Q9D3B1
Gene name |
Hacd2 |
Protein name |
Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 2 |
Names |
3-hydroxyacyl-CoA dehydratase 2, HACD2, Protein-tyrosine phosphatase-like member B |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:70757 |
EC number |
4.2.1.134: Hydro-lyases |
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 Q9D3B1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9D3B1-F1 | Predicted | AlphaFoldDB |
5 variants for Q9D3B1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389383161 | 119 | W>R | No | EVA | |
| rs3389423671 | 127 | E>* | No | EVA | |
| rs3413055106 | 155 | S>N | No | EVA | |
| rs3389394670 | 213 | D>E | No | EVA | |
| rs3389416830 | 246 | H>L | No | EVA |
No associated diseases with Q9D3B1
3 regional properties for Q9D3B1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Fibronectin type III | 357 - 606 | IPR003961-1 |
| domain | Fibronectin type III | 609 - 709 | IPR003961-2 |
| repeat | Kelch repeat type 1 | 22 - 59 | IPR006652 |
Functions
| Description | ||
|---|---|---|
| EC Number | 4.2.1.134 | Hydro-lyases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
| integral component of endoplasmic reticulum membrane | The component of the endoplasmic reticulum membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
7 GO annotations of molecular function
| Name | Definition |
|---|---|
| 3-hydroxy-arachidoyl-CoA dehydratase activity | Catalysis of the reaction: (R)-3-hydroxyicosanoyl-CoA <=> trans-2-icosenoyl-CoA + H2O. |
| 3-hydroxy-behenoyl-CoA dehydratase activity | Catalysis of the reaction: (R)-3-hydroxybehenoyl-CoA <=> trans-2-docosenoyl-CoA + H2O. |
| 3-hydroxy-lignoceroyl-CoA dehydratase activity | Catalysis of the reaction: (R)-3-hydroxylignoceroyl-CoA(4-) <=> trans-2-tetracosenoyl-CoA + H2O. |
| 3-hydroxyacyl-CoA dehydratase activity | Catalysis of the reaction: alkene-CoA + H2O = alcohol-CoA. Substrates are crotonoyl-CoA (producing 3-hydroxyacyl-CoA) and 2,3-didehydro-pimeloyl-CoA (producing 3-hydroxypimeloyl-CoA). |
| 3R-hydroxyacyl-CoA dehydratase activity | Catalysis of the reaction: 3R-hydroxyacyl-CoA = 2E-enoyl-CoA + H2O. |
| enzyme binding | Binding to an enzyme, a protein with catalytic activity. |
| very-long-chain 3-hydroxyacyl-CoA dehydratase activity | Catalysis of the reaction: a very-long-chain (3R)-3-hydroxyacyl-CoA = H2O + a very-long-chain trans-2,3-dehydroacyl-CoA. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| fatty acid elongation | The elongation of a fatty acid chain by the sequential addition of two-carbon units. |
| sphingolipid biosynthetic process | The chemical reactions and pathways resulting in the formation of sphingolipids, any of a class of lipids containing the long-chain amine diol sphingosine or a closely related base (a sphingoid). |
| very long-chain fatty acid biosynthetic process | The chemical reactions and pathways resulting in the formation of a fatty acid which has a chain length greater than C22. |
4 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q2KIP8 | HACD2 | Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 2 | Bos taurus (Bovine) | PR |
| Q9P035 | HACD3 | Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 3 | Homo sapiens (Human) | PR |
| Q6Y1H2 | HACD2 | Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 2 | Homo sapiens (Human) | PR |
| Q7SY06 | hacd3 | Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase | Danio rerio (Zebrafish) (Brachydanio rerio) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAAAAATAAT | KGNGGGSGRV | GAGDSSGARK | KKGPGPVATA | YLVIYNVVMT | AGWLVIAVGL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VRAYLAKGSY | HSLYYSIERP | LKFFQTGALL | EILHCAIGIV | PSSVVLTSFQ | VMSRVFLIWA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VTHSVKEVQS | EDSVLLFVIA | WTITEIIRYS | FYTFSLLNHL | PYIIKWARYT | LFIVLYPMGV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TGELLTIYAA | LPFVRQAGLY | SISLPNKYNF | SFDYHAFLIL | IMISYIPLFP | QLYFHMIHQR |
| 250 | |||||
| RKVLSHTEEH | KKFE |