ID ABC3B_HUMAN Reviewed; 382 AA. AC Q9UH17; B0QYD2; O95618; Q20WL1; Q5IFJ4; Q7Z2N3; Q7Z6D6; Q9UE74; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 184. DE RecName: Full=DNA dC->dU-editing enzyme APOBEC-3B; DE Short=A3B; DE EC=3.5.4.38; DE AltName: Full=Phorbolin-1-related protein; DE AltName: Full=Phorbolin-2/3; GN Name=APOBEC3B; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LYS-146, AND INDUCTION. RC TISSUE=Keratinocyte; RX PubMed=10469298; DOI=10.1046/j.1523-1747.1999.00682.x; RA Madsen P.P., Anant S., Rasmussen H.H., Gromov P., Vorum H., Dumanski J.P., RA Tommerup N., Collins J.E., Wright C.L., Dunham I., Macginnitie A.J., RA Davidson N.O., Celis J.E.; RT "Psoriasis upregulated phorbolin-1 shares structural but not functional RT similarity to the mRNA-editing protein apobec-1."; RL J. Invest. Dermatol. 113:162-169(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION. RX PubMed=16060832; DOI=10.1089/aid.2005.21.611; RA Rose K.M., Marin M., Kozak S.L., Kabat D.; RT "Regulated production and anti-HIV type 1 activities of cytidine deaminases RT APOBEC3B, 3F, and 3G."; RL AIDS Res. Hum. Retroviruses 21:611-619(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS GLU-62 AND RP LYS-146. RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT LYS-146. RC TISSUE=Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP GENE FAMILY ORGANIZATION, TISSUE SPECIFICITY, RNA-BINDING, ZINC-BINDING, RP AND INTERACTION WITH APOBEC3G. RX PubMed=11863358; DOI=10.1006/geno.2002.6718; RA Jarmuz A., Chester A., Bayliss J., Gisbourne J., Dunham I., Scott J., RA Navaratnam N.; RT "An anthropoid-specific locus of orphan C to U RNA-editing enzymes on RT chromosome 22."; RL Genomics 79:285-296(2002). RN [7] RP REVIEW ON APOBEC FAMILIES. RX PubMed=12683974; DOI=10.1016/s0168-9525(03)00054-4; RA Wedekind J.E., Dance G.S.C., Sowden M.P., Smith H.C.; RT "Messenger RNA editing in mammals: new members of the APOBEC family seeking RT roles in the family business."; RL Trends Genet. 19:207-216(2003). RN [8] RP FUNCTION IN HIV-1 INFECTIVITY. RX PubMed=12859895; DOI=10.1016/s0092-8674(03)00515-4; RA Mariani R., Chen D., Schroefelbauer B., Navarro F., Koenig R., Bollman B., RA Muenk C., Nymark-McMahon H., Landau N.R.; RT "Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif."; RL Cell 114:21-31(2003). RN [9] RP FUNCTION IN SIV RESTRICTION. RX PubMed=15466872; DOI=10.1074/jbc.m408802200; RA Yu Q., Chen D., Koenig R., Mariani R., Unutmaz D., Landau N.R.; RT "APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency RT virus replication."; RL J. Biol. Chem. 279:53379-53386(2004). RN [10] RP FUNCTION IN RETROTRANSPOSITION. RX PubMed=16527742; DOI=10.1016/j.cub.2006.01.031; RA Chen H., Lilley C.E., Yu Q., Lee D.V., Chou J., Narvaiza I., Landau N.R., RA Weitzman M.D.; RT "APOBEC3A is a potent inhibitor of adeno-associated virus and RT retrotransposons."; RL Curr. Biol. 16:480-485(2006). RN [11] RP DOMAIN CMP/DCMP DEAMINASE. RX PubMed=17020885; DOI=10.1074/jbc.m604980200; RA Hakata Y., Landau N.R.; RT "Reversed functional organization of mouse and human APOBEC3 cytidine RT deaminase domains."; RL J. Biol. Chem. 281:36624-36631(2006). RN [12] RP SUBCELLULAR LOCATION. RX PubMed=16699599; DOI=10.1371/journal.ppat.0020041; RA Wichroski M.J., Robb G.B., Rana T.M.; RT "Human retroviral host restriction factors APOBEC3G and APOBEC3F localize RT to mRNA processing bodies."; RL PLoS Pathog. 