ABC3D_HUMAN
ID ABC3D_HUMAN Reviewed; 386 AA.
AC Q96AK3; Q5JZ91; Q7Z2N2; Q7Z2N5; Q7Z2N6;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=DNA dC->dU-editing enzyme APOBEC-3D;
DE Short=A3D;
DE Short=A3DE {ECO:0000303|PubMed:23001005};
DE EC=3.5.4.38;
GN Name=APOBEC3D {ECO:0000312|HGNC:HGNC:17354};
GN Synonyms=APOBEC3DE {ECO:0000312|HGNC:HGNC:17354};
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 [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 [2]
RP GENE FAMILY ORGANIZATION.
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 [3]
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 [4]
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 [5]
RP FUNCTION, MUTAGENESIS OF ASP-140, INTERACTION WITH HIV-1 VIF (MICROBIAL
RP INFECTION), AND INTERACTION WITH APOBEC3F AND APOBEC3G.
RX PubMed=16920826; DOI=10.1128/jvi.01123-06;
RA Dang Y., Wang X., Esselman W.J., Zheng Y.-H.;
RT "Identification of APOBEC3DE as another antiretroviral factor from the
RT human APOBEC family.";
RL J. Virol. 80:10522-10533(2006).
RN [6]
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 [7]
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 [8]
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 [9]
RP FUNCTION IN HIV-1 RESTRICTION, SUBCELLULAR LOCATION, AND ACTIVITY
RP REGULATION.
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 [10]
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 [11]
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 [12]
RP INTERACTION WITH HIV-1 VIF (MICROBIAL INFECTION), AND MUTAGENESIS OF
RP GLU-264; LEU-268; PHE-271; CYS-272; 275-ILE-LEU-276; SER-277; TYR-282;
RP GLU-302; PHE-303; HIS-307 AND GLU-337.
RX PubMed=23001005; DOI=10.1038/nsmb.2378;
RA Kitamura S., Ode H., Nakashima M., Imahashi M., Naganawa Y., Kurosawa T.,
RA Yokomaku Y., Yamane T., Watanabe N., Suzuki A., Sugiura W., Iwatani Y.;
RT "The APOBEC3C crystal structure and the interface for HIV-1 Vif binding.";
RL Nat. Struct. Mol. Biol. 19:1005-1010(2012).
RN [13]
RP FUNCTION IN HIV-1 RESTRICTION.
RX PubMed=22807680; DOI=10.1371/journal.ppat.1002800;
RA Refsland E.W., Hultquist J.F., Harris R.S.;
RT "Endogenous origins of HIV-1 G-to-A hypermutation and restriction in the
RT nonpermissive T cell line CEM2n.";
RL PLoS Pathog. 8:E1002800-E1002800(2012).
RN [14]
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).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH L1RE1.
RX PubMed=27428332; DOI=10.1371/journal.pone.0157220;
RA Liang W., Xu J., Yuan W., Song X., Zhang J., Wei W., Yu X.F., Yang Y.;
RT "APOBEC3DE Inhibits LINE-1 Retrotransposition by Interacting with ORF1p and
RT Influencing LINE Reverse Transcriptase Activity.";
RL PLoS ONE 11:e0157220-e0157220(2016).
RN [16]
RP FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, AND INTERACTION WITH
RP APOBEC3F AND APOBEC3G.
RX PubMed=27289067; DOI=10.1016/j.jmb.2016.05.022;
RA Bouzidi M.S., Caval V., Suspene R., Hallez C., Pineau P., Wain-Hobson S.,
RA Vartanian J.P.;
RT "APOBEC3DE Antagonizes Hepatitis B Virus Restriction Factors APOBEC3F and
RT APOBEC3G.";
RL J. Mol. Biol. 428:3514-3528(2016).
RN [17]
RP FUNCTION IN HIV-1 RESTRICTION.
RX PubMed=23097438; DOI=10.1128/jvi.00676-12;
RA Chaipan C., Smith J.L., Hu W.S., Pathak V.K.;
RT "APOBEC3G restricts HIV-1 to a greater extent than APOBEC3F and APOBEC3DE
RT in human primary CD4+ t cells and macrophages.";
RL J. Virol. 87:444-453(2013).
RN [18]
RP FUNCTION IN HIV-1 RESTRICTION.
RX PubMed=23152537; DOI=10.1128/jvi.02587-12;
RA Gillick K., Pollpeter D., Phalora P., Kim E.Y., Wolinsky S.M., Malim M.H.;
RT "The suppression of HIV-1 infection by APOBEC3 proteins in primary human
RT CD4+ T cells is associated with the inhibition of processive reverse
RT transcription as well as excessive cytidine deamination.";
RL J. Virol. 87:1508-1517(2013).
