Q7ZW24
Gene name |
alg11 |
Protein name |
GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase |
Names |
Asparagine-linked glycosylation protein 11 homolog, Glycolipid 2-alpha-mannosyltransferase |
Species |
Danio rerio (Zebrafish) (Brachydanio rerio) |
KEGG Pathway |
|
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 Q7ZW24
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q7ZW24-F1 | Predicted | AlphaFoldDB |
No variants for Q7ZW24
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q7ZW24 | |||||
No associated diseases with Q7ZW24
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. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| 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. |
3 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P53954 | ALG11 | GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| Q9XEE9 | ALG11 | GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q6P312 | alg11 | GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSAHDHFSLC | LCDLIRLLWS | LMLPCFYLSF | LLTTILFLFI | MGVRSWLQMK | RKTRRVQDGR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PAVAFFHPYC | NAGGGGERVL | WCALRALQNR | YQDVSFVVYT | GDQGVTAEEI | LDGARRRFNI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RLPRPVKFVF | LKHRLLVEAK | LYPHFTLLGQ | SVGSIFLGWE | ALTEFVPDLY | IDSMGFAFTL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PVFRYLGGCQ | VGSYVHYPTI | STDMLSVVRE | RNPRFNNADY | ISSNPVLSAI | KVIYYCVFAL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LYGLAGSCSD | VIMVNSTWTL | GHILALWRTP | NRTSVVYPPC | DVQAFLDVPI | GEDNEEKEQK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KCHSLVSVGQ | FRPEKDHQLQ | IRAFKKLLDR | KEAEPAGREA | VKLVLIGGCR | NQEDEDRVLM |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LRGLCQELGI | ADRVEFKLNI | PFQELKKDLT | DATIGLHTMW | NEHFGIGIVE | CMAAGTIILA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| HKSGGPKLDI | VVPYDGGPTG | FLADDEDNYA | DAMERILSMS | PATRLEMRRR | ARLSVSRFSD |
| 490 | |||||
| QEFEGSFLSA | MEPLMSTLRA |