U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

APOBEC3F apolipoprotein B mRNA editing enzyme catalytic subunit 3F [ Homo sapiens (human) ]

Gene ID: 200316, updated on 11-Apr-2024

Summary

Go to the top of the page Help
Official Symbol
APOBEC3Fprovided by HGNC
Official Full Name
apolipoprotein B mRNA editing enzyme catalytic subunit 3Fprovided by HGNC
Primary source
HGNC:HGNC:17356
See related
Ensembl:ENSG00000128394 MIM:608993; AllianceGenome:HGNC:17356
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as
A3F; KA6; ARP8; BK150C2.4.MRNA
Summary
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. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Jul 2008]
Expression
Broad expression in lymph node (RPKM 2.8), ovary (RPKM 2.8) and 24 other tissues See more
Orthologs
all
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help
See APOBEC3F in Genome Data Viewer
Location:
22q13.1
Exon count:
9
Annotation release Status Assembly Chr Location
RS_2023_10 current GRCh38.p14 (GCF_000001405.40) 22 NC_000022.11 (39040864..39055972)
RS_2023_10 current T2T-CHM13v2.0 (GCF_009914755.1) 22 NC_060946.1 (39511283..39526391)
105.20220307 previous assembly GRCh37.p13 (GCF_000001405.25) 22 NC_000022.10 (39436869..39451977)

Chromosome 22 - NC_000022.11Genomic Context describing neighboring genes Neighboring gene H3K27ac-H3K4me1 hESC enhancers GRCh37_chr22:39409474-39410092 and GRCh37_chr22:39410093-39410710 Neighboring gene apolipoprotein B mRNA editing enzyme catalytic subunit 3C Neighboring gene OCT4-H3K27ac-H3K4me1 hESC enhancer GRCh37_chr22:39415894-39416734 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr22:39417574-39418413 Neighboring gene apolipoprotein B mRNA editing enzyme catalytic subunit 3D Neighboring gene H3K4me1 hESC enhancer GRCh37_chr22:39423978-39424906 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr22:39426361-39427157 Neighboring gene OCT4-NANOG hESC enhancer GRCh37_chr22:39432783-39433673 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 19027 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr22:39437791-39438568 Neighboring gene ReSE screen-validated silencer GRCh37_chr22:39439415-39439645 Neighboring gene P300/CBP strongly-dependent group 1 enhancer GRCh37_chr22:39445317-39446516 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 13739 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr22:39448525-39449459 Neighboring gene ReSE screen-validated silencer GRCh37_chr22:39458436-39458615 Neighboring gene uncharacterized LOC107985563 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 13740 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr22:39465577-39466080 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr22:39466081-39466585 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 13741 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 19028 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 19029 Neighboring gene apolipoprotein B mRNA editing enzyme catalytic subunit 3G Neighboring gene H3K4me1 hESC enhancer GRCh37_chr22:39477470-39477970 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr22:39480765-39481338 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr22:39483746-39484555

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to nucleotide: Graphics FASTA GenBank

Expression

Go to the top of the page Help
  • Project title: HPA RNA-seq normal tissues
  • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
  • BioProject: PRJEB4337
  • Publication: PMID 24309898
  • Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

Go to the top of the pageHelp

Related articles in PubMed

  1. Stability of APOBEC3F in the Presence of the APOBEC3 Antagonist HIV-1 Vif Increases at the Expense of Co-Expressed APOBEC3H Haplotype I. Yousefi M, et al. Viruses, 2023 Feb 7. PMID 36851677, Free PMC Article
  2. An insight into the dependence of the deamination rate of human APOBEC3F on the length of single-stranded DNA, which is affected by the concentrations of APOBEC3F and single-stranded DNA. Wan L, et al. Biochim Biophys Acta Gen Subj, 2020 Feb. PMID 30986508
  3. Polymorphisms of the cytidine deaminase APOBEC3F have different HIV-1 restriction efficiencies. Mohammadzadeh N, et al. Virology, 2019 Jan 15. PMID 30448640
  4. Role of APOBEC3F Gene Variation in HIV-1 Disease Progression and Pneumocystis Pneumonia. An P, et al. PLoS Genet, 2016 Mar. PMID 26942578, Free PMC Article
  5. Overexpression of APOBEC3F in tumor tissues is potentially predictive for poor recurrence-free survival from HBV-related hepatocellular carcinoma. Yang Z, et al. Discov Med, 2015 Dec. PMID 26760979

