Q99NB7
Gene name |
Acot12 (Cach, Cach1) |
Protein name |
Acetyl-coenzyme A thioesterase |
Names |
Acyl-CoA thioester hydrolase 12, Acyl-coenzyme A thioesterase 12, Acyl-CoA thioesterase 12, Cytoplasmic acetyl-CoA hydrolase 1, CACH-1, rACH, rCACH-1 |
Species |
Rattus norvegicus (Rat) |
KEGG Pathway |
rno:170570 |
EC number |
3.1.2.1: 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 Q99NB7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q99NB7-F1 | Predicted | AlphaFoldDB |
No variants for Q99NB7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q99NB7 | |||||
No associated diseases with Q99NB7
5 regional properties for Q99NB7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | START domain | 349 - 550 | IPR002913 |
| domain | Thioesterase domain | 29 - 96 | IPR006683-1 |
| domain | Thioesterase domain | 198 - 273 | IPR006683-2 |
| domain | Hotdog acyl-CoA thioesterase (ACOT)-type domain | 6 - 118 | IPR033120-1 |
| domain | Hotdog acyl-CoA thioesterase (ACOT)-type domain | 180 - 295 | IPR033120-2 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.1.2.1 | Thiolester hydrolases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| acetyl-CoA hydrolase activity | Catalysis of the reaction: acetyl-CoA + H(2)O = acetate + CoA + H(+). |
| acyl-CoA hydrolase activity | Catalysis of the reaction: acyl-CoA + H2O = CoA + a carboxylate. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| carboxylic ester hydrolase activity | Catalysis of the hydrolysis of a carboxylic ester bond. |
| 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. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| acetyl-CoA metabolic process | The chemical reactions and pathways involving acetyl-CoA, a derivative of coenzyme A in which the sulfhydryl group is acetylated; it is a metabolite derived from several pathways (e.g. glycolysis, fatty acid oxidation, amino-acid catabolism) and is further metabolized by the tricarboxylic acid cycle. It is a key intermediate in lipid and terpenoid biosynthesis. |
| 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. |
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 |
| Q91V12 | Acot7 | Cytosolic acyl coenzyme A thioester hydrolase | Mus musculus (Mouse) | PR |
| Q8VHQ9 | Acot11 | Acyl-coenzyme A thioesterase 11 | Mus musculus (Mouse) | PR |
| Q9DBK0 | Acot12 | Acetyl-coenzyme A thioesterase | Mus musculus (Mouse) | PR |
| Q64559 | Acot7 | Cytosolic acyl coenzyme A thioester hydrolase | Rattus norvegicus (Rat) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEPTVAPGEV | LMSQAIQPAH | ADSRGELSAG | QLLKWMDTTA | CLAAEKHAGI | SCVTASMDDI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LFEDTARIGQ | IVTIRAKVTR | AFSTSMEISI | KVRVQDKFTG | IQKLLCVAFS | TFVVKPLGKE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KVHLKPVLLQ | TEQEQVEHRL | ASERRKVRLQ | HENTFSNIMK | ESNWLRDPVC | NEEEGTATTM |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ATSVQSIELV | LPPHANHHGN | TFGGQIMAWM | ETVATISASR | LCHGHPFLKS | VDMFKFRGPS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TVGDRLVFNA | IVNNTFQNSV | EVGVRVEAFD | CREWAEGQGR | HINSAFLIYN | AVDDQEELIT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FPRIQPISKD | DFRRYQGAIA | RRRIRLGRKY | VISHKKEVPL | GTQWDISKKG | SISNTNVEAL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KNLASKSGWE | ITTTLEKIKI | YTLEEQDAIS | VKVEKQVGSP | ARVAYHLLSD | FTKRPLWDPH |
| 430 | 440 | 450 | 460 | 470 | 480 |
| YISCEVIDQV | SEDDQIYYIT | CSVVNGDKPK | DFVVLVSQRK | PLKDDNTYIV | ALMSVVLPSV |
| 490 | 500 | 510 | 520 | 530 | 540 |
| PPSPQYIRSQ | VICAGFLIQP | VDSSSCTVAY | LNQMSDSILP | YFAGNIGGWS | KSIEEAAASC |
| 550 | |||||
| IKFIENATHD | GLKSVL |