OSBPL3

OSBPL3
Identifiers
Aliases	OSBPL3, ORP-3, ORP3, OSBP3, oxysterol binding protein like 3
External IDs	MGI: 1918970 HomoloGene: 49422 GeneCards: OSBPL3
Gene ontology Molecular function • cholesterol binding • protein binding • lipid binding Cellular component • perinuclear endoplasmic reticulum • cell projection • cytoplasm • endoplasmic reticulum membrane • filopodium tip • nuclear membrane • cytosol • endoplasmic reticulum • plasma membrane • nucleus • membrane Biological process • lipid transport • transport Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	26031	71720
Ensembl	ENSG00000070882	ENSMUSG00000029822
UniProt	Q9H4L5	Q9DBS9
RefSeq (mRNA)	NM_015550 NM_145320 NM_145321 NM_145322 NM_145323 NM_145324	NM_001163645 NM_027881
RefSeq (protein)	NP_056365.1 NP_663160.1 NP_663161.1 NP_663162.1	NP_001157117.1 NP_082157.2
Location (UCSC)	Chr 7: 24.8 – 24.98 Mb	Chr 6: 50.29 – 50.46 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

View/Edit Mouse

Oxysterol-binding protein-related protein 3 is a protein that in humans is encoded by the OSBPL3 gene.^[3][4]

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.^[4]

Model organisms

Model organisms have been used in the study of OSBPL3 function. A conditional knockout mouse line called Osbpl3^{tm1a(EUCOMM)Wtsi} was generated at the Wellcome Trust Sanger Institute.^[5] Male and female animals underwent a standardized phenotypic screen^[6] to determine the effects of deletion.^{[7][8][9][10]} Additional screens performed: - In-depth immunological phenotyping^[11]

Osbpl3 knockout mouse phenotype

Characteristic	Phenotype
All data available at.[6][11]{
Peripheral blood leukocytes 6 Weeks	Normal
Haematology 6 Weeks	Normal
Insulin	Normal
Homozygous viability at P14	Normal
Homozygous Fertility	Normal
Body weight	Normal
Neurological assessment	Normal
Grip strength	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Eye morphology	Normal
Clinical chemistry	Normal
Haematology 16 Weeks	Normal
Peripheral blood leukocytes 16 Weeks	Normal
Heart weight	Normal
Salmonella infection	Normal
Cytotoxic T Cell Function	Normal
Spleen Immunophenotyping	Normal
Mesenteric Lymph Node Immunophenotyping	Normal
Epidermal Immune Composition	Normal
Influenza Challenge	Normal

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. 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.
4. "Entrez Gene: OSBPL3 oxysterol binding protein-like 3".
5. 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.
6. "International Mouse Phenotyping Consortium".
7. 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.
8. Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
9. 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.
10. 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.
11. "Infection and Immunity Immunophenotyping (3i) Consortium".

Further reading

• "Toward a complete human genome sequence". Genome Research. 8 (11): 1097–108. Nov 1998. 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.