See all (207) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. APOBEC3F Is a Mutational Driver of the Human Monkeypox Virus Identified in the 2022 Outbreak.
    Title: APOBEC3F Is a Mutational Driver of the Human Monkeypox Virus Identified in the 2022 Outbreak.
  2. Stability of APOBEC3F in the Presence of the APOBEC3 Antagonist HIV-1 Vif Increases at the Expense of Co-Expressed APOBEC3H Haplotype I.
    Title: Stability of APOBEC3F in the Presence of the APOBEC3 Antagonist HIV-1 Vif Increases at the Expense of Co-Expressed APOBEC3H Haplotype I.
  3. Differential Activity of APOBEC3F, APOBEC3G, and APOBEC3H in the Restriction of HIV-2.
    Title: Differential Activity of APOBEC3F, APOBEC3G, and APOBEC3H in the Restriction of HIV-2.
  4. analysis of the dependence of the deamination rate of human APOBEC3F on the length of single-stranded DNA, which is affected by the concentrations of APOBEC3F and single-stranded DNA
    Title: An insight into the dependence of the deamination rate of human APOBEC3F on the length of single-stranded DNA, which is affected by the concentrations of APOBEC3F and single-stranded DNA.
  5. The cryo-EM structure of the Vif-targeted C-terminal domain of human A3F in complex with HIV-1 Vif and the cellular cofactor core-binding factor beta (CBFbeta) at 3.9-A resolution shows that Vif and CBFbeta form a platform to recruit A3F, revealing a direct A3F-recruiting role of CBFbeta beyond Vif stabilization, and it captures multiple independent A3F-Vif interfaces.
    Title: Structural basis of antagonism of human APOBEC3F by HIV-1 Vif.
  6. Apolipoprotein B mRNA editing enzyme catalytic subunit 3F (A3F) polymorphism A3F 231V restrict HIV-1 infection more efficiently than A3F 231 and is partially protected from Vif-mediated degradation. A3F 231V induces more mutations than A3F 231I in HIV-1 proviral DNA. A3F genotypes are commonly heterozygous. Hetero-oligomerization with A3F 231V results in partial stabilization of A3F 231I and A3G in the presence of Vif.
    Title: Polymorphisms of the cytidine deaminase APOBEC3F have different HIV-1 restriction efficiencies.
  7. APOBEC3DE binds to itself, APOBEC3F, and APOBEC3G and antagonizes APOBEC3F and, to a lesser extent, APOBEC3G restriction of hepatitis B virus replication.
    Title: APOBEC3DE Antagonizes Hepatitis B Virus Restriction Factors APOBEC3F and APOBEC3G.
  8. These results indicate that APOBEC3 proteins can be copackaged and can comutate the same genomes, and can cooperate to inhibit HIV replication.
    Title: APOBEC3 proteins can copackage and comutate HIV-1 genomes.
  9. an APOBEC3F/APOBEC3G hetero-oligomer can form that has unique properties compared to each APOBEC3 alone. This hetero-oligomer has increased efficiency of virus hypermutation, raising the idea that we still may not fully realize the antiviral mechanisms of endogenous APOBEC3 enzymes. Hetero-oligomerization may be a mechanism to increase their antiviral activity in the presence of Vif.
    Title: Mechanism of Enhanced HIV Restriction by Virion Coencapsidated Cytidine Deaminases APOBEC3F and APOBEC3G.
  10. virus adaptation and computational studies to interrogate the APOBEC3F-Vif interface and build a robust structural model; taken together with mutagenesis results, propose a wobble model to explain how HIV-1 Vif has evolved to bind different APOBEC3 enzymes
    Title: The Binding Interface between Human APOBEC3F and HIV-1 Vif Elucidated by Genetic and Computational Approaches.
Submit: New GeneRIF Correction See all GeneRIFs (68)

Phenotypes

Go to the top of the page Help

Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Variation

Go to the top of the page Help

See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

Genotypes

HIV-1 interactions

Go to the top of the page Help

Replication interactions

Interaction Pubs
HIV/tuberculosis coinfection upregulates APOBEC3F expression in pleural fluid mononuclear cells (PFMC) isolated from antiretroviral-naive coinfected patients (relative to patients infected with only tuberculosis) PubMed
Knockdown of APOBEC3F by siRNA enhances HIV-1 infection of immature dendritic cells (iDCs), indicating that APOBEC3F controls the sensitivity of iDCs to HIV-1 infection PubMed

