APOBEC3F
entrez
200316
canonical
uniprot
Q8IUX4
canonical
ensembl
ENSG00000128394
resolver
ensp
ENSP00000309749
resolver
ensp
ENSP00000370977
resolver
ensp
ENSP00000659108
resolver
genesymbol
APOBEC3F
resolver
hgnc
HGNC:17356
resolver
uniprot
B0QYD4
resolver
uniprot
Q45F03
resolver
uniprot
Q6ICH3
resolver
uniprot
Q7Z2N2
resolver
uniprot
Q7Z2N5
resolver
uniprot_entry
ABC3F_HUMAN
resolver
uniprot_sec
B0QYD4
resolver
uniprot_sec
Q45F03
resolver
uniprot_sec
Q6ICH3
resolver
uniprot_sec
Q7Z2N2
resolver
uniprot_sec
Q7Z2N5
resolver
activity_regulation
ACTIVITY REGULATION: (Microbial infection) Antiviral activity is neutralized by the HIV-1 virion infectivity factor (Vif), that prevents its incorporation into progeny virions by both inhibiting its translation and/or by inducing its ubiquitination and subsequent degradation by the 26S proteasome. {ECO:0000269|PubMed:21835787, ECO:0000269|PubMed:22190037, ECO:0000269|PubMed:31792451}.
uniprot
proteins
amino_acid_sequence
MKPHFRNTVERMYRDTFSYNFYNRPILSRRNTVWLCYEVKTKGPSRPRLDAKIFRGQVYSQPEHHAEMCFLSWFCGNQLPAYKCFQITWFVSWTPCPDCVAKLAEFLAEHPNVTLTISAARLYYYWERDYRRALCRLSQAGARVKIMDDEEFAYCWENFVYSEGQPFMPWYKFDDNYAFLHRTLKEILRNPMEAMYPHIFYFHFKNLRKAYGRNESWLCFTMEVVKHHSPVSWKRGVFRNQVDPETHCHAERCFLSWFCDDILSPNTNYEVTWYTSWSPCPECAGEVAEFLARHSNVNLTIFTARLYYFWDTDYQEGLRSLSQEGASVEIMGYKDFKYCWENFVYNDDEPFKPWKGLKYNFLFLDSKLQEILE
uniprot
proteins
ec_number
3.5.4.38
uniprot
proteins
function
FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms (PubMed:15141007, PubMed:17121840, PubMed:20062055, PubMed:22915799, PubMed:34774569). Exhibits antiviral activity against viruse such as HIV-1 or HIV-2 (PubMed:15141007, PubMed:15152192, PubMed:17121840, PubMed:20219927, PubMed:21835787, PubMed:22807680, PubMed:23001005, PubMed:23097438, PubMed:23152537, PubMed:34774569). 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 (PubMed:15141007). 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 (PubMed:15141007). Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA (PubMed:15141007). 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 (PubMed:16378963, PubMed:16527742, PubMed:19458006, PubMed:20062055, PubMed:20335265). May also play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation (PubMed:21496894). {ECO:0000269|PubMed:15141007, ECO:0000269|PubMed:15152192, ECO:0000269|PubMed:16378963, ECO:0000269|PubMed:16527742, ECO:0000269|PubMed:17121840, ECO:0000269|PubMed:19458006, ECO:0000269|PubMed:20062055, ECO:0000269|PubMed:20219927, ECO:0000269|PubMed:20335265, ECO:0000269|PubMed:21496894, ECO:0000269|PubMed:21835787, ECO:0000269|PubMed:22807680, ECO:0000269|PubMed:22915799, ECO:0000269|PubMed:23001005, ECO:0000269|PubMed:23097438, ECO:0000269|PubMed:23152537, ECO:0000269|PubMed:34774569}.
uniprot
proteins
mass_dalton
45020
uniprot
proteins
mutagenesis
MUTAGEN 65; /note="H->C: Reduced but not abolished antiviral activity."; /evidence="ECO:0000269|PubMed:17121840"; MUTAGEN 65; /note="H->R: Nearly abolished antiviral activity; when associated with R-249."; /evidence="ECO:0000269|PubMed:17121840"; MUTAGEN 67; /note="E->A: Decrease in cytidine deaminase and antiviral activity; when associated with A-251."; /evidence="ECO:0000269|PubMed:17020885"; MUTAGEN 67; /note="E->A: No effect on cytidine deaminase and antiviral activity."; /evidence="ECO:0000269|PubMed:17020885"; MUTAGEN 67; /note="E->Q: Reduced but not abolished antiviral activity. Nearly abolished antiviral activity; when associated with Q-251."; /evidence="ECO:0000269|PubMed:17121840"; MUTAGEN 96; /note="Missing: Reduced but not abolished antiviral activity. Nearly abolished antiviral activity; when associated with Q-280."; /evidence="ECO:0000269|PubMed:17121840"; MUTAGEN 99; /note="C->S: Reduced but not abolished antiviral activityy. Nearly abolished antiviral activity; when associated with S-283."; /evidence="ECO:0000269|PubMed:17121840"; MUTAGEN 249; /note="H->C: Reduced but not abolished antiviral activity."; /evidence="ECO:0000269|PubMed:17121840"; MUTAGEN 249; /note="H->R: Nearly abolished antiviral activity; when associated with R-65."; /evidence="ECO:0000269|PubMed:17121840"; MUTAGEN 251; /note="E->A: Decrease in cytidine deaminase and antiviral activity."; /evidence="ECO:0000269|PubMed:17020885"; MUTAGEN 251; /note="E->A: Decrease in cytidine deaminase and antiviral activity; when associated with A-67."; /evidence="ECO:0000269|PubMed:17020885"; MUTAGEN 251; /note="E->Q: Remains able to bind Vif."; /evidence="ECO:0000269|PubMed:23001005"; MUTAGEN 251; /note="Missing: Reduced but not