Acyl-CoA thioesterase 9
| ACOT9 | |||
|---|---|---|---|
| Identifiers | |||
Gene ontology | |||
| Molecular function | |||
| Cellular component | |||
| Biological process | |||
| Sources:Amigo / QuickGO | |||
Ensembl | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| UniProt | |||||||||
| RefSeq (mRNA) | |||||||||
| RefSeq (protein) | |||||||||
| Location (UCSC) | Chr X: 23.7 – 23.77 Mb | Chr X: 154.05 – 154.08 Mb | |||||||
| PubMed search | [3] | [4] | |||||||
| View/Edit Human | View/Edit Mouse |
Acyl-CoA thioesterase 9 is a
hydrolyze Coenzyme A esters. There is no known function, however it has been shown to act as a long-chain thioesterase at low concentrations, and a short-chain thioesterase at high concentrations.[5]
Gene
Locus
The ACOT9 gene is located at p22.11 on
base pairs.[6]
Aliases
ACOT9 gene is known primarily for encoding the Acyl-CoA thioesterase 9 protein. Other, less commonly used names for the gene are ACATE2,[7] and MT-ACT48.[8]
Function
The protein encoded by the ACOT9 gene is part of a family of Acyl-CoA thioesterases, which catalyze the hydrolysis of various Coenzyme A esters of various molecules to the free acid plus CoA. These enzymes have also been referred to in the literature as acyl-CoA hydrolases, acyl-CoA thioester hydrolases, and palmitoyl-CoA hydrolases. The reaction carried out by these enzymes is as follows:
CoA ester + H2O → free acid + coenzyme A
These enzymes use the same
NADH/NAD+ ratio in order to maintain optimal mitochondrial beta oxidation of fatty acids.[17] The role of CoA esters in lipid metabolism and numerous other intracellular processes are well defined, and thus it is hypothesized that ACOT- enzymes play a role in modulating the processes these metabolites are involved in.[18]
Homology/Evolution
_vs._Time_(MYA)_in_ACOT9.png)
Orthologs
There are many
orthologs of ACOT9, the house mouse (Mus musculus) being one of the most similar, where the ACOT9 gene is found at 72.38cM on chromosome X.[19] The range of orthologs extends to mammals, birds, amphibians, anamorphic fungi, and others.[citation needed
]
| Sequence number | Genus and species | Common name | Date of divergence (MYA) | Accession number | Sequence length | Sequence identity | Sequence similarity | Notes |
|---|---|---|---|---|---|---|---|---|
| 1 | Homo sapiens | Human | 0 | NP_001028755.2 | 439 | 100% | 100% | Human |
| 2 | Mus musculus | House mouse | 91 | NP_062710.2 | 439 | 83% | 90% | Rodent |
| 3 | Pteropus alecto | Black flying fox | 97.4 | XP_006911668.1 | 480 | 81% | 91% | Bat |
| 4 | Gallus gallus | Chicken | 324.5 | NP_001012841.1 | 425 | 69% | 87% | Bird |
| 5 | Pseudopodoces humilis | Ground tit | 324.5 | XP_005516751.1 | 417 | 68% | 85% | Bird |
| 6 | Columba livia | Rock dove | 324.5 | XP_005503782.1 | 402 | 67% | 86% | Bird |
| 7 | Geospiza fortis | Medium ground finch | 324.5 | XP_005424946.1 | 417 | 67% | 85% | Bird |
| 8 | Pelodiscus sinensis | Chinese soft shelled turtle | 324.5 | XP_006112565.1 | 439 | 67% | 85% | Reptile |
| 9 | Xenopus tropicalis | Western clawed frog | 361.2 | AAI61600.1 | 418 | 65% | 82% | Amphibian |
| 10 | Danio rerio | Zebrafish | 454.6 | AAI59216.1 | 434 | 60% | 80% | Fish |
| 11 | Ceratitis capitata | Mediterranean fruit fly | 910 | JAB97119.1 | 433 | 32% | 58% | Insect |
| 12 | Glarea lozoyensis 74030 | Anamorphic fungus | 1368 | EHL00310.1 | 350 | 24% | 47% | Fungus |
Paralogs
In mice, which is one of the closest orthologs, ACOT10 is a known paralog of the ACOT9 gene.[20]
Expression
Expression of the ACOT9 is
ubiquitous/near ubiquitous, expression throughout human tissues.[22]
Transcription factors
There are numerous transcription factors throughout the ACOT9 promoter sequence. Some of the notable factors are heat shock factors and transcription factor II B (TFIIB) recognition elements.[citation needed]
| Transcription factor | Start | End | Strand | Sequence |
|---|---|---|---|---|
| X gene core promoter element 1 | 683 | 693 | - | ggGCGGgaccg |
| Doublesex and mab-3 related transcription factor 1 | 81 | 101 | + | tttttttgagacaTTGTctcc |
| cAMP-responsive element binding protein 1 | 491 | 511 | - | agggcgTGACgtcgagaagag |
| Sp4 transcription factor | 660 | 676 | - | ccagggGGCGtggccgc |