Protein interactions

Protein Gene Interaction Pubs
Envelope surface glycoprotein gp120 env HIV-1 Env gp120 variable loop 3 (V3) region mutation is increased by incomplete Vif neutralization (Vif K22E) of APOBEC3G/F activity and may contribute to genetic evolution from CCR5 to CXCR4 co-receptor usage PubMed
Pol gag-pol Analyses of longitudinal HIV-1 pol sequences from patients without hypermutated viruses during chronic infection indicate that A3F may increase HIV-1 diversification and facilitate viral adaption and propagation in vivo PubMed
Pr55(Gag) gag R7R10K11S, A30P, P31L, R32G, and RKK32-34SSS mutations in the NC domain of HIV-1 Gag result in a significant decrease in APOBEC3F incorporation into virus-like particles PubMed
gag Amino acids 104-156, located between the two cytidine deaminase domains of APOBEC3F, are required for its incorporation into Gag virus-like particles PubMed
gag The NC domain of HIV-1 Gag is required for 7SL RNA and APOBEC3F packaging PubMed
gag APOBEC3F may be incorporated into virions by HIV-1 Gag polyprotein PubMed
gag Single-virion fluorescence microscopy analysis demonstrates that the efficiency of A3G-YFP and A3F-YFP incorporation into HIV-1 Gag-CeFP virions is higher than that of A3C-YFP incorporation into HIV-1 Gag-CeFP virions PubMed
gag The efficiency of incorporation of Mov10, A3G, and A3F into viral particles, which contains both HIV-1 Gag and genomic RNA, is much higher than that of the other P-body proteins AGO2, DCP1a, DCP2, and DDX6 PubMed
gag In HIV-1 virions, APOBEC3F interacts with HIV-1 IN and NC, which are known to be important for reverse transcription and integration PubMed
Vif vif HIV-1 Vif binds APOBEC3F; the interaction is between amino acid residue R15 in Vif and E289 in APOBEC3F PubMed
vif HIV-1 Vif degrades APOBEC3F; degradation is dependent on interactions between amino acid residue R15 in Vif and E289 in APOBEC3F PubMed
vif HIV-1 Vif degrades APOBEC3F dependent upon L291, A292, R293, and E324 in APOBEC3F PubMed
vif HIV-1 Vif binds amino acids L291, A292 and R293 in APOBEC3F PubMed
vif HIV-1 Vif degrades APOBEC3C and APOBEC3F and is dependent on Vif F1, F2, and F3 box mutations involving residues D14, R15, M16, W79, D172, and W174 PubMed
vif HIV-1 Vif degrades APOBEC3F and APOBEC3C PubMed
vif HIV-1 Vif internal amino acid salt bridge (E171-K167-D101) mediates human APOBEC3C and APOBEC3F degradation PubMed
vif HIV-1 Vif specifically binds APOBEC3F, and Vif suppresses both the inhibition of virus infectivity caused by APOBEC3F and virion incorporation of APOBEC3F PubMed
vif APOBEC3F levels are increased by compound N.41 treatment only in cells co-expressing HIV-1 Vif, and APOBEC3F levels in virus particles are also increased PubMed
vif APOBEC3F, similar to APOBEC3G, induces G to A hypermutations in HIV-1 genomic DNA, and the HIV-1 Vif protein inhibits this activity PubMed
vif Certain residues L125, G126, R127, E134, Y135, G138 in HCCH motif (residues 125-141) of HIV-1 Vif are required for inhibition of APOBEC3F PubMed
vif Immunoblotting and crystal structure analyses reveal ten amino acids L225, F258, C259, I262, L263, S264, Y269, D289, F290, and H294 in APOBEC3F are involved in forming Vif-interaction interface PubMed
vif A potent small molecular compound VEC-5 protects APOBEC3G, APOBEC3F, and APOBEC3C from HIV-1 Vif-induced degradation and enhances A3G incorporation into HIV-1 virions by inhibiting the interaction between Vif and elongin C PubMed
vif HIV-1 Vif W21A, S32A, W38A, Y69A, E76A, W79A, H108A, C114S, C133S, and H139A mutants have no viral ability to neutralize APOBEC3F PubMed