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 (PubMed:16920826,
CC PubMed:20062055, PubMed:21835787). Exhibits antiviral activity against
CC HIV-1. After the penetration of retroviral nucleocapsids into target
CC cells of infection and the initiation of reverse transcription, it can
CC induce the conversion of cytosine to uracil in the minus-sense single-
CC strand viral DNA, leading to G-to-A hypermutations in the subsequent
CC plus-strand viral DNA (PubMed:16920826). The resultant detrimental
CC levels of mutations in the proviral genome, along with a deamination-
CC independent mechanism that works prior to the proviral integration,
CC together exert efficient antiretroviral effects in infected target
CC cells. Selectively targets single-stranded DNA and does not deaminate
CC double-stranded DNA or single- or double-stranded RNA. Inhibits also
CC the mobility of LTR and non-LTR retrotransposons (PubMed:27428332).
CC {ECO:0000269|PubMed:12859895, ECO:0000269|PubMed:16920826,
CC ECO:0000269|PubMed:20062055, ECO:0000269|PubMed:21835787,
CC ECO:0000269|PubMed:22807680, ECO:0000269|PubMed:23097438,
CC ECO:0000269|PubMed:23152537}.
CC -!- FUNCTION: (Microbial infection) Enhances hepatitis B virus/HBV
CC replication by excluding restriction factors APOBEC3F and APOBEC3G from
CC HBV capsids. {ECO:0000269|PubMed:27289067}.
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; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: (Microbial infection) Antiviral activity is
CC neutralized by the HIV-1 virion infectivity factor (Vif), that prevents
CC its incorporation into progeny virions by both inhibiting its
CC translation and/or by inducing its ubiquitination and subsequent
CC degradation by the 26S proteasome. {ECO:0000269|PubMed:21835787}.
CC -!- SUBUNIT: Can form homo- and heterodimers with APOBEC3F and APOBEC3G
CC (PubMed:16920826, PubMed:27289067). Interacts with L1RE1; this
CC interaction inhibits LINE-1 retrotransposition (PubMed:27428332).
CC {ECO:0000269|PubMed:16920826, ECO:0000269|PubMed:27289067,
CC ECO:0000269|PubMed:27428332}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Vif
CC (PubMed:16920826, PubMed:23001005). This interaction triggers APOBEC3D
CC polyubiquitylation and degradation by the 26S proteasome
CC (PubMed:16920826). {ECO:0000269|PubMed:16920826,
CC ECO:0000269|PubMed:23001005}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27289067,
CC ECO:0000269|PubMed:27428332}. Cytoplasm, P-body.
CC -!- TISSUE SPECIFICITY: Expressed in lymphoid organs. Also detected in non-
CC lymphoid tissues including lung. {ECO:0000269|PubMed:20308164}.
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.
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 -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
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DR EMBL; AL022318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS46709.1; -.
DR AlphaFoldDB; Q96AK3; -.
DR SMR; Q96AK3; -.
DR IntAct; Q96AK3; 59.
DR MINT; Q96AK3; -.
DR STRING; 9606.ENSP00000216099; -.
DR iPTMnet; Q96AK3; -.
DR PhosphoSitePlus; Q96AK3; -.
DR BioMuta; APOBEC3D; -.
DR DMDM; 48474596; -.
DR EPD; Q96AK3; -.
DR jPOST; Q96AK3; -.
DR MassIVE; Q96AK3; -.
DR MaxQB; Q96AK3; -.
DR PaxDb; Q96AK3; -.
DR PeptideAtlas; Q96AK3; -.
DR PRIDE; Q96AK3; -.
DR ProteomicsDB; 75971; -.
DR Antibodypedia; 35025; 172 antibodies from 27 providers.
DR DNASU; 140564; -.
DR Ensembl; ENST00000216099.13; ENSP00000216099.7; ENSG00000243811.12.
DR MANE-Select; ENST00000216099.13; ENSP00000216099.7; NM_152426.4; NP_689639.2.
DR UCSC; uc003awt.5; human.
DR GeneCards; APOBEC3D; -.
DR HGNC; HGNC:17354; APOBEC3D.
DR HPA; ENSG00000243811; Tissue enhanced (lymphoid).
DR MIM; 609900; gene.
DR neXtProt; NX_Q96AK3; -.
DR OpenTargets; ENSG00000243811; -.
DR PharmGKB; PA24894; -.
DR VEuPathDB; HostDB:ENSG00000243811; -.
DR eggNOG; KOG4075; Eukaryota.
DR GeneTree; ENSGT00940000162695; -.
DR HOGENOM; CLU_047918_0_0_1; -.
DR OMA; HTELCIL; -.
DR OrthoDB; 586309at2759; -.
DR PhylomeDB; Q96AK3; -.
DR TreeFam; TF331356; -.
