Basic Information:
| Symbol | OSBPL1A |
| Synonyms | ORP1; OSBP8; OSBPL1; OSBPL1B |
| Protein Name | Oxysterol-binding protein-related protein 1 (ORP-1) (OSBP-related protein 1) |
| Species | Human |
| Entrez ID | 114876 |
| Uniprot ID | Q9BXW6 |
| Membrane Contact Site |
ER-Endosome; Endosome-ER
|
| Location (from literature) | Endosome |
| Cell line/Tissue | MelJuSo cells; HeLa cells; HEK293 cells; HEK293T cells |
| Experimental Method | Low throughput experimental methods |
| Protein Sequence | |
| More related results |
Complex Information:
| Complex ID | Subunit of complex | Subcellular location | Species | More |
| CMCS00004 | VAPA; OSBPL1A; sterol; PI(4)P; NPC1 | ER-Endosome; Endosome-ER | Human | more | CMCS00011 | VAPA; VAPB; OSBPL1A | ER-Endosome; Endosome-ER | Human | more | CMCS00015 | MOSPD2; OSBPL1A | ER-Endosome; Endosome-ER | Human | more | CMCS00027 | VAPB; VAPA; OSBPL1A; RAB7A; RILP | ER-Endosome; Endosome-ER | Human | more |
Expression Overview of OSBPL1A:
Homology Information of OSBPL1A:
| Uniprot ID | Q9BXW6 |
| EggNOG | KOG2209 |
| HOGENOM | CLU_007105_5_1_1 |
| OrthoDB | 960at2759 |
| TreeFam | TF320922 |
| GeneTree | ENSGT00940000155295 |
References:
| Pubmed ID | 19564404 |
| DOI | 10.1083/jcb.200811005 |
| Description | ORP1L conformation induces the formation of endoplasmic reticulum (ER)-LE membrane contact sites. |
| Description of experimental evidence | The protein was validated by microscopy, FLIM, Immuno-EM and filipin stainings in MelJuSo cells, and these data explain how the ER and cholesterol control the association of LEs with motor proteins and their positioning in cells. |
| More related results |
| Pubmed ID | 28564600 |
| DOI | 10.1016/j.celrep.2017.05.028 |
| Description | Cholesterol delivery to the ER required the sterol-, phosphatidylinositol 4-phosphate-, and vesicle-associated membrane protein-associated protein (VAP)-binding activities of ORP1L, as well as NPC1 expression. |
| Description of experimental evidence | The protein was validated by PCR analysis, immunoblotting, immunoprecipitation, fluorescence and electron microscopy in HeLa cells and HEK293 cells. |
| More related results |
| Pubmed ID | 29858488 |
| DOI | 10.15252/embr.201745453 |
| Description | Consequently, MOSPD2 and these organelle‐bound proteins mediate the formation of contact sites between the ER and endosomes, mitochondria, or Golgi.; ll these proteins, by binding VAP proteins, are known to build contact sites between the ER and endosomes (STARD3, STARD3NL, ORP1L), mitochondria (PTPIP51), and Golgi (STARD11). |
| Description of experimental evidence | The protein was validated by immunofluorescence, colocalization analysis, SDS–PAGE, western blot, coomassie blue staining, pull‐down assays, GFP‐Trap, mass spectrometry analysis, electron microscopy and immunoprecipitation in HeLa cells and HEK293T cells. |
| More related results |
| Pubmed ID | 27270042 |
| DOI | 10.1016/j.devcel.2016.05.005 |
| Description | This sterol traffic depends on interaction between ER-localized VAP and endosomal oxysterol-binding protein ORP1L, and is required for the formation of ILVs within the MVB and thus for the spatial regulation of EGFR signaling. |
| Description of experimental evidence | The protein was validated by electron microscopy, florescence Imaging, western blotting, immunoprecipitation, and quantitative RT-PCR in HeLa cells, which has important role in the sterol traffic. |
| More related results |
| Pubmed ID | 36136097 |
| DOI | 10.1083/jcb.202112032 |
| Description | Dynamic endoplasmic reticulum (ER)-late endosome (LE) membrane contact sites (MCS) through ORP1L have the distinct capacity to modulate this process by affecting LE motility, maturation state, and small GTPase association. |
| Description of experimental evidence | The protein was validated by RT-PCR, light microscopy, electron microscopy/CLEM and western blotting in HeLa cells, which has a stimulatory effect on MVB/PM fusion activity. |
| More related results |