UniProt ID | VP26A_RAT | |
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UniProt AC | Q6AY86 | |
Protein Name | Vacuolar protein sorting-associated protein 26A | |
Gene Name | Vps26a | |
Organism | Rattus norvegicus (Rat). | |
Sequence Length | 327 | |
Subcellular Localization |
Cytoplasm . Endosome membrane Peripheral membrane protein . Early endosome . Localizes to tubular profiles adjacent to endosomes. Predominantly found in early not late endosomes. |
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Protein Description | Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3.The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC complex seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5. Required for retrograde transport of lysosomal enzyme receptor IGF2R. Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA). Required for the endosomal localization of WASHC2 (indicative for the WASH complex). Required for the endosomal localization of TBC1D5. Mediates retromer cargo recognition of SORL1 and is involved in trafficking of SORL1 implicated in sorting and processing of APP. Involved in retromer-independent lysosomal sorting of F2R. Involved in recycling of ADRB2. Acts redundantly with VSP26B in SNX-27 mediated endocytic recycling of SLC2A1/GLUT1. Enhances the affinity of SNX27 for PDZ-binding motifs in cargo proteins (By similarity).. | |
Protein Sequence | MSFLGGFFGPICEIDVALSDGETRKMAEMKTEDGKVEKHYLFYDGESVSGKVNLAFKQPGKRLEHQGIRIEFVGQIELFNDKSNTHEFVNLVKELALPGELTQSRSYDFEFMQVEKPYESYIGANVRLRYFLKVTIVRRLTDLVKEYDLIVHQLATYPEVNNSIKMEVGIEDCLHIEFEYNKSKYHLKDVIVGKIYFLLVRIKIQHMELQLIKKEITGIGPSTTTETETIAKYEIMDGAPVKGESIPIRLFLAGYDPTPTMRDVNKKFSVRYFLNLVLVDEEDRRYFKQQEIILWRKAPEKLRKQRTNFHQRFESPESQASAEQPEM | |
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 |
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2 | Phosphorylation | ------MSFLGGFFG ------CCCCCCCCC | 29.22 | 27097102 | |
35 | Acetylation | EMKTEDGKVEKHYLF EEECCCCCEEEEEEE | 60.59 | 22902405 | |
47 | Phosphorylation | YLFYDGESVSGKVNL EEEECCCCCCCEEEE | 27.41 | 23984901 | |
49 | Phosphorylation | FYDGESVSGKVNLAF EECCCCCCCEEEEEE | 42.02 | 30181290 | |
242 | Ubiquitination | IMDGAPVKGESIPIR EECCCCCCCCCCCEE | 56.77 | - | |
315 | Phosphorylation | NFHQRFESPESQASA CHHHHHCCHHHHHHH | 31.12 | 27097102 | |
318 | Phosphorylation | QRFESPESQASAEQP HHHCCHHHHHHHCCC | 34.14 | 27097102 | |
321 | Phosphorylation | ESPESQASAEQPEM- CCHHHHHHHCCCCC- | 25.38 | 27097102 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of VP26A_RAT !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of VP26A_RAT !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
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Oops, there are no SNP-PTM records of VP26A_RAT !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
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Oops, there are no PPI records of VP26A_RAT !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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