UniProtKB - Q8IUX4 (ABC3F_HUMAN)
DNA dC->dU-editing enzyme APOBEC-3F
APOBEC3F
Functioni
DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Exhibits antiviral activity against Vif-deficient HIV-1 (PubMed:15152192, PubMed:23001005).
After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA. Exhibits antiviral activity also against hepatitis B virus (HBV), equine infectious anemia virus (EIAV), xenotropic MuLV-related virus (XMRV) and simian foamy virus (SFV) and may inhibit the mobility of LTR and non-LTR retrotransposons. May also play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation.
14 PublicationsMiscellaneous
Catalytic activityi
- a 2'-deoxycytidine in single-stranded DNA + H+ + H2O = a 2'-deoxyuridine in single-stranded DNA + NH4+EC:3.5.4.38
Cofactori
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 65 | ZincPROSITE-ProRule annotation | 1 | |
Metal bindingi | 96 | ZincPROSITE-ProRule annotation | 1 | |
Metal bindingi | 99 | ZincPROSITE-ProRule annotation | 1 | |
Metal bindingi | 249 | Zinc; catalyticPROSITE-ProRule annotation | 1 | |
Active sitei | 251 | Proton donorPROSITE-ProRule annotation | 1 | |
Metal bindingi | 280 | Zinc; catalyticPROSITE-ProRule annotation | 1 | |
Metal bindingi | 283 | Zinc; catalyticPROSITE-ProRule annotation | 1 |
GO - Molecular functioni
- cytidine deaminase activity Source: HGNC-UCL
- deoxycytidine deaminase activity Source: GO_Central
- identical protein binding Source: IntAct
- RNA binding Source: HGNC-UCL
- zinc ion binding Source: HGNC-UCL
GO - Biological processi
- base conversion or substitution editing Source: HGNC-UCL
- cytidine to uridine editing Source: GO_Central
- defense response to virus Source: UniProtKB
- DNA cytosine deamination Source: UniProtKB
- DNA demethylation Source: UniProtKB
- innate immune response Source: HGNC-UCL
- negative regulation of single stranded viral RNA replication via double stranded DNA intermediate Source: UniProtKB
- negative regulation of transposition Source: UniProtKB
- negative regulation of viral genome replication Source: UniProtKB
- negative regulation of viral process Source: HGNC-UCL
- positive regulation of defense response to virus by host Source: HGNC-UCL
Keywordsi
Molecular function | Hydrolase |
Biological process | Antiviral defense, Immunity, Innate immunity |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
BRENDAi | 3.5.4.38, 2681 |
PathwayCommonsi | Q8IUX4 |
SignaLinki | Q8IUX4 |
SIGNORi | Q8IUX4 |
Names & Taxonomyi
Protein namesi | Recommended name: DNA dC->dU-editing enzyme APOBEC-3F (EC:3.5.4.38)Alternative name(s): Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3F Short name: A3F |
Gene namesi | Name:APOBEC3F |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:17356, APOBEC3F |
MIMi | 608993, gene |
neXtProti | NX_Q8IUX4 |
VEuPathDBi | HostDB:ENSG00000128394 |
Subcellular locationi
Nucleus
- apolipoprotein B mRNA editing enzyme complex Source: HGNC-UCL
- nucleus Source: GO_Central
Other locations
- cytoplasm Source: UniProtKB
- P-body Source: UniProtKB
- ribonucleoprotein complex Source: UniProtKB
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 67 | E → A: Decrease in cytidine deaminase and antiviral activity; when associated with A-251. 1 Publication | 1 | |
Mutagenesisi | 67 | E → A: No effect on cytidine deaminase and antiviral activity. 1 Publication | 1 | |
Mutagenesisi | 251 | E → A: Decrease in cytidine deaminase and antiviral activity. 1 Publication | 1 | |
Mutagenesisi | 251 | E → A: Decrease in cytidine deaminase and antiviral activity; when associated with A-67. 1 Publication | 1 | |
Mutagenesisi | 251 | E → Q: Remains able to bind Vif. 1 Publication | 1 | |
