APOBEC3C

Protein-coding gene in humans
APOBEC3C
Available structures
PDBHuman UniProt search: PDBe RCSB
List of PDB id codes

3VM8, 3VOW

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
Gene location (Human)
Chromosome 22 (human)
Chr.Chromosome 22 (human)[1]
Chromosome 22 (human)
Genomic location for APOBEC3C
Genomic location for APOBEC3C
Band22q13.1Start39,014,257 bp[1]
End39,020,352 bp[1]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • white blood cell

  • granulocyte

  • monocyte

  • lymph node

  • right adrenal cortex

  • left adrenal gland

  • left adrenal cortex

  • rectum

  • stromal cell of endometrium

  • smooth muscle tissue
    n/a
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • protein binding
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
  • catalytic activity
  • zinc ion binding
  • hydrolase activity
  • metal ion binding
  • RNA binding
  • cytidine deaminase activity
Cellular component
  • nucleus
  • cytoplasm
  • P-body
Biological process
  • negative regulation of viral genome replication
  • immune system process
  • defense response to virus
  • cytidine deamination
  • innate immune response
  • viral process
  • negative regulation of transposition
  • DNA demethylation
  • cytidine to uridine editing
  • negative regulation of single stranded viral RNA replication via double stranded DNA intermediate
  • DNA cytosine deamination
Sources:Amigo / QuickGO
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. S2CID 9029300.
  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. S2CID 24306371.
  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. S2CID 5549252.
  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. 432 (23): 6200–6227. doi:10.1016/j.jmb.2020.10.014. PMID 33068636. S2CID 224318971.
  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. S2CID 7871310.
  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

  • Wedekind JE, Dance GS, Sowden MP, Smith HC (April 2003). "Messenger RNA editing in mammals: new members of the APOBEC family seeking roles in the family business". Trends in Genetics. 19 (4): 207–16. doi:10.1016/S0168-9525(03)00054-4. PMID 12683974.
  • Cullen BR (February 2006). "Role and mechanism of action of the APOBEC3 family of antiretroviral resistance factors". Journal of Virology. 80 (3): 1067–76. doi:10.1128/JVI.80.3.1067-1076.2006. PMC 1346961. PMID 16414984.
  • Vasudevan AA, Smits SH, Höppner A, Häussinger D, Koenig BW, Münk C (November 2013). "Structural features of antiviral DNA cytidine deaminases" (PDF). Biological Chemistry. 394 (11): 1357–70. doi:10.1515/hsz-2013-0165. PMID 23787464. S2CID 4151961.
  • Haché G, Mansky LM, Harris RS (2006). "Human APOBEC3 proteins, retrovirus restriction, and HIV drug resistance". AIDS Reviews. 8 (3): 148–57. PMID 17078485.
  • Madsen P, Anant S, Rasmussen HH, Gromov P, Vorum H, Dumanski JP, Tommerup N, Collins JE, Wright CL, Dunham I, MacGinnitie AJ, Davidson NO, Celis JE (August 1999). "Psoriasis upregulated phorbolin-1 shares structural but not functional similarity to the mRNA-editing protein apobec-1". The Journal of Investigative Dermatology. 113 (2): 162–9. doi:10.1046/j.1523-1747.1999.00682.x. PMID 10469298.
  • Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP (December 1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–95. Bibcode:1999Natur.402..489D. doi:10.1038/990031. PMID 10591208.
  • Mariani R, Chen D, Schröfelbauer B, Navarro F, König R, Bollman B, Münk C, Nymark-McMahon H, Landau NR (July 2003). "Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif". Cell. 114 (1): 21–31. doi:10.1016/S0092-8674(03)00515-4. PMID 12859895.
  • Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I (2005). "A genome annotation-driven approach to cloning the human ORFeome". Genome Biology. 5 (10): R84. doi:10.1186/gb-2004-5-10-r84. PMC 545604. PMID 15461802.
  • 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.
  • Langlois MA, Beale RC, Conticello SG, Neuberger MS (2005). "Mutational comparison of the single-domained APOBEC3C and double-domained APOBEC3F/G anti-retroviral cytidine deaminases provides insight into their DNA target site specificities". Nucleic Acids Research. 33 (6): 1913–23. doi:10.1093/nar/gki343. PMC 1074398. PMID 15809227.
  • Pope SN, Lee IR (February 2005). "Yeast two-hybrid identification of prostatic proteins interacting with human sex hormone-binding globulin". The Journal of Steroid Biochemistry and Molecular Biology. 94 (1–3): 203–8. doi:10.1016/j.jsbmb.2005.01.007. PMID 15862967. S2CID 9746088.
  • Doehle BP, Schäfer A, Wiegand HL, Bogerd HP, Cullen BR (July 2005). "Differential sensitivity of murine leukemia virus to APOBEC3-mediated inhibition is governed by virion exclusion". Journal of Virology. 79 (13): 8201–7. doi:10.1128/JVI.79.13.8201-8207.2005. PMC 1143768. PMID 15956565.
  • Rose KM, Marin M, Kozak SL, Kabat D (July 2005). "Regulated production and anti-HIV type 1 activities of cytidine deaminases APOBEC3B, 3F, and 3G". AIDS Research and Human Retroviruses. 21 (7): 611–9. doi:10.1089/aid.2005.21.611. PMID 16060832.
  • Muckenfuss H, Hamdorf M, Held U, Perkovic M, Löwer J, Cichutek K, Flory E, Schumann GG, Münk C (August 2006). "APOBEC3 proteins inhibit human LINE-1 retrotransposition". The Journal of Biological Chemistry. 281 (31): 22161–72. doi:10.1074/jbc.M601716200. PMID 16735504.
  • Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
  • Kinomoto M, Kanno T, Shimura M, Ishizaka Y, Kojima A, Kurata T, Sata T, Tokunaga K (2007). "All APOBEC3 family proteins differentially inhibit LINE-1 retrotransposition". Nucleic Acids Research. 35 (9): 2955–64. doi:10.1093/nar/gkm181. PMC 1888823. PMID 17439959.
  • Human APOBEC3C genome location and APOBEC3C gene details page in the UCSC Genome Browser.
  • Overview of all the structural information available in the PDB for UniProt: Q9NRW3 ( DNA dC->dU-editing enzyme APOBEC-3C) at the PDBe-KB.
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