OSBPL9
| OSBPL9 | |||||||||||||||||
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| Identifiers | |||||||||||||||||
| Aliases | OSBPL9, ORP-9, ORP9, oxysterol binding protein like 9 | ||||||||||||||||
| External IDs | MGI: 1923784 HomoloGene: 69380 GeneCards: OSBPL9 | ||||||||||||||||
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| Orthologs | |||||||||||||||||
| Species | Human | Mouse | |||||||||||||||
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| Ensembl | |||||||||||||||||
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| RefSeq (mRNA) |
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| RefSeq (protein) |
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| Location (UCSC) | Chr 1: 51.58 – 51.8 Mb | Chr 4: 109.06 – 109.2 Mb | |||||||||||||||
| PubMed search | [1] | [2] | |||||||||||||||
| Wikidata | |||||||||||||||||
| View/Edit Human | View/Edit Mouse |
Oxysterol binding protein-like 9 is a protein that in humans is encoded by the OSBPL9 gene.[3]
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 family member functions as a cholesterol transfer protein that regulates Golgi structure and function. Multiple transcript variants, most of which encode distinct isoforms, have been identified. Related pseudogenes have been identified on chromosomes 3, 11 and 12.[3]
Model organisms
| Characteristic | Phenotype |
|---|---|
| Homozygote viability | Normal |
| Fertility | Normal |
| Body weight | Normal |
| Anxiety | Normal |
| Neurological assessment | Normal |
| Grip strength | Normal |
| Hot plate | Normal |
| Dysmorphology | Normal |
| Indirect calorimetry | Normal |
| Glucose tolerance test | Normal |
| Auditory brainstem response | Normal |
| DEXA | Normal |
| Radiography | Normal |
| Body temperature | Normal |
| Eye morphology | Normal |
| Clinical chemistry | Normal |
| Haematology | Normal |
| Peripheral blood lymphocytes | Normal |
| Micronucleus test | Normal |
| Heart weight | Normal |
| Skin Histopathology | Normal |
| Eye Histopathology | Normal |
| Salmonella infection | Normal[4] |
| Citrobacter infection | Normal[5] |
| All tests and analysis from[6][7] |
Model organisms have been used in the study of OSBPL9 function. A conditional knockout mouse line, called Osbpl9tm1a(KOMP)Wtsi[8][9] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists — at the Wellcome Trust Sanger Institute.[10][11][12]
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[6][13] Twenty four tests were carried out on homozygous mutant adult mice, however no significant abnormalities were observed.[6]
References
- ↑ "Human PubMed Reference:".
- ↑ "Mouse PubMed Reference:".
- 1 2 "Entrez Gene: oxysterol binding protein-like 9". Retrieved 2011-08-30.
- ↑ "Salmonella infection data for Osbpl9". Wellcome Trust Sanger Institute.
- ↑ "Citrobacter infection data for Osbpl9". Wellcome Trust Sanger Institute.
- 1 2 3 Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88 (S248). doi:10.1111/j.1755-3768.2010.4142.x.
- ↑ Mouse Resources Portal, Wellcome Trust Sanger Institute.
- ↑ "International Knockout Mouse Consortium".
- ↑ "Mouse Genome Informatics".
- ↑ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410
. PMID 21677750. - ↑ Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
- ↑ Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
- ↑ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biology. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
Further reading
- Ngo M, Ridgway ND (Mar 2009). "Oxysterol binding protein-related Protein 9 (ORP9) is a cholesterol transfer protein that regulates Golgi structure and function". Molecular Biology of the Cell. 20 (5): 1388–99. doi:10.1091/mbc.E08-09-0905. PMC 2649274. PMID 19129476.
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S (Jun 2009). "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach". Analytical Chemistry. 81 (11): 4493–501. doi:10.1021/ac9004309. PMID 19413330.
