ID   ABC3H_PONPY             Reviewed;         211 AA.
AC   Q1WBT4;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 60.
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   Pongo pygmaeus (Bornean orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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).
CC   -!- FUNCTION: DNA deaminase (cytidine deaminase) which may act as an
CC       inhibitor of retrovirus replication and retrotransposon mobility via
CC       deaminase-dependent and -independent mechanisms. {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; DQ408610; ABD72581.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1WBT4; -.
DR   SMR; Q1WBT4; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR   GO; GO:