Q91V12
PR
Gene name |
Acot7 (Bach) |
Protein name |
Cytosolic acyl coenzyme A thioester hydrolase |
Names |
Acyl-CoA thioesterase 7, Brain acyl-CoA hydrolase, BACH, CTE-IIa, CTE-II, Long chain acyl-CoA thioester hydrolase |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:70025 |
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
5 structures for Q91V12
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 2Q2B | X-ray | 250 A | A/B | 203-381 | PDB |
| 2V1O | X-ray | 178 A | A/B/C/D/E/F | 59-206 | PDB |
| 4ZV3 | X-ray | 310 A | A/B/C | 55-369 | PDB |
| 6VFY | X-ray | 260 A | D/E/F | 55-369 | PDB |
| AF-Q91V12-F1 | Predicted | AlphaFoldDB |
13 variants for Q91V12
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs242266329 | 9 | R>C | No | EVA | |
| rs3388736983 | 16 | Q>H | No | EVA | |
| rs215170552 | 18 | A>V | No | EVA | |
| rs229429473 | 55 | V>I | No | EVA | |
| rs3388736998 | 101 | C>* | No | EVA | |
| rs221900128 | 127 | A>G | No | EVA | |
| rs13472220 | 137 | V>L | No | EVA | |
| rs3388712017 | 251 | T>S | No | EVA | |
| rs3388729675 | 262 | V>M | No | EVA | |
| rs3388740151 | 263 | A>G | No | EVA | |
| rs3388727074 | 270 | N>K | No | EVA | |
| rs3412982496 | 304 | S>F | No | EVA | |
| rs3388722932 | 344 | P>S | No | EVA |
No associated diseases with Q91V12
4 regional properties for Q91V12
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Thioesterase domain | 70 - 148 | IPR006683-1 |
| domain | Thioesterase domain | 243 - 313 | IPR006683-2 |
| domain | Hotdog acyl-CoA thioesterase (ACOT)-type domain | 51 - 169 | IPR033120-1 |
| domain | Hotdog acyl-CoA thioesterase (ACOT)-type domain | 225 - 339 | 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 | |
6 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. |
| neuron projection | A prolongation or process extending from a nerve cell, e.g. an axon or dendrite. |
| neuronal cell body | The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites. |
| nucleoplasm | That part of the nuclear content other than the chromosomes or the nucleolus. |
8 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. |
| fatty-acyl-CoA binding | Binding to a fatty-acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with a fatty acyl group. |
| identical protein binding | Binding to an identical protein or proteins. |
| 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. |
| protein homodimerization activity | Binding to an identical protein to form a homodimer. |
8 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. |
| coenzyme A biosynthetic process | The chemical reactions and pathways resulting in the formation of coenzyme A, 3'-phosphoadenosine-(5')diphospho(4')pantatheine, an acyl carrier in many acylation and acyl-transfer reactions in which the intermediate is a thiol ester. |
| fatty acid catabolic process | The chemical reactions and pathways resulting in the breakdown of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes. |
| fatty acid metabolic process | The chemical reactions and pathways involving fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis. |
| long-chain fatty-acyl-CoA catabolic process | The chemical reactions and pathways resulting in the breakdown of long-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a medium-chain fatty-acyl group. A long-chain fatty acid is a fatty acid with a chain length between C13 and C22. |
| medium-chain fatty acid biosynthetic process | The chemical reactions and pathways resulting in the formation of any fatty acid with a chain length of between C6 and C12. |
| medium-chain fatty-acyl-CoA catabolic process | The chemical reactions and pathways resulting in the breakdown of medium-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a medium-chain fatty-acyl group. A medium-chain fatty acid is a fatty acid with a chain length of between C6 and C12. |
| palmitic acid biosynthetic process | The chemical reactions and pathways resulting in the formation of palmitic acid. |
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 |
| Q8WYK0 | ACOT12 | Acetyl-coenzyme A thioesterase | Homo sapiens (Human) | PR |
| Q9Y305 | ACOT9 | Acyl-coenzyme A thioesterase 9, mitochondrial | Homo sapiens (Human) | PR |
| O00154 | ACOT7 | Cytosolic acyl coenzyme A thioester hydrolase | 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 |
| Q8VHQ9 | Acot11 | Acyl-coenzyme A thioesterase 11 | Mus musculus (Mouse) | PR |
| Q99NB7 | Acot12 | Acetyl-coenzyme A thioesterase | Rattus norvegicus (Rat) | PR |
| Q64559 | Acot7 | Cytosolic acyl coenzyme A thioester hydrolase | Rattus norvegicus (Rat) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKLLVGTLRL | WEVGRQVAFS | SLTPGQECSG | LRKTFWAAMR | AVRTRADHQK | LGHCVTMGRI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| MRPDDANVAG | NVHGGTILKM | IEEAGAIIST | RHCNSQNGER | CVAALARVER | TDFLSPMCIG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EVAHVSAEIT | YTSKHSVEVQ | VHVMSENILT | GTKKLTNKAT | LWYVPLSLKN | VDKVLEVPPI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VYLRQEQEEE | GRKRYEAQKL | ERMETKWRNG | DIVQPVLNPE | PNTVSYSQSS | LIHLVGPSDC |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TLHGFVHGGV | TMKLMDEVAG | IVAARHCKTN | IVTASVDAIN | FHDKIRKGCV | ITISGRMTFT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SNKSMEIEVL | VDADPVVDNS | QKRYRAASAF | FTYVSLNQEG | KPMPVPQLVP | ETEDEKKRFE |
| 370 | 380 | ||||
| EGKGRYLQMK | AKRQGHTEPQ | P |