APOBEC3C: Difference between revisions

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{{Infobox_gene}}
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'''DNA dC->dU-editing enzyme APOBEC-3C''' is a [[protein]] that in humans is encoded by the ''APOBEC3C'' [[gene]].<ref name="pmid11863358">{{cite journal | vauthors = Jarmuz A, Chester A, Bayliss J, Gisbourne J, Dunham I, Scott J, Navaratnam N | title = An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22 | journal = Genomics | volume = 79 | issue = 3 | pages = 285–96 | date = March 2002 | pmid = 11863358 | pmc =  | doi = 10.1006/geno.2002.6718 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: APOBEC3C apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3C| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27350| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
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, [[Viral infectivity factor|Vif]].<ref>{{cite journal | vauthors = Yu Q, Chen D, König R, Mariani R, Unutmaz D, Landau NR | title = APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication | journal = The Journal of Biological Chemistry | volume = 279 | issue = 51 | pages = 53379–86 | date = December 2004 | pmid = 15466872 | doi = 10.1074/jbc.M408802200 }}</ref> Enhancing A3C's catalytic activity had only a marginal effect on HIV-1 replication (in absence of Vif), the counteractive viral mechanism is unclear.<ref>{{cite journal | vauthors = Jaguva Vasudevan AA, Hofmann H, Willbold D, Häussinger D, Koenig BW, Münk C | title = Enhancing the Catalytic Deamination Activity of APOBEC3C Is Insufficient to Inhibit Vif-Deficient HIV-1 | journal = Journal of Molecular Biology | volume = 429 | issue = 8 | pages = 1171–1191 | date = April 2017 | pmid = 28315663 | doi = 10.1016/j.jmb.2017.03.015 }}</ref> A3C was also shown to inhibit other viruses.<ref>{{cite journal | vauthors = Baumert TF, Rösler C, Malim MH, von Weizsäcker F | title = Hepatitis B virus DNA is subject to extensive editing by the human deaminase APOBEC3C | journal = Hepatology | volume = 46 | issue = 3 | pages = 682–9 | date = September 2007 | pmid = 17625792 | doi = 10.1002/hep.21733 }}</ref><ref>{{cite journal | vauthors = Suspène R, Aynaud MM, Koch S, Pasdeloup D, Labetoulle M, Gaertner B, Vartanian JP, Meyerhans A, Wain-Hobson S | title = Genetic editing of herpes simplex virus 1 and Epstein-Barr herpesvirus genomes by human APOBEC3 cytidine deaminases in culture and in vivo | journal = Journal of Virology | volume = 85 | issue = 15 | pages = 7594–602 | date = August 2011 | pmid = 21632763 | pmc = 3147940 | doi = 10.1128/JVI.00290-11 }}</ref><ref>{{cite journal | vauthors = Köck J, Blum HE | title = Hypermutation of hepatitis B virus genomes by APOBEC3G, APOBEC3C and APOBEC3H | journal = The Journal of General Virology | volume = 89 | issue = Pt 5 | pages = 1184–91 | date = May 2008 | pmid = 18420796 | doi = 10.1099/vir.0.83507-0 }}</ref><ref>{{cite journal | vauthors = Li D, Liu J, Kang F, Guan W, Gao X, Wang Y, Sun D | title = Core-APOBEC3C chimerical protein inhibits hepatitis B virus replication | journal = Journal of Biochemistry | volume = 150 | issue = 4 | pages = 371–4 | date = October 2011 | pmid = 21746770 | doi = 10.1093/jb/mvr086 }}</ref><ref>{{cite journal | vauthors = 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 | title = APOBEC3A and 3C decrease human papillomavirus 16 pseudovirion infectivity | journal = Biochemical and Biophysical Research Communications | volume = 457 | issue = 3 | pages = 295–9 | date = February 2015 | pmid = 25576866 | doi = 10.1016/j.bbrc.2014.12.103 }}</ref>
{{GNF_Protein_box
| image =
| image_source =
| PDB =  
| Name = Apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3C
| HGNCid = 17353
| Symbol = APOBEC3C
| AltSymbols =; APOBEC1L; PBI; ARDC2; ARDC4; ARP5; MGC19485; bK150C2.3
| OMIM = 607750
| ECnumber =
| Homologene =
| MGIid =
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}} {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0016814 |text = hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}}
| Process = {{GNF_GO|id=GO:0008150 |text = biological_process}}  
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 27350
    | Hs_Ensembl =
    | Hs_RefseqProtein = NP_055323
    | Hs_RefseqmRNA = NM_014508
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr =
    | Hs_GenLoc_start =
    | Hs_GenLoc_end =
    | Hs_Uniprot =
    | Mm_EntrezGene =
    | Mm_Ensembl =
    | Mm_RefseqmRNA =
    | Mm_RefseqProtein =
    | Mm_GenLoc_db =
    | Mm_GenLoc_chr =
    | Mm_GenLoc_start =
    | Mm_GenLoc_end =
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}}
'''Apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3C''', also known as '''APOBEC3C''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: APOBEC3C apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3C| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27350| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{PBB_Summary
| section_title =  
| summary_text = 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. It is thought that the proteins may be RNA editing enzymes and have roles in growth or cell cycle control.<ref name="entrez">{{cite web | title = Entrez Gene: APOBEC3C apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3C| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27350| accessdate = }}</ref>
}}


