Q8VHQ9
Gene name |
Acot11 (Bfit, Thea) |
Protein name |
Acyl-coenzyme A thioesterase 11 |
Names |
Acyl-CoA thioesterase 11, Acyl-CoA thioester hydrolase 11, Adipose-associated thioesterase, Brown fat-inducible thioesterase, BFIT, Palmitoyl-coenzyme A thioesterase |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:329910 |
EC number |
3.1.2.2: Thiolester hydrolases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q8VHQ9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8VHQ9-F1 | Predicted | AlphaFoldDB |
39 variants for Q8VHQ9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388699880 | 9 | L>* | No | EVA | |
| rs232228938 | 34 | P>A | No | EVA | |
| rs3388696843 | 38 | A>VSDG* | No | EVA | |
| rs3394649178 | 48 | E>V | No | EVA | |
| rs3394645233 | 62 | H>L | No | EVA | |
| rs3394694697 | 118 | N>H | No | EVA | |
| rs3388685862 | 169 | T>S | No | EVA | |
| rs3388700786 | 200 | C>G | No | EVA | |
| rs3388693648 | 204 | D>V | No | EVA | |
| rs3388694799 | 222 | E>V | No | EVA | |
| rs3388694692 | 224 | V>D | No | EVA | |
| rs3388704085 | 257 | R>Q | No | EVA | |
| rs3388703269 | 257 | R>W | No | EVA | |
| rs3388696906 | 284 | V>M | No | EVA | |
| rs3388700419 | 286 | K>T | No | EVA | |
| rs3388699829 | 288 | I>N | No | EVA | |
| rs3388685875 | 294 | K>M | No | EVA | |
| rs3388691597 | 301 | V>E | No | EVA | |
| rs3388688430 | 302 | C>* | No | EVA | |
| rs3388693626 | 317 | I>V | No | EVA | |
| rs3388685947 | 342 | Q>K | No | EVA | |
| rs3388700764 | 379 | P>H | No | EVA | |
| rs3388703227 | 380 | W>* | No | EVA | |
| rs3388700789 | 406 | V>M | No | EVA | |
| rs3394649187 | 449 | R>S | No | EVA | |
| rs3388704009 | 458 | S>* | No | EVA | |
| rs3388678145 | 464 | Q>* | No | EVA | |
| rs28168845 | 466 | D>Y | No | EVA | |
| rs3388700483 | 471 | I>F | No | EVA | |
| rs3388693641 | 473 | H>R | No | EVA | |
| rs3388698656 | 475 | I>F | No | EVA | |
| rs3388697224 | 484 | K>M | No | EVA | |
| rs3388691601 | 489 | V>L | No | EVA | |
| rs3388697306 | 520 | P>S | No | EVA | |
| rs3388694811 | 521 | E>D | No | EVA | |
| rs3388678185 | 576 | C>R | No | EVA | |
| rs3388699862 | 581 | L>* | No | EVA | |
| rs3388691586 | 588 | A>D | No | EVA | |
| rs3388700436 | 595 | L>L | No | EVA |
No associated diseases with Q8VHQ9
5 regional properties for Q8VHQ9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | START domain | 385 - 583 | IPR002913 |
| domain | Thioesterase domain | 69 - 135 | IPR006683-1 |
| domain | Thioesterase domain | 235 - 304 | IPR006683-2 |
| domain | Hotdog acyl-CoA thioesterase (ACOT)-type domain | 45 - 157 | IPR033120-1 |
| domain | Hotdog acyl-CoA thioesterase (ACOT)-type domain | 217 - 330 | IPR033120-2 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.1.2.2 | Thiolester hydrolases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| mitochondrial matrix | The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| acyl-CoA hydrolase activity | Catalysis of the reaction: acyl-CoA + H2O = CoA + a carboxylate. |
| carboxylic ester hydrolase activity | Catalysis of the hydrolysis of a carboxylic ester bond. |
| long-chain acyl-CoA hydrolase activity | Catalysis of the reaction: H2O + a long-chain acyl-CoA = a long-chain carboxylate + CoA. A long chain is a chain of greater than 12 carbons in length. |
| long-chain fatty acyl-CoA binding | Binding to a long-chain fatty acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a long-chain fatty-acyl group. Long-chain fatty-acyl-CoAs have chain lengths of C13 or more. |