2:E41-E41(2006). RN [13] RP REVIEW. RX PubMed=18304004; DOI=10.1146/annurev.immunol.26.021607.090350; RA Chiu Y.L., Greene W.C.; RT "The APOBEC3 cytidine deaminases: an innate defensive network opposing RT exogenous retroviruses and endogenous retroelements."; RL Annu. Rev. Immunol. 26:317-353(2008). RN [14] RP REVIEW ON FUNCTION IN HBV RESTRICTION. RX PubMed=18448976; DOI=10.1097/qco.0b013e3282fe1bb2; RA Bonvin M., Greeve J.; RT "Hepatitis B: modern concepts in pathogenesis--APOBEC3 cytidine deaminases RT as effectors in innate immunity against the hepatitis B virus."; RL Curr. Opin. Infect. Dis. 21:298-303(2008). RN [15] RP SUBCELLULAR LOCATION. RX PubMed=18667511; DOI=10.1128/jvi.02471-07; RA Stenglein M.D., Matsuo H., Harris R.S.; RT "Two regions within the amino-terminal half of APOBEC3G cooperate to RT determine cytoplasmic localization."; RL J. Virol. 82:9591-9599(2008). RN [16] RP TISSUE SPECIFICITY. RX PubMed=20308164; DOI=10.1093/nar/gkq174; RA Refsland E.W., Stenglein M.D., Shindo K., Albin J.S., Brown W.L., RA Harris R.S.; RT "Quantitative profiling of the full APOBEC3 mRNA repertoire in lymphocytes RT and tissues: implications for HIV-1 restriction."; RL Nucleic Acids Res. 38:4274-4284(2010). RN [17] RP FUNCTION IN RETROTRANSPOSITION. RX PubMed=20062055; DOI=10.1038/nsmb.1744; RA Stenglein M.D., Burns M.B., Li M., Lengyel J., Harris R.S.; RT "APOBEC3 proteins mediate the clearance of foreign DNA from human cells."; RL Nat. Struct. Mol. Biol. 17:222-229(2010). RN [18] RP SUBCELLULAR LOCATION. RX PubMed=21835787; DOI=10.1128/jvi.05238-11; RA Hultquist J.F., Lengyel J.A., Refsland E.W., LaRue R.S., Lackey L., RA Brown W.L., Harris R.S.; RT "Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H demonstrate a RT conserved capacity to restrict Vif-deficient HIV-1."; RL J. Virol. 85:11220-11234(2011). RN [19] RP REVIEW. RX PubMed=22912627; DOI=10.3389/fmicb.2012.00275; RA Arias J.F., Koyama T., Kinomoto M., Tokunaga K.; RT "Retroelements versus APOBEC3 family members: No great escape from the RT magnificent seven."; RL Front. Microbiol. 3:275-275(2012). RN [20] RP FUNCTION IN HTLV-1 RESTRICTION. RX PubMed=22457529; DOI=10.1128/jvi.06570-11; RA Ooms M., Krikoni A., Kress A.K., Simon V., Muenk C.; RT "APOBEC3A, APOBEC3B, and APOBEC3H haplotype 2 restrict human T-lymphotropic RT virus type 1."; RL J. Virol. 86:6097-6108(2012). RN [21] RP SUBCELLULAR LOCATION. RX PubMed=22915799; DOI=10.1128/jvi.00595-12; RA Phalora P.K., Sherer N.M., Wolinsky S.M., Swanson C.M., Malim M.H.; RT "HIV-1 replication and APOBEC3 antiviral activity are not regulated by P RT bodies."; RL J. Virol. 86:11712-11724(2012). RN [22] RP REVIEW. RX PubMed=22001110; DOI=10.1016/j.semcdb.2011.10.004; RA Smith H.C., Bennett R.P., Kizilyer A., McDougall W.M., Prohaska K.M.; RT "Functions and regulation of the APOBEC family of proteins."; RL Semin. Cell Dev. Biol. 23:258-268(2012). CC -!- FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor CC of retrovirus replication and retrotransposon mobility via deaminase- CC dependent and -independent mechanisms. After the penetration of CC retroviral nucleocapsids into target cells of infection and the CC initiation of reverse transcription, it can induce the conversion of CC cytosine to uracil in the minus-sense single-strand viral DNA, leading CC to G-to-A hypermutations in the subsequent plus-strand viral DNA. The CC resultant detrimental levels of mutations in the proviral genome, along CC with a deamination-independent mechanism that works prior to the CC proviral integration, together exert efficient antiretroviral effects CC in infected target cells. Selectively targets single-stranded DNA and CC does not deaminate double-stranded DNA or single- or double-stranded CC RNA. Exhibits antiviral activity against simian immunodeficiency virus CC (SIV), hepatitis B virus (HBV) and human T-cell leukemia virus type 1 CC (HTLV-1) and may inhibit the mobility of LTR and non-LTR CC retrotransposons. {ECO:0000269|PubMed:12859895, CC ECO:0000269|PubMed:15466872, ECO:0000269|PubMed:16060832, CC ECO:0000269|PubMed:16527742, ECO:0000269|PubMed:20062055, CC ECO:0000269|PubMed:22457529}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxycytidine in single-stranded DNA + H(+) + H2O = a 2'- CC deoxyuridine in single-stranded DNA + NH4(+); Xref=Rhea:RHEA:50948, CC Rhea:RHEA-COMP:12846, Rhea:RHEA-COMP:12847, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:85452, CC ChEBI:CHEBI:133902; EC=3.5.4.38; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC -!- SUBUNIT: Homodimer. Interacts with APOBEC3G. Does not interact with CC APOBEC1. {ECO:0000269|PubMed:11863358}. CC -!- INTERACTION: CC Q9UH17; P11802: CDK4; NbExp=9; IntAct=EBI-2967317, EBI-295644; CC Q9UH17-2; O95994: AGR2; NbExp=3; IntAct=EBI-17624977, EBI-712648; CC Q9UH17-2; Q12982: BNIP2; NbExp=3; IntAct=EBI-17624977, EBI-752094; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16699599, CC ECO:0000269|PubMed:18667511, ECO:0000269|PubMed:21835787, CC ECO:0000269|PubMed:22915799}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9UH17-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UH17-2; Sequence=VSP_009802; CC Name=3; CC IsoId=Q9UH17-3; Sequence=VSP_044900; CC -!- TISSUE SPECIFICITY: Expressed at high and moderate levels in peripheral CC blood leukocytes, spleen, testes, heart, thymus, prostate and ovary. CC Also expressed at low levels in several other tissues. CC {ECO:0000269|PubMed:11863358, ECO:0000269|PubMed:20308164}. CC -!- INDUCTION: Phorbol 12-myristate 13-acetate (PMA) induces overexpression CC in keratinocytes. Up-regulated by IFN-alpha. CC {ECO:0000269|PubMed:10469298}. CC -!- DOMAIN: The CMP/dCMP deaminase domain 1 mediates RNA binding, RNA- CC dependent oligomerization and virion incorporation whereas the CMP/dCMP CC deaminase domain 2 confers deoxycytidine deaminase activity and CC substrate sequence specificity. {ECO:0000269|PubMed:17020885}. CC -!- MISCELLANEOUS: It is one of seven related genes or pseudogenes found in CC a cluster, thought to result from gene duplication, on chromosome 22. CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice CC site. