APOBEC3C

APOBEC3C
Available structures
PDB	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	OMIM: 607750; HomoloGene: 129856; GeneCards: APOBEC3C; OMA:APOBEC3C - orthologs
Gene location (Human)
Chr.	Chromosome 22 (human)
End	39,020,352 bp
RNA expression pattern
	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
	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
	27350
	n/a
	ENSG00000244509
	n/a
	Q9NRW3
	n/a
	NM_014508
	n/a
	NP_055323
	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.^[3]^[4] APOBEC3C (A3C) was reported to inhibit simian immunodeficiency deficiency virus potently rather than HIV-1, in absence of viral infectivity factor, Vif^[5]. Template:PBB Summary

The crystal structure of A3C suggesting putative HIV-1 vif binding regions was reported on 2012 ^[6]. And a following study was reported the distinct binding sites, found in A3C for different Vif proteins^[7]. A3C was found to inhibit LINE-1 elements by directly interacting with ORF1p proteins, in a deaminase-indepedent manner^[8].

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000244509 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ "Entrez Gene: APOBEC3C apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3C".
^ Yu, Q; Chen, D; König, R; Mariani, R; Unutmaz, D; Landau, NR (17 December 2004). "APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication". The Journal of biological chemistry. 279 (51): 53379–86. PMID 15466872.
^ 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. PMID 23001005.
^ 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 (15 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. PMID 27581978.
^ 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. PMID 24101588.

External links

Human APOBEC3C genome location and APOBEC3C gene details page in the UCSC Genome Browser.

v t e Hydrolases: carbon-nitrogen non-peptide (EC 3.5)
3.5.1: Linear amides / Amidohydrolases	Asparaginase Glutaminase Urease Biotinidase Aminoacylase ACY1 Aspartoacylase(ACY2) ACY3 Ceramidase Aspartylglucosaminidase Fatty acid amide hydrolase Histone deacetylase Sirtuin
3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase Beta-lactamase Dihydroorotase
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

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

References

External links

Further reading