Mutagenesisi | 255 | L → D: Resistant to HIV-1 Vif and reduces Vif binding but is still efficiently incorporated into the virion. 1 Publication | 1 | |
Mutagenesisi | 258 | F → A: Resistant to HIV-1 Vif and reduces Vif binding but is still efficiently incorporated into the virion. 1 Publication | 1 | |
Mutagenesisi | 259 | C → K: Resistant to HIV-1 Vif and reduces Vif binding but is still efficiently incorporated into the virion. 1 Publication | 1 | |
Mutagenesisi | 262 – 263 | IL → AA: Resistant to HIV-1 Vif and abolishes Vif binding but is still efficiently incorporated into the virion. 1 Publication | 2 | |
Mutagenesisi | 264 | S → D: Resistant to HIV-1 Vif and reduces Vif binding but is still efficiently incorporated into the virion. 1 Publication | 1 | |
Mutagenesisi | 269 | Y → A: Resistant to HIV-1 Vif and reduces Vif binding but is still efficiently incorporated into the virion. 1 Publication | 1 | |
Mutagenesisi | 289 | E → K: Resistant to HIV-1 Vif and reduces Vif binding but is still efficiently incorporated into the virion. 1 Publication | 1 | |
Mutagenesisi | 290 | F → K: Resistant to HIV-1 Vif and reduces Vif binding but is still efficiently incorporated into the virion. 1 Publication | 1 | |
Mutagenesisi | 294 | H → D: Resistant to HIV-1 Vif, reduces Vif binding and abolishes incorporation into the virion. 1 Publication | 1 | |
Mutagenesisi | 324 | E → K or A: Resistant to HIV-1 Vif and reduces Vif binding. 1 Publication | 1 |
Organism-specific databases
DisGeNETi | 200316 |
OpenTargetsi | ENSG00000128394 |
PharmGKBi | PA24896 |
Miscellaneous databases
Pharosi | Q8IUX4, Tbio |
Chemistry databases
ChEMBLi | CHEMBL2007626 |
Genetic variation databases
BioMutai | APOBEC3F |
DMDMi | 161784334 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000171757 | 1 – 373 | DNA dC->dU-editing enzyme APOBEC-3FAdd BLAST | 373 |
Proteomic databases
EPDi | Q8IUX4 |
jPOSTi | Q8IUX4 |
MassIVEi | Q8IUX4 |
MaxQBi | Q8IUX4 |
PaxDbi | Q8IUX4 |
PeptideAtlasi | Q8IUX4 |
PRIDEi | Q8IUX4 |
ProteomicsDBi | 70623 [Q8IUX4-1] 70624 [Q8IUX4-2] 70625 [Q8IUX4-3] |
PTM databases
iPTMneti | Q8IUX4 |
PhosphoSitePlusi | Q8IUX4 |
Expressioni
Tissue specificityi
Inductioni
Gene expression databases
Bgeei | ENSG00000128394, Expressed in muscle tissue and 150 other tissues |
Genevisiblei | Q8IUX4, HS |
Organism-specific databases
HPAi | ENSG00000128394, Low tissue specificity |
Interactioni
Subunit structurei
Binary interactionsi
Q8IUX4
With | #Exp. | IntAct |
---|---|---|
itself | 2 | EBI-11306991,EBI-11306991 |
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 128319, 146 interactors |
DIPi | DIP-59966N |
IntActi | Q8IUX4, 13 interactors |
STRINGi | 9606.ENSP00000309749 |
Miscellaneous databases
RNActi | Q8IUX4, protein |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | Q8IUX4 |
SMRi | Q8IUX4 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 29 – 137 | CMP/dCMP-type deaminase 1PROSITE-ProRule annotationAdd BLAST | 109 | |
Domaini | 174 – 321 | CMP/dCMP-type deaminase 2PROSITE-ProRule annotationAdd BLAST | 148 |
Domaini
Sequence similaritiesi
Keywords - Domaini
RepeatPhylogenomic databases
eggNOGi | KOG4075, Eukaryota |
GeneTreei | ENSGT00940000162695 |
HOGENOMi | CLU_047918_0_0_1 |
OMAi | PWNGLNE |
PhylomeDBi | Q8IUX4 |
TreeFami | TF331356 |
Family and domain databases
InterProi | View protein in InterPro IPR016192, APOBEC/CMP_deaminase_Zn-bd IPR002125, CMP_dCMP_dom IPR016193, Cytidine_deaminase-like |
SUPFAMi | SSF53927, SSF53927, 2 hits |
PROSITEi | View protein in PROSITE PS00903, CYT_DCMP_DEAMINASES_1, 2 hits PS51747, CYT_DCMP_DEAMINASES_2, 2 hits |
s (3)i Sequence
Sequence statusi: Complete.
