Q9FG93
Gene name |
MNS4 (At5g43710, MQD19.4, MQO24.4) |
Protein name |
Alpha-mannosidase I MNS4 |
Names |
|
Species |
Arabidopsis thaliana (Mouse-ear cress) |
KEGG Pathway |
ath:AT5G43710 |
EC number |
|
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 Q9FG93
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9FG93-F1 | Predicted | AlphaFoldDB |
75 variants for Q9FG93
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| tmp_5_17556520_C_A | 2 | D>Y | No | 1000Genomes | |
| tmp_5_17556506_C_G,T | 6 | K>N | No | 1000Genomes | |
| tmp_5_17556507_T_C | 6 | K>R | No | 1000Genomes | |
| ENSVATH12461162 | 19 | S>L | No | 1000Genomes | |
| tmp_5_17556454_G_A | 24 | H>Y | No | 1000Genomes | |
| ENSVATH00702247 | 33 | K>N | No | 1000Genomes | |
| ENSVATH12461161 | 39 | Q>R | No | 1000Genomes | |
| ENSVATH03340041 | 53 | D>E | No | 1000Genomes | |
| ENSVATH14580294 | 53 | D>N | No | 1000Genomes | |
| tmp_5_17555855_G_A | 93 | L>F | No | 1000Genomes | |
| tmp_5_17555840_G_A | 98 | R>C | No | 1000Genomes | |
| ENSVATH00702235 | 100 | T>I | No | 1000Genomes | |
| tmp_5_17555813_C_T | 107 | G>S | No | 1000Genomes | |
| tmp_5_17555795_T_G | 113 | N>H | No | 1000Genomes | |
| tmp_5_17555650_T_G | 115 | N>T | No | 1000Genomes | |
| ENSVATH03340039 | 120 | V>L | No | 1000Genomes | |
| tmp_5_17555582_C_A | 138 | A>S | No | 1000Genomes | |
| tmp_5_17555576_C_T | 140 | D>N | No | 1000Genomes | |
| tmp_5_17555298_T_A | 147 | I>F | No | 1000Genomes | |
| ENSVATH12461012 | 157 | L>M | No | 1000Genomes | |
| ENSVATH07321611 | 159 | E>D | No | 1000Genomes | |
| ENSVATH12461011 | 163 | R>Q | No | 1000Genomes | |
| tmp_5_17555242_C_A | 165 | M>I | No | 1000Genomes | |
| tmp_5_17555226_T_A | 171 | T>S | No | 1000Genomes | |
| ENSVATH07321596 | 229 | L>I | No | 1000Genomes | |
| ENSVATH12460882 | 231 | A>S | No | 1000Genomes | |
| tmp_5_17554498_C_A | 237 | D>Y | No | 1000Genomes | |
| ENSVATH12460876 | 276 | G>E | No | 1000Genomes | |
| tmp_5_17554061_G_T | 285 | Q>K | No | 1000Genomes | |
| ENSVATH07321584 | 292 | M>R | No | 1000Genomes | |
| ENSVATH07321583 | 293 | Q>R | No | 1000Genomes | |
| tmp_5_17554022_C_A | 298 | D>Y | No | 1000Genomes | |
| ENSVATH12460833 | 334 | D>H | No | 1000Genomes | |
| ENSVATH12460832 | 340 | H>Y | No | 1000Genomes | |
| tmp_5_17553646_C_A | 363 | S>I | No | 1000Genomes | |
| ENSVATH12460826 | 371 | Y>F | No | 1000Genomes | |
| tmp_5_17553324_T_A | 405 | Q>L | No | 1000Genomes | |
| ENSVATH03340007 | 427 | D>N | No | 1000Genomes | |
| ENSVATH00702196 | 470 | L>F | No | 1000Genomes | |
| tmp_5_17552927_G_T | 479 | L>I | No | 1000Genomes | |
| tmp_5_17552920_C_T | 481 | R>Q | No | 1000Genomes | |
| ENSVATH12460759 | 481 | R>W | No | 1000Genomes | |
| tmp_5_17552885_T_G | 493 | S>R | No | 1000Genomes | |
| ENSVATH03340000 | 500 | Q>H | No | 1000Genomes | |
| ENSVATH12460758 | 502 | V>G | No | 1000Genomes | |
| ENSVATH00702195 | 504 | G>E | No | 1000Genomes | |
| ENSVATH00702194 | 506 | D>N | No | 1000Genomes | |
| ENSVATH03339999 | 508 | S>N | No | 1000Genomes | |
| ENSVATH03339998 | 509 | N>I | No | 1000Genomes | |
| tmp_5_17552831_C_T | 511 | D>N | No | 1000Genomes | |
| tmp_5_17552824_C_A | 513 | S>I | No | 1000Genomes | |
| ENSVATH00702193 | 515 | D>G | No | 1000Genomes | |
