Q6BVB2
Gene name |
ALG11 (DEHA2C03982g) |
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 |
Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) |
KEGG Pathway |
dha:DEHA2C03982g |
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 Q6BVB2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q6BVB2-F1 | Predicted | AlphaFoldDB |
No variants for Q6BVB2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q6BVB2 | |||||
No associated diseases with Q6BVB2
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 | |
2 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. |
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. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGYLVVIGVI | ACVAYGILQV | VSTVLPRLLL | VPSQNWQDKI | KKEIEQPMVR | YLKVGNKRSS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| YRRRLVLASK | QPSFYTNFVN | NKIKVASVDS | QNDEGEFLAE | MKKRDVRDPQ | RKIIYGFFHP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| YANNGGGGER | VLWQAVQATL | ATSDRNIVAI | YTTNYESDPT | SILDKVEAKF | QISRLDEDRI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VFVYLRKYAR | LIDGDYWKRF | TLIGQLFGSM | VLSWEAMFEL | SPDVWIDTIG | LPGSYLLVSL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VLKIPIMSYV | HYPIIQPEMF | NKLKFQGLSQ | IRVPKLSEIK | TDVFSIGKLI | YWSGVFYFYK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| YLGSLVNITL | ANGSWTFNHI | SNIWTINKDE | AGYEMDILYP | PCGTETLTKN | VETLGSRENK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LLFIAQFRPE | KRHSLILRQY | SKFLVNATSI | GTPLKNIPTL | VFLGSCRTPD | DTKTLHDLKQ |
| 430 | 440 | 450 | 460 | 470 | 480 |
| EVDDLELNGY | VEFVVDCSYE | DIMVWLSKVK | FGLNAMWNEH | FGIGVVEYMS | RGVIPLCHAS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| AGPLLDIVTN | WDNEPTSVSW | YNNTGFFFKD | KSDPDFDLSL | QSDTASEFLQ | FSSRDNKDST |
| 550 | 560 | 570 | 580 | 590 | 600 |
| STYPTLARLL | DELFITNPDL | ISETRLQSMR | ENGVKSVLEK | FSNGVFTLKW | MQYSNQLGDL |
| 610 | |||||
| EKSYREERRS | GIEKVY |