APOBEC3C

Protein-coding gene in humans From Wikipedia, the free encyclopedia

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

PDBHuman UniProt search: PDBe RCSB
AliasesAPOBEC3C, A3C, APOBEC1L, ARDC2, ARDC4, ARP5, PBI, bK150C2.3, apolipoprotein B mRNA editing enzyme catalytic subunit 3C
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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
Ensembl
UniProt
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
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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

Further reading

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