| tmp_5_17552804_C_T | 520 | E>K | No | 1000Genomes | |
| ENSVATH12460756 | 523 | P>S | No | 1000Genomes | |
| tmp_5_17552781_C_A | 527 | L>F | No | 1000Genomes | |
| ENSVATH12460755 | 527 | L>S | No | 1000Genomes | |
| ENSVATH12460754 | 528 | I>V | No | 1000Genomes | |
| ENSVATH07321548 | 536 | T>I | No | 1000Genomes | |
| ENSVATH07321548 | 536 | T>K | No | 1000Genomes | |
| ENSVATH07321549 | 536 | T>S | No | 1000Genomes | |
| tmp_5_17552502_C_T | 542 | G>D | No | 1000Genomes | |
| tmp_5_17552471_A_T | 552 | D>E | No | 1000Genomes | |
| tmp_5_17552446_G_A | 561 | P>S | No | 1000Genomes | |
| ENSVATH00702191 | 563 | V>I | No | 1000Genomes | |
| ENSVATH03339980 | 577 | E>V | No | 1000Genomes | |
| tmp_5_17552385_T_A | 581 | Q>L | No | 1000Genomes | |
| ENSVATH12460688 | 583 | E>K | No | 1000Genomes | |
| ENSVATH07321546 | 588 | S>F | No | 1000Genomes | |
| tmp_5_17552337_G_T | 597 | S>Y | No | 1000Genomes | |
| ENSVATH07321545 | 599 | G>D | No | 1000Genomes | |
| ENSVATH07321545 | 599 | G>V | No | 1000Genomes | |
| tmp_5_17552319_T_G | 603 | D>A | No | 1000Genomes | |
| tmp_5_17552307_T_G | 607 | Q>P | No | 1000Genomes | |
| ENSVATH07321544 | 617 | D>E | No | 1000Genomes | |
| ENSVATH12460686 | 622 | Y>C | No | 1000Genomes |
No associated diseases with Q9FG93
No regional properties for Q9FG93
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q9FG93 | |||
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 membrane | The lipid bilayer surrounding 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. |
| integral component of membrane | The component of a 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. |
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. |
5 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). |
| 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). |
| 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. |
| ubiquitin-dependent ERAD pathway | The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDSNFKWLLF | AILISLTFSG | FVLHHGVLAE | SVKPDEAKQL | RDEVRGMFYH | AFDGYMNNAF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PLDELRPLSC | QGEDTLGGYA | LTLIDSLDTL | ALLGDRERFT | SSVEWIGKNL | QFNINKTVSV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FETTIRVLGG | LLSAHLIASD | YATGMRIPSY | NNELLVLAEN | LARRMLPAFD | TPTGIPFGSV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NLMYGVDKHE | SKITSTAGGG | TLSLEFGVLS | RLTNDPVFEQ | VAKNAVRGLW | ARRSNLDLVG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AHINVFTGEW | TQKDAGIGTS | IDSFYEYLLK | AYILFGDEEY | LYIFQEAYRS | AMQYLHKDPW |
| 310 | 320 | 330 | 340 | 350 | 360 |
| YVEVNMDSAA | IVWPVFNSLQ | AFWPGLQVLA | GDVDPAIRTH | TAFFSVWKRY | GFTPEGFNLA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TLSVQYGQKS | YPLRPELIES | TYWLYKATRD | PRYLDAGRDF | VASLQYGAKC | PCGYCHITDV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ELHKQEDHME | SFFLAETVKY | LWLLFDLAVD | SDNLVDNGPY | KYIFSTEGHL | LPITPQISLA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| REHCSYFGGY | CPSNSTKLEQ | EVLGEDSSND | DHSNDYPYHE | SFPVTGLIKG | LCPGLTHAQK |
| 550 | 560 | 570 | 580 | 590 | 600 |
| YGFSYVLPEK | TDREDVNQPK | PVVTSSSIVL | ISDQTVEKRP | QEEEGFTSQS | EPIMTISGGS |
| 610 | 620 | ||||
| SNDQTGQELT | LLESETDDQR | SYSS |