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APOBEC3C

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APOBEC3C
Available structures
PDBHuman UniProt search: PDBe RCSB
Identifiers
AliasesAPOBEC3C, A3C, APOBEC1L, ARDC2, ARDC4, ARP5, PBI, bK150C2.3, apolipoprotein B mRNA editing enzyme catalytic subunit 3C
External IDsOMIM: 607750; HomoloGene: 129856; GeneCards: APOBEC3C; OMA:APOBEC3C - orthologs
Orthologs
SpeciesHumanMouse
Entrez

27350

n/a

Ensembl

ENSG00000244509

n/a

UniProt

Q9NRW3

n/a

RefSeq (mRNA)

NM_014508

n/a

RefSeq (protein)

NP_055323

n/a

Location (UCSC)Chr 22: 39.01 – 39.02 Mbn/a
PubMed search[2]n/a
Wikidata
View/Edit Human

DNA dC->dU-editing enzyme APOBEC-3C is a protein that in humans is encoded by the APOBEC3C gene.[3][4]

A3C belong to the A3 family of cytidine deaminases that act as restriction factors against diverse retroviruses. A3C was reported to inhibit simian immunodeficiency deficiency virus potently rather than HIV-1, in absence of viral infectivity factor, Vif.[5] Enhancing A3C's catalytic activity had only a marginal effect on HIV-1 replication (in absence of Vif), the counteractive viral mechanism is unclear.[6] A3C was also shown to inhibit other viruses.[7][8][9][10][11]

Function

This gene is a member of the cytidine deaminase gene family. It is one of seven related genes or pseudogenes found in a cluster thought to result from gene duplication, on chromosome 22. Members of the cluster encode proteins that are structurally and functionally related to the C to U RNA-editing cytidine deaminase APOBEC1. Conversely, A3 proteins enzymatically convert cytidine to uridine present in the single stranded DNA.[12][13][14][15][16] Two residues in loop 1 of A3C were demonstrated to determine its antiviral activity against HIV-1.[17]