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD00089.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAD00090.1; Type=Frameshift; Note=Frameshifts result in two separate ORFs termed phorbolins 2 and 3.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U61083; AAD00089.1; ALT_INIT; mRNA. DR EMBL; U61084; AAD00090.1; ALT_FRAME; mRNA. DR EMBL; AY743217; AAW31743.1; -; mRNA. DR EMBL; CT841510; CAJ86440.1; -; mRNA. DR EMBL; AL022318; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC053859; AAH53859.1; -; mRNA. DR CCDS; CCDS13982.1; -. [Q9UH17-1] DR CCDS; CCDS58807.1; -. [Q9UH17-3] DR RefSeq; NP_001257340.1; NM_001270411.1. [Q9UH17-3] DR RefSeq; NP_004891.4; NM_004900.4. [Q9UH17-1] DR PDB; 2NBQ; NMR; -; A=187-382. DR PDB; 5CQD; X-ray; 2.08 A; A/C=187-378. DR PDB; 5CQH; X-ray; 1.73 A; A=187-378. DR PDB; 5CQI; X-ray; 1.68 A; A=187-378. DR PDB; 5CQK; X-ray; 1.88 A; A=187-378. DR PDB; 5SXG; X-ray; 1.93 A; A/B=191-378. DR PDB; 5SXH; X-ray; 1.78 A; A/B=191-378. DR PDB; 5TD5; X-ray; 1.72 A; A=187-378. DR PDB; 5TKM; X-ray; 1.90 A; A/B=1-191. DR PDB; 6NFK; X-ray; 1.86 A; A=187-378. DR PDB; 6NFL; X-ray; 1.73 A; A=187-378. DR PDB; 6NFM; X-ray; 2.53 A; A=187-378. DR PDB; 7RW6; EM; 2.55 A; B/D=193-382. DR PDBsum; 2NBQ; -. DR PDBsum; 5CQD; -. DR PDBsum; 5CQH; -. DR PDBsum; 5CQI; -. DR PDBsum; 5CQK; -. DR PDBsum; 5SXG; -. DR PDBsum; 5SXH; -. DR PDBsum; 5TD5; -. DR PDBsum; 5TKM; -. DR PDBsum; 6NFK; -. DR PDBsum; 6NFL; -. DR PDBsum; 6NFM; -. DR PDBsum; 7RW6; -. DR AlphaFoldDB; Q9UH17; -. DR EMDB; EMD-24709; -. DR SMR; Q9UH17; -. DR BioGRID; 114950; 143. DR IntAct; Q9UH17; 29. DR MINT; Q9UH17; -. DR STRING; 9606.ENSP00000327459; -. DR ChEMBL; CHEMBL4523487; -. DR GlyGen; Q9UH17; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9UH17; -. DR PhosphoSitePlus; Q9UH17; -. DR SwissPalm; Q9UH17; -. DR BioMuta; APOBEC3B; -. DR DMDM; 12643884; -. DR EPD; Q9UH17; -. DR jPOST; Q9UH17; -. DR MassIVE; Q9UH17; -. DR MaxQB; Q9UH17; -. DR PaxDb; 9606-ENSP00000327459; -. DR PeptideAtlas; Q9UH17; -. DR ProteomicsDB; 2630; -. DR ProteomicsDB; 84274; -. [Q9UH17-1] DR ProteomicsDB; 84275; -. [Q9UH17-2] DR Pumba; Q9UH17; -. DR ABCD; Q9UH17; 1 sequenced antibody. DR Antibodypedia; 35027; 187 antibodies from 29 providers. DR DNASU; 9582; -. DR Ensembl; ENST00000333467.4; ENSP00000327459.3; ENSG00000179750.16. [Q9UH17-1] DR Ensembl; ENST00000335760.9; ENSP00000338897.5; ENSG00000179750.16. [Q9UH17-2] DR Ensembl; ENST00000407298.7; ENSP00000385068.3; ENSG00000179750.16. [Q9UH17-3] DR GeneID; 9582; -. DR KEGG; hsa:9582; -. DR MANE-Select; ENST00000333467.4; ENSP00000327459.3; NM_004900.5; NP_004891.5. DR UCSC; uc003awo.3; human. [Q9UH17-1] DR AGR; HGNC:17352; -. DR CTD; 9582; -. DR DisGeNET; 9582; -. DR GeneCards; APOBEC3B; -. DR HGNC; HGNC:17352; APOBEC3B. DR HPA; ENSG00000179750; Tissue enhanced (bone marrow, intestine). DR MIM; 607110; gene. DR neXtProt; NX_Q9UH17; -. DR OpenTargets; ENSG00000179750; -. DR PharmGKB; PA24892; -. DR VEuPathDB; HostDB:ENSG00000179750; -. DR eggNOG; KOG4075; Eukaryota. DR GeneTree; ENSGT00940000164701; -. DR HOGENOM; CLU_047918_0_0_1; -. DR InParanoid; Q9UH17; -. DR OMA; LCHKVEL; -. DR OrthoDB; 5355962at2759; -. DR PhylomeDB; Q9UH17; -. DR