O08992
SS
Gene name |
Sdcbp |
Protein name |
Syntenin-1 |
Names |
Scaffold protein Pbp1 , Syndecan-binding protein 1 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:53378 |
EC number |
|
Protein Class |
|
Descriptions
SDCBP (Syntenin-1) is a multifunctional adapter protein that regulates TGFB1-mediated SMAD2/3 activation, TGFB1-induced epithelial-to-mesenchymal transition (EMT) and cell migration in various cell types. The 100 amino acid long N-terminal domain (NTD) works as an autoinhibitory region, which restricts the membrane targeting by flanking to PDZ tandem. The deletion of the first 102 amino acids confers a strong plasma membrane enrichment. The region between amino acids 56 and 59 is highly conserved among systenin-1 proteins. In particular, phosphorylation of Tyr56 may regulate the plasma membrane binding of syntenin-1 by modulating the interaction strength between the internal peptide stretch and PDZ1-PDZ2.
Autoinhibitory domains (AIDs)
Target domain |
104-276 (PDZ tandem) |
Relief mechanism |
PTM |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for O08992
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O08992-F1 | Predicted | AlphaFoldDB |
13 variants for O08992
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388666416 | 9 | D>V | No | EVA | |
| rs3388669293 | 23 | S>F | No | EVA | |
| rs3388671065 | 63 | N>K | No | EVA | |
| rs250297689 | 79 | A>T | No | EVA | |
| rs3388651280 | 99 | G>D | No | EVA | |
| rs3388659120 | 104 | I>F | No | EVA | |
| rs3388666497 | 157 | D>N | No | EVA | |
| rs3388666472 | 159 | V>L | No | EVA | |
| rs3388670215 | 161 | Q>* | No | EVA | |
| rs3388666872 | 194 | R>S | No | EVA | |
| rs27663392 | 222 | I>L | No | EVA | |
| rs3388675725 | 227 | S>Y | No | EVA | |
| rs3388675176 | 270 | I>N | No | EVA |
No associated diseases with O08992
2 regional properties for O08992
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | PDZ domain | 113 - 195 | IPR001478-1 |
| domain | PDZ domain | 197 - 274 | IPR001478-2 |
Functions
14 GO annotations of cellular component
| Name | Definition |
|---|---|
| adherens junction | A cell-cell junction composed of the epithelial cadherin-catenin complex. The epithelial cadherins, or E-cadherins, of each interacting cell extend through the plasma membrane into the extracellular space and bind to each other. The E-cadherins bind to catenins on the cytoplasmic side of the membrane, where the E-cadherin-catenin complex binds to cytoskeletal components and regulatory and signaling molecules. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytoskeleton | A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| extracellular exosome | A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. |
| focal adhesion | A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ). |
| interleukin-5 receptor complex | A protein complex that binds interleukin-3; comprises an alpha and a beta subunit. The alpha chain is specific to the interleukin-5 receptor, whereas the beta chain is shared with the receptors for granulocyte-macrophage colony-stimulating factor and interleukin-3. |
| melanosome | A tissue-specific, membrane-bounded cytoplasmic organelle within which melanin pigments are synthesized and stored. Melanosomes are synthesized in melanocyte cells. |
| membrane raft | Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions. |
| nuclear membrane | Either of the lipid bilayers that surround the nucleus and form the nuclear envelope; excludes the intermembrane space. |
| nucleoplasm | That part of the nuclear content other than the chromosomes or the nucleolus. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| presynapse | The part of a synapse that is part of the presynaptic cell. |
13 GO annotations of molecular function
| Name | Definition |
|---|---|
| cell adhesion molecule binding | Binding to a cell adhesion molecule. |
| ephrin receptor binding | Binding to an ephrin receptor. |
| frizzled binding | Binding to a frizzled (fz) receptor. |
| growth factor binding | Binding to a growth factor, proteins or polypeptides that stimulate a cell or organism to grow or proliferate. |
| identical protein binding | Binding to an identical protein or proteins. |
| interleukin-5 receptor binding | Binding to an interleukin-5 receptor. |
| ionotropic glutamate receptor binding | Binding to an ionotropic glutamate receptor. Ionotropic glutamate receptors bind glutamate and exert an effect through the regulation of ion channels. |