Structure

The crystal structure of A3C suggests a putative HIV-1 vif binding region.[18][19] A3C was found to inhibit LINE-1 elements by directly interacting with ORF1p proteins, in a deaminase-independent manner.[20]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000244509 – Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ Jarmuz A, Chester A, Bayliss J, Gisbourne J, Dunham I, Scott J, Navaratnam N (March 2002). "An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22". Genomics. 79 (3): 285–96. doi:10.1006/geno.2002.6718. PMID 11863358.
  4. ^ "Entrez Gene: APOBEC3C apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3C".
  5. ^ Yu Q, Chen D, König R, Mariani R, Unutmaz D, Landau NR (December 2004). "APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication". The Journal of Biological Chemistry. 279 (51): 53379–86. doi:10.1074/jbc.M408802200. PMID 15466872.
  6. ^ Jaguva Vasudevan AA, Hofmann H, Willbold D, Häussinger D, Koenig BW, Münk C (April 2017). "Enhancing the Catalytic Deamination Activity of APOBEC3C Is Insufficient to Inhibit Vif-Deficient HIV-1". Journal of Molecular Biology. 429 (8): 1171–1191. doi:10.1016/j.jmb.2017.03.015. PMID 28315663.
  7. ^ Baumert TF, Rösler C, Malim MH, von Weizsäcker F (September 2007). "Hepatitis B virus DNA is subject to extensive editing by the human deaminase APOBEC3C". Hepatology. 46 (3): 682–9. doi:10.1002/hep.21733. PMID 17625792.
  8. ^ Suspène R, Aynaud MM, Koch S, Pasdeloup D, Labetoulle M, Gaertner B, Vartanian JP, Meyerhans A, Wain-Hobson S (August 2011). "Genetic editing of herpes simplex virus 1 and Epstein-Barr herpesvirus genomes by human APOBEC3 cytidine deaminases in culture and in vivo". Journal of Virology. 85 (15): 7594–602. doi:10.1128/JVI.00290-11. PMC 3147940. PMID 21632763.
  9. ^ Köck J, Blum HE (May 2008). "Hypermutation of hepatitis B virus genomes by APOBEC3G, APOBEC3C and APOBEC3H". The Journal of General Virology. 89 (Pt 5): 1184–91. doi:10.1099/vir.0.83507-0. PMID 18420796.
  10. ^ Li D, Liu J, Kang F, Guan W, Gao X, Wang Y, Sun D (October 2011). "Core-APOBEC3C chimerical protein inhibits hepatitis B virus replication". Journal of Biochemistry. 150 (4): 371–4. doi:10.1093/jb/mvr086. PMID 21746770.
  11. ^ Ahasan MM, Wakae K, Wang Z, Kitamura K, Liu G, Koura M, Imayasu M, Sakamoto N, Hanaoka K, Nakamura M, Kyo S, Kondo S, Fujiwara H, Yoshizaki T, Mori S, Kukimoto I, Muramatsu M (February 2015). "APOBEC3A and 3C decrease human papillomavirus 16 pseudovirion infectivity". Biochemical and Biophysical Research Communications. 457 (3): 295–9. doi:10.1016/j.bbrc.2014.12.103. hdl:2297/44628. PMID 25576866.
  12. ^ Yu Q, König R, Pillai S, Chiles K, Kearney M, Palmer S, Richman D, Coffin JM, Landau NR (May 2004). "Single-strand specificity of APOBEC3G accounts for minus-strand deamination of the HIV genome". Nature Structural & Molecular Biology. 11 (5): 435–42. doi:10.1038/nsmb758. PMID 15098018.
  13. ^ Harris RS, Petersen-Mahrt SK, Neuberger MS (November 2002). "RNA editing enzyme APOBEC1 and some of its homologs can act as DNA mutators". Molecular Cell. 10 (5): 1247–53. doi:10.1016/s1097-2765(02)00742-6. PMID 12453430.
  14. ^ Harris RS, Sheehy AM, Craig HM, Malim MH, Neuberger MS (July 2003). "DNA deamination: not just a trigger for antibody diversification but also a mechanism for defense against retroviruses". Nature Immunology. 4 (7): 641–3. doi:10.1038/ni0703-641. PMID 12830140.
  15. ^ Harris RS, Bishop KN, Sheehy AM, Craig HM, Petersen-Mahrt SK, Watt IN, Neuberger MS, Malim MH (June 2003). "DNA deamination mediates innate immunity to retroviral infection". Cell. 113 (6): 803–9. doi:10.1016/s0092-8674(03)00423-9. PMID 12809610.
  16. ^ Yu Q, Chen D, König R, Mariani R, Unutmaz D, Landau NR (December 2004). "APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication". The Journal of Biological Chemistry. 279 (51): 53379–86. doi:10.1074/jbc.M408802200. PMID 15466872.
  17. ^ Ayyappan Jaguva Vasudevan, Ananda; Balakrishnan, Kannan; G. W. Gertzen, Christoph; Borvető, Fanni; Zhang, Zeli; Sangwiman, Anucha; Held, Ulrike; Küstermann, Caroline; Banerjee, Sharmistha; Schumann, Gerald G.; Häussinger, Dieter (October 2020). "Loop 1 of APOBEC3C regulates its antiviral activity against HIV-1". Journal of Molecular Biology: S0022283620305891. doi:10.1016/j.jmb.2020.10.014.
  18. ^ Kitamura S, Ode H, Nakashima M, Imahashi M, Naganawa Y, Kurosawa T, Yokomaku Y, Yamane T, Watanabe N, Suzuki A, Sugiura W, Iwatani Y (October 2012). "The APOBEC3C crystal structure and the interface for HIV-1 Vif binding". Nature Structural & Molecular Biology. 19 (10): 1005–10. doi:10.1038/nsmb.2378. PMID 23001005.
  19. ^ Zhang Z, Gu Q, Jaguva Vasudevan AA, Jeyaraj M, Schmidt S, Zielonka J, Perković M, Heckel JO, Cichutek K, Häussinger D, Smits SH, Münk C (November 2016). "Vif Proteins from Diverse Human Immunodeficiency Virus/Simian Immunodeficiency Virus Lineages Have Distinct Binding Sites in A3C". Journal of Virology. 90 (22): 10193–10208. doi:10.1128/JVI.01497-16. PMC 5105656. PMID 27581978.
  20. ^ Horn AV, Klawitter S, Held U, Berger A, Vasudevan AA, Bock A, Hofmann H, Hanschmann KM, Trösemeier JH, Flory E, Jabulowsky RA, Han JS, Löwer J, Löwer R, Münk C, Schumann GG (January 2014). "Human LINE-1 restriction by APOBEC3C is deaminase independent and mediated by an ORF1p interaction that affects LINE reverse transcriptase activity". Nucleic Acids Research. 42 (1): 396–416. doi:10.1093/nar/gkt898. PMC 3874205. PMID 24101588.

Further reading

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