ABC3H_MACMU
ID ABC3H_MACMU Reviewed; 210 AA.
AC Q19Q52;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=DNA dC->dU-editing enzyme APOBEC-3H;
DE EC=3.5.4.38;
DE AltName: Full=Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3H;
GN Name=APOBEC3H;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Spleen;
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 [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [3]
RP 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 [4]
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).
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. Exhibits antiviral activity
CC against vif-deficient HIV-1. After the penetration of retroviral
CC nucleocapsids into target cells of infection and the initiation of
CC reverse transcription, it can induce the conversion of cytosine to
CC uracil in the minus-sense single-strand viral DNA, leading to G-to-A
CC hypermutations in the subsequent plus-strand viral DNA. The resultant
CC detrimental levels of mutations in the proviral genome, along with a
CC deamination-independent mechanism that works prior to the proviral
CC integration, together exert efficient antiretroviral effects in
CC infected target cells. Selectively targets single-stranded DNA and does
CC not deaminate double-stranded DNA or single- or double-stranded RNA.
CC {ECO:0000269|PubMed:16571802, ECO:0000269|PubMed:18779051,
CC ECO:0000269|PubMed:21835787}.
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 simian
CC immunodeficiency virus rhesus (SIV-mac) virion infectivity factor
CC (VIF). {ECO:0000269|PubMed:21835787}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18779051,
CC ECO:0000269|PubMed:21653666, ECO:0000269|PubMed:21835787}.
CC -!- MISCELLANEOUS: APOBEC3H from old world monkeys has retained its
CC antiviral activity, while it is lost in other primates.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
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DR EMBL; DQ507277; ABF72849.1; -; mRNA.
DR RefSeq; NP_001035831.1; NM_001042372.1.
DR AlphaFoldDB; Q19Q52; -.
DR SMR; Q19Q52; -.
DR STRING; 9544.ENSMMUP00000001363; -.
DR eggNOG; KOG4075; Eukaryota.
DR InParanoid; Q19Q52; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; ISS: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; IBA:GO_Central.
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 Antiviral defense; Cytoplasm; Hydrolase; Immunity; Innate immunity;
KW Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..210
FT /note="DNA dC->dU-editing enzyme APOBEC-3H"
FT /id="PRO_0000291664"
FT DOMAIN 4..126
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT REGION 182..210
FT /note="Necessary and sufficient for localization to the
FT cytoplasm"
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"
SQ SEQUENCE 210 AA; 24327 MW; 71EC09F63C440F55 CRC64;
MALLTAKTFS LQFNNKRRVN KPYYPRKALL CYQLTPQNGS TPTRGHLKNK KKDHAEIRFI
NKIKSMGLDE TQCYQVTCYL TWSPCPSCAG ELVDFIKAHR HLNLRIFASR LYYHWRPNYQ
EGLLLLCGSQ VPVEVMGLPE FTDCWENFVD HKEPPSFNPS EKLEELDKNS QAIKRRLERI
KSRSVDVLEN GLRSLQLGPV TPSSSIRNSR