DR BRENDA; 3.5.4.38; 2681.
DR PathwayCommons; Q96AK3; -.
DR SignaLink; Q96AK3; -.
DR SIGNOR; Q96AK3; -.
DR Pharos; Q96AK3; Tbio.
DR PRO; PR:Q96AK3; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q96AK3; protein.
DR Bgee; ENSG00000243811; Expressed in granulocyte and 98 other tissues.
DR ExpressionAtlas; Q96AK3; baseline and differential.
DR Genevisible; Q96AK3; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0004126; F:cytidine deaminase activity; IBA:GO_Central.
DR GO; GO:0047844; F:deoxycytidine deaminase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0010529; P:negative regulation of transposition; IDA:UniProtKB.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR SUPFAM; SSF53927; SSF53927; 2.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 2.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 2.
PE 1: Evidence at protein level;
KW Antiviral defense; Cytoplasm; Hydrolase; Immunity; Innate immunity;
KW Metal-binding; Reference proteome; Repeat; Zinc.
FT CHAIN 1..386
FT /note="DNA dC->dU-editing enzyme APOBEC-3D"
FT /id="PRO_0000171756"
FT DOMAIN 29..145
FT /note="CMP/dCMP-type deaminase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT DOMAIN 187..334
FT /note="CMP/dCMP-type deaminase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 264
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT MUTAGEN 140
FT /note="D->K: About two-third loss of anti HIV-1 activity."
FT /evidence="ECO:0000269|PubMed:16920826"
FT MUTAGEN 264
FT /note="E->Q: No effect on Vif binding."
FT /evidence="ECO:0000269|PubMed:23001005"
FT MUTAGEN 268
FT /note="L->D: Resistant to HIV-1 Vif and abolishes Vif
FT binding."
FT /evidence="ECO:0000269|PubMed:23001005"
FT MUTAGEN 271
FT /note="F->A: Resistant to HIV-1 Vif and abolishes Vif
FT binding."
FT /evidence="ECO:0000269|PubMed:23001005"
FT MUTAGEN 272
FT /note="C->K: Resistant to HIV-1 Vif and reduces Vif
FT binding."
FT /evidence="ECO:0000269|PubMed:23001005"
FT MUTAGEN 275..276
FT /note="IL->AA: Resistant to HIV-1 Vif and abolishes Vif
FT binding."
FT /evidence="ECO:0000269|PubMed:23001005"
FT MUTAGEN 277
FT /note="S->D: Resistant to HIV-1 Vif and reduces Vif
FT binding."
FT /evidence="ECO:0000269|PubMed:23001005"
FT MUTAGEN 282
FT /note="Y->A: Resistant to HIV-1 Vif and abolishes Vif
FT binding."
FT /evidence="ECO:0000269|PubMed:23001005"
FT MUTAGEN 302
FT /note="E->K: Resistant to HIV-1 Vif and abolishes Vif
FT binding."
FT /evidence="ECO:0000269|PubMed:23001005"
FT MUTAGEN 303
FT /note="F->K: Resistant to HIV-1 Vif and abolishes Vif
FT binding."
FT /evidence="ECO:0000269|PubMed:23001005"
FT MUTAGEN 307
FT /note="H->D: Resistant to HIV-1 Vif and abolishes Vif
FT binding."
FT /evidence="ECO:0000269|PubMed:23001005"
FT MUTAGEN 337
FT /note="E->A: Resistant to HIV-1 Vif and reduces Vif
FT binding."
FT /evidence="ECO:0000269|PubMed:23001005"
FT MUTAGEN 337
FT /note="E->K: Resistant to HIV-1 Vif and abolishes Vif
FT binding."
FT /evidence="ECO:0000269|PubMed:23001005"
SQ SEQUENCE 386 AA; 46598 MW; 94C7253BDCC85B22 CRC64;
MNPQIRNPME RMYRDTFYDN FENEPILYGR SYTWLCYEVK IKRGRSNLLW DTGVFRGPVL
PKRQSNHRQE VYFRFENHAE MCFLSWFCGN RLPANRRFQI TWFVSWNPCL PCVVKVTKFL
AEHPNVTLTI SAARLYYYRD RDWRWVLLRL HKAGARVKIM DYEDFAYCWE NFVCNEGQPF
MPWYKFDDNY ASLHRTLKEI LRNPMEAMYP HIFYFHFKNL LKACGRNESW LCFTMEVTKH
HSAVFRKRGV FRNQVDPETH CHAERCFLSW FCDDILSPNT NYEVTWYTSW SPCPECAGEV
AEFLARHSNV NLTIFTARLC YFWDTDYQEG LCSLSQEGAS VKIMGYKDFV SCWKNFVYSD
DEPFKPWKGL QTNFRLLKRR LREILQ