| Stimulating protein 1, ubiquitous zinc finger transcription factor | 682 | 698 | - | tccggGGGCgggaccgc |
| Heat shock factor 1 | 24 | 48 | + | caggactaaactAGAAtctccagcc |
| E2F transcription factor 2 | 808 | 824 | + | ccatcGCGCgcacggca |
| Nuclear factor of activated T-cells 5 | 380 | 398 | + | tttGGAAagttgcccagga |
| ZF5 POZ domain zinc finger, zinc finger protein 161 (secondary DNA binding preference) | 811 | 825 | + | tcgCGCGcacggcag |
| B-cell-specific activator protein | 678 | 706 | - | cagcggtgtccgggGGCGggaccgcggcg |
| Pax-6 paired domain binding site | 54 | 72 | + | gtctcAAGCatcagttttt |
| ZF5 POZ domain zinc finger, zinc finger protein 161 (secondary DNA binding preference) | 651 | 665 | - | ggcCGCGctgtgccg |
| Pax-6 paired domain binding site | 758 | 776 | + | ttttaTCGCctcagtttcc |
| Mammalian C-type LTR TATA box | 751 | 767 | - | ggcgaTAAAagacgcac |
| Nuclear factor Y (Y-box binding factor) | 624 | 638 | + | cccgCCAAtgaacgg |
| Transcription factor II B (TFIIB) recognition element | 356 | 362 | + | ccgCGCC |
| Transcription factor II B (TFIIB) recognition element | 440 | 446 | - | ccgCGCC |
| Transcription factor II B (TFIIB) recognition element | 734 | 740 | - | ccgCGCC |
| Nuclear factor Y (Y-box binding factor) | 581 | 595 | - | ccacTCAAtcagttg |
| CCAAT/enhancer binding protein alpha | 529 | 543 | - | tcggttgaGTAAacg |
Secondary structure
There are two regions in the ACOT9 gene sequence that are labeled as BFIT (Brown Fat Inducible Thioesterase) and BACH (Brain Acyl CoA Hydrolase) regions. These regions are part of a hotdog fold
alpha-helices throughout the structure,[24] suggesting it is a transmembrane protein
.
Interactions
A mitochondrial cleavage site can be found at amino acid 30 in the ACOT9 sequence, and the probability of export to the
plasma membrane, and 4.3% in the endoplasmic reticulum.[26]
The ACOT9 protein has been found to interact with the following proteins either experimentally or through co-expression:[27]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000123130 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000025287 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- S2CID 18767370.
- ^ Kent WJ, Sugnet CW, Furey TS, Roskin KM, Pringle TH, Zahler AM, Haussler D (June 12, 2002). "Human Feb. 2009 (GRCh37/hg19) Assembly". The human genome browser at UCSC. UCSC Genome Bioinformatics. Retrieved March 12, 2014.
- PMID 21059062.
- PMID 10383425.
- PMID 15292367.
- PMID 29756.
- PMID 5881327.
- PMID 9756869.
- S2CID 31065063.
- S2CID 4306469.
- PMID 10799735.
- PMID 9624183.
- PMID 8120000.
- PMID 11755680.
- ^ "ACOT9 gene detail". Mouse Genome Database. Retrieved 2014-06-19.
- ^ "Gene: Acot9". Ensembl release 75.
- ^ "Large-scale analysis of the human transcriptome (HG-U133A)". National Center for Biotechnology Information. Retrieved 10 May 2014.
- ^ "EST Profile Hs.298885 - ACOT9: Acyl-CoA thioesterase 9". Retrieved 10 May 2014.
- PMID 15307895.
- ^ "SDSC Biology WorkBench 3.2 Pele Program". [dead link]
- PMID 8944766.
- ^ "PSORTII Prediction Tool".[verification needed]
- PMID 18940858.
External links
- Human ACOT9 genome location and ACOT9 gene details page in the UCSC Genome Browser.
Further reading
- Mulkearns EE, Cooper JA (Apr 2012). "FCH domain only-2 organizes clathrin-coated structures and interacts with Disabled-2 for low-density lipoprotein receptor endocytosis". Molecular Biology of the Cell. 23 (7): 1330–42. PMID 22323290.
- Hunt MC, Yamada J, Maltais LJ, Wright MW, Podesta EJ, Alexson SE (Sep 2005). "A revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases". Journal of Lipid Research. 46 (9): 2029–32. PMID 16103133.
- Alkhaja AK, Jans DC, Nikolov M, Vukotic M, Lytovchenko O, Ludewig F, Schliebs W, Riedel D, Urlaub H, Jakobs S, Deckers M (Jan 2012). "MINOS1 is a conserved component of mitofilin complexes and required for mitochondrial function and cristae organization" (PDF). Molecular Biology of the Cell. 23 (2): 247–57. PMID 22114354.
- Poupon V, Bègue B, Gagnon J, Dautry-Varsat A, Cerf-Bensussan N, Benmerah A (Jul 1999). "Molecular cloning and characterization of MT-ACT48, a novel mitochondrial acyl-CoA thioesterase". The Journal of Biological Chemistry. 274 (27): 19188–94. PMID 10383425.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.