TreeFam; TF331356; -. DR BRENDA; 3.5.4.38; 2681. DR PathwayCommons; Q9UH17; -. DR Reactome; R-HSA-72200; mRNA Editing: C to U Conversion. DR Reactome; R-HSA-75094; Formation of the Editosome. DR SignaLink; Q9UH17; -. DR SIGNOR; Q9UH17; -. DR BioGRID-ORCS; 9582; 12 hits in 1155 CRISPR screens. DR ChiTaRS; APOBEC3B; human. DR GeneWiki; APOBEC3B; -. DR GenomeRNAi; 9582; -. DR Pharos; Q9UH17; Tbio. DR PRO; PR:Q9UH17; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; Q9UH17; Protein. DR Bgee; ENSG00000179750; Expressed in primordial germ cell in gonad and 91 other cell types or tissues. DR ExpressionAtlas; Q9UH17; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0000932; C:P-body; IBA:GO_Central. DR GO; GO:0004126; F:cytidine deaminase activity; IBA:GO_Central. DR GO; GO:0047844; F:deoxycytidine deaminase activity; IMP:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0044355; P:clearance of foreign intracellular DNA; IDA:GO_Central. DR GO; GO:0016554; P:cytidine to uridine editing; IBA:GO_Central. DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB. DR GO; GO:0070383; P:DNA cytosine deamination; IBA:GO_Central. DR GO; GO:0080111; P:DNA demethylation; IBA:GO_Central. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; IBA:GO_Central. DR GO; GO:0010526; P:retrotransposon silencing; IDA:UniProtKB. DR CDD; cd01283; cytidine_deaminase; 1. DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 2. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR002125; CMP_dCMP_dom. DR InterPro; IPR016193; Cytidine_deaminase-like. DR PANTHER; PTHR13857:SF39; DNA DC-DU-EDITING ENZYME APOBEC-3A-RELATED; 1. DR PANTHER; PTHR13857; MRNA EDITING ENZYME; 1. DR Pfam; PF18782; NAD2; 2. DR SUPFAM; SSF53927; Cytidine deaminase-like; 2. DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 2. DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 2. DR Genevisible; Q9UH17; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Antiviral defense; Hydrolase; Immunity; KW Innate immunity; Metal-binding; Nucleus; Reference proteome; Repeat; KW RNA-binding; Zinc. FT CHAIN 1..382 FT /note="DNA dC->dU-editing enzyme APOBEC-3B" FT /id="PRO_0000171753" FT DOMAIN 29..138 FT /note="CMP/dCMP-type deaminase 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083" FT DOMAIN 210..326 FT /note="CMP/dCMP-type deaminase 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083" FT ACT_SITE 255 FT /note="Proton donor" FT /evidence="ECO:0000255" FT BINDING 66 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 97 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 100 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 253 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 284 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 289 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT VAR_SEQ 191..382 FT /note="YLMDPDTFTFNFNNDPLVLRRRQTYLCYEVERLDNGTWVLMDQHMGFLCNEA FT KNLLCGFYGRHAELRFLDLVPSLQLDPAQIYRVTWFISWSPCFSWGCAGEVRAFLQENT FT HVRLRIFAARIYDYDPLYKEALQMLRDAGAQVSIMTYDEFEYCWDTFVYRQGCPFQPWD FT GLEEHSQALSGRLRAILQNQGN -> LRIFSVAFTAAMRSCASWTWFLLCSWTRPRSTG FT SLGSSPGAPASPGAVPGKCVRSFRRTHT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_009802" FT VAR_SEQ 