ABC3H_HUMAN
ID ABC3H_HUMAN Reviewed; 200 AA.
AC Q6NTF7; B0QYP0; B0QYP1; B7TQM5; E9PF38; M4W6S4; Q5JYL9; Q6IC87;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 4.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=DNA dC->dU-editing enzyme APOBEC-3H;
DE EC=3.5.4.38;
DE AltName: Full=APOBEC-related protein 10;
DE Short=ARP-10;
DE AltName: Full=Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3H;
DE Short=A3H;
GN Name=APOBEC3H;
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), AND ALTERNATIVE SPLICING.
RX PubMed=18945781; DOI=10.1128/jvi.01665-08;
RA Harari A., Ooms M., Mulder L.C., Simon V.;
RT "Polymorphisms and splice variants influence the antiretroviral activity of
RT human APOBEC3H.";
RL J. Virol. 83:295-303(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS ASN-15
RP DEL; LEU-18; ARG-105 AND ASP-178.
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Dad R., Sawal H.A., Rehman Z., Fahim A., Sadia H.;
RT "Sequence analysis of APOBEC-3 members in chronic HBV patients.";
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
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] (ISOFORMS 2 AND 3).
RC TISSUE=Astrocyte;
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 REVIEW ON APOBEC FAMILY.
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 [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16571802; DOI=10.1128/jvi.80.8.3853-3862.2006;
RA OhAinle M., Kerns J.A., Malik H.S., Emerman M.;
RT "Adaptive evolution and antiviral activity of the conserved mammalian
RT cytidine deaminase APOBEC3H.";
RL J. Virol. 80:3853-3862(2006).
RN [8]
RP FUNCTION.
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 [9]
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 [10]
RP FUNCTION, AND CHARACTERIZATION OF VARIANTS ASN-15 DEL AND ARG-105.
RX PubMed=18779051; DOI=10.1016/j.chom.2008.07.005;
RA OhAinle M., Kerns J.A., Li M.M., Malik H.S., Emerman M.;
RT "Antiretroelement activity of APOBEC3H was lost twice in recent human
RT evolution.";
RL Cell Host Microbe 4:249-259(2008).
RN [11]
RP FUNCTION IN HIV-1 RESTRICTION.
RX PubMed=18299330; DOI=10.1074/jbc.m707586200;
RA Dang Y., Siew L.M., Wang X., Han Y., Lampen R., Zheng Y.H.;
RT "Human cytidine deaminase APOBEC3H restricts HIV-1 replication.";
RL J. Biol. Chem. 283:11606-11614(2008).
RN [12]
RP FUNCTION, CHARACTERIZATION OF ALLELE A3H-VAR, AND MUTAGENESIS OF GLU-56.
RX PubMed=18827027; DOI=10.1096/fj.07-088781;
RA Tan L., Sarkis P.T., Wang T., Tian C., Yu X.F.;
RT "Sole copy of Z2-type human cytidine deaminase APOBEC3H has inhibitory
RT activity against retrotransposons and HIV-1.";
RL FASEB J. 23:279-287(2009).
RN [13]
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 [14]
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 [15]
RP CHARACTERIZATION OF ALLELE A3H-VAR, AND SUBCELLULAR LOCATION.
RX PubMed=21653666; DOI=10.1128/jvi.00624-11;
RA Li M.M., Emerman M.;
RT "Polymorphism in human APOBEC3H affects a phenotype dominant for
RT subcellular localization and antiviral activity.";
RL J. Virol. 85:8197-8207(2011).
RN [16]
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 [17]
RP REVIEW.
RA Love R.;
RT "Cytosine deaminases APOBEC3A, APOBEC3C, and APOBEC3H: Current
RT understanding of their functional roles.";
RL Student Perspec. Contemp. Virol. 0:0-0(2011).
RN [18]
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 [19]
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 [20]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH AGO1; AGO2 AND AGO3.