- Perttilä J, Merikanto K, Naukkarinen J, Surakka I, Martin NW, Tanhuanpää K, Grimard V, Taskinen MR, Thiele C, Salomaa V, Jula A, Perola M, Virtanen I, Peltonen L, Olkkonen VM (Aug 2009). "OSBPL10, a novel candidate gene for high triglyceride trait in dyslipidemic Finnish subjects, regulates cellular lipid metabolism". Journal of Molecular Medicine. 87 (8): 825–35. doi:10.1007/s00109-009-0490-z. PMC 2707950. PMID 19554302.
- Chen T, Huang Z, Wang L, Wang Y, Wu F, Meng S, Wang C (Jul 2009). "MicroRNA-125a-5p partly regulates the inflammatory response, lipid uptake, and ORP9 expression in oxLDL-stimulated monocyte/macrophages". Cardiovascular Research. 83 (1): 131–9. doi:10.1093/cvr/cvp121. PMID 19377067.
- Wyles JP, Ridgway ND (Jul 2004). "VAMP-associated protein-A regulates partitioning of oxysterol-binding protein-related protein-9 between the endoplasmic reticulum and Golgi apparatus". Experimental Cell Research. 297 (2): 533–47. doi:10.1016/j.yexcr.2004.03.052. PMID 15212954.
- Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (Jan 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
- Sowa ME, Bennett EJ, Gygi SP, Harper JW (Jul 2009). "Defining the human deubiquitinating enzyme interaction landscape". Cell. 138 (2): 389–403. doi:10.1016/j.cell.2009.04.042. PMC 2716422. PMID 19615732.
- Talmud PJ, Drenos F, Shah S, Shah T, Palmen J, Verzilli C, Gaunt TR, Pallas J, Lovering R, Li K, Casas JP, Sofat R, Kumari M, Rodriguez S, Johnson T, Newhouse SJ, Dominiczak A, Samani NJ, Caulfield M, Sever P, Stanton A, Shields DC, Padmanabhan S, Melander O, Hastie C, Delles C, Ebrahim S, Marmot MG, Smith GD, Lawlor DA, Munroe PB, Day IN, Kivimaki M, Whittaker J, Humphries SE, Hingorani AD (Nov 2009). "Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip". American Journal of Human Genetics. 85 (5): 628–42. doi:10.1016/j.ajhg.2009.10.014. PMC 2775832. PMID 19913121.
- Lessmann E, Ngo M, Leitges M, Minguet S, Ridgway ND, Huber M (Feb 2007). "Oxysterol-binding protein-related protein (ORP) 9 is a PDK-2 substrate and regulates Akt phosphorylation". Cellular Signalling. 19 (2): 384–92. doi:10.1016/j.cellsig.2006.07.009. PMID 16962287.
- Jaworski CJ, Moreira E, Li A, Lee R, Rodriguez IR (Dec 2001). "A family of 12 human genes containing oxysterol-binding domains". Genomics. 78 (3): 185–96. doi:10.1006/geno.2001.6663. PMID 11735225.
- Lehto M, Laitinen S, Chinetti G, Johansson M, Ehnholm C, Staels B, Ikonen E, Olkkonen VM (Aug 2001). "The OSBP-related protein family in humans". Journal of Lipid Research. 42 (8): 1203–13. PMID 11483621.
- Zhou Y, Li S, Mäyränpää MI, Zhong W, Bäck N, Yan D, Olkkonen VM (Nov 2010). "OSBP-related protein 11 (ORP11) dimerizes with ORP9 and localizes at the Golgi-late endosome interface". Experimental Cell Research. 316 (19): 3304–16. doi:10.1016/j.yexcr.2010.06.008. PMID 20599956.
- Bailey SD, Xie C, Do R, Montpetit A, Diaz R, Mohan V, Keavney B, Yusuf S, Gerstein HC, Engert JC, Anand S (Oct 2010). "Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study". Diabetes Care. 33 (10): 2250–3. doi:10.2337/dc10-0452. PMC 2945168. PMID 20628086.
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