APOBEC3C

Available structures

Human UniProt search: PDBe RCSB

List of PDB id codes
3VM8, 3VOW

Identifiers

Aliases

APOBEC3C, A3C, APOBEC1L, ARDC2, ARDC4, ARP5, PBI, bK150C2.3, apolipoprotein B mRNA editing enzyme catalytic subunit 3C

External IDs

HomoloGene: 129856 GeneCards: APOBEC3C

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 • poly(A) RNA binding • metal ion binding
Cellular component	• nucleus • cytoplasm
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
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


27350


n/a

Ensembl


ENSG00000244509


n/a

UniProt


Q9NRW3


n/a

RefSeq (mRNA)


NM_014508


n/a

RefSeq (protein)


NP_055323.2


n/a

Location (UCSC)

Chr 22: 39.01 – 39.02 Mb

n/a

PubMed search

^[1]

n/a

Wikidata

View/Edit Human

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

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.^[3]

References

↑ "Human PubMed Reference:".
↑ Jarmuz A, Chester A, Bayliss J, Gisbourne J, Dunham I, Scott J, Navaratnam N (Feb 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.
1 2 "Entrez Gene: APOBEC3C apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3C".

Wedekind JE, Dance GS, Sowden MP, Smith HC (2003). "Messenger RNA editing in mammals: new members of the APOBEC family seeking roles in the family business.". Trends Genet. 19 (4): 207–16. doi:10.1016/S0168-9525(03)00054-4. PMID 12683974.
Cullen BR (2006). "Role and mechanism of action of the APOBEC3 family of antiretroviral resistance factors.". J. Virol. 80 (3): 1067–76. doi:10.1128/JVI.80.3.1067-1076.2006. PMC 1346961. PMID 16414984.
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, et al. (1999). "Psoriasis upregulated phorbolin-1 shares structural but not functional similarity to the mRNA-editing protein apobec-1.". J. Invest. Dermatol. 113 (2): 162–9. doi:10.1046/j.1523-1747.1999.00682.x. PMID 10469298.
Dunham I, Shimizu N, Roe BA, et al. (1999). "The DNA sequence of human chromosome 22.". Nature. 402 (6761): 489–95. doi:10.1038/990031. PMID 10591208.
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.
Mariani R, Chen D, Schröfelbauer B, et al. (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, et al. (2005). "A genome annotation-driven approach to cloning the human ORFeome.". Genome Biol. 5 (10): R84. doi:10.1186/gb-2004-5-10-r84. PMC 545604. PMID 15461802.
Yu Q, Chen D, König R, et al. (2005). "APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication.". J. Biol. Chem. 279 (51): 53379–86. doi:10.1074/jbc.M408802200. PMID 15466872.
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.
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 Res. 33 (6): 1913–23. doi:10.1093/nar/gki343. PMC 1074398. PMID 15809227.
Pope SN, Lee IR (2005). "Yeast two-hybrid identification of prostatic proteins interacting with human sex hormone-binding globulin.". J. Steroid Biochem. Mol. Biol. 94 (1-3): 203–8. doi:10.1016/j.jsbmb.2005.01.007. PMID 15862967.
Doehle BP, Schäfer A, Wiegand HL, et al. (2005). "Differential sensitivity of murine leukemia virus to APOBEC3-mediated inhibition is governed by virion exclusion.". J. Virol. 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 (2005). "Regulated production and anti-HIV type 1 activities of cytidine deaminases APOBEC3B, 3F, and 3G.". AIDS Res. Hum. Retroviruses. 21 (7): 611–9. doi:10.1089/aid.2005.21.611. PMID 16060832.
Muckenfuss H, Hamdorf M, Held U, et al. (2006). "APOBEC3 proteins inhibit human LINE-1 retrotransposition.". J. Biol. Chem. 281 (31): 22161–72. doi:10.1074/jbc.M601716200. PMID 16735504.
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.
Kinomoto M, Kanno T, Shimura M, et al. (2007). "All APOBEC3 family proteins differentially inhibit LINE-1 retrotransposition.". Nucleic Acids Res. 35 (9): 2955–64. doi:10.1093/nar/gkm181. PMC 1888823. PMID 17439959.

Hydrolases: carbon-nitrogen non-peptide (EC 3.5)

3.5.1: Linear amides / Amidohydrolases	Asparaginase Glutaminase Urease Biotinidase Aspartoacylase Ceramidase Aspartylglucosaminidase Fatty acid amide hydrolase Histone deacetylase Sirtuin

3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase Beta-lactamase

3.5.3: Linear amidines/ Ureohydrolases	Arginase Agmatinase Protein-arginine deiminase

3.5.4: Cyclic amidines/ Aminohydrolases	Guanine deaminase Adenosine deaminase AMP deaminase Inosine monophosphate synthase DCMP deaminase GTP cyclohydrolase I Cytidine deaminase AICDA Activation-induced cytidine deaminase

3.5.5: Nitriles/ Aminohydrolases	Nitrilase

3.5.99: Other	Riboflavinase Thiaminase II

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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APOBEC3C

References

Further reading