OSBPL2
Sign in to saveAlso known as ORP-2, ORP2, DFNA67, DNFA67, oxysterol binding protein like 2
Oxysterol-binding protein-related protein 2 is a protein that in humans is encoded by the OSBPL2 gene.
Gene data
OSBPL2- Name
- oxysterol binding protein like 2
- Type
- protein-coding
- Position
- 62,231,922–62,296,213 (+)
- Aliases
- DFNA67, DIDA, DNFA67, ORP-2, ORP2
- Ensembl
- ENSG00000130703
- RefSeq RNA
- NM_001001691.1, NM_001278649.3, NM_001363878.2, NM_014835.5, NM_144498.4
- RefSeq protein
- NP_001265578.1, NP_001350807.1, NP_055650.1, NP_653081.1
This gene encodes a member of the oxysterol-binding protein (OSBP) family, a group of intracellular lipid receptors. Most members contain an N-terminal pleckstrin homology domain and a highly conserved C-terminal OSBP-like sterol-binding domain, although the encoded protein contains only the sterol-binding domain. In vitro studies have shown that the encoded protein can bind strongly to phosphatic acid and weakly to phosphatidylinositol 3-phosphate, but cannot bind to 25-hydroxycholesterol. The protein associates with the Golgi apparatus. Transcript variants encoding different isoforms have been described. [provided by RefSeq, Sep 2014].
Gene Ontology
Biological process
Molecular function
Pathways
via MyGene.info
Wikidata facts
- Image
- 5zm8.jpg
Show 5 more facts
- HomoloGene ID
- 77324
- exact match
- identifiers.org/ncbigene/9885
- genomic start
- 60813580
- genomic end
- 60871268
- cytogenetic location
- 20q13.33
Sources (3)
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- References
- Further reading
Oxysterol-binding protein-related protein 2 is a protein that in humans is encoded by the OSBPL2 gene.
This gene encodes a member of the oxysterol-binding protein (OSBP) family, a group of intracellular lipid receptors. Most members contain an N-terminal pleckstrin homology domain and a highly conserved C-terminal OSBP-like sterol-binding domain, although some members contain only the sterol-binding domain. This encoded protein contains only the sterol-binding domain. In vitro studies have shown that the encoded protein can bind strongly to phosphatic acid and weakly to phosphatidylinositol 3-phosphate, but cannot bind to 25-hydroxycholesterol. The protein associates with the Golgi apparatus. Transcript variants encoding different isoforms have been described.