==References==
This gene is a member of the [[cytidine deaminase]] [[gene family]]. It is one of seven related genes or [[pseudogene]]s found in a [[Genetic cluster|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.<ref>{{cite journal | vauthors = Yu Q, König R, Pillai S, Chiles K, Kearney M, Palmer S, Richman D, Coffin JM, Landau NR | title = Single-strand specificity of APOBEC3G accounts for minus-strand deamination of the HIV genome | journal = Nature Structural & Molecular Biology | volume = 11 | issue = 5 | pages = 435–42 | date = May 2004 | pmid = 15098018 | doi = 10.1038/nsmb758 }}</ref><ref>{{cite journal | vauthors = Harris RS, Petersen-Mahrt SK, Neuberger MS | title = RNA editing enzyme APOBEC1 and some of its homologs can act as DNA mutators | journal = Molecular Cell | volume = 10 | issue = 5 | pages = 1247–53 | date = November 2002 | pmid = 12453430 }}</ref><ref>{{cite journal | vauthors = Harris RS, Sheehy AM, Craig HM, Malim MH, Neuberger MS | title = DNA deamination: not just a trigger for antibody diversification but also a mechanism for defense against retroviruses | journal = Nature Immunology | volume = 4 | issue = 7 | pages = 641–3 | date = July 2003 | pmid = 12830140 | doi = 10.1038/ni0703-641 }}</ref><ref>{{cite journal | vauthors = Harris RS, Bishop KN, Sheehy AM, Craig HM, Petersen-Mahrt SK, Watt IN, Neuberger MS, Malim MH | title = DNA deamination mediates innate immunity to retroviral infection | journal = Cell | volume = 113 | issue = 6 | pages = 803–9 | date = June 2003 | pmid = 12809610 }}</ref><ref>{{cite journal | vauthors = Yu Q, Chen D, König R, Mariani R, Unutmaz D, Landau NR | title = APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication | journal = The Journal of Biological Chemistry | volume = 279 | issue = 51 | pages = 53379–86 | date = December 2004 | pmid = 15466872 | doi = 10.1074/jbc.M408802200 }}</ref>
{{reflist|2}}
 
==Further reading==
== Structure ==
{{refbegin | 2}}
The crystal structure of A3C suggests a putative HIV-1 vif binding region.<ref>{{cite journal | vauthors = Kitamura S, Ode H, Nakashima M, Imahashi M, Naganawa Y, Kurosawa T, Yokomaku Y, Yamane T, Watanabe N, Suzuki A, Sugiura W, Iwatani Y | title = The APOBEC3C crystal structure and the interface for HIV-1 Vif binding | journal = Nature Structural & Molecular Biology | volume = 19 | issue = 10 | pages = 1005–10 | date = October 2012 | pmid = 23001005 | doi = 10.1038/nsmb.2378 }}</ref><ref>{{cite journal | vauthors = 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 | title = Vif Proteins from Diverse Human Immunodeficiency Virus/Simian Immunodeficiency Virus Lineages Have Distinct Binding Sites in A3C | journal = Journal of Virology | volume = 90 | issue = 22 | pages = 10193–10208 | date = November 2016 | pmid = 27581978 | doi = 10.1128/JVI.01497-16 }}</ref> A3C was found to inhibit [[Long interspersed nuclear element|LINE-1]] elements by directly interacting with ORF1p proteins, in a deaminase-independent manner.<ref>{{cite journal | vauthors = 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 | title = Human LINE-1 restriction by APOBEC3C is deaminase independent and mediated by an ORF1p interaction that affects LINE reverse transcriptase activity | journal = Nucleic Acids Research | volume = 42 | issue = 1 | pages = 396–416 | date = January 2014 | pmid = 24101588 | doi = 10.1093/nar/gkt898 }}</ref>
{{PBB_Further_reading
{{clear}}
| citations =
== References ==
*{{cite journal | author=Wedekind JE, Dance GS, Sowden MP, Smith HC |title=Messenger RNA editing in mammals: new members of the APOBEC family seeking roles in the family business. |journal=Trends Genet. |volume=19 |issue= 4 |pages= 207-16 |year= 2003 |pmid= 12683974 |doi= }}
{{reflist|33em}}
*{{cite journal | author=Cullen BR |title=Role and mechanism of action of the APOBEC3 family of antiretroviral resistance factors. |journal=J. Virol. |volume=80 |issue= 3 |pages= 1067-76 |year= 2006 |pmid= 16414984 |doi= 10.1128/JVI.80.3.1067-1076.2006 }}
 
