CPSF3

Cleavage and polyadenylation specific factor 3, 73kDa
PDB rendering based on 2i7t.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2I7T​, 2I7V​
Identifiers
Symbols	CPSF3 ; CPSF-73; CPSF73
External IDs	OMIM: 606029 MGI: 1859328 HomoloGene: 6499 GeneCards: CPSF3 Gene
Gene ontology Molecular function • RNA binding • endoribonuclease activity • protein binding • 5'-3' exonuclease activity • metal ion binding Cellular component • nucleoplasm • mRNA cleavage and polyadenylation specificity factor complex • ribonucleoprotein complex Biological process • mRNA splicing, via spliceosome • transcription from RNA polymerase II promoter • termination of RNA polymerase II transcription • mRNA polyadenylation • mRNA cleavage • histone mRNA 3'-end processing • mRNA export from nucleus • RNA splicing • gene expression • mRNA 3'-end processing • RNA phosphodiester bond hydrolysis, endonucleolytic Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	51692	54451
Ensembl	ENSG00000119203	ENSMUSG00000054309
UniProt	Q9UKF6	Q9QXK7
RefSeq (mRNA)	NM_016207	NM_018813
RefSeq (protein)	NP_057291	NP_061283
Location (UCSC)	Chr 2: 9.42 – 9.47 Mb	Chr 12: 21.29 – 21.32 Mb
PubMed search

Cleavage and polyadenylation specificity factor subunit 3 is a protein that in humans is encoded by the CPSF3 gene.^[1][2]

Model organisms

Model organisms have been used in the study of CPSF3 function. A conditional knockout mouse line called Cpsf3^{tm1b(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]

Cpsf3 knockout mouse phenotype

Characteristic	Phenotype
All data available at.[4][9]
Insulin	Normal
Homozygous viability at P14	Abnormal
Recessive lethal study	Abnormal
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
Salmonella infection	Normal
Epidermal Immune Composition	Normal
Influenza Challenge	Normal

References

1. Jenny A, Minvielle-Sebastia L, Preker PJ, Keller W (Dec 1996). "Sequence similarity between the 73-kilodalton protein of mammalian CPSF and a subunit of yeast polyadenylation factor I". Science 274 (5292): 1514–7. doi:10.1126/science.274.5292.1514. PMID 8929409.
2. "Entrez Gene: CPSF3 cleavage and polyadenylation specific factor 3, 73kDa".
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. "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, Sanger Institute Mouse Genetics Project, 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 (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. "Infection and Immunity Immunophenotyping (3i) Consortium".

Further reading

• Murthy KG, Manley JL (1995). "The 160-kD subunit of human cleavage-polyadenylation specificity factor coordinates pre-mRNA 3'-end formation.". Genes Dev. 9 (21): 2672–83. doi:10.1101/gad.9.21.2672. PMID 7590244.
• Jenny A, Hauri HP, Keller W (1994). "Characterization of cleavage and polyadenylation specificity factor and cloning of its 100-kilodalton subunit.". Mol. Cell. Biol. 14 (12): 8183–90. PMC 359357. PMID 7969155.
• 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.
• Thuresson AC, Aström J, Aström A; et al. (1994). "Multiple forms of poly(A) polymerases in human cells.". Proc. Natl. Acad. Sci. U.S.A. 91 (3): 979–83. doi:10.1073/pnas.91.3.979. PMC 521437. PMID 8302877.
• McCracken S, Fong N, Yankulov K; et al. (1997). "The C-terminal domain of RNA polymerase II couples mRNA processing to transcription.". Nature 385 (6614): 357–61. doi:10.1038/385357a0. PMID 9002523.
• 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.
• Takagaki Y, Manley JL (2000). "Complex protein interactions within the human polyadenylation machinery identify a novel component.". Mol. Cell. Biol. 20 (5): 1515–25. doi:10.1128/MCB.20.5.1515-1525.2000. PMC 85326. PMID 10669729.
• de Vries H, Rüegsegger U, Hübner W; et al. (2000). "Human pre-mRNA cleavage factor II(m) contains homologs of yeast proteins and bridges two other cleavage factors.". EMBO J. 19 (21): 5895–904. doi:10.1093/emboj/19.21.5895. PMC 305781. PMID 11060040.
• 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.
• Kaufmann I, Martin G, Friedlein A; et al. (2005). "Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements and stimulates poly(A) polymerase.". EMBO J. 23 (3): 616–26. doi:10.1038/sj.emboj.7600070. PMC 1271804. PMID 14749727.
• Calzado MA, Sancho R, Muñoz E (2004). "Human immunodeficiency virus type 1 Tat increases the expression of cleavage and polyadenylation specificity factor 73-kilodalton subunit modulating cellular and viral expression.". J. Virol. 78 (13): 6846–54. doi:10.1128/JVI.78.13.6846-6854.2004. PMC 421638. PMID 15194760.
• Jin J, Smith FD, Stark C; et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization.". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
• 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.
• Mandel CR, Kaneko S, Zhang H; et al. (2007). "Polyadenylation factor CPSF-73 is the pre-mRNA 3'-end-processing endonuclease.". Nature 444 (7121): 953–6. doi:10.1038/nature05363. PMID 17128255.
• de la Vega L, Sánchez-Duffhues G, Fresno M; et al. (2007). "The 73 kDa subunit of the CPSF complex binds to the HIV-1 LTR promoter and functions as a negative regulatory factor that is inhibited by the HIV-1 Tat protein.". J. Mol. Biol. 372 (2): 317–30. doi:10.1016/j.jmb.2007.06.075. PMID 17669424.