This entry describes 3 produced by isoformsialternative splicing. AlignAdd to basketThis isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MKPHFRNTVE RMYRDTFSYN FYNRPILSRR NTVWLCYEVK TKGPSRPRLD
60 70 80 90 100
AKIFRGQVYS QPEHHAEMCF LSWFCGNQLP AYKCFQITWF VSWTPCPDCV
110 120 130 140 150
AKLAEFLAEH PNVTLTISAA RLYYYWERDY RRALCRLSQA GARVKIMDDE
160 170 180 190 200
EFAYCWENFV YSEGQPFMPW YKFDDNYAFL HRTLKEILRN PMEAMYPHIF
210 220 230 240 250
YFHFKNLRKA YGRNESWLCF TMEVVKHHSP VSWKRGVFRN QVDPETHCHA
260 270 280 290 300
ERCFLSWFCD DILSPNTNYE VTWYTSWSPC PECAGEVAEF LARHSNVNLT
310 320 330 340 350
IFTARLYYFW DTDYQEGLRS LSQEGASVEI MGYKDFKYCW ENFVYNDDEP
360 370
FKPWKGLKYN FLFLDSKLQE ILE
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_038355 | 48 | R → P1 PublicationCorresponds to variant dbSNP:rs35053197Ensembl. | 1 | |
Natural variantiVAR_018145 | 61 | Q → L. Corresponds to variant dbSNP:rs2076109Ensembl. | 1 | |
Natural variantiVAR_018146 | 97 | P → L. Corresponds to variant dbSNP:rs201939303Ensembl. | 1 | |
Natural variantiVAR_018147 | 108 | A → S1 PublicationCorresponds to variant dbSNP:rs2020390Ensembl. | 1 | |
Natural variantiVAR_025058 | 178 | A → T1 PublicationCorresponds to variant dbSNP:rs34182094Ensembl. | 1 | |
Natural variantiVAR_018148 | 231 | V → I1 PublicationCorresponds to variant dbSNP:rs2076101Ensembl. | 1 | |
Natural variantiVAR_025059 | 307 | Y → C1 PublicationCorresponds to variant dbSNP:rs12157816EnsemblClinVar. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_009803 | 58 – 79 | VYSQP…CGNQL → VPPGLQSLCRQELSQLGKQT TH in isoform 2. 1 PublicationAdd BLAST | 22 | |
Alternative sequenceiVSP_042754 | 59 – 113 | YSQPE…EHPNV → PRSFIRAPFQVLSSPFGQCA PPHGTAQVQWPPQLTAGREQ GRP in isoform 3. 1 PublicationAdd BLAST | 55 | |
Alternative sequenceiVSP_009804 | 80 – 373 | Missing in isoform 2. 1 PublicationAdd BLAST | 294 | |
Alternative sequenceiVSP_042755 | 114 – 373 | Missing in isoform 3. 1 PublicationAdd BLAST | 260 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CR456395 mRNA Translation: CAG30281.1 DQ146365 Genomic DNA Translation: AAZ38720.1 AL022318 Genomic DNA No translation available. CH471095 Genomic DNA Translation: EAW60288.1 CH471095 Genomic DNA Translation: EAW60289.1 BC038808 mRNA Translation: AAH38808.1 BC061914 mRNA Translation: AAH61914.1 |
CCDSi | CCDS33648.1 [Q8IUX4-1] CCDS33649.1 [Q8IUX4-3] |
RefSeqi | NP_001006667.1, NM_001006666.1 [Q8IUX4-3] NP_660341.2, NM_145298.5 [Q8IUX4-1] XP_016884132.1, XM_017028643.1 [Q8IUX4-3] |
Genome annotation databases
Ensembli | ENST00000308521.10; ENSP00000309749.5; ENSG00000128394.17 ENST00000381565.2; ENSP00000370977.2; ENSG00000128394.17 [Q8IUX4-3] |
GeneIDi | 200316 |
KEGGi | hsa:200316 |
MANE-Selecti | ENST00000308521.10; ENSP00000309749.5; NM_145298.6; NP_660341.2 |
UCSCi | uc003awv.4, human [Q8IUX4-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Web resourcesi
SeattleSNPs |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CR456395 mRNA Translation: CAG30281.1 DQ146365 Genomic DNA Translation: AAZ38720.1 AL022318 Genomic DNA No translation available. CH471095 Genomic DNA Translation: EAW60288.1 CH471095 Genomic DNA Translation: EAW60289.1 BC038808 mRNA Translation: AAH38808.1 BC061914 mRNA Translation: AAH61914.1 |
CCDSi | CCDS33648.1 [Q8IUX4-1] CCDS33649.1 [Q8IUX4-3] |
