OSBPL3

Jump to navigation Jump to search
VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Oxysterol-binding protein-related protein 3 is a protein that in humans is encoded by the OSBPL3 gene.[1][2]

Function

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. Several transcript variants encoding different isoforms have been identified.[2]

Model organisms

Model organisms have been used in the study of OSBPL3 function. A conditional knockout mouse line called Osbpl3tm1a(EUCOMM)Wtsi was generated at the Wellcome Trust Sanger Institute.[3] Male and female animals underwent a standardized phenotypic screen[4] to determine the effects of deletion.[5][6][7][8] Additional screens performed: - In-depth immunological phenotyping[9]

References

  1. Ishikawa K, Nagase T, Suyama M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (Jun 1998). "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Research. 5 (3): 169–76. doi:10.1093/dnares/5.3.169. PMID 9734811.
  2. 2.0 2.1 "Entrez Gene: OSBPL3 oxysterol binding protein-like 3".
  3. Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
  4. 4.0 4.1 "International Mouse Phenotyping Consortium".
  5. 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.
  6. Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  7. 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.
  8. White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP (Jul 2013). "Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes". Cell. 154 (2): 452–64. doi:10.1016/j.cell.2013.06.022. PMC 3717207. PMID 23870131.
  9. 9.0 9.1 "Infection and Immunity Immunophenotyping (3i) Consortium".

Further reading

  • Sanger Centre, The; Washington University Genome Sequencing Cente, The (Nov 1998). "Toward a complete human genome sequence". Genome Research. 8 (11): 1097–108. doi:10.1101/gr.8.11.1097. PMID 9847074.
  • Laitinen S, Olkkonen VM, Ehnholm C, Ikonen E (Dec 1999). "Family of human oxysterol binding protein (OSBP) homologues. A novel member implicated in brain sterol metabolism". Journal of Lipid Research. 40 (12): 2204–11. PMID 10588946.
  • 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.
  • Gregorio-King CC, Collier GR, McMillan JS, Waugh CM, McLeod JL, Collier FM, Kirkland MA (Oct 2001). "ORP-3, a human oxysterol-binding protein gene differentially expressed in hematopoietic cells". Blood. 98 (7): 2279–81. doi:10.1182/blood.V98.7.2279. PMID 11568019.
  • 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.
  • Collier FM, Gregorio-King CC, Apostolopoulos J, Walder K, Kirkland MA (Jan 2003). "ORP3 splice variants and their expression in human tissues and hematopoietic cells". DNA and Cell Biology. 22 (1): 1–9. doi:10.1089/104454903321112442. PMID 12590732.
  • Lehto M, Tienari J, Lehtonen S, Lehtonen E, Olkkonen VM (Jan 2004). "Subfamily III of mammalian oxysterol-binding protein (OSBP) homologues: the expression and intracellular localization of ORP3, ORP6, and ORP7". Cell and Tissue Research. 315 (1): 39–57. doi:10.1007/s00441-003-0817-y. PMID 14593528.
  • Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T (Aug 2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Current Biology. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
  • Benzinger A, Muster N, Koch HB, Yates JR, Hermeking H (Jun 2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer". Molecular & Cellular Proteomics. 4 (6): 785–95. doi:10.1074/mcp.M500021-MCP200. PMID 15778465.
  • Lehto M, Hynynen R, Karjalainen K, Kuismanen E, Hyvärinen K, Olkkonen VM (Nov 2005). "Targeting of OSBP-related protein 3 (ORP3) to endoplasmic reticulum and plasma membrane is controlled by multiple determinants". Experimental Cell Research. 310 (2): 445–62. doi:10.1016/j.yexcr.2005.08.003. PMID 16143324.