*{{cite journal | author=Haché G, Mansky LM, Harris RS |title=Human APOBEC3 proteins, retrovirus restriction, and HIV drug resistance. |journal=AIDS reviews |volume=8 |issue= 3 |pages= 148-57 |year= 2006 |pmid= 17078485 |doi= }}
== Further reading ==
*{{cite journal | author=Madsen P, Anant S, Rasmussen HH, ''et al.'' |title=Psoriasis upregulated phorbolin-1 shares structural but not functional similarity to the mRNA-editing protein apobec-1. |journal=J. Invest. Dermatol. |volume=113 |issue= 2 |pages= 162-9 |year= 1999 |pmid= 10469298 |doi= 10.1046/j.1523-1747.1999.00682.x }}
{{refbegin|33em}}
*{{cite journal | author=Dunham I, Shimizu N, Roe BA, ''et al.'' |title=The DNA sequence of human chromosome 22. |journal=Nature |volume=402 |issue= 6761 |pages= 489-95 |year= 1999 |pmid= 10591208 |doi= 10.1038/990031 }}
* {{cite journal | vauthors = Wedekind JE, Dance GS, Sowden MP, Smith HC | title = Messenger RNA editing in mammals: new members of the APOBEC family seeking roles in the family business | journal = Trends in Genetics | volume = 19 | issue = 4 | pages = 207–16 | date = April 2003 | pmid = 12683974 | doi = 10.1016/S0168-9525(03)00054-4 }}
*{{cite journal | author=Jarmuz A, Chester A, Bayliss J, ''et al.'' |title=An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22. |journal=Genomics |volume=79 |issue= 3 |pages= 285-96 |year= 2002 |pmid= 11863358 |doi= 10.1006/geno.2002.6718 }}
* {{cite journal | vauthors = Cullen BR | title = Role and mechanism of action of the APOBEC3 family of antiretroviral resistance factors | journal = Journal of Virology | volume = 80 | issue = 3 | pages = 1067–76 | date = February 2006 | pmid = 16414984 | pmc = 1346961 | doi = 10.1128/JVI.80.3.1067-1076.2006 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Vasudevan AA, Smits SH, Höppner A, Häussinger D, Koenig BW, Münk C | title = Structural features of antiviral DNA cytidine deaminases | journal = Biological Chemistry | volume = 394 | issue = 11 | pages = 1357–70 | date = November 2013 | pmid = 23787464 | doi = 10.1515/hsz-2013-0165 }}
*{{cite journal | author=Mariani R, Chen D, Schröfelbauer B, ''et al.'' |title=Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif. |journal=Cell |volume=114 |issue= 1 |pages= 21-31 |year= 2003 |pmid= 12859895 |doi= }}
* {{cite journal | vauthors = Haché G, Mansky LM, Harris RS | title = Human APOBEC3 proteins, retrovirus restriction, and HIV drug resistance | journal = AIDS Reviews | volume = 8 | issue = 3 | pages = 148–57 | year = 2006 | pmid = 17078485 | doi = }}
*{{cite journal  | author=Collins JE, Wright CL, Edwards CA, ''et al.'' |title=A genome annotation-driven approach to cloning the human ORFeome. |journal=Genome Biol. |volume=5 |issue= 10 |pages= R84 |year= 2005 |pmid= 15461802 |doi= 10.1186/gb-2004-5-10-r84 }}
* {{cite journal | vauthors = 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 | title = Psoriasis upregulated phorbolin-1 shares structural but not functional similarity to the mRNA-editing protein apobec-1 | journal = The Journal of Investigative Dermatology | volume = 113 | issue = 2 | pages = 162–9 | date = August 1999 | pmid = 10469298 | doi = 10.1046/j.1523-1747.1999.00682.x }}
*{{cite journal | author=Yu Q, Chen D, König R, ''et al.'' |title=APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication. |journal=J. Biol. Chem. |volume=279 |issue= 51 |pages= 53379-86 |year= 2005 |pmid= 15466872 |doi= 10.1074/jbc.M408802200 }}
* {{cite journal | vauthors = 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 | title = The DNA sequence of human chromosome 22 | journal = Nature | volume = 402 | issue = 6761 | pages = 489–95 | date = December 1999 | pmid = 10591208 | doi = 10.1038/990031 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
* {{cite journal | vauthors = Mariani R, Chen D, Schröfelbauer B, Navarro F, König R, Bollman B, Münk C, Nymark-McMahon H, Landau NR | title = Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif | journal = Cell | volume = 114 | issue = 1 | pages = 21–31 | date = July 2003 | pmid = 12859895 | doi = 10.1016/S0092-8674(03)00515-4 }}
*{{cite journal | author=Langlois MA, Beale RC, Conticello SG, Neuberger MS |title=Mutational comparison of the single-domained APOBEC3C and double-domained APOBEC3F/G anti-retroviral cytidine deaminases provides insight into their DNA target site specificities. |journal=Nucleic Acids Res. |volume=33 |issue= 6 |pages= 1913-23 |year= 2005 |pmid= 15809227 |doi= 10.1093/nar/gki343 }}
