Oxysterol-binding protein 2 (OSBP2)
The protein contains 916 amino acids for an estimated molecular weight of 101266 Da.
Binds 7-ketocholesterol. (updated: April 1, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology.
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| Variant | Description |
|---|---|
| dbSNP:rs34240867 |
No binding partner found
The reference OMIM entry for this protein is 606729
Oxysterol-binding protein 2; osbp2
Osbp-related protein 4; orp4
Kiaa1664
DESCRIPTION
Oxysterols accumulate in tissues and exert pharmacologic effects on cellular sterol biosynthesis and uptake. They are oxidized byproducts of cholesterol that cause cytotoxic effects on a variety of cells. Oxysterol-binding proteins such as OSBP1 (167040) and OSBP2 may mediate oxysterol cytotoxicity in tissues.CLONING
By database searching for sequences similar to OSBP1, followed by probing a retina library and 5-prime and 3-prime RACE, Moreira et al. (2001) obtained a cDNA encoding OSPBP2. Sequence analysis predicted that the 878-amino acid protein, which is 63% identical to OSBP1, contains an N-terminal pleckstrin homology domain, an oxysterol-binding domain, and a conserved C terminus. By Northern blot analysis, Moreira et al. (2001) detected expression of a predominant 2.7-kb OSBP2 transcript mainly in retina, pineal gland, and fetal liver, and a 4.2-kb transcript that was most abundant in testis and cerebellum. In contrast, OSBP1 was more widely expressed. RT-PCR analysis detected expression of an OSBP2 splice variant that lacks exon 12, resulting in a protein with an aberrant C terminus after the first 692 amino acids, only in retina. In monkey retina, significant expression of OSBP2 was found in neural macula and peripheral neural retina, with little or no expression in macular or peripheral pigment epithelium choroids. OSBP1, on the other hand, was expressed equivalently in all but the peripheral pigment epithelium choroid. Western blot analysis showed expression of a 90-kD OSBP2 protein associated with retinal membranes. Immunocytochemical analysis demonstrated expression of OSBP2 in monkey retinal ganglion cells distinct from those expressing OSBP1, and in retinal pigment epithelium, where the low density lipoprotein receptor (606945) is expressed. Moreira et al. (2001) concluded that OSBPs and their oxysterol ligands, which accumulate gradually with age, may play an important role in the pathogenesis of age-related ocular diseases, such as macular degeneration.GENE FUNCTION
Using binding analysis, Moreira et al. (2001) showed that OSBP2 interacts preferentially with 7-ketocholesterol.GENE STRUCTURE
By genomic sequence analysis, Moreira et al. (2001) determined that the OSBP2 gene contains 14 exons, like OSBP1, and spans 217 kb.MAPPING
By sequence analysis, Moreira et al. (2001) mapped the OSBP2 gene to chromosome 22q12. ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 606729 was added.