abolished antiviral activity. Nearly abolished antiviral activity; when associated with Q-67."; /evidence="ECO:0000269|PubMed:17121840"; MUTAGEN 255; /note="L->D: Resistant to HIV-1 Vif and reduces Vif binding but is still efficiently incorporated into the virion."; /evidence="ECO:0000269|PubMed:23001005"; MUTAGEN 258; /note="F->A: Resistant to HIV-1 Vif and reduces Vif binding but is still efficiently incorporated into the virion."; /evidence="ECO:0000269|PubMed:23001005"; MUTAGEN 259; /note="C->K: Resistant to HIV-1 Vif and reduces Vif binding but is still efficiently incorporated into the virion."; /evidence="ECO:0000269|PubMed:23001005"; MUTAGEN 260..261; /note="DD->RR: Does not affect interaction with APOBEC3G."; /evidence="ECO:0000269|PubMed:31792451"; MUTAGEN 262..263; /note="IL->AA: Resistant to HIV-1 Vif and abolishes Vif binding but is still efficiently incorporated into the virion."; /evidence="ECO:0000269|PubMed:23001005"; MUTAGEN 264; /note="S->D: Resistant to HIV-1 Vif and reduces Vif binding but is still efficiently incorporated into the virion."; /evidence="ECO:0000269|PubMed:23001005"; MUTAGEN 265; /note="P->A: Impaired interaction with HIV-1 Vif protein."; /evidence="ECO:0000269|PubMed:31792451"; MUTAGEN 269; /note="Y->A: Resistant to HIV-1 Vif and reduces Vif binding but is still efficiently incorporated into the virion."; /evidence="ECO:0000269|PubMed:23001005"; MUTAGEN 280; /note="C->S: Reduced but not abolished antiviral activity. Nearly abolished antiviral activity; when associated with Q-96."; /evidence="ECO:0000269|PubMed:17121840"; MUTAGEN 283; /note="C->S: Reduced but not abolished antiviral activity. Nearly abolished antiviral activity; when associated with S-99."; /evidence="ECO:0000269|PubMed:17121840"; MUTAGEN 289; /note="E->K: Abolished interaction with HIV-1 Vif protein. Resistant to HIV-1 Vif and reduces Vif binding but is still efficiently incorporated into the virion."; /evidence="ECO:0000269|PubMed:23001005, ECO:0000269|PubMed:31792451"; MUTAGEN 290; /note="F->K: Resistant to HIV-1 Vif and reduces Vif binding but is still efficiently incorporated into the virion."; /evidence="ECO:0000269|PubMed:23001005"; MUTAGEN 293; /note="R->D: Abolished interaction with HIV-1 Vif protein."; /evidence="ECO:0000269|PubMed:31792451"; MUTAGEN 294; /note="H->D: Resistant to HIV-1 Vif, reduces Vif binding and abolishes incorporation into the virion."; /evidence="ECO:0000269|PubMed:23001005"; MUTAGEN 324; /note="E->K,A: Resistant to HIV-1 Vif and reduces Vif binding."; /evidence="ECO:0000269|PubMed:23001005"; MUTAGEN 324; /note="E->R: Abolished interaction with HIV-1 Vif protein."; /evidence="ECO:0000269|PubMed:31792451"; MUTAGEN 347; /note="D->R: Does not affect interaction with HIV-1 Vif protein."; /evidence="ECO:0000269|PubMed:31792451
uniprot
proteins
post_translational_modification
PTM: (Microbial infection) Following infection by HIV-1, ubiquitinated by a cullin-5-RING E3 ubiquitin-protein ligase complex (ECS complex) hijacked by the HIV-1 Vif protein, leading to its degradation. {ECO:0000269|PubMed:22190037, ECO:0000269|PubMed:31792451}.
uniprot
proteins
protein_family
Cytidine and deoxycytidylate deaminase family
uniprot
proteins
pubmed
10591208
uniprot
proteins
pubmed
11863358
uniprot
proteins
pubmed
12683974
uniprot
proteins
pubmed
15141007
uniprot
proteins
pubmed
15152192
uniprot
proteins
pubmed
15461802
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16378963
uniprot
proteins
pubmed
16527742
uniprot
proteins
pubmed
16699599
uniprot
proteins
pubmed
17020885
uniprot
proteins
pubmed
17121840
uniprot
proteins
pubmed
18304004
uniprot
proteins
pubmed
18448976
uniprot
proteins
pubmed
19458006
uniprot
proteins
pubmed
20062055
uniprot
proteins
pubmed
20219927
uniprot
proteins
pubmed
20308164
uniprot
proteins
pubmed
20335265
uniprot
proteins
pubmed
21496894
uniprot
proteins
pubmed
21835787
uniprot
proteins
pubmed
22001110
uniprot
proteins
pubmed
22190037
uniprot
proteins
pubmed
22807680
uniprot
proteins
pubmed
22912627
uniprot
proteins
pubmed
22915799
uniprot
proteins
pubmed
23001005
uniprot
proteins
pubmed
23097438
uniprot
proteins
pubmed
23152537
uniprot
proteins
pubmed
23318957
uniprot
proteins
pubmed
27139641
uniprot
proteins
pubmed
31792451
uniprot
proteins
pubmed
34774569
uniprot
proteins
sequence_length
373
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16527742, ECO:0000269|PubMed:16699599, ECO:0000269|PubMed:21835787}. Cytoplasm, P-body {ECO:0000269|PubMed:16699599, ECO:0000269|PubMed:22915799}.
uniprot
proteins