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 [21]
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 [22]
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).
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. The A3H-var/haplotype 2 exhibits
CC antiviral activity against vif-deficient HIV-1. After the penetration
CC of 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 also against T-cell leukemia virus
CC type 1 (HTLV-1) and may inhibit the mobility of LTR and non-LTR
CC retrotransposons. {ECO:0000269|PubMed:16571802,
CC ECO:0000269|PubMed:16920826, ECO:0000269|PubMed:18299330,
CC ECO:0000269|PubMed:18779051, ECO:0000269|PubMed:18827027,
CC ECO:0000269|PubMed:20062055, ECO:0000269|PubMed:21835787,
CC ECO:0000269|PubMed:22457529, ECO:0000269|PubMed:22915799,
CC ECO:0000269|PubMed:23097438}.
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: Antiviral activity is neutralized by the HIV-1
CC virion infectivity factor (VIF), that prevents its incorporation into
CC progeny virions by both inhibiting its translation and/or by inducing
CC its ubiquitination and subsequent degradation by the 26S proteasome.
CC {ECO:0000269|PubMed:21835787}.
CC -!- SUBUNIT: Interacts with AGO1, AGO2 and AGO3.
CC {ECO:0000269|PubMed:22915799}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, P-body.
CC Note=Haplotype 1 is distributed in both the nucleus and cytoplasm,
CC whereas haplotype 2 is predominantly cytoplasmic.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6NTF7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NTF7-2; Sequence=VSP_035034;
CC Name=3;
CC IsoId=Q6NTF7-3; Sequence=VSP_039975;
CC Name=4;
CC IsoId=Q6NTF7-4; Sequence=VSP_047044;
CC -!- TISSUE SPECIFICITY: Expressed in lymphoid organs. Also detected in non-
CC lymphoid tissues including lung, testis, ovary, fetal liver and skin.
CC {ECO:0000269|PubMed:16571802, ECO:0000269|PubMed:20308164}.
CC -!- POLYMORPHISM: There are at least 4 different haplotypes in the human
CC population. The allele A3H-var/haplotype 2 encodes a more stable
CC protein which is able to block HIV-1 replication. The displayed allele
CC (haplotype 1) is unstable and inefficient to block HIV-1 replication.
CC -!- MISCELLANEOUS: APOBEC3H from old world monkeys has retained its
CC antiviral activity, while it is lost in other primates.
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; FJ376613; ACK77774.1; -; mRNA.
DR EMBL; CR456481; CAG30367.3; -; mRNA.
DR EMBL; KC329529; AGI04217.1; -; mRNA.
DR EMBL; AL031846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF457460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069023; AAH69023.1; -; mRNA.
DR EMBL; BQ052182; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS13985.1; -. [Q6NTF7-3]
DR CCDS; CCDS54530.1; -. [Q6NTF7-1]
DR CCDS; CCDS54531.1; -. [Q6NTF7-2]
DR CCDS; CCDS54532.1; -. [Q6NTF7-4]
DR RefSeq; NP_001159474.2; NM_001166002.2. [Q6NTF7-2]
DR RefSeq; NP_001159475.2; NM_001166003.2. [Q6NTF7-1]
DR RefSeq; NP_001159476.2; NM_001166004.2.
DR RefSeq; NP_861438.3; NM_181773.4. [Q6NTF7-3]
DR RefSeq; XP_011528294.1; XM_011529992.2. [Q6NTF7-1]
DR PDB; 5W45; X-ray; 2.49 A; A/B=2-177.
DR PDB; 6B0B; X-ray; 3.28 A; A/E=1-181.
DR PDB; 6BBO; X-ray; 3.43 A; A/E=3-181.
DR PDBsum; 5W45; -.
DR PDBsum; 6B0B; -.
DR PDBsum; 6BBO; -.
DR AlphaFoldDB; Q6NTF7; -.
