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DNA dC->dU-editing enzyme APOBEC-3F (EC 3.5.4.-) (Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3F) (A3F)

 ABC3F_HUMAN             Reviewed;         373 AA.
Q8IUX4; B0QYD4; Q45F03; Q6ICH3; Q7Z2N2; Q7Z2N5;
29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
23-OCT-2007, sequence version 3.
07-NOV-2018, entry version 145.
RecName: Full=DNA dC->dU-editing enzyme APOBEC-3F;
EC=3.5.4.-;
AltName: Full=Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3F;
Short=A3F;
Name=APOBEC3F;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS THR-178;
ILE-231 AND CYS-307.
SeattleSNPs variation discovery resource;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
VARIANTS PRO-48 AND SER-108.
TISSUE=Pancreas, Spleen, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
GENE FAMILY ORGANIZATION, AND TISSUE SPECIFICITY.
PubMed=11863358; DOI=10.1006/geno.2002.6718;
Jarmuz A., Chester A., Bayliss J., Gisbourne J., Dunham I., Scott J.,
Navaratnam N.;
"An anthropoid-specific locus of orphan C to U RNA-editing enzymes on
chromosome 22.";
Genomics 79:285-296(2002).
[7]
REVIEW ON APOBEC FAMILIES.
PubMed=12683974; DOI=10.1016/S0168-9525(03)00054-4;
Wedekind J.E., Dance G.S.C., Sowden M.P., Smith H.C.;
"Messenger RNA editing in mammals: new members of the APOBEC family
seeking roles in the family business.";
Trends Genet. 19:207-216(2003).
[8]
FUNCTION IN HIV-1 INFECTIVITY, AND TISSUE SPECIFICITY.
PubMed=15152192; DOI=10.1038/sj.emboj.7600246;
Wiegand H.L., Doehle B.P., Bogerd H.P., Cullen B.R.;
"A second human antiretroviral factor, APOBEC3F, is suppressed by the
HIV-1 and HIV-2 Vif proteins.";
EMBO J. 23:2451-2458(2004).
[9]
FUNCTION IN RETROTRANSPOSITION, AND SUBCELLULAR LOCATION.
PubMed=16527742; DOI=10.1016/j.cub.2006.01.031;
Chen H., Lilley C.E., Yu Q., Lee D.V., Chou J., Narvaiza I.,
Landau N.R., Weitzman M.D.;
"APOBEC3A is a potent inhibitor of adeno-associated virus and
retrotransposons.";
Curr. Biol. 16:480-485(2006).
[10]
DOMAIN CMP/DCMP DEAMINASE, AND MUTAGENESIS OF GLU-67 AND GLU-251.
PubMed=17020885; DOI=10.1074/jbc.M604980200;
Hakata Y., Landau N.R.;
"Reversed functional organization of mouse and human APOBEC3 cytidine
deaminase domains.";
J. Biol. Chem. 281:36624-36631(2006).
[11]
FUNCTION IN SFV RESTRICTION.
PubMed=16378963; DOI=10.1128/JVI.80.2.605-614.2006;
Delebecque F., Suspene R., Calattini S., Casartelli N., Saib A.,
Froment A., Wain-Hobson S., Gessain A., Vartanian J.P., Schwartz O.;
"Restriction of foamy viruses by APOBEC cytidine deaminases.";
J. Virol. 80:605-614(2006).
[12]
SUBCELLULAR LOCATION, AND INTERACTION WITH APOBEC3G.
PubMed=16699599; DOI=10.1371/journal.ppat.0020041;
Wichroski M.J., Robb G.B., Rana T.M.;
"Human retroviral host restriction factors APOBEC3G and APOBEC3F
localize to mRNA processing bodies.";
PLoS Pathog. 2:E41-E41(2006).
[13]
REVIEW.
PubMed=18304004; DOI=10.1146/annurev.immunol.26.021607.090350;
Chiu Y.L., Greene W.C.;
"The APOBEC3 cytidine deaminases: an innate defensive network opposing
exogenous retroviruses and endogenous retroelements.";
Annu. Rev. Immunol. 26:317-353(2008).
[14]
REVIEW ON FUNCTION IN HBV RESTRICTION.
PubMed=18448976; DOI=10.1097/QCO.0b013e3282fe1bb2;
Bonvin M., Greeve J.;
"Hepatitis B: modern concepts in pathogenesis--APOBEC3 cytidine
deaminases as effectors in innate immunity against the hepatitis B
virus.";
Curr. Opin. Infect. Dis. 21:298-303(2008).
