Q8BX94
Gene name |
Osbpl2 |
Protein name |
Oxysterol-binding protein-related protein 2 |
Names |
ORP-2, OSBP-related protein 2 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:228983 |
EC number |
|
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
1 structures for Q8BX94
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8BX94-F1 | Predicted | AlphaFoldDB |
24 variants for Q8BX94
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388618381 | 2 | N>H | No | EVA | |
| rs3388615212 | 14 | F>L | No | EVA | |
| rs3388614380 | 14 | F>Y | No | EVA | |
| rs47839858 | 21 | I>T | No | EVA | |
| rs27694430 | 49 | E>D | No | EVA | |
| rs255592831 | 75 | S>T | No | EVA | |
| rs3388620818 | 81 | K>N | No | EVA | |
| rs27694384 | 137 | A>S | No | EVA | |
| rs3388618243 | 199 | S>Y | No | EVA | |
| rs3388615293 | 221 | L>Q | No | EVA | |
| rs3388615287 | 222 | E>V | No | EVA | |
| rs3388620827 | 231 | T>S | No | EVA | |
| rs3388610204 | 240 | H>L | No | EVA | |
| rs3388618433 | 259 | N>H | No | EVA | |
| rs27679344 | 315 | E>D | No | EVA | |
| rs3388615297 | 321 | E>K | No | EVA | |
| rs236627914 | 335 | G>S | No | EVA | |
| rs3388619928 | 343 | V>L | No | EVA | |
| rs3388619957 | 351 | V>L | No | EVA | |
| rs3392626059 | 409 | R>H | No | EVA | |
| rs3388615196 | 411 | D>G | No | EVA | |
| rs3388602846 | 433 | K>R | No | EVA | |
| rs3388615292 | 447 | E>* | No | EVA | |
| rs3388602861 | 482 | D>A | No | EVA |
No associated diseases with Q8BX94
1 regional properties for Q8BX94
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Oxysterol-binding protein, conserved site | 174 - 184 | IPR018494 |
Functions
5 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| extrinsic component of cytoplasmic side of plasma membrane | The component of a plasma membrane consisting of gene products and protein complexes that are loosely bound to its cytoplasmic surface, but not integrated into the hydrophobic region. |
| intracellular membrane-bounded organelle | Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane. |
| lipid droplet | An intracellular non-membrane-bounded organelle comprising a matrix of coalesced lipids surrounded by a phospholipid monolayer. May include associated proteins. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| cholesterol binding | Binding to cholesterol (cholest-5-en-3-beta-ol); the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones. |
| cholesterol transfer activity | Removes cholesterol from a membrane or a monolayer lipid particle, transports it through the aqueous phase while protected in a hydrophobic pocket, and brings it to an acceptor membrane or lipid particle. |
| phosphatidylinositol transfer activity | Removes phosphatidylinositol from a membrane or a monolayer lipid particle, transports it through the aqueous phase while protected in a hydrophobic pocket, and brings it to an acceptor membrane or lipid particle. |
| 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. |
| sterol binding | Binding to a sterol, a steroid containing a hydroxy group in the 3 position, closely related to cholestan-3-ol. |
| sterol transporter activity | Enables the directed movement of sterols into, out of or within a cell, or between cells. Sterol are steroids with one or more hydroxyl groups and a hydrocarbon side-chain in the molecule. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| cholesterol transport | The directed movement of cholesterol, cholest-5-en-3-beta-ol, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
| intracellular cholesterol transport | The directed movement of cholesterol, cholest-5-en-3-beta-ol, within cells. |
| phospholipid transport | The directed movement of phospholipids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Phospholipids are any lipids containing phosphoric acid as a mono- or diester. |
| plasma membrane organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the plasma membrane. |
| protein homotetramerization | The formation of a protein homotetramer, a macromolecular structure consisting of four noncovalently associated identical subunits. |
4 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9H1P3 | OSBPL2 | Oxysterol-binding protein-related protein 2 | Homo sapiens (Human) | PR |
| Q5QNQ6 | Osbp2 | Oxysterol-binding protein 2 | Mus musculus (Mouse) | PR |
| B9EJ86 | Osbpl8 | Oxysterol-binding protein-related protein 8 | Mus musculus (Mouse) | PR |
| Q3B7Z2 | Osbp | Oxysterol-binding protein 1 | Mus musculus (Mouse) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNGEEEFFDA | VTGFDSDNSS | IGEFSEANKI | SGMIDLDTSK | STRSGKNGEK | PQQENGIQKH |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RTALPAPMFT | RSDFSVWSIL | KKCIGLELSK | ITMPIAFNEP | LSFLQRITEY | MEHVYLIHKA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SSQSQPLERM | QSVAAFAVSA | VASQWERTGK | PFNPLLGETY | ELIREDLGFR | FISEQVSHHP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PISAFYSEGL | NQDFRFHGSI | YPKLKFWGKS | VEAEPRGTIT | LELLKHNEAY | TWTNPTCCVH |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NVILGQLWIE | QYGIVEIVNH | RTGDKCILHF | KPCGLFGKEL | HRVEGYIQDK | NRKKLFIMYG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KWTECLWGID | PASYESFKKQ | EKRGDQARKA | KMDDGPEKAN | SDVPGDVADD | VPVAQETVQV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IPGSKLLWRI | NSRPPNSAQM | YNFTSFTVSL | NELESGMEKT | LPPTDCRLRP | DIRGMENGNM |
| 430 | 440 | 450 | 460 | 470 | 480 |
| DLASQEKERL | EEKQREARKE | RAKEDAEWRT | RWFSPGNNPY | TGAPDWLYAG | HYFERNFSDC |
| PDIY |