RPN2

RPN2
Identifiers
Aliases	RPN2, RIBIIR, RPN-II, RPNII, SWP1, ribophorin II
External IDs	MGI: 98085 HomoloGene: 2214 GeneCards: RPN2
Gene ontology Molecular function • transferase activity • dolichyl-diphosphooligosaccharide-protein glycotransferase activity • transferase activity, transferring glycosyl groups • ribosome binding • protein binding Cellular component • integral component of membrane • rough endoplasmic reticulum • autophagosome membrane • nucleus • membrane • endoplasmic reticulum membrane • oligosaccharyltransferase complex • endoplasmic reticulum Biological process • aging • protein N-linked glycosylation via asparagine • protein glycosylation • cellular protein modification process • response to drug • protein N-linked glycosylation Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	6185	20014
Ensembl	ENSG00000118705	ENSMUSG00000027642
UniProt	P04844	Q9DBG6
RefSeq (mRNA)	NM_001135771 NM_002951 NM_001324299 NM_001324301 NM_001324302 NM_001324303 NM_001324304 NM_001324305 NM_001324306	NM_019642
RefSeq (protein)	NP_001129243.1 NP_002942.2 NP_001311228.1 NP_001311230.1 NP_001311231.1 NP_001311232.1 NP_001311233.1 NP_001311234.1 NP_001311235.1	NP_062616.2
Location (UCSC)	Chr 20: 37.18 – 37.24 Mb	Chr 2: 157.28 – 157.33 Mb
PubMed search	[1]	[2]
Wikidata

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Dolichyl-diphosphooligosaccharide—protein glycosyltransferase subunit 2 is an enzyme that in humans is encoded by the RPN2 gene.^[3] This gene encodes a type I integral ribophorin membrane protein found only in the rough endoplasmic reticulum. The encoded protein is part of an N-oligosaccharyl transferase complex that links high mannose oligosaccharides to asparagine residues found in the Asn-X-Ser/Thr consensus motif of nascent polypeptide chains. This protein is similar in sequence to the yeast oligosaccharyl transferase subunit SWP1.^[3]

Model organisms

Rpn2 knockout mouse phenotype

Characteristic	Phenotype
Homozygote viability	Abnormal
Recessive lethal study	Abnormal
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
Plasma immunoglobulins	Normal
Haematology	Normal
Peripheral blood lymphocytes	Normal
Micronucleus test	Normal
Heart weight	Normal
Brain 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 RPN2 function. A conditional knockout mouse line, called Rpn2^{tm1a(EUCOMM)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.^[10][11][12]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.^[6][13] Twenty six tests were carried out on mutant mice and two significant abnormalities were observed.^[6] No homozygous mutant embryos were identified during gestation, and therefore none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice; no additional significant abnormalities were observed in these animals.^[6]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. "Entrez Gene: RPN2 ribophorin II".
4. "Salmonella infection data for Rpn2". Wellcome Trust Sanger Institute.
5. "Citrobacter infection data for Rpn2". Wellcome Trust Sanger Institute.
6. 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.
7. Mouse Resources Portal, Wellcome Trust Sanger Institute.
8. "International Knockout Mouse Consortium".
9. "Mouse Genome Informatics".
10. 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.
11. Dolgin E (2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
12. Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
13. 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

• Stoffel M, Xiang K, Bell GI (1993). "Dinucleotide repeat polymorphism at the human ribophorin II locus (RPN2) on chromosome 20q". Hum. Mol. Genet. 1 (8): 656. doi:10.1093/hmg/1.8.656. PMID 1301181.
• Löffler C, Rao VV, Hansmann I (1991). "Mapping of the ribophorin II (RPN II) gene to human chromosome 20q12-q13.1 by in-situ hybridization". Hum. Genet. 87 (2): 221–2. doi:10.1007/BF00204188. PMID 2066112.
• Crimaudo C, Hortsch M, Gausepohl H, Meyer DI (1987). "Human ribophorins I and II: the primary structure and membrane topology of two highly conserved rough endoplasmic reticulum-specific glycoproteins". EMBO J. 6 (1): 75–82. PMC 553359. PMID 3034581.
• Kumar V, Heinemann FS, Ozols J (1998). "Interleukin-2 induces N-glycosylation in T-cells: characterization of human lymphocyte oligosaccharyltransferase". Biochem. Biophys. Res. Commun. 247 (2): 524–9. doi:10.1006/bbrc.1998.8780. PMID 9642163.
• Fu J, Kreibich G (2000). "Retention of subunits of the oligosaccharyltransferase complex in the endoplasmic reticulum". J. Biol. Chem. 275 (6): 3984–90. doi:10.1074/jbc.275.6.3984. PMID 10660554.
• 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.
• Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
• Kelleher DJ, Karaoglu D, Mandon EC, Gilmore R (2003). "Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties". Mol. Cell. 12 (1): 101–11. doi:10.1016/S1097-2765(03)00243-0. PMID 12887896.
• 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.
• 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.
• Shibatani T, David LL, McCormack AL, et al. (2005). "Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits". Biochemistry. 44 (16): 5982–92. doi:10.1021/bi047328f. PMID 15835887.
• Tu LC, Yan X, Hood L, Lin B (2007). "Proteomics analysis of the interactome of N-myc downstream regulated gene 1 and its interactions with the androgen response program in prostate cancer cells". Mol. Cell Proteomics. 6 (4): 575–88. doi:10.1074/mcp.M600249-MCP200. PMID 17220478.
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.