human-ACOT2
Homo sapiens (Human) peroxisomal long-chain Acyl-CoA thioesterase 2 (zap128) (protein for mgc:3983) mitochondrial (EC 3.1.2.2) CTE-1a
Comment
Trembl Q86TX2 genbank BX161396 humant-cte1 some aa different the two genes are adjacent. Acyl-CoA thioesterase 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. Displays high levels of activity on medium- and long chain acyl CoAs || The mouse ACOT gene cluster comprises six genes with localizations in cytosol (ACOT1), mitochondria (ACOT2), and peroxisomes (ACOT3-6). The corresponding human gene cluster contains only three genes (ACOT1, ACOT2, and ACOT4) coding for full-length thioesterase proteins only ACOT4 is peroxisomal
Relationship
Molecular evidence
Sequence
Peptide
MSNKLLSPHP HSVVLRSEFK MASSPAVLRA SRLYQWSLKS SAQFLGSPQL RQVGQIIRVP ARMAATLILE PAGRCCWDEP VRIAVRGLAP EQPVTLRASL RDEKGALFQA HARYRADTLG ELDLERAPAL GGSFAGLEPM GLLWALEPEK PLVRLVKRDV RTPLAVVLEV LDGHDPDPGR LLCQTRHERY FLPPGVRREP VRVGRVRGTL FLPPEPGPFP GIVDMFGTGG GLLEYRASLL AGKGFAVMAL AYYNYEDLPK TMETLHLEYF EEAMNYLLSH PEVKGPGVGL LGISKGGELC LSMASFLKGI TAAVVINGSV ANVGGTLRYK GETLPPVGVN RNRIKVTKDG YADIVDVLNS PLEGPDQKSF IPVERAESTF LFLVGQDDHN WKSEFYANEA CKRLQAHGRR KPQIICYPET GHYIEPPYFP LCRASLHALV GSPIIWGGEP RAHAMAQVDA WKQLQTFFHK HLGGREGTIP SKV
References
| Title : Remodeling natural products: chemistry and serine hydrolase activity of a rocaglate-derived beta-lactone - Lajkiewicz_2014_J.Am.Chem.Soc_136_2659 |
| Author(s) : Lajkiewicz NJ , Cognetta AB, 3rd , Niphakis MJ , Cravatt BF , Porco JA, Jr. |
| Ref : Journal of the American Chemical Society , 136 :2659 , 2014 |
| Abstract : Lajkiewicz_2014_J.Am.Chem.Soc_136_2659 |
| ESTHER : Lajkiewicz_2014_J.Am.Chem.Soc_136_2659 |
| PubMedSearch : Lajkiewicz_2014_J.Am.Chem.Soc_136_2659 |
| PubMedID: 24447064 |
| Gene_locus related to this paper: human-ABHD10 , human-ACOT1 , human-ACOT2 , human-CTSA , human-SCPEP1 , mouse-abhda |
| Title : Crystal structure of human mitochondrial acyl-CoA thioesterase (ACOT2) - Mandel_2009_Biochem.Biophys.Res.Commun_385_630 |
| Author(s) : Mandel CR , Tweel B , Tong L |
| Ref : Biochemical & Biophysical Research Communications , 385 :630 , 2009 |
| Abstract : Mandel_2009_Biochem.Biophys.Res.Commun_385_630 |
| ESTHER : Mandel_2009_Biochem.Biophys.Res.Commun_385_630 |
| PubMedSearch : Mandel_2009_Biochem.Biophys.Res.Commun_385_630 |
| PubMedID: 19497300 |
| Gene_locus related to this paper: human-ACOT2 |
| Title : Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs - Hunt_2006_FASEB.J_20_1855 |
| Author(s) : Hunt MC , Rautanen A , Westin MA , Svensson LT , Alexson SE |
| Ref : FASEB Journal , 20 :1855 , 2006 |
| Abstract : Hunt_2006_FASEB.J_20_1855 |
| ESTHER : Hunt_2006_FASEB.J_20_1855 |
| PubMedSearch : Hunt_2006_FASEB.J_20_1855 |
| PubMedID: 16940157 |
| Gene_locus related to this paper: human-ACOT1 , human-ACOT2 , human-ACOT4 , human-ACOT6 , mouse-acot1 , mouse-acot2 , mouse-acot3 , mouse-acot4 , mouse-acot5 , mouse-ACOT6 |
| Title : Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase. - |
| Author(s) : Jones JM , Gould SJ |
| Ref : Biochemical & Biophysical Research Communications , 275 :233 , 2000 |
| PubMedID: 10944470 |
| Gene_locus related to this paper: human-ACOT2 |
| Title : Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library - Suzuki_1997_Gene_200_149 |
| Author(s) : Suzuki Y , Yoshitomo-Nakagawa K , Maruyama K , Suyama A , Sugano S |
| Ref : Gene , 200 :149 , 1997 |
| Abstract : Suzuki_1997_Gene_200_149 |
| ESTHER : Suzuki_1997_Gene_200_149 |
| PubMedSearch : Suzuki_1997_Gene_200_149 |
| PubMedID: 9373149 |
| Gene_locus related to this paper: human-ACOT2 , human-LIPF , human-LPL , human-PLA1A , human-PLA2G15 |
| Title : Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. - |
| Author(s) : Sherrington R , Rogaev EI , Liang Y , Rogaeva EA , Levesque G , Ikeda M , Chi H , Lin C , Li G , Holman K , Tsuda T , Mar L , Foncin J-F , Bruni AC , Montesi MP , Sorbi S , Rainero I , Pinessi L , Nee L , Chumakov I , Pollen D , Brookes A , Sanseau P , Polinsky RJ , Wasco W , da Silva HAR , Haines JL , Pericak-Vance MA , Tanzi RE , Roses AD , Fraser PE , Rommens JM , St George-Hyslop PH |
| Ref : Nature , 375 :754 , 1995 |
| PubMedID: 7596406 |
| Gene_locus related to this paper: human-ACOT2 |
| Title : Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides - Maruyama_1994_Gene_138_171 |
| Author(s) : Maruyama K , Sugano S |
| Ref : Gene , 138 :171 , 1994 |
| Abstract : Maruyama_1994_Gene_138_171 |
| ESTHER : Maruyama_1994_Gene_138_171 |
| PubMedSearch : Maruyama_1994_Gene_138_171 |
| PubMedID: 8125298 |
| Gene_locus related to this paper: human-ACOT2 , human-LIPF , human-LPL , human-PLA1A , human-PLA2G15 |