Q2HXL6
PR
Gene name |
Edem3 |
Protein name |
ER degradation-enhancing alpha-mannosidase-like protein 3 |
Names |
Alpha-1,2-mannosidase EDEM3 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:66967 |
EC number |
3.2.1.113: Glycosidases, ie enzymes hydrolyzing O- and S-glycosyl compounds |
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 Q2HXL6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q2HXL6-F1 | Predicted | AlphaFoldDB |
42 variants for Q2HXL6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388506688 | 57 | V>A | No | EVA | |
| rs3390808572 | 71 | H>Q | No | EVA | |
| rs3390794330 | 72 | A>V | No | EVA | |
| rs3388503886 | 85 | G>S | No | EVA | |
| rs3388506685 | 135 | V>I | No | EVA | |
| rs3388506186 | 136 | N>S | No | EVA | |
| rs3388507159 | 160 | H>R | No | EVA | |
| rs3388506627 | 201 | L>H | No | EVA | |
| rs3388505246 | 225 | T>I | No | EVA | |
| rs3388501997 | 229 | C>F | No | EVA | |
| rs3388503136 | 231 | G>D | No | EVA | |
| rs3388507536 | 234 | I>N | No | EVA | |
| rs3388506140 | 235 | L>F | No | EVA | |
| rs3390708306 | 261 | W>* | No | EVA | |
| rs3390806009 | 261 | W>R | No | EVA | |
| rs3390746129 | 261 | W>S | No | EVA | |
| rs3388503837 | 279 | T>S | No | EVA | |
| rs3388506210 | 291 | A>V | No | EVA | |
| rs3390632779 | 356 | F>Y | No | EVA | |
| rs3388504811 | 410 | S>G | No | EVA | |
| rs3388504085 | 440 | V>M | No | EVA | |
| rs3388503141 | 483 | F>L | No | EVA | |
| rs3388503835 | 489 | I>F | No | EVA | |
| rs3388504031 | 500 | W>C | No | EVA | |
| rs3390632821 | 521 | D>V | No | EVA | |
| rs3390790712 | 526 | D>V | No | EVA | |
| rs3390824052 | 529 | C>S | No | EVA | |
| rs3390746113 | 531 | N>I | No | EVA | |
| rs3388503147 | 580 | R>G | No | EVA | |
| rs259423034 | 594 | K>R | No | EVA | |
| rs3388504275 | 704 | M>V | No | EVA | |
| rs3388506252 | 722 | R>L | No | EVA | |
| rs3388508737 | 723 | N>H | No | EVA | |
| rs3390824057 | 737 | D>N | No | EVA | |
| rs51369827 | 784 | E>K | No | EVA | |
| rs3388504797 | 805 | D>E | No | EVA | |
| rs252879141 | 821 | M>V | No | EVA | |
| rs3388503850 | 829 | D>N | No | EVA | |
| rs3390789405 | 840 | A>ASSLSDGDASE* | No | EVA | |
| rs3388505177 | 846 | A>G | No | EVA | |
| rs3388506602 | 847 | S>Y | No | EVA | |
| rs3388504203 | 903 | G>A | No | EVA |
No associated diseases with Q2HXL6
Functions
| Description | ||
|---|---|---|
| EC Number | 3.2.1.113 | Glycosidases, ie enzymes hydrolyzing O- and S-glycosyl compounds |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
4 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). |
| endoplasmic reticulum lumen | The volume enclosed by the membranes of the endoplasmic reticulum. |
| endoplasmic reticulum quality control compartment | A subcompartment of the endoplasmic reticulum in which proteins with improper or incorrect folding accumulate. Enzymes in this compartment direct proteins with major folding problems to translocation to the cytosol and degradation, and proteins with minor folding problems to the ER, to interact with chaperon proteins. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| alpha-mannosidase activity | Catalysis of the hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides. |
| calcium ion binding | Binding to a calcium ion (Ca2+). |