DR SMR; Q6NTF7; -.
DR BioGRID; 127899; 3.
DR STRING; 9606.ENSP00000385741; -.
DR iPTMnet; Q6NTF7; -.
DR PhosphoSitePlus; Q6NTF7; -.
DR BioMuta; APOBEC3H; -.
DR DMDM; 205371798; -.
DR MassIVE; Q6NTF7; -.
DR PaxDb; Q6NTF7; -.
DR PeptideAtlas; Q6NTF7; -.
DR PRIDE; Q6NTF7; -.
DR ProteomicsDB; 66670; -. [Q6NTF7-1]
DR Antibodypedia; 26556; 47 antibodies from 19 providers.
DR DNASU; 164668; -.
DR Ensembl; ENST00000348946.8; ENSP00000216123.5; ENSG00000100298.16. [Q6NTF7-2]
DR Ensembl; ENST00000401756.5; ENSP00000385741.1; ENSG00000100298.16. [Q6NTF7-1]
DR Ensembl; ENST00000442487.8; ENSP00000411754.3; ENSG00000100298.16. [Q6NTF7-3]
DR Ensembl; ENST00000613677.4; ENSP00000483689.1; ENSG00000100298.16. [Q6NTF7-1]
DR GeneID; 164668; -.
DR KEGG; hsa:164668; -.
DR MANE-Select; ENST00000442487.8; ENSP00000411754.3; NM_181773.5; NP_861438.3. [Q6NTF7-3]
DR UCSC; uc021wps.2; human. [Q6NTF7-1]
DR UCSC; uc062ejr.1; human.
DR CTD; 164668; -.
DR DisGeNET; 164668; -.
DR GeneCards; APOBEC3H; -.
DR HGNC; HGNC:24100; APOBEC3H.
DR HPA; ENSG00000100298; Low tissue specificity.
DR MIM; 610976; gene.
DR neXtProt; NX_Q6NTF7; -.
DR OpenTargets; ENSG00000100298; -.
DR PharmGKB; PA162376694; -.
DR VEuPathDB; HostDB:ENSG00000100298; -.
DR eggNOG; ENOG502TFVZ; Eukaryota.
DR GeneTree; ENSGT00940000162772; -.
DR HOGENOM; CLU_080056_4_0_1; -.
DR OMA; HVQGCYI; -.
DR OrthoDB; 1288872at2759; -.
DR PhylomeDB; Q6NTF7; -.
DR TreeFam; TF331356; -.
DR BRENDA; 3.5.4.38; 2681.
DR PathwayCommons; Q6NTF7; -.
DR Reactome; R-HSA-72200; mRNA Editing: C to U Conversion.
DR Reactome; R-HSA-75094; Formation of the Editosome.
DR SignaLink; Q6NTF7; -.
DR SIGNOR; Q6NTF7; -.
DR BioGRID-ORCS; 164668; 4 hits in 1064 CRISPR screens.
DR GeneWiki; APOBEC3H; -.
DR GenomeRNAi; 164668; -.
DR Pharos; Q6NTF7; Tbio.
DR PRO; PR:Q6NTF7; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q6NTF7; protein.
DR Bgee; ENSG00000100298; Expressed in granulocyte and 91 other tissues.
DR ExpressionAtlas; Q6NTF7; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0004126; F:cytidine deaminase activity; IDA:UniProtKB.
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 GO; GO:0048525; P:negative regulation of viral process; IMP:UniProtKB.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR041512; APOBEC3H.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR Pfam; PF18771; APOBEC3; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Antiviral defense; Coiled coil;
KW Cytoplasm; Hydrolase; Immunity; Innate immunity; Metal-binding; Nucleus;
KW Reference proteome; Zinc.
