Q9WTS2
PR
Gene name |
Fut8 |
Protein name |
Alpha-(1,6)-fucosyltransferase |
Names |
Alpha1-6FucT, Fucosyltransferase 8, GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,6-fucosyltransferase, GDP-fucose--glycoprotein fucosyltransferase, Glycoprotein 6-alpha-L-fucosyltransferase |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:53618 |
EC number |
2.4.1.68: 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
3 structures for Q9WTS2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 6VLF | X-ray | 180 A | A/B | 68-575 | PDB |
| 6VLG | X-ray | 250 A | A/B/C/D | 68-575 | PDB |
| AF-Q9WTS2-F1 | Predicted | AlphaFoldDB |
20 variants for Q9WTS2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389231596 | 23 | F>I | No | EVA | |
| rs3403781477 | 25 | I>M | No | EVA | |
| rs3403064257 | 36 | P>I* | No | EVA | |
| rs3403244286 | 36 | P>L | No | EVA | |
| rs3403064257 | 37 | D>I | No | EVA | |
| rs3403534869 | 37 | D>IK* | No | EVA | |
| rs3389248043 | 305 | P>L | No | EVA | |
| rs3389244122 | 306 | L>P | No | EVA | |
| rs3389256088 | 330 | Q>H | No | EVA | |
| rs3389247986 | 428 | S>C | No | EVA | |
| rs3389238355 | 446 | S>* | No | EVA | |
| rs3389259050 | 466 | T>I | No | EVA | |
| rs3389231608 | 471 | V>I | No | EVA | |
| rs3389253181 | 494 | D>H | No | EVA | |
| rs3389177588 | 500 | G>V | No | EVA | |
| rs3389204998 | 539 | Y>N | No | EVA | |
| rs3389238404 | 540 | S>Y | No | EVA | |
| rs3389253251 | 550 | T>R | No | EVA | |
| rs3389259125 | 551 | G>R | No | EVA | |
| rs3389214535 | 571 | P>H | No | EVA |
No associated diseases with Q9WTS2
4 regional properties for Q9WTS2
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.1.68 | 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 |
|---|---|
| Golgi cisterna membrane | The lipid bilayer surrounding any of the thin, flattened compartments that form the central portion of the Golgi complex. |
| 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. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| alpha-(1->6)-fucosyltransferase activity | Catalysis of the transfer of an L-fucosyl group from GDP-beta-L-fucose to an acceptor molecule to form an alpha-(1->6) linkage. |
| glycoprotein 6-alpha-L-fucosyltransferase activity | Catalysis of the reaction: N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl}-L-asparagine + GDP-L-fucose = N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-[alpha-L-fucosyl-(1->6)]-N-acetyl-beta-D-glucosaminyl}asparagine + GDP + H(+). |
| glycosyltransferase activity | Catalysis of the transfer of a glycosyl group from one compound (donor) to another (acceptor). |
| SH3 domain binding | Binding to a SH3 domain (Src homology 3) of a protein, small protein modules containing approximately 50 amino acid residues found in a great variety of intracellular or membrane-associated proteins. |
13 GO annotations of biological process
| Name | Definition |
|---|---|
| cell migration | The controlled self-propelled movement of a cell from one site to a destination guided by molecular cues. Cell migration is a central process in the development and maintenance of multicellular organisms. |
| fibroblast migration | Cell migration that is accomplished by extension and retraction of a fibroblast pseudopodium. A fibroblast is a connective tissue cell which secretes an extracellular matrix rich in collagen and other macromolecules. |
| GDP-L-fucose metabolic process | The chemical reactions and pathways involving GDP-L-fucose, a substance composed of L-fucose in glycosidic linkage with guanosine diphosphate. |
| integrin-mediated signaling pathway | The series of molecular signals initiated by an extracellular ligand binding to an integrin on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. |
| N-glycan fucosylation | The process of transferring a fucosyl group to an N-glycan. An N-glycan is the carbohydrate portion of an N-glycoprotein when attached to a nitrogen from asparagine or arginine side-chains. |
| N-glycan processing | The conversion of N-linked glycan (N = nitrogen) structures from the initially transferred oligosaccharide to a mature form, by the actions of glycosidases and glycosyltransferases. The early processing steps are conserved and play roles in glycoprotein folding and trafficking. |
| 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. |
| protein N-linked glycosylation via asparagine | The glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification. |
| receptor metabolic process | The chemical reactions and pathways involving a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function. |
| regulation of cellular response to oxidative stress | Any process that modulates the frequency, rate or extent of cellular response to oxidative stress. |
| regulation of gene expression | Any process that modulates the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product (protein or RNA). |
| respiratory gaseous exchange by respiratory system | The process of gaseous exchange between an organism and its environment. In plants, microorganisms, and many small animals, air or water makes direct contact with the organism's cells or tissue fluids, and the processes of diffusion supply the organism with dioxygen (O2) and remove carbon dioxide (CO2). In larger animals the efficiency of gaseous exchange is improved by specialized respiratory organs, such as lungs and gills, which are ventilated by breathing mechanisms. |
| transforming growth factor beta receptor signaling pathway | The series of molecular signals initiated by an extracellular ligand binding to a transforming growth factor beta receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MRAWTGSWRW | IMLILFAWGT | LLFYIGGHLV | RDNDHPDHSS | RELSKILAKL | ERLKQQNEDL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RRMAESLRIP | EGPIDQGTAT | GRVRVLEEQL | VKAKEQIENY | KKQARNGLGK | DHEILRRRIE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NGAKELWFFL | QSELKKLKHL | EGNELQRHAD | EILLDLGHHE | RSIMTDLYYL | SQTDGAGDWR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EKEAKDLTEL | VQRRITYLQN | PKDCSKARKL | VCNINKGCGY | GCQLHHVVYC | FMIAYGTQRT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LILESQNWRY | ATGGWETVFR | PVSETCTDRS | GLSTGHWSGE | VNDKNIQVVE | LPIVDSLHPR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PPYLPLAVPE | DLADRLLRVH | GDPAVWWVSQ | FVKYLIRPQP | WLEKEIEEAT | KKLGFKHPVI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GVHVRRTDKV | GTEAAFHPIE | EYMVHVEEHF | QLLARRMQVD | KKRVYLATDD | PTLLKEAKTK |
| 430 | 440 | 450 | 460 | 470 | 480 |
| YSNYEFISDN | SISWSAGLHN | RYTENSLRGV | ILDIHFLSQA | DFLVCTFSSQ | VCRVAYEIMQ |
| 490 | 500 | 510 | 520 | 530 | 540 |
| TLHPDASANF | HSLDDIYYFG | GQNAHNQIAV | YPHKPRTEEE | IPMEPGDIIG | VAGNHWDGYS |
| 550 | 560 | 570 | |||
| KGINRKLGKT | GLYPSYKVRE | KIETVKYPTY | PEAEK |