242..266 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15461802" FT /id="VSP_044900" FT VARIANT 62 FT /note="K -> E (in dbSNP:rs2076109)" FT /evidence="ECO:0000269|PubMed:15461802" FT /id="VAR_018142" FT VARIANT 98 FT /note="P -> L (in dbSNP:rs2076110)" FT /id="VAR_018143" FT VARIANT 109 FT /note="S -> A (in dbSNP:rs17000697)" FT /id="VAR_033455" FT VARIANT 146 FT /note="T -> K (in dbSNP:rs5995649)" FT /evidence="ECO:0000269|PubMed:10469298, FT ECO:0000269|PubMed:15461802, ECO:0000269|PubMed:15489334" FT /id="VAR_018144" FT VARIANT 351 FT /note="R -> H (in dbSNP:rs1053813)" FT /id="VAR_048722" FT CONFLICT 103..104 FT /note="KL -> NV (in Ref. 1; AAD00090)" FT /evidence="ECO:0000305" FT CONFLICT 227..228 FT /note="TW -> WM (in Ref. 1; AAD00089)" FT /evidence="ECO:0000305" FT CONFLICT 255..256 FT /note="EL -> DW (in Ref. 1; AAD00089)" FT /evidence="ECO:0000305" FT CONFLICT 306 FT /note="R -> P (in Ref. 1; AAD00089)" FT /evidence="ECO:0000305" FT CONFLICT 356 FT /note="F -> S (in Ref. 2; AAW31743)" FT /evidence="ECO:0000305" FT HELIX 14..21 FT /evidence="ECO:0007829|PDB:5TKM" FT STRAND 32..43 FT /evidence="ECO:0007829|PDB:5TKM" FT STRAND 46..61 FT /evidence="ECO:0007829|PDB:5TKM" FT HELIX 63..65 FT /evidence="ECO:0007829|PDB:5TKM" FT HELIX 67..78 FT /evidence="ECO:0007829|PDB:5TKM" FT STRAND 86..94 FT /evidence="ECO:0007829|PDB:5TKM" FT HELIX 98..110 FT /evidence="ECO:0007829|PDB:5TKM" FT STRAND 114..122 FT /evidence="ECO:0007829|PDB:5TKM" FT HELIX 128..131 FT /evidence="ECO:0007829|PDB:5TKM" FT HELIX 134..140 FT /evidence="ECO:0007829|PDB:5TKM" FT STRAND 144..147 FT /evidence="ECO:0007829|PDB:5TKM" FT HELIX 150..160 FT /evidence="ECO:0007829|PDB:5TKM" FT HELIX 174..188 FT /evidence="ECO:0007829|PDB:5TKM" FT HELIX 195..202 FT /evidence="ECO:0007829|PDB:5CQI" FT HELIX 206..208 FT /evidence="ECO:0007829|PDB:7RW6" FT STRAND 215..224 FT /evidence="ECO:0007829|PDB:5CQI" FT STRAND 227..230 FT /evidence="ECO:0007829|PDB:5CQI" FT HELIX 232..234 FT /evidence="ECO:0007829|PDB:5CQI" FT STRAND 236..239 FT /evidence="ECO:0007829|PDB:5CQI" FT HELIX 245..247 FT /evidence="ECO:0007829|PDB:2NBQ" FT HELIX 254..261 FT /evidence="ECO:0007829|PDB:5CQI" FT HELIX 262..265 FT /evidence="ECO:0007829|PDB:5CQI" FT STRAND 269..271 FT /evidence="ECO:0007829|PDB:2NBQ" FT STRAND 273..281 FT /evidence="ECO:0007829|PDB:5CQI" FT HELIX 289..299 FT /evidence="ECO:0007829|PDB:5CQI" FT TURN 300..302 FT /evidence="ECO:0007829|PDB:2NBQ" FT STRAND 303..311 FT /evidence="ECO:0007829|PDB:5CQI" FT HELIX 319..328 FT /evidence="ECO:0007829|PDB:5CQI" FT STRAND 332..335 FT /evidence="ECO:0007829|PDB:5CQI" FT HELIX 338..348 FT /evidence="ECO:0007829|PDB:5CQI" FT HELIX 362..377 FT /evidence="ECO:0007829|PDB:5CQI" SQ SEQUENCE 382 AA; 45924 MW; DA6EDD23E8856240 CRC64; MNPQIRNPME RMYRDTFYDN FENEPILYGR SYTWLCYEVK IKRGRSNLLW DTGVFRGQVY FKPQYHAEMC FLSWFCGNQL PAYKCFQITW FVSWTPCPDC VAKLAEFLSE HPNVTLTISA ARLYYYWERD YRRALCRLSQ AGARVTIMDY EEFAYCWENF VYNEGQQFMP WYKFDENYAF LHRTLKEILR YLMDPDTFTF NFNNDPLVLR RRQTYLCYEV ERLDNGTWVL MDQHMGFLCN EAKNLLCGFY GRHAELRFLD LVPSLQLDPA QIYRVTWFIS WSPCFSWGCA GEVRAFLQEN THVRLRIFAA RIYDYDPLYK EALQMLRDAG AQVSIMTYDE FEYCWDTFVY RQGCPFQPWD GLEEHSQALS GRLRAILQNQ GN //