Q6C9T3
Gene name |
ALG11 (YALI0D08558g) |
Protein name |
GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase |
Names |
Alpha-1,2-mannosyltransferase ALG11, Asparagine-linked glycosylation protein 11, Glycolipid 2-alpha-mannosyltransferase |
Species |
Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica) |
KEGG Pathway |
yli:YALI0D08558g |
EC number |
2.4.1.131: Hexosyltransferases |
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 Q6C9T3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q6C9T3-F1 | Predicted | AlphaFoldDB |
No variants for Q6C9T3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q6C9T3 | |||||
No associated diseases with Q6C9T3
4 regional properties for Q6C9T3
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.1.131 | Hexosyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| 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. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity | Catalysis of the reaction: an alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc-diphosphodolichol + 2 GDP-alpha-D-mannose = an alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc-diphosphodolichol + 2 GDP + 2 H+. This reaction is the transfer of an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| dolichol-linked oligosaccharide biosynthetic process | The chemical reactions and pathways resulting in the formation of dolichol-linked oligosaccharide, usually by a stepwise addition of glycosyl chains to endoplasmic reticulum membrane-bound dolichol-P. |
| oligosaccharide-lipid intermediate biosynthetic process | The chemical reactions and pathways resulting in the formation of an oligosaccharide-lipid intermediate, such as a molecule of dolichol-P-man or dolicol-P-Glc used in N-linked glycosylation. |
| protein N-linked glycosylation | A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the N4 atom of peptidyl-asparagine, the omega-N of arginine, or the N1' atom peptidyl-tryptophan. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MALQLDLPTL | HDLRVVLNAD | FLAALAALLL | LAVILVPLCS | YISLYAWSAI | LAFKLRSPPA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NWEKSIVKGV | QANGTSTLFG | FGFWQAAAVR | RQLILQSNDP | SYYSVTHVSR | RSEIAISPED |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RNTEFRNRAQ | DSGAPRRVIY | GFFHPYANAG | GGGERVLWAA | VKDTLMYDDN | IICAIYCGEQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DLPTRTSPST | VLDAAVSNFH | VTELADKELR | KRIVFIGMRG | RRLVDPKTWP | RFTLMMQAAG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SVWMAWHGIS | TLVPDVFVDT | MGYPFAYPLV | SWVTHVPVAA | YVHYPVISKD | MLATVSLKQS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PVRAALAVAK | LVYWRVFALT | YTFAGSYCSV | VMTNSSWTNN | HMQHMWWYNH | KAEHIKIVYP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PCGTQALSEI | AMSEETSARS | PNIVYIAQFR | PEKRHDIVLR | EFNKFYKEYT | EKYPNQPAPH |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LTFVGTVRND | DDKSRVYLLR | LQARDLVNPD | SVSFVLDAPF | DKVRDILRTA | SMGVNAMWNE |
| 490 | 500 | 510 | 520 | 530 | 540 |
| HFGIVVVEYM | SAGLIPVVHN | SGGPKCDIVV | PYEGQSTGNS | GTLSAMPSST | SIRSHYEAVP |
| 550 | 560 | 570 | 580 | 590 | 600 |
| PGPTGFHFNC | PGSDPTTDSG | PSYDGEPIGT | LAETLMRAFE | LSESDTHNMR | ARARESVKKR |
| 610 | 620 | 630 | |||
| FSNEQFGSHW | QVRMRILEKL | EQIRRGHRLT | RGDFD |