vif An extensive mutational analysis of HIV-1 Vif reveals that two distinct regions of Vif, amino acids Y(40)RHHY(44) and D(14)RMR(17), which are essential for binding to A3G and A3F, respectively PubMed
vif CBF-beta-mediated increase of HIV-1 Vif steady-state levels results in decreased cellular levels of all Vif-sensitive APOBEC proteins (A3C, A3D, A3F, A3G, and A3H haplotype II) PubMed
vif Endogenous APOBEC3 proteins, particularly APOBEC3D, APOBEC3F, and APOBEC3G, can potently inhibit HIV-1 propagation in a mouse model by mutating 14DRMR17 and/or 40YRHHY44 motifs in Vif PubMed
vif Amino acids P281, E282, D313, E316, Q323, and E324 in APOBEC3F are required for the interface binding to HIV-1 Vif(IIIB) PubMed
vif HIV-1 Vif mutants 84DVAAAA89, 88EW/AA89, G84A, G84D, W89A, D104A, L106S, and I107S result in upregulated APOBEC3F expression and show a reduced ability to neutralize the antiviral activity of APOBEC3F PubMed
vif HIV-1 Vif mutant E88A/W89A fails to bind to CBF-beta, which impairs Vif-mediated degradation of both A3F and A3G proteins and HIV-1 replication in non-permissive CEM cells PubMed
vif A novel conserved 69YXXL72 motif in HIV-1 Vif mediates binding to human A3F and its subsequent degradation. Tyr69 and Leu72 residues in the YXXL motif are important for degradation of A3F PubMed
vif HIV-1 Vif, which suppresses both APOBEC3G and APOBEC3F antiviral function by inducing their degradation, may selectively remove these proteins from, and/or restrict their localization to, P-bodies PubMed
vif HIV-1 Vif mutants W11R and R15G are restricted in permissive SupT11 and nonpermissive CEM2n cell lines that express A3F, while H43N and H43N/E117K Vif mutants are capable of spreading efficiently in the presence of A3F PubMed
vif HIV-1 Vif mutants W5S, W21S, W38S, W89S, F112S, and F115S have a reduced ability to interact with CBF-beta and these Vif hydrophobic residues are important for Vif-mediated degradation of A3F PubMed
vif The crystal structure provides a structural basis that L255A, L255D, F258A, C259K, C259S, I262A, Y269A, E286A, E289Q, F290A, F290K, H294A, H294D, E316Q, S320A, and E324Q mutations fail to bind to HIV-1 Vif PubMed
vif The HIV-1 Vif N-terminal motif (residues 18-38) binds CUL5 in mammalian cells and is reguired for A3F and A3G degradation and HIV-1 infectivity PubMed
vif Replacement of all lysines with arginines in A3F results in inhibition of HIV-1 Vif-mediated A3F degradation by polyubiquitination. Lysines at positions 40, 52, 209, 334, 337, 355, and 358 in A3F are important for its degradation by Vif PubMed
vif A3F mutants C259K and IL262-263AA are resistant to HIV-1 Vif-mediated A3F degradation PubMed
vif The amino acids 223-232 of A3F-CTD beta1-2 loop is conserved to the amino acids 23-32 of HIV-1 Vif, while the amino acids 305-313 of A3F-CTD beta4-alpha4 loop is conserved to the amino acids 108-113 of HIV-1 Vif PubMed
vif Unusual substitutions V13I, V55T, and L81M in HIV-1 Vif from children infected perinatally without progression to AIDS are located in three distinct Vif motifs important for the interaction with A3G/A3F PubMed
vif The antiviral activity of A3G to HIV-1 vif mutants NL4-3 40YRHHY44>A5 and NL4-3 14DRMR17>A4 with G-to-A hypermutations confers a greater restriction than the combined antiviral activity of A3F and A3DE in activated CD4+ T cells and macrophages PubMed
vif HIV-1 Vif alleles from seven HIV-1 subtypes show their abilities to degrade and counteract A3F efficiently PubMed
vif Highly conserved Tryptophan residues in the N-terminal region of HIV-1 Vif are required for the suppression of both APOBEC3G and APOBEC3F PubMed
vif HIV-1 Vif motif TGERxW (amino acids 74-79) is important for A3F interaction and inhibition PubMed