| mannosyl-oligosaccharide 1,2-alpha-mannosidase activity | Catalysis of the hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in an oligo-mannose oligosaccharide. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| carbohydrate metabolic process | The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. |
| endoplasmic reticulum mannose trimming | Any protein alpha-1,2-demannosylation that takes place in the endoplasmic reticulum quality control compartment (ERQC). |
| glycoprotein catabolic process | The chemical reactions and pathways resulting in the breakdown of a glycoprotein, a protein that contains covalently bound glycose (i.e. monosaccharide) residues; the glycose occurs most commonly as oligosaccharide or fairly small polysaccharide but occasionally as monosaccharide. |
| mannose trimming involved in glycoprotein ERAD pathway | The removal of one or more alpha 1,2-linked mannose residues from a mannosylated protein that occurs as part of glycoprotein ER-associated glycoprotein degradation (gpERAD). |
| proteasome-mediated ubiquitin-dependent protein catabolic process | The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome. |
| protein glycosylation | A protein modification process that results in the addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid, e.g. the addition of glycan chains to proteins. |
| response to unfolded protein | 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 an unfolded protein stimulus. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSKAGGCRGC | GCRVPQRASW | SLVAATAALC | LVLATSVCTA | GAAPMSREEK | QKLGNQVLEM |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FDHAYGNYME | HAYPADELMP | LTCRGRVRGQ | EPSRGDVDDA | LGKFSLTLID | SLDTLVVLNK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TKEFEDAVRK | VLRDVNLDND | VVVSVFETNI | RVLGGLLGGH | SLAIMLKEKG | EHMQWYNDEL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LHMAKQLGYK | LLPAFNTTSG | LPYPRINLKF | GIRKPEARTG | TETDTCTACA | GTLILEFAAL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SRFTGATIFE | EYARKALDFL | WEKRQRSSNL | VGVTINIHTG | DWVRKDSGVG | AGIDSYYEYL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LKAYVLLGDD | SFLERFNTHY | DAIMRYISQP | PLLLDVHIHK | PMLNARTWMD | ALLAFFPGLQ |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VLKGDIRPAI | ETHEMLYQVI | KKHNFLPEAF | TTDFRVHWAQ | HPLRPEFAES | TYFLYKATGD |
| 430 | 440 | 450 | 460 | 470 | 480 |
| PYYLEVGKTL | IENLNKYARV | PCGFAAMKDV | RTGSHEDRMD | SFFLAEMFKY | LYLLFADKED |
| 490 | 500 | 510 | 520 | 530 | 540 |
| IIFDIEDYIF | TTEAHLLPLW | LSTTNRSISK | KNTTSEYTEL | DDSNFDWTCP | NTQILFPNDP |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LYAQSIREPL | KNVVDKSCPR | GIIRVEESFR | SGAKPPLRAR | DFMATNPEHL | EILKKMGVSL |
| 610 | 620 | 630 | 640 | 650 | 660 |
| IHLKDGRVQL | VQHAIQAASS | IDAEDGLRFM | QEMIELSSQQ | QKEQQLPPRA | VQIISHPFFG |
| 670 | 680 | 690 | 700 | 710 | 720 |
| RVVLTAGPAQ | FGLDLSKHKE | TRGFVASSKP | YNGCSELTNP | EAVMGKIALI | QRGQCMFAEK |
| 730 | 740 | 750 | 760 | 770 | 780 |
| ARNIQNAGAI | GGIVIDDNEG | SSSDTAPLFQ | MAGDGKDTDD | IKIPMLFLFS | KEGSIILDAI |
| 790 | 800 | 810 | 820 | 830 | 840 |
| REHEQVEVLL | SDKARDRDPE | MENEDQPSSE | NDSQNQSAEQ | MLSLSQTVDL | ADKESPEHPA |
| 850 | 860 | 870 | 880 | 890 | 900 |
| DSHSEASPSD | SEEAAGFAPS | EQISGSTENH | ETTSLDGECT | DLDNQVQEQS | ETEEDSSPNV |
| 910 | 920 | 930 | |||
| SWGTKAQPID | SILADWNEDI | EAFEMMEKDE | L |