[15]
FUNCTION IN EIAV RESTRICTION.
PubMed=19458006; DOI=10.1128/JVI.00015-09;
Zielonka J., Bravo I.G., Marino D., Conrad E., Perkovic M.,
Battenberg M., Cichutek K., Muenk C.;
"Restriction of equine infectious anemia virus by equine APOBEC3
cytidine deaminases.";
J. Virol. 83:7547-7559(2009).
[16]
FUNCTION IN HIV-1 RESTRICTION.
PubMed=20219927; DOI=10.1128/JVI.02358-09;
Mbisa J.L., Bu W., Pathak V.K.;
"APOBEC3F and APOBEC3G inhibit HIV-1 DNA integration by different
mechanisms.";
J. Virol. 84:5250-5259(2010).
[17]
FUNCTION IN XMRV RESTRICTION.
PubMed=20335265; DOI=10.1128/JVI.00134-10;
Paprotka T., Venkatachari N.J., Chaipan C., Burdick R.,
Delviks-Frankenberry K.A., Hu W.S., Pathak V.K.;
"Inhibition of xenotropic murine leukemia virus-related virus by
APOBEC3 proteins and antiviral drugs.";
J. Virol. 84:5719-5729(2010).
[18]
FUNCTION IN RETROTRANSPOSITION.
PubMed=20062055; DOI=10.1038/nsmb.1744;
Stenglein M.D., Burns M.B., Li M., Lengyel J., Harris R.S.;
"APOBEC3 proteins mediate the clearance of foreign DNA from human
cells.";
Nat. Struct. Mol. Biol. 17:222-229(2010).
[19]
TISSUE SPECIFICITY.
PubMed=20308164; DOI=10.1093/nar/gkq174;
Refsland E.W., Stenglein M.D., Shindo K., Albin J.S., Brown W.L.,
Harris R.S.;
"Quantitative profiling of the full APOBEC3 mRNA repertoire in
lymphocytes and tissues: implications for HIV-1 restriction.";
Nucleic Acids Res. 38:4274-4284(2010).
[20]
FUNCTION IN DNA DEMETHYLATION.
PubMed=21496894; DOI=10.1016/j.cell.2011.03.022;
Guo J.U., Su Y., Zhong C., Ming G.L., Song H.;
"Hydroxylation of 5-methylcytosine by TET1 promotes active DNA
demethylation in the adult brain.";
Cell 145:423-434(2011).
[21]
FUNCTION IN HIV-1 RESTRICTION, SUBCELLULAR LOCATION, AND ACTIVITY
REGULATION.
PubMed=21835787; DOI=10.1128/JVI.05238-11;
Hultquist J.F., Lengyel J.A., Refsland E.W., LaRue R.S., Lackey L.,
Brown W.L., Harris R.S.;
"Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H
demonstrate a conserved capacity to restrict Vif-deficient HIV-1.";
J. Virol. 85:11220-11234(2011).
[22]
REVIEW.
PubMed=22912627; DOI=10.3389/fmicb.2012.00275;
Arias J.F., Koyama T., Kinomoto M., Tokunaga K.;
"Retroelements versus APOBEC3 family members: No great escape from the
magnificent seven.";
Front. Microbiol. 3:275-275(2012).
[23]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH AGO1; AGO2 AND
AGO3.
PubMed=22915799; DOI=10.1128/JVI.00595-12;
Phalora P.K., Sherer N.M., Wolinsky S.M., Swanson C.M., Malim M.H.;
"HIV-1 replication and APOBEC3 antiviral activity are not regulated by
P bodies.";
J. Virol. 86:11712-11724(2012).
[24]
FUNCTION IN HIV-1 RESTRICTION.
PubMed=22807680; DOI=10.1371/journal.ppat.1002800;
Refsland E.W., Hultquist J.F., Harris R.S.;
"Endogenous origins of HIV-1 G-to-A hypermutation and restriction in
the nonpermissive T cell line CEM2n.";
PLoS Pathog. 8:E1002800-E1002800(2012).
[25]
REVIEW.
PubMed=22001110; DOI=10.1016/j.semcdb.2011.10.004;
Smith H.C., Bennett R.P., Kizilyer A., McDougall W.M., Prohaska K.M.;
"Functions and regulation of the APOBEC family of proteins.";
Semin. Cell Dev. Biol. 23:258-268(2012).
