SNX5

SNX5
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1SYS
Identifiers
Aliases	SNX5
External IDs	MGI: 1916428 HomoloGene: 40944 GeneCards: SNX5
Gene ontology Molecular function • dynactin binding • protein binding • phosphatidylinositol binding • protein heterodimerization activity • lipid binding • cadherin binding involved in cell-cell adhesion Cellular component • cytoplasm • endosome • cell projection • early endosome membrane • retromer, tubulation complex • membrane • ruffle • extrinsic component of cytoplasmic side of plasma membrane • plasma membrane • extrinsic component of endosome membrane • tubular endosome • retromer complex • early endosome • phagocytic cup • cytoplasmic vesicle membrane • macropinocytic cup • cytoplasmic vesicle • cell-cell adherens junction • cytosol • intracellular Biological process • endocytosis • vesicle organization • retrograde transport, endosome to Golgi • transport • protein transport • pinocytosis • intracellular protein transport • regulation of macroautophagy • cell-cell adhesion Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	27131	69178
Ensembl	ENSG00000089006	ENSMUSG00000027423
UniProt	Q9Y5X3 Q5QPE4	Q9D8U8
RefSeq (mRNA)	NM_152227 NM_001282454 NM_014426	NM_001199188 NM_024225
RefSeq (protein)	NP_055241.1 NP_689413.1	NP_001186117.1 NP_077187.1
Location (UCSC)	Chr 20: 17.94 – 17.97 Mb	Chr 2: 144.25 – 144.27 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

View/Edit Mouse

Sorting nexin-5 is a protein that in humans is encoded by the SNX5 gene.^[3][4][5]

This gene encodes a member of the sorting nexin family. Members of this family contain a phox (PX) domain, which is a phosphoinositide binding domain, and are involved in intracellular trafficking. This protein is a component of the mammalian retromer complex,^[4] which facilitates cargo retrieval from endosomes to the trans-Golgi network. It has also been shown to bind to the Fanconi anemia, complementation group A protein. This gene results in two transcript variants encoding the same protein.^[5]

Model organisms

Snx5 knockout mouse phenotype

Characteristic	Phenotype
Homozygote viability	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
Plasma immunoglobulins	Normal
Haematology	Normal[6]
Peripheral blood lymphocytes	Normal
Micronucleus test	Normal
Heart weight	Normal
Skin Histopathology	Normal
Brain histopathology	Normal
Eye Histopathology	Normal
Salmonella infection	Normal[7]
Citrobacter infection	Normal[8]
All tests and analysis from[9][10]

Model organisms have been used in the study of SNX5 function. A conditional knockout mouse line, called Snx5^{tm1a(KOMP)Wtsi[11][12]} 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.^[13][14][15] Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.^[9][16] Twenty five tests were carried out on homozygous mutant adult mice, however no significant abnormalities were observed.^[9]

Interactions

SNX5 has been shown to interact with FANCA.^[3]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Otsuki T; Kajigaya S; Ozawa K; Liu JM (Jan 2000). "SNX5, a new member of the sorting nexin family, binds to the Fanconi anemia complementation group A protein". Biochem Biophys Res Commun. 265 (3): 630–5. doi:10.1006/bbrc.1999.1731. PMID 10600472.
4. Wassmer T; Attar N; Bujny MV; Oakley J; Traer CJ; Cullen PJ (Dec 2006). "A loss-of-function screen reveals SNX5 and SNX6 as potential components of the mammalian retromer". J Cell Sci. 120 (Pt 1): 45–54. doi:10.1242/jcs.03302. PMID 17148574.
5. "Entrez Gene: SNX5 sorting nexin 5".
6. "Haematology data for Snx5". Wellcome Trust Sanger Institute.
7. "Salmonella infection data for Snx5". Wellcome Trust Sanger Institute.
8. "Citrobacter infection data for Snx5". Wellcome Trust Sanger Institute.
9. 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.
10. Mouse Resources Portal, Wellcome Trust Sanger Institute.
11. "International Knockout Mouse Consortium".
12. "Mouse Genome Informatics".
13. Skarnes, W. C.; Rosen, B.; West, A. P.; Koutsourakis, M.; Bushell, W.; Iyer, V.; Mujica, A. O.; Thomas, M.; Harrow, J.; Cox, T.; Jackson, D.; Severin, J.; Biggs, P.; Fu, J.; Nefedov, M.; De Jong, P. J.; Stewart, A. F.; Bradley, A. (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
14. Dolgin E (June 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
15. Collins FS; Rossant J; Wurst W (January 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
16. van der Weyden L; White JK; Adams DJ; Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism.". Genome Biol. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.

Further reading

• Maruyama K; Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Teasdale RD, Loci D, Houghton F, et al. (2001). "A large family of endosome-localized proteins related to sorting nexin 1". Biochem. J. 358 (Pt 1): 7–16. doi:10.1042/0264-6021:3580007. PMC 1222026. PMID 11485546.
• Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Towler MC, Gleeson PA, Hoshino S, et al. (2005). "Clathrin Isoform CHC22, a Component of Neuromuscular and Myotendinous Junctions, Binds Sorting Nexin 5 and Has Increased Expression during Myogenesis and Muscle Regeneration". Mol. Biol. Cell. 15 (7): 3181–95. doi:10.1091/mbc.E04-03-0249. PMC 452575. PMID 15133132.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Merino-Trigo A, Kerr MC, Houghton F, et al. (2005). "Sorting nexin 5 is localized to a subdomain of the early endosomes and is recruited to the plasma membrane following EGF stimulation". J. Cell. Sci. 117 (Pt 26): 6413–24. doi:10.1242/jcs.01561. PMID 15561769.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.