* {{cite journal | vauthors = 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 | title = A genome annotation-driven approach to cloning the human ORFeome | journal = Genome Biology | volume = 5 | issue = 10 | pages = R84 | year = 2005 | pmid = 15461802 | pmc = 545604 | doi = 10.1186/gb-2004-5-10-r84 }}
*{{cite journal | author=Pope SN, Lee IR |title=Yeast two-hybrid identification of prostatic proteins interacting with human sex hormone-binding globulin. |journal=J. Steroid Biochem. Mol. Biol. |volume=94 |issue= 1-3 |pages= 203-8 |year= 2005 |pmid= 15862967 |doi= 10.1016/j.jsbmb.2005.01.007 }}
* {{cite journal | vauthors = Yu Q, Chen D, König R, Mariani R, Unutmaz D, Landau NR | title = APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication | journal = The Journal of Biological Chemistry | volume = 279 | issue = 51 | pages = 53379–86 | date = December 2004 | pmid = 15466872 | doi = 10.1074/jbc.M408802200 }}
*{{cite journal | author=Doehle BP, Schäfer A, Wiegand HL, ''et al.'' |title=Differential sensitivity of murine leukemia virus to APOBEC3-mediated inhibition is governed by virion exclusion. |journal=J. Virol. |volume=79 |issue= 13 |pages= 8201-7 |year= 2005 |pmid= 15956565 |doi= 10.1128/JVI.79.13.8201-8207.2005 }}
* {{cite journal | vauthors = Langlois MA, Beale RC, Conticello SG, Neuberger MS | title = Mutational comparison of the single-domained APOBEC3C and double-domained APOBEC3F/G anti-retroviral cytidine deaminases provides insight into their DNA target site specificities | journal = Nucleic Acids Research | volume = 33 | issue = 6 | pages = 1913–23 | year = 2005 | pmid = 15809227 | pmc = 1074398 | doi = 10.1093/nar/gki343 }}
*{{cite journal | author=Rose KM, Marin M, Kozak SL, Kabat D |title=Regulated production and anti-HIV type 1 activities of cytidine deaminases APOBEC3B, 3F, and 3G. |journal=AIDS Res. Hum. Retroviruses |volume=21 |issue= 7 |pages= 611-9 |year= 2005 |pmid= 16060832 |doi= 10.1089/aid.2005.21.611 }}
* {{cite journal | vauthors = Pope SN, Lee IR | title = Yeast two-hybrid identification of prostatic proteins interacting with human sex hormone-binding globulin | journal = The Journal of Steroid Biochemistry and Molecular Biology | volume = 94 | issue = 1-3 | pages = 203–8 | date = February 2005 | pmid = 15862967 | doi = 10.1016/j.jsbmb.2005.01.007 }}
*{{cite journal | author=Muckenfuss H, Hamdorf M, Held U, ''et al.'' |title=APOBEC3 proteins inhibit human LINE-1 retrotransposition. |journal=J. Biol. Chem. |volume=281 |issue= 31 |pages= 22161-72 |year= 2006 |pmid= 16735504 |doi= 10.1074/jbc.M601716200 }}
* {{cite journal | vauthors = Doehle BP, Schäfer A, Wiegand HL, Bogerd HP, Cullen BR | title = Differential sensitivity of murine leukemia virus to APOBEC3-mediated inhibition is governed by virion exclusion | journal = Journal of Virology | volume = 79 | issue = 13 | pages = 8201–7 | date = July 2005 | pmid = 15956565 | pmc = 1143768 | doi = 10.1128/JVI.79.13.8201-8207.2005 }}
*{{cite journal | author=Ewing RM, Chu P, Elisma F, ''et al.'' |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue=  |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 }}
* {{cite journal | vauthors = Rose KM, Marin M, Kozak SL, Kabat D | title = Regulated production and anti-HIV type 1 activities of cytidine deaminases APOBEC3B, 3F, and 3G | journal = AIDS Research and Human Retroviruses | volume = 21 | issue = 7 | pages = 611–9 | date = July 2005 | pmid = 16060832 | doi = 10.1089/aid.2005.21.611 }}
}}
* {{cite journal | vauthors = Muckenfuss H, Hamdorf M, Held U, Perkovic M, Löwer J, Cichutek K, Flory E, Schumann GG, Münk C | title = APOBEC3 proteins inhibit human LINE-1 retrotransposition | journal = The Journal of Biological Chemistry | volume = 281 | issue = 31 | pages = 22161–72 | date = August 2006 | pmid = 16735504 | doi = 10.1074/jbc.M601716200 }}
* {{cite journal | vauthors = 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 | title = Large-scale mapping of human protein-protein interactions by mass spectrometry | journal = Molecular Systems Biology | volume = 3 | issue = 1 | pages = 89 | year = 2007 | pmid = 17353931 | pmc = 1847948 | doi = 10.1038/msb4100134 }}
* {{cite journal | vauthors = Kinomoto M, Kanno T, Shimura M, Ishizaka Y, Kojima A, Kurata T, Sata T, Tokunaga K | title = All APOBEC3 family proteins differentially inhibit LINE-1 retrotransposition | journal = Nucleic Acids Research | volume = 35 | issue = 9 | pages = 2955–64 | year = 2007 | pmid = 17439959 | pmc = 1888823 | doi = 10.1093/nar/gkm181 }}
{{refend}}
{{refend}}