[26]
FUNCTION IN HIV-1 RESTRICTION.
PubMed=23097438; DOI=10.1128/JVI.00676-12;
Chaipan C., Smith J.L., Hu W.S., Pathak V.K.;
"APOBEC3G restricts HIV-1 to a greater extent than APOBEC3F and
APOBEC3DE in human primary CD4+ t cells and macrophages.";
J. Virol. 87:444-453(2013).
[27]
FUNCTION IN HIV-1 RESTRICTION.
PubMed=23152537; DOI=10.1128/JVI.02587-12;
Gillick K., Pollpeter D., Phalora P., Kim E.Y., Wolinsky S.M.,
Malim M.H.;
"The suppression of HIV-1 infection by APOBEC3 proteins in primary
human CD4+ T cells is associated with the inhibition of processive
reverse transcription as well as excessive cytidine deamination.";
J. Virol. 87:1508-1517(2013).
-!- FUNCTION: 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. 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.
{ECO:0000269|PubMed:15152192, ECO:0000269|PubMed:16378963,
ECO:0000269|PubMed:16527742, 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:23097438,
ECO:0000269|PubMed:23152537}.
-!- CATALYTIC ACTIVITY: Cytidine + H(2)O = uridine + NH(3).
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
-!- ACTIVITY REGULATION: 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}.
-!- SUBUNIT: Binds HIV-1 Vif. In the absence of Vif protein,
specifically packaged into HIV-1 virions. Interacts with APOBEC3G
in an RNA-dependent manner. Interacts with AGO1, AGO2 and AGO3.
{ECO:0000269|PubMed:16699599, ECO:0000269|PubMed:22915799}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-11306991, EBI-11306991;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, P-body.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8IUX4-1; Sequence=Displayed;
Name=2;
IsoId=Q8IUX4-2; Sequence=VSP_009803, VSP_009804;
Note=May be due to a competing donor splice site. No
experimental confirmation available.;
Name=3;
IsoId=Q8IUX4-3; Sequence=VSP_042754, VSP_042755;
-!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in ovary.
{ECO:0000269|PubMed:11863358, ECO:0000269|PubMed:15152192,
ECO:0000269|PubMed:20308164}.
-!- INDUCTION: Up-regulated by IFN-alpha.
-!- DOMAIN: The CMP/dCMP deaminase domain 1 mediates RNA binding, RNA-
dependent oligomerization and virion incorporation whereas the
CMP/dCMP deaminase domain 2 confers deoxycytidine deaminase
activity and substrate sequence specificity.
{ECO:0000269|PubMed:17020885}.
-!- MISCELLANEOUS: It is one of seven related genes or pseudogenes
found in a cluster, thought to result from gene duplication, on
chromosome 22.
-!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/apobec3f/";
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EMBL; CR456395; CAG30281.1; -; mRNA.
EMBL; DQ146365; AAZ38720.1; -; Genomic_DNA.
EMBL; AL022318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471095; EAW60288.1; -; Genomic_DNA.
EMBL; CH471095; EAW60289.1; -; Genomic_DNA.
EMBL; BC038808; AAH38808.1; -; mRNA.
EMBL; BC061914; AAH61914.1; -; mRNA.
CCDS; CCDS33648.1; -. [Q8IUX4-1]
CCDS; CCDS33649.1; -. [Q8IUX4-3]
RefSeq; NP_001006667.1; NM_001006666.1. [Q8IUX4-3]
RefSeq; NP_660341.2; NM_145298.5. [Q8IUX4-1]
RefSeq; XP_016884132.1; XM_017028643.1. [Q8IUX4-3]
UniGene; Hs.659809; -.
UniGene; Hs.660143; -.
PDB; 3WUS; X-ray; 2.54 A; A/B=187-373.
PDB; 4IOU; X-ray; 2.75 A; A/B/C/D=185-373.
PDB; 4J4J; X-ray; 3.10 A; A/B=218-373.
PDB; 5HX4; X-ray; 1.92 A; A/B=185-373.
PDB; 5HX5; X-ray; 2.33 A; A/B=185-373.
PDB; 5W2M; X-ray; 3.70 A; A/B/C/D/J/K/L/M=190-373.
PDBsum; 3WUS; -.
PDBsum; 4IOU; -.
PDBsum; 4J4J; -.
PDBsum; 5HX4; -.
PDBsum; 5HX5; -.
PDBsum; 5W2M; -.
ProteinModelPortal; Q8IUX4; -.