vif Stress causes A3A, A3B, A3C, and A3F to co-localize efficiently with Vif(IIIB) and mRNA-PABP1 complexes in stress granules PubMed
vif Vif-deficient HIV-1 replicates as equally well as wild-type virus in CEM-T4 cells expressing high levels of A3G and A3F, indicating CEM-T4 cells lack a cellular co-factor for these endogenous antiretroviral proteins PubMed
vif Small molecule RN-18 specifically inhibits HIV-1 Vif-mediated downregulation of APOBEC3C/F/G proteins by decreasing Vif protein levels when Vif interacts with these proteins PubMed
vif Amino acids 283 to 300 of A3F are critical for binding to the DRMR region of HIV-1 Vif and for A3F degradation PubMed
vif The SLV portion of the Vif SLV/Ix4Yx9Y motif is required for optimal suppression of A3F PubMed
vif The carboxyl-terminal domain (residues 183-373) of A3F alone binds to HIV-1 Vif and behaves like the full-length A3F in terms of Vif sensitivity PubMed
vif Human T cell line CEM.NKR clones display inhibition of HIV-1 replication although these clones retain low levels of A3DE, A3F, A3G, and A3H expression, suggesting that a novel restriction factor distinct from APOBEC3s exists in CEM.NKR cells PubMed
vif Incorporation of Vif into virions is dependent on its interaction with A3G/A3F PubMed
vif Long-term restriction by A3F selects HIV-1 clones with Vif Q26-Q27 or Y26-Q27 mutations, which are fully capable of overcoming A3F but susceptible to restriction by A3G PubMed
vif Alternative splice removal of exon 2 of A3F produces a Vif-resistant protein that retains significant antiviral activity. Splice removal of exons 2-4 results in a Vif-sensitive A3F protein with weaker antiviral activity PubMed
vif The T(Q/D/E)x(5)ADx(2)(I/L) motif, located at residues 96 to 107 in HIV-1 Vif, plays a critical role in neutralizing activity toward A3F. This motif regulates Vif interaction with Cul5 PubMed
vif All residues except N175 in the (171)EDRWN(175) domain of Vif are equally important for regulation of A3F neutralization PubMed
vif Residues L81, G82, and G84, and, to a lesser extent, I87 and W89 within the (81)LGxGxxIxW(89) domain affect Vif binding to A3F and play very critical roles in A3F neutralizing activity PubMed
vif Amino-acid residues QE323-324EK in A3F affect the differential susceptibility of human A3F and monkey A3F to HIV-1 Vif. Mutation of A3F E324 alone alters functional susceptibility of its binding to Vif PubMed
vif Amino acid E289 in the EFLARH sequence of A3F is critical for HIV-1 Vif sensitivity PubMed
Vpu vpu The expression of APOBEC3F is enhanced in Vpu-deficient HIV-1-infected cells as compared to that in wild-type-infected cells PubMed
capsid gag HIV-1 CA mutations (K203A and E128A/R132A) that alter HIV-1 core stability decrease nuclear import of A3F-YFP-labeled preintegration complexes (PICs) in infected cells PubMed
integrase gag-pol In HIV-1 virions, APOBEC3F interacts with HIV-1 IN and NC, which are known to be important for reverse transcription and integration PubMed
nucleocapsid gag The NC domain of HIV-1 Gag is required for 7SL RNA and APOBEC3F packaging PubMed
gag In HIV-1 virions, APOBEC3F interacts with HIV-1 IN and NC, which are known to be important for reverse transcription and integration PubMed
reverse transcriptase gag-pol Vif-negative HIV-1 produced from 293T cells transiently expressing hA3F is impaired in early and late viral DNA production, and in viral infectivity, effects that are correlated with an inability of tRNA(3)(Lys) to prime reverse transcription PubMed
gag-pol APOBEC3-driven mutagenesis contributes to the generation of both M184I and E138K mutations in HIV-1 RT in the absence of drug exposure PubMed

