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 Q6UC88
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q6UC88-F1 | Predicted | AlphaFoldDB |
25 variants for Q6UC88
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs134821996 | 30 | I>L | No | EVA | |
| rs452141209 | 39 | M>V | No | EVA | |
| rs475431631 | 41 | V>A | No | EVA | |
| rs437604621 | 44 | V>G | No | EVA | |
| rs457612834 | 57 | A>S | No | EVA | |
| rs443181689 | 86 | S>G | No | EVA | |
| rs469848507 | 162 | L>M | No | EVA | |
| rs519785581 | 185 | A>V | No | EVA | |
| rs523374902 | 188 | L>P | No | EVA | |
| rs801282579 | 211 | A>T | No | EVA | |
| rs722954404 | 212 | V>I | No | EVA | |
| rs797303452 | 218 | S>L | No | EVA | |
| rs458724404 | 244 | A>V | No | EVA | |
| rs476648124 | 248 | F>V | No | EVA | |
| rs435459203 | 253 | G>V | No | EVA | |
| rs455664505 | 257 | C>G | No | EVA | |
| rs472352299 | 261 | R>G | No | EVA | |
| rs443846963 | 262 | Y>C | No | EVA | |
| rs463813650 | 270 | N>Y | No | EVA | |
| rs459728965 | 283 | V>A | No | EVA | |
| rs479899890 | 287 | K>Q | No | EVA | |
| rs445096975 | 296 | E>D | No | EVA | |
| rs465223077 | 300 | M>I | No | EVA | |
| rs519977580 | 303 | T>M | No | EVA | |
| rs436916380 | 305 | E>D | No | EVA |
No associated diseases with Q6UC88
16 regional properties for Q6UC88
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| ptm | EGF-type aspartate/asparagine hydroxylation site | 589 - 600 | IPR000152-1 |
| ptm | EGF-type aspartate/asparagine hydroxylation site | 744 - 755 | IPR000152-2 |
| domain | EGF-like domain | 573 - 614 | IPR000742-1 |
| domain | EGF-like domain | 732 - 769 | IPR000742-2 |
| domain | CUB domain | 348 - 460 | IPR000859-1 |
| domain | CUB domain | 461 - 573 | IPR000859-2 |
| domain | CUB domain | 617 - 729 | IPR000859-3 |
| domain | CUB domain | 773 - 885 | IPR000859-4 |
| domain | CUB domain | 886 - 1002 | IPR000859-5 |
| domain | Peptidase M12A | 146 - 346 | IPR001506 |
| domain | EGF-like calcium-binding domain | 573 - 614 | IPR001881-1 |
| domain | EGF-like calcium-binding domain | 729 - 769 | IPR001881-2 |
| domain | Peptidase, metallopeptidase | 152 - 294 | IPR006026 |
| conserved_site | EGF-like calcium-binding, conserved site | 573 - 598 | IPR018097-1 |
| conserved_site | EGF-like calcium-binding, conserved site | 729 - 753 | IPR018097-2 |
| domain | Tolloid/BMP1 peptidase domain | 147 - 346 | IPR034036 |
Functions
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| cargo receptor activity | Binding specifically to a substance (cargo) to deliver it to a transport vesicle. Cargo receptors span a membrane (either the plasma membrane or a vesicle membrane), binding simultaneously to cargo molecules and coat adaptors, to efficiently recruit soluble proteins to nascent vesicles. |
| hyaluronic acid binding | Binding to hyaluronic acid, a polymer composed of repeating dimeric units of glucuronic acid and N-acetyl glucosamine. |
| transmembrane signaling receptor activity | Combining with an extracellular or intracellular signal and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity or state as part of signal transduction. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| cell adhesion | The attachment of a cell, either to another cell or to an underlying substrate such as the extracellular matrix, via cell adhesion molecules. |
| hyaluronan catabolic process | The chemical reactions and pathways resulting in the breakdown of hyaluronan, the naturally occurring anionic form of hyaluronic acid, any member of a group of glycosaminoglycans, the repeat units of which consist of beta-1,4 linked D-glucuronyl-beta-(1,3)-N-acetyl-D-glucosamine. |
| positive regulation of cellular extravasation | Any process that activates or increases the frequency, rate, or extent of cellular extravasation. |
| receptor-mediated endocytosis | An endocytosis process in which cell surface receptors ensure specificity of transport. A specific receptor on the cell surface binds tightly to the extracellular macromolecule (the ligand) that it recognizes; the plasma-membrane region containing the receptor-ligand complex then undergoes endocytosis, forming a transport vesicle containing the receptor-ligand complex and excluding most other plasma-membrane proteins. Receptor-mediated endocytosis generally occurs via clathrin-coated pits and vesicles. |
4 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9Y5Y7 | LYVE1 | Lymphatic vessel endothelial hyaluronic acid receptor 1 | Homo sapiens (Human) | PR |
| P98066 | TNFAIP6 | Tumor necrosis factor-inducible gene 6 protein | Homo sapiens (Human) | PR |
| Q8BHC0 | Lyve1 | Lymphatic vessel endothelial hyaluronic acid receptor 1 | Mus musculus (Mouse) | PR |
| O08859 | Tnfaip6 | Tumor necrosis factor-inducible gene 6 protein | Mus musculus (Mouse) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAKFFSLGLL | LASIWTTRLL | VQGSLRSEEI | SILGPCRIMG | VTLVTKKTQP | LLNFTEAQEA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| CRLVGLTLAS | QDQVEEARKF | GFETCSYGWV | KNQFVVIPRI | ISNPKCGKSG | VGVVIWRSSL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SSRHRSYCHN | SSDIWINSCL | PEIITTDDPL | FNTETATYTT | KLMVSDSTHS | ELSTDGPDYV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TTTVAPPLAS | TSTPRKRKLI | CITEAFMDTS | AVATERESDI | QNRPAFKNEA | VGFGGVPTAL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LVLALLFFAA | AAGLAVCYVK | RYVKAFPFTN | KNQQKEMIET | KVVKEEKADD | SNPNEESKKM |
| 310 | 320 | ||||
| NKTPEEPKSP | PKTTVRCLEA | EV |