SMR; Q8IUX4; -.
BioGrid; 128319; 11.
DIP; DIP-59966N; -.
IntAct; Q8IUX4; 7.
STRING; 9606.ENSP00000309749; -.
ChEMBL; CHEMBL2007626; -.
iPTMnet; Q8IUX4; -.
PhosphoSitePlus; Q8IUX4; -.
BioMuta; APOBEC3F; -.
DMDM; 161784334; -.
EPD; Q8IUX4; -.
MaxQB; Q8IUX4; -.
PaxDb; Q8IUX4; -.
PeptideAtlas; Q8IUX4; -.
PRIDE; Q8IUX4; -.
ProteomicsDB; 70623; -.
ProteomicsDB; 70624; -. [Q8IUX4-2]
ProteomicsDB; 70625; -. [Q8IUX4-3]
DNASU; 200316; -.
Ensembl; ENST00000308521; ENSP00000309749; ENSG00000128394. [Q8IUX4-1]
Ensembl; ENST00000381565; ENSP00000370977; ENSG00000128394. [Q8IUX4-3]
GeneID; 200316; -.
KEGG; hsa:200316; -.
UCSC; uc003awv.4; human. [Q8IUX4-1]
CTD; 200316; -.
DisGeNET; 200316; -.
EuPathDB; HostDB:ENSG00000128394.16; -.
GeneCards; APOBEC3F; -.
H-InvDB; HIX0213264; -.
HGNC; HGNC:17356; APOBEC3F.
HPA; HPA073637; -.
MIM; 608993; gene.
neXtProt; NX_Q8IUX4; -.
OpenTargets; ENSG00000128394; -.
PharmGKB; PA24896; -.
eggNOG; ENOG410JBA1; Eukaryota.
eggNOG; ENOG41119MS; LUCA.
GeneTree; ENSGT00530000062933; -.
HOGENOM; HOG000033755; -.
HOVERGEN; HBG050434; -.
KO; K18750; -.
OMA; FEYCWDN; -.
OrthoDB; EOG091G07EI; -.
PhylomeDB; Q8IUX4; -.
TreeFam; TF331356; -.
ChiTaRS; APOBEC3F; human.
GeneWiki; APOBEC3F; -.
GenomeRNAi; 200316; -.
PRO; PR:Q8IUX4; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000128394; Expressed in 130 organ(s), highest expression level in leukocyte.
CleanEx; HS_APOBEC3F; -.
Genevisible; Q8IUX4; HS.
GO; GO:0030895; C:apolipoprotein B mRNA editing enzyme complex; TAS:HGNC.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0000932; C:P-body; IDA:UniProtKB.
GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0004126; F:cytidine deaminase activity; IDA:HGNC.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0003723; F:RNA binding; IDA:HGNC.
GO; GO:0008270; F:zinc ion binding; IDA:HGNC.
GO; GO:0016553; P:base conversion or substitution editing; IDA:HGNC.
GO; GO:0016554; P:cytidine to uridine editing; IBA:GO_Central.
GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
GO; GO:0070383; P:DNA cytosine deamination; IDA:UniProtKB.
GO; GO:0080111; P:DNA demethylation; IDA:UniProtKB.
GO; GO:0045087; P:innate immune response; IDA:HGNC.
GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; IDA:UniProtKB.
GO; GO:0010529; P:negative regulation of transposition; IDA:UniProtKB.
GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
GO; GO:0048525; P:negative regulation of viral process; IDA:HGNC.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IDA:HGNC.
InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
InterPro; IPR013158; APOBEC_N.
InterPro; IPR002125; CMP_dCMP_dom.
InterPro; IPR016193; Cytidine_deaminase-like.
Pfam; PF08210; APOBEC_N; 2.
SUPFAM; SSF53927; SSF53927; 2.
PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 2.
PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Antiviral defense;
Complete proteome; Cytoplasm; Hydrolase; Immunity; Innate immunity;
Metal-binding; Polymorphism; Reference proteome; Repeat; Zinc.
CHAIN 1 373 DNA dC->dU-editing enzyme APOBEC-3F.
/FTId=PRO_0000171757.
DOMAIN 29 137 CMP/dCMP-type deaminase 1.
{ECO:0000255|PROSITE-ProRule:PRU01083}.
DOMAIN 174 321 CMP/dCMP-type deaminase 2.
{ECO:0000255|PROSITE-ProRule:PRU01083}.
ACT_SITE 251 251 Proton donor. {ECO:0000250}.
