2159621. Acot4.

Subcellular locationi

GO - Cellular componenti

  • peroxisome Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 421421Acyl-coenzyme A thioesterase 4PRO_0000202150Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421N6-acetyllysineBy similarity
Modified residuei313 – 3131N6-succinyllysineCombined sources
Modified residuei408 – 4081N6-succinyllysineBy similarity
Modified residuei418 – 4181PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8BWN8.
MaxQBiQ8BWN8.
PaxDbiQ8BWN8.
PRIDEiQ8BWN8.

PTM databases

iPTMnetiQ8BWN8.
PhosphoSiteiQ8BWN8.

Expressioni

Tissue specificityi

Expressed in liver, kidney, intestine, adrenal gland and white and brown tissues. Not detected in other tissues.1 Publication

Inductioni

In the liver, by peroxisome proliferator (Clofibrate) treatment, via the peroxisome proliferator-activated receptors (PPARs) or fasting for 24 hours.1 Publication

Gene expression databases

BgeeiQ8BWN8.
CleanExiMM_ACOT4.
ExpressionAtlasiQ8BWN8. baseline and differential.
GenevisibleiQ8BWN8. MM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ8BWN8. 3 interactions.
MINTiMINT-1850016.
STRINGi10090.ENSMUSP00000021652.

Structurei

3D structure databases

ProteinModelPortaliQ8BWN8.
SMRiQ8BWN8. Positions 3-410.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi419 – 4213Microbody targeting signalSequence analysis

Sequence similaritiesi

Belongs to the C/M/P thioester hydrolase family.Curated

Phylogenomic databases

eggNOGiENOG410II3X. Eukaryota.
COG1073. LUCA.
GeneTreeiENSGT00390000001046.
HOGENOMiHOG000116219.
HOVERGENiHBG000331.
InParanoidiQ8BWN8.
KOiK01068.
OMAiCCWNEPV.
OrthoDBiEOG75TMC9.
PhylomeDBiQ8BWN8.
TreeFamiTF314911.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR016662. Acyl-CoA_thioEstase_long-chain.
IPR014940. BAAT_C.
IPR006862. Thio_Ohase/aa_AcTrfase.
[Graphical view]
PfamiPF08840. BAAT_C. 1 hit.
PF04775. Bile_Hydr_Trans. 1 hit.
[Graphical view]
PIRSFiPIRSF016521. Acyl-CoA_hydro. 1 hit.
SUPFAMiSSF53474. SSF53474. 2 hits.

Sequencei

Sequence statusi: Complete.

Q8BWN8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATLSVEPT GRSCWDEPLS IAVRGLAPEQ PVTLRSVLRD EKGALFRAHA
60 70 80 90 100
RYRADSHGEL DLARVPALGG SFSGLEPMGL LWAMEPDRPF WRLIKRDVQT
110 120 130 140 150
PFLVELEVLD GHEPDGGRRL ARTVHERHFM APGVRRVPVR EGRVRATLFL
160 170 180 190 200
PPGQGPFPGI IDVYGVGGGL LEYRAGLVAG HGFATLALAF YDFEDLPKEL
210 220 230 240 250
NVIEVDYFEE AVRYMLRHPK VKGPDIGLLG LSLGADVCLI MASFLNNVSA
260 270 280 290 300
TVSINGSAFS GNRHIKYKQT MIPPLGHDLR RMKVAFSGIL DIVDIRNDAV
310 320 330 340 350
GGCENPSMIP IEKAKGPILF VAGQDDHCWR SELYTQIASD RLQAHGKERP
360 370 380 390 400
QVLSYPGTGH YIEPPYFPMC PASLHKIVNE AVIWGGEVKA HSKAQIDAWK
410 420
QILFFFGKHL GSTHSRASCR L
Length:421
Mass (Da):46,481
Last modified:March 1, 2003 - v1
Checksum:i93DB75F0191D49F7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti87 – 871D → N in BAC32814 (PubMed:16141072).Curated
Sequence conflicti136 – 1361R → G in AAF13872 (PubMed:10567408).Curated
Sequence conflicti215 – 2151M → K in BAC38060 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF180801, AF180799, AF180800 Genomic DNA. Translation: AAF13872.1.
AK046630 mRNA. Translation: BAC32814.1.
AK050420 mRNA. Translation: BAC34246.1.
AK080883 mRNA. Translation: BAC38060.1.
CCDSiCCDS26035.1.
RefSeqiNP_599008.3. NM_134247.3.
UniGeneiMm.482217.

Genome annotation databases

EnsembliENSMUST00000021652; ENSMUSP00000021652; ENSMUSG00000052392.
GeneIDi171282.
KEGGimmu:171282.
UCSCiuc007oed.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF180801, AF180799, AF180800 Genomic DNA. Translation: AAF13872.1.
AK046630 mRNA. Translation: BAC32814.1.
AK050420 mRNA. Translation: BAC34246.1.
AK080883 mRNA. Translation: BAC38060.1.
CCDSiCCDS26035.1.
RefSeqiNP_599008.3. NM_134247.3.
UniGeneiMm.482217.

3D structure databases

ProteinModelPortaliQ8BWN8.
SMRiQ8BWN8. Positions 3-410.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8BWN8. 3 interactions.
MINTiMINT-1850016.
STRINGi10090.ENSMUSP00000021652.

Chemistry

SwissLipidsiSLP:000000593.

Protein family/group databases

ESTHERimouse-acot4. Acyl-CoA_Thioesterase.
MEROPSiS09.A60.

PTM databases

iPTMnetiQ8BWN8.
PhosphoSiteiQ8BWN8.

Proteomic databases

EPDiQ8BWN8.
MaxQBiQ8BWN8.
PaxDbiQ8BWN8.
PRIDEiQ8BWN8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021652; ENSMUSP00000021652; ENSMUSG00000052392.
GeneIDi171282.
KEGGimmu:171282.
UCSCiuc007oed.1. mouse.

Organism-specific databases

CTDi122970.
MGIiMGI:2159621. Acot4.

Phylogenomic databases

eggNOGiENOG410II3X. Eukaryota.
COG1073. LUCA.
GeneTreeiENSGT00390000001046.
HOGENOMiHOG000116219.
HOVERGENiHBG000331.
InParanoidiQ8BWN8.
KOiK01068.
OMAiCCWNEPV.
OrthoDBiEOG75TMC9.
PhylomeDBiQ8BWN8.
TreeFamiTF314911.

Enzyme and pathway databases

ReactomeiR-MMU-75105. Fatty Acyl-CoA Biosynthesis.

Miscellaneous databases

NextBioi370951.
PROiQ8BWN8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BWN8.
CleanExiMM_ACOT4.
ExpressionAtlasiQ8BWN8. baseline and differential.
GenevisibleiQ8BWN8. MM.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR016662. Acyl-CoA_thioEstase_long-chain.
IPR014940. BAAT_C.
IPR006862. Thio_Ohase/aa_AcTrfase.
[Graphical view]
PfamiPF08840. BAAT_C. 1 hit.
PF04775. Bile_Hydr_Trans. 1 hit.
[Graphical view]
PIRSFiPIRSF016521. Acyl-CoA_hydro. 1 hit.
SUPFAMiSSF53474. SSF53474. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, INDUCTION.
    Strain: C57BL/6J.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Adipose tissue and Liver.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney and Liver.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-313, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiACOT4_MOUSE
AccessioniPrimary (citable) accession number: Q8BWN8
Secondary accession number(s): Q8BJQ1, Q8BL20, Q9QYR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: March 1, 2003
Last modified: March 16, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.