| UniProt ID | WNTG_DROME | |
|---|---|---|
| UniProt AC | P09615 | |
| Protein Name | Protein wingless | |
| Gene Name | wg | |
| Organism | Drosophila melanogaster (Fruit fly). | |
| Sequence Length | 468 | |
| Subcellular Localization |
Secreted . Cell junction, synapse . Membrane Lipid-anchor. Secreted, extracellular space, extracellular matrix . Palmitoleoylation converts wg into a membrane-anchored protein that is partitioned into specialized lipid raft microdomains before secre |
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| Protein Description | Binds as a ligand to a family of frizzled seven-transmembrane receptors and acts through a cascade of genes on the nucleus. Segment polarity protein. May be a growth factor. Acts on neighboring cells to regulate at least one gene, the homeobox segmentation gene engrailed. Wg signal represses arm phosphorylation. Wg signaling operates by inactivating the sgg repression of engrailed autoactivation. Wg and Wnt2 have a role in the developing trachea and together are responsible for all dorsal trunk formation. Wg also acts in the developing epidermis. Acts as a morphogen, and diffuses long distances despite its lipidation. Lipophorin is required for diffusion, probably by acting as vehicle for its movement, explaining how it can spread over long distances despite its lipidation. In non-neuronal cells, wls directs wg secretion via clathrin-mediated endocytosis and the retromer complex (a conserved protein complex consisting of Vps26 and Vps35) to sustain a wls traffic loop encompassing the Golgi, the cell surface, an endocytic compartment and a retrograde route leading back to the Golgi. In neuronal cells (the larval motorneuron NMJ), wg signal moves across the synapse through the release of wls-containing exosome-like vesicles.. | |
| Protein Sequence | MDISYIFVICLMALCSGGSSLSQVEGKQKSGRGRGSMWWGIAKVGEPNNITPIMYMDPAIHSTLRRKQRRLVRDNPGVLGALVKGANLAISECQHQFRNRRWNCSTRNFSRGKNLFGKIVDRGCRETSFIYAITSAAVTHSIARACSEGTIESCTCDYSHQSRSPQANHQAGSVAGVRDWEWGGCSDNIGFGFKFSREFVDTGERGRNLREKMNLHNNEAGRAHVQAEMRQECKCHGMSGSCTVKTCWMRLANFRVIGDNLKARFDGATRVQVTNSLRATNALAPVSPNAAGSNSVGSNGLIIPQSGLVYGEEEERMLNDHMPDILLENSHPISKIHHPNMPSPNSLPQAGQRGGRNGRRQGRKHNRYHFQLNPHNPEHKPPGSKDLVYLEPSPSFCEKNLRQGILGTHGRQCNETSLGVDGCGLMCCGRGYRRDEVVVVERCACTFHWCCEVKCKLCRTKKVIYTCL | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 103 | N-linked_Glycosylation | QFRNRRWNCSTRNFS HHHHCCCCCCCCCCC | 14.19 | 11821428 | |
| 108 | N-linked_Glycosylation | RWNCSTRNFSRGKNL CCCCCCCCCCCCCCH | 39.06 | - | |
| 239 | O-palmitoleoylation | ECKCHGMSGSCTVKT HCCCCCCCCCCEEEE | 31.95 | - | |
| 414 | N-linked_Glycosylation | GTHGRQCNETSLGVD CCCCCCCCCCCCCCC | 47.44 | 11821428 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of WNTG_DROME !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of WNTG_DROME !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of WNTG_DROME !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| N-linked Glycosylation | |
| Reference | PubMed |
| "Drosophila segment polarity gene product porcupine stimulates theposttranslational N-glycosylation of wingless in the endoplasmicreticulum."; Tanaka K., Kitagawa Y., Kadowaki T.; J. Biol. Chem. 277:12816-12823(2002). Cited for: SUBUNIT, GLYCOSYLATION BY PORCUPINE, INTERACTION WITH PORCUPINE,GLYCOSYLATION AT ASN-103 AND ASN-414, AND MUTAGENESIS OF THR-51;SER-105; SER-110 AND THR-416. | |