Go to the HIV-1, Human Interaction Database

Interactions

Go to the top of the page Help
Products Interactant Other Gene Complex Source Pubs Description

General gene information

Go to the top of the page Help

Markers

Homology

Clone Names

  • MGC74891

Gene Ontology Provided by GOA

Function Evidence Code Pubs
enables RNA binding HDA PubMed 
enables RNA binding IBA
Inferred from Biological aspect of Ancestor
more info
  
enables RNA binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables cytidine deaminase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables cytidine deaminase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables deoxycytidine deaminase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables identical protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables zinc ion binding IDA
Inferred from Direct Assay
more info
 PubMed 
Process Evidence Code Pubs
involved_in DNA cytosine deamination IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in DNA cytosine deamination IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in DNA demethylation IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in base conversion or substitution editing IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in clearance of foreign intracellular DNA IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in cytidine deamination IEA
Inferred from Electronic Annotation
more info
  
involved_in cytidine to uridine editing IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in defense response to virus IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in defense response to virus IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in innate immune response IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in negative regulation of single stranded viral RNA replication via double stranded DNA intermediate IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in negative regulation of single stranded viral RNA replication via double stranded DNA intermediate IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in negative regulation of viral genome replication IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in negative regulation of viral process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in positive regulation of defense response to virus by host IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in positive regulation of gene expression via chromosomal CpG island demethylation IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in retrotransposon silencing IDA
Inferred from Direct Assay
more info
 PubMed 
Component Evidence Code Pubs
is_active_in P-body IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in P-body IDA
Inferred from Direct Assay
more info
 PubMed 
part_of apolipoprotein B mRNA editing enzyme complex TAS
Traceable Author Statement
more info
 PubMed 
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytoplasm IDA
Inferred from Direct Assay
more info
 PubMed 
is_active_in nucleus IBA
Inferred from Biological aspect of Ancestor
more info
  
part_of ribonucleoprotein complex IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

Go to the top of the page Help
Preferred Names
DNA dC->dU-editing enzyme APOBEC-3F
Names
apolipoprotein B editing enzyme catalytic polypeptide-like 3F
apolipoprotein B mRNA editing enzyme cytidine deaminase
apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3F
induced upon T-cell activation
NP_001006667.1
NP_660341.2
XP_016884131.1
XP_047297140.1
XP_047297141.1
XP_054181200.1
XP_054181201.1
XP_054181202.1

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_001006666.2 → NP_001006667.1  DNA dC->dU-editing enzyme APOBEC-3F isoform b

    See identical proteins and their annotated locations for NP_001006667.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (2) contains a distinct 3' UTR and 3' coding region, compared to variant 1. The resulting isoform (b) is shorter and has a distinct C-terminus when compared to isoform a.
    Source sequence(s)
    BM681311, CR456395
    Consensus CDS
    CCDS33649.1
    UniProtKB/Swiss-Prot
    Q8IUX4
    Related
    ENSP00000370977.2, ENST00000381565.2
    Conserved Domains (1) summary
    pfam08210
    Location:17 → 88
    APOBEC_N; APOBEC-like N-terminal domain

  2. NM_145298.6 → NP_660341.2  DNA dC->dU-editing enzyme APOBEC-3F isoform a

    See identical proteins and their annotated locations for NP_660341.2

    Status: REVIEWED

    Description
    Transcript Variant: This variant (1) represents the longer transcript, and encodes the longer isoform (a).
    Source sequence(s)
    AL022318, BC038808, BQ182066, CX165430, DA221480
    Consensus CDS
    CCDS33648.1
    UniProtKB/Swiss-Prot
    B0QYD4, Q45F03, Q6ICH3, Q8IUX4
    UniProtKB/TrEMBL
    M4VR43
    Related
    ENSP00000309749.5, ENST00000308521.10
    Conserved Domains (2) summary
    pfam18772
    Location:195 → 373
    APOBEC2
    pfam18782
    Location:10 → 188
    NAD2; Novel AID APOBEC clade 2

RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2023_10

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p14 Primary Assembly

Genomic

  1. NC_000022.11 Reference GRCh38.p14 Primary Assembly

    Range
    39040864..39055972
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_047441184.1 → XP_047297140.1  DNA dC->dU-editing enzyme APOBEC-3F isoform X1

  2. XM_047441185.1 → XP_047297141.1  DNA dC->dU-editing enzyme APOBEC-3F isoform X2

  3. XM_017028642.3 → XP_016884131.1  DNA dC->dU-editing enzyme APOBEC-3F isoform X3

    UniProtKB/TrEMBL
    B4DGW8

Alternate T2T-CHM13v2.0

Genomic

  1. NC_060946.1 Alternate T2T-CHM13v2.0

    Range
    39511283..39526391
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_054325225.1 → XP_054181200.1  DNA dC->dU-editing enzyme APOBEC-3F isoform X1

  2. XM_054325226.1 → XP_054181201.1  DNA dC->dU-editing enzyme APOBEC-3F isoform X2

  3. XM_054325227.1 → XP_054181202.1  DNA dC->dU-editing enzyme APOBEC-3F isoform X3

Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
Q8IUX4.3 GenPept UniProtKB/Swiss-Prot:Q8IUX4

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

Chemical Information
Molecular Biology Databases
Research Materials
Tools
Miscellaneous