| neurexin family protein binding | Binding to a neurexin, a synaptic cell surface protein related to latrotoxin receptor, laminin and agrin. Neurexins act as cell recognition molecules at nerve terminals. |
| phosphatidylinositol-4,5-bisphosphate binding | Binding to phosphatidylinositol-4,5-bisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 4' and 5' positions. |
| protein heterodimerization activity | Binding to a nonidentical protein to form a heterodimer. |
| protein sequestering activity | Binding to a protein to prevent it from interacting with other partners or to inhibit its localization to the area of the cell or complex where it is active. |
| protein-containing complex binding | Binding to a macromolecular complex. |
| syndecan binding | Binding to syndecan, an integral membrane proteoglycan (250-300 kDa) associated largely with epithelial cells. |
13 GO annotations of biological process
| Name | Definition |
|---|---|
| negative regulation of receptor internalization | Any process that stops, prevents, or reduces the frequency, rate or extent of receptor internalization. |
| negative regulation of transcription by RNA polymerase II | Any process that stops, prevents, or reduces the frequency, rate or extent of transcription mediated by RNA polymerase II. |
| positive regulation of cell growth | Any process that activates or increases the frequency, rate, extent or direction of cell growth. |
| positive regulation of cell migration | Any process that activates or increases the frequency, rate or extent of cell migration. |
| positive regulation of cell population proliferation | Any process that activates or increases the rate or extent of cell proliferation. |
| positive regulation of epithelial to mesenchymal transition | Any process that increases the rate, frequency, or extent of epithelial to mesenchymal transition. Epithelial to mesenchymal transition is where an epithelial cell loses apical/basolateral polarity, severs intercellular adhesive junctions, degrades basement membrane components and becomes a migratory mesenchymal cell. |
| positive regulation of exosomal secretion | Any process that activates or increases the frequency, rate or extent of exosomal secretion. |
| positive regulation of extracellular exosome assembly | Any process that activates or increases the frequency, rate or extent of extracellular vesicular exosome assembly. |
| positive regulation of phosphorylation | Any process that activates or increases the frequency, rate or extent of addition of phosphate groups to a molecule. |
| positive regulation of transforming growth factor beta receptor signaling pathway | Any process that activates or increases the frequency, rate or extent of TGF-beta receptor signaling pathway activity. |
| presynapse assembly | The aggregation, arrangement and bonding together of a set of components to form a presynapse. |
| Ras protein signal transduction | The series of molecular signals within the cell that are mediated by a member of the Ras superfamily of proteins switching to a GTP-bound active state. |
| regulation of mitotic cell cycle | Any process that modulates the rate or extent of progress through the mitotic cell cycle. |
7 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| O00560 | SDCBP | Syntenin-1 | Homo sapiens (Human) | EV |
| Q9H190 | SDCBP2 | Syntenin-2 | Homo sapiens (Human) | SS |
| B2RUJ5 | Apba1 | Amyloid-beta A4 precursor protein-binding family A member 1 | Mus musculus (Mouse) | SS |
| P98084 | Apba2 | Amyloid-beta A4 precursor protein-binding family A member 2 | Mus musculus (Mouse) | SS |
| Q99JZ0 | Sdcbp2 | Syntenin-2 | Mus musculus (Mouse) | SS |
| Q9JI92 | Sdcbp | Syntenin-1 | Rattus norvegicus (Rat) | SS |
| Q4KLN0 | Sdcbp2 | Syntenin-2 | Rattus norvegicus (Rat) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSLYPSLEDL | KVDKVIQAQT | AYSANPASQA | FVLVDASAAL | PPDGNLYPKL | YPELSQYMGL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SLNEAEICES | MPMVSGAPAQ | GQLVARPSSV | NYMVAPVTGN | DAGIRRAEIK | QGIREVILCK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DQDGKIGLRL | KSIDNGIFVQ | LVQANSPASL | VGLRFGDQVL | QINGENCAGW | SSDKAHKVLK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QAFGEKITMT | IRDRPFERTV | TMHKDSSGHV | GFIFKSGKIT | SIVKDSSAAR | NGLLTDHHIC |
| 250 | 260 | 270 | 280 | 290 | |
| EINGQNVIGL | KDAQIADILS | TAGTVVTITI | MPTFIFEHII | KRMAPSIMKS | LMDHTIPEV |