RefSeqi | NP_001006667.1, NM_001006666.1 [Q8IUX4-3] NP_660341.2, NM_145298.5 [Q8IUX4-1] XP_016884132.1, XM_017028643.1 [Q8IUX4-3] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3WUS | X-ray | 2.54 | A/B | 187-373 | [»] | |
4IOU | X-ray | 2.75 | A/B/C/D | 185-373 | [»] | |
4J4J | X-ray | 3.10 | A/B | 218-373 | [»] | |
5HX4 | X-ray | 1.92 | A/B | 185-373 | [»] | |
5HX5 | X-ray | 2.33 | A/B | 185-373 | [»] | |
5W2M | X-ray | 3.70 | A/B/C/D/J/K/L/M | 190-373 | [»] | |
5ZVB | X-ray | 2.00 | A/B | 220-373 | [»] | |
6NIL | electron microscopy | 3.90 | A/D/G/J | 185-373 | [»] | |
AlphaFoldDBi | Q8IUX4 | |||||
SMRi | Q8IUX4 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 128319, 146 interactors |
DIPi | DIP-59966N |
IntActi | Q8IUX4, 13 interactors |
STRINGi | 9606.ENSP00000309749 |
Chemistry databases
ChEMBLi | CHEMBL2007626 |
PTM databases
iPTMneti | Q8IUX4 |
PhosphoSitePlusi | Q8IUX4 |
Genetic variation databases
BioMutai | APOBEC3F |
DMDMi | 161784334 |
Proteomic databases
EPDi | Q8IUX4 |
jPOSTi | Q8IUX4 |
MassIVEi | Q8IUX4 |
MaxQBi | Q8IUX4 |
PaxDbi | Q8IUX4 |
PeptideAtlasi | Q8IUX4 |
PRIDEi | Q8IUX4 |
ProteomicsDBi | 70623 [Q8IUX4-1] 70624 [Q8IUX4-2] 70625 [Q8IUX4-3] |
Protocols and materials databases
Antibodypediai | 34783, 202 antibodies from 21 providers |
DNASUi | 200316 |
Genome annotation databases
Ensembli | ENST00000308521.10; ENSP00000309749.5; ENSG00000128394.17 ENST00000381565.2; ENSP00000370977.2; ENSG00000128394.17 [Q8IUX4-3] |
GeneIDi | 200316 |
KEGGi | hsa:200316 |
MANE-Selecti | ENST00000308521.10; ENSP00000309749.5; NM_145298.6; NP_660341.2 |
UCSCi | uc003awv.4, human [Q8IUX4-1] |
Organism-specific databases
CTDi | 200316 |
DisGeNETi | 200316 |
GeneCardsi | APOBEC3F |
HGNCi | HGNC:17356, APOBEC3F |
HPAi | ENSG00000128394, Low tissue specificity |
MIMi | 608993, gene |
neXtProti | NX_Q8IUX4 |
OpenTargetsi | ENSG00000128394 |
PharmGKBi | PA24896 |
VEuPathDBi | HostDB:ENSG00000128394 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG4075, Eukaryota |
GeneTreei | ENSGT00940000162695 |
HOGENOMi | CLU_047918_0_0_1 |
OMAi | PWNGLNE |
PhylomeDBi | Q8IUX4 |
TreeFami | TF331356 |
Enzyme and pathway databases
BRENDAi | 3.5.4.38, 2681 |
PathwayCommonsi | Q8IUX4 |
SignaLinki | Q8IUX4 |
SIGNORi | Q8IUX4 |
Miscellaneous databases
BioGRID-ORCSi | 200316, 13 hits in 1019 CRISPR screens |
ChiTaRSi | APOBEC3F, human |
GeneWikii | APOBEC3F |
GenomeRNAii | 200316 |
Pharosi | Q8IUX4, Tbio |
PROi | PR:Q8IUX4 |
RNActi | Q8IUX4, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000128394, Expressed in muscle tissue and 150 other tissues |
Genevisiblei | Q8IUX4, HS |
Family and domain databases
InterProi | View protein in InterPro IPR016192, APOBEC/CMP_deaminase_Zn-bd IPR002125, CMP_dCMP_dom IPR016193, Cytidine_deaminase-like |
SUPFAMi | SSF53927, SSF53927, 2 hits |
PROSITEi | View protein in PROSITE PS00903, CYT_DCMP_DEAMINASES_1, 2 hits PS51747, CYT_DCMP_DEAMINASES_2, 2 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | ABC3F_HUMAN | |
Accessioni | Q8IUX4Primary (citable) accession number: Q8IUX4 Secondary accession number(s): B0QYD4 Q7Z2N5 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 29, 2004 |
Last sequence update: | October 23, 2007 | |
Last modified: | May 25, 2022 | |
This is version 167 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Human chromosome 22
Human chromosome 22: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families