METAL 65 65 Zinc. {ECO:0000250}.
METAL 96 96 Zinc. {ECO:0000250}.
METAL 99 99 Zinc. {ECO:0000250}.
VAR_SEQ 58 79 VYSQPEHHAEMCFLSWFCGNQL -> VPPGLQSLCRQELSQ
LGKQTTH (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_009803.
VAR_SEQ 59 113 YSQPEHHAEMCFLSWFCGNQLPAYKCFQITWFVSWTPCPDC
VAKLAEFLAEHPNV -> PRSFIRAPFQVLSSPFGQCAPPH
GTAQVQWPPQLTAGREQGRP (in isoform 3).
{ECO:0000303|PubMed:15461802}.
/FTId=VSP_042754.
VAR_SEQ 80 373 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_009804.
VAR_SEQ 114 373 Missing (in isoform 3).
{ECO:0000303|PubMed:15461802}.
/FTId=VSP_042755.
VARIANT 48 48 R -> P (in dbSNP:rs35053197).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_038355.
VARIANT 61 61 Q -> L (in dbSNP:rs2076109).
/FTId=VAR_018145.
VARIANT 97 97 P -> L (in dbSNP:rs2076110).
/FTId=VAR_018146.
VARIANT 108 108 A -> S (in dbSNP:rs2020390).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_018147.
VARIANT 178 178 A -> T (in dbSNP:rs34182094).
{ECO:0000269|Ref.2}.
/FTId=VAR_025058.
VARIANT 231 231 V -> I (in dbSNP:rs2076101).
{ECO:0000269|Ref.2}.
/FTId=VAR_018148.
VARIANT 307 307 Y -> C (in dbSNP:rs12157816).
{ECO:0000269|Ref.2}.
/FTId=VAR_025059.
MUTAGEN 67 67 E->A: Decrease in cytidine deaminase and
antiviral activity; when associated with
A-251. {ECO:0000269|PubMed:17020885}.
MUTAGEN 67 67 E->A: No effect on cytidine deaminase and
antiviral activity.
{ECO:0000269|PubMed:17020885}.
MUTAGEN 251 251 E->A: Decrease in cytidine deaminase and
antiviral activity.
{ECO:0000269|PubMed:17020885}.
MUTAGEN 251 251 E->A: Decrease in cytidine deaminase and
antiviral activity; when associated with
A-67. {ECO:0000269|PubMed:17020885}.
HELIX 197 204 {ECO:0000244|PDB:5HX4}.
HELIX 208 212 {ECO:0000244|PDB:5HX4}.
STRAND 217 226 {ECO:0000244|PDB:5HX4}.
STRAND 232 239 {ECO:0000244|PDB:5HX4}.
STRAND 243 245 {ECO:0000244|PDB:4J4J}.
HELIX 250 261 {ECO:0000244|PDB:5HX4}.
STRAND 267 277 {ECO:0000244|PDB:5HX4}.
HELIX 281 293 {ECO:0000244|PDB:5HX4}.
STRAND 297 305 {ECO:0000244|PDB:5HX4}.
TURN 307 310 {ECO:0000244|PDB:3WUS}.
HELIX 312 323 {ECO:0000244|PDB:5HX4}.
STRAND 327 330 {ECO:0000244|PDB:5HX4}.
HELIX 333 343 {ECO:0000244|PDB:5HX4}.
HELIX 357 372 {ECO:0000244|PDB:5HX4}.
SEQUENCE 373 AA; 45020 MW; AF1A0E13830695F4 CRC64;
MKPHFRNTVE RMYRDTFSYN FYNRPILSRR NTVWLCYEVK TKGPSRPRLD AKIFRGQVYS
QPEHHAEMCF LSWFCGNQLP AYKCFQITWF VSWTPCPDCV AKLAEFLAEH PNVTLTISAA
RLYYYWERDY RRALCRLSQA GARVKIMDDE EFAYCWENFV YSEGQPFMPW YKFDDNYAFL
HRTLKEILRN PMEAMYPHIF YFHFKNLRKA YGRNESWLCF TMEVVKHHSP VSWKRGVFRN
QVDPETHCHA ERCFLSWFCD DILSPNTNYE VTWYTSWSPC PECAGEVAEF LARHSNVNLT
IFTARLYYFW DTDYQEGLRS LSQEGASVEI MGYKDFKYCW ENFVYNDDEP FKPWKGLKYN
FLFLDSKLQE ILE


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