{{protein-stub}}
== External links ==
{{WikiDoc Sources}}
* {{UCSC gene info|APOBEC3C}}
 
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{{Enzymes}}
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[[Category:EC 3.5.4]]

Revision as of 18:08, 29 August 2017

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External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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Ensembl

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View/Edit Human

DNA dC->dU-editing enzyme APOBEC-3C is a protein that in humans is encoded by the APOBEC3C gene.[1][2]

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.[3] Enhancing A3C's catalytic activity had only a marginal effect on HIV-1 replication (in absence of Vif), the counteractive viral mechanism is unclear.[4] A3C was also shown to inhibit other viruses.[5][6][7][8][9]

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.[10][11][12][13][14]

Structure

The crystal structure of A3C suggests a putative HIV-1 vif binding region.[15][16] A3C was found to inhibit LINE-1 elements by directly interacting with ORF1p proteins, in a deaminase-independent manner.[17]

References

  1. ↑ 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.
  2. ↑ "Entrez Gene: APOBEC3C apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3C".
  3. ↑ 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.
  4. ↑ 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.
  5. ↑ 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.
  6. ↑ 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.
  7. ↑ 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.
  8. ↑ 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.
  9. ↑ 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. PMID 25576866.
  10. ↑ 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.
  11. ↑ 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. PMID 12453430.
  12. ↑ 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.
  13. ↑ 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. PMID 12809610.
  14. ↑ 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.
  15. ↑ 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.
  16. ↑ 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. PMID 27581978.
  17. ↑ 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. PMID 24101588.

Further reading

External links

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