| myristoyl-CoA hydrolase activity | Catalysis of the reaction: myristoyl-CoA + H2O <=> H+ + tetradecanoate + coenzyme A. |
| palmitoyl-CoA hydrolase activity | Catalysis of the reaction: palmitoyl-CoA + H2O = CoA + palmitate. |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| acyl-CoA metabolic process | The chemical reactions and pathways involving acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with an acyl group. |
| fatty acid metabolic process | The chemical reactions and pathways involving fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis. |
| intracellular signal transduction | The process in which a signal is passed on to downstream components within the cell, which become activated themselves to further propagate the signal and finally trigger a change in the function or state of the cell. |
| negative regulation of cold-induced thermogenesis | Any process that stops, prevents, or reduces the rate of cold-induced thermogenesis. |
| response to cold | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cold stimulus, a temperature stimulus below the optimal temperature for that organism. |
| response to temperature stimulus | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a temperature stimulus. |
10 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q3SWX2 | ACOT9 | Acyl-coenzyme A thioesterase 9, mitochondrial | Bos taurus (Bovine) | PR |
| O00154 | ACOT7 | Cytosolic acyl coenzyme A thioester hydrolase | Homo sapiens (Human) | PR |
| Q9Y305 | ACOT9 | Acyl-coenzyme A thioesterase 9, mitochondrial | Homo sapiens (Human) | PR |
| Q8WYK0 | ACOT12 | Acetyl-coenzyme A thioesterase | Homo sapiens (Human) | PR |
| Q9R0X4 | Acot9 | Acyl-coenzyme A thioesterase 9, mitochondrial | Mus musculus (Mouse) | PR |
| Q32MW3 | Acot10 | Acyl-coenzyme A thioesterase 10, mitochondrial | Mus musculus (Mouse) | PR |
| Q9DBK0 | Acot12 | Acetyl-coenzyme A thioesterase | Mus musculus (Mouse) | PR |
| Q91V12 | Acot7 | Cytosolic acyl coenzyme A thioester hydrolase | Mus musculus (Mouse) | PR |
| Q64559 | Acot7 | Cytosolic acyl coenzyme A thioester hydrolase | Rattus norvegicus (Rat) | PR |
| Q99NB7 | Acot12 | Acetyl-coenzyme A thioesterase | Rattus norvegicus (Rat) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MIQNVGNHLR | RGFASMFSNR | TSRKSISHPE | SGDPPTMAEG | EGYRNPTEVQ | MSQLVLPCHT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NHRGELSIGQ | LLKWIDTTAC | LSAERHAGCP | CVTASMDDIY | FDHTISVGQV | VNIKAKVNRA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FNSSMEVGIQ | VVSEDLCSEK | QWSVCKALAT | FVAHRELSKV | KLKQVIPLTE | EEKTEHGVAA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ERRRMRLVYA | DTIKDLLTHC | VIQDDLDKDC | SNMVPAEKTR | VESVELVLPP | HANHQGNTFG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GQIMAWMENV | ATIAASRLCH | AHPTLKAIEM | FHFRGPSQVG | DRLVLKAIVN | NAFKHSMEVG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VCVEAYRQEA | ETQRRHINSA | FMTFVVLDKD | DQPQKLPWIR | PQPGEGERRY | REASARKKIR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LDRKYLVSCK | QAEVALSVPW | DPSNQVYLSY | YNVSSLKTLM | AKDNWVLSVE | ISEVRLYILE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| EDFLSFHLEM | VVNVDAAQVF | QLLSDLRRRP | EWDKHYRSVE | LVQQVDEDDA | IYHVISPALS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| GNTKPQDFVI | LASRRKPCDN | GDPYVIALRS | VTLPTHHETP | EYQRGETLCS | GFCLWREGDQ |
| 550 | 560 | 570 | 580 | 590 | |
| MTKVSYYNQA | TPGFLNYVTT | NVSGLSSEFY | NTFKACESFL | LDNRNDLAPS | LQTL |