FT CHAIN 1..200
FT /note="DNA dC->dU-editing enzyme APOBEC-3H"
FT /id="PRO_0000291663"
FT DOMAIN 4..126
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT COILED 160..182
FT /evidence="ECO:0000255"
FT ACT_SITE 56
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT VAR_SEQ 140..200
FT /note="EFADCWENFVDHEKPLSFNPYKMLEELDKNSRAIKRRLERIKIPGVRAQGRY
FT MDILCDAEV -> NSRGTCAGSLHGYIV (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_047044"
FT VAR_SEQ 182..200
FT /note="IPGVRAQGRYMDILCDAEV -> S (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15461802,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_035034"
FT VAR_SEQ 182..200
FT /note="IPGVRAQGRYMDILCDAEV -> QS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039975"
FT VARIANT 15
FT /note="Missing (decreases protein stability)"
FT /evidence="ECO:0000269|PubMed:15461802,
FT ECO:0000269|PubMed:18779051"
FT /id="VAR_065622"
FT VARIANT 18
FT /note="R -> L (in dbSNP:rs139293)"
FT /evidence="ECO:0000269|PubMed:15461802"
FT /id="VAR_032835"
FT VARIANT 105
FT /note="G -> R (in allele A3H-Var; haplotype 2; allele
FT presenting a higher expression and which is more effective
FT in retrotransposons and HIV-1 restriction; increases
FT protein stability; dbSNP:rs139297)"
FT /evidence="ECO:0000269|PubMed:15461802,
FT ECO:0000269|PubMed:18779051"
FT /id="VAR_032836"
FT VARIANT 121
FT /note="K -> E (in allele A3H-Var; haplotype 2; allele
FT presenting a higher expression and more effective in
FT retrotransposons and HIV-1 restriction; dbSNP:rs139298)"
FT /id="VAR_032837"
FT VARIANT 121
FT /note="K -> N (in dbSNP:rs139299)"
FT /id="VAR_032838"
FT VARIANT 140
FT /note="E -> K (in dbSNP:rs139300)"
FT /id="VAR_067444"
FT VARIANT 178
FT /note="E -> D (in allele A3H-Var; haplotype 2; allele
FT presenting a higher expression and more effective in
FT retrotransposons and HIV-1 restriction; dbSNP:rs139302)"
FT /evidence="ECO:0000269|PubMed:15461802"
FT /id="VAR_032839"
FT MUTAGEN 56
FT /note="E->Q: Reduces the ability to inhibit the
FT retrotransposition of LINE-1 elements."
FT /evidence="ECO:0000269|PubMed:18827027"
FT CONFLICT 121
FT /note="K -> D (in Ref. 2; CAG30367)"
FT /evidence="ECO:0000305"
FT HELIX 6..13
FT /evidence="ECO:0007829|PDB:5W45"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:6B0B"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:5W45"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:6B0B"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:5W45"
FT HELIX 55..66
FT /evidence="ECO:0007829|PDB:5W45"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:6B0B"
FT STRAND 74..82
FT /evidence="ECO:0007829|PDB:5W45"
FT HELIX 86..98
FT /evidence="ECO:0007829|PDB:5W45"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:5W45"
FT HELIX 117..129
FT /evidence="ECO:0007829|PDB:5W45"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:5W45"
FT HELIX 138..148
FT /evidence="ECO:0007829|PDB:5W45"
FT HELIX 159..177
FT /evidence="ECO:0007829|PDB:5W45"
SQ SEQUENCE 200 AA; 23532 MW; 67A9E01382CC9388 CRC64;
MALLTAETFR LQFNNKRRLR RPYYPRKALL CYQLTPQNGS TPTRGYFENK KKCHAEICFI
NEIKSMGLDE TQCYQVTCYL TWSPCSSCAW ELVDFIKAHD HLNLGIFASR LYYHWCKPQQ
KGLRLLCGSQ VPVEVMGFPE FADCWENFVD HEKPLSFNPY KMLEELDKNS RAIKRRLERI
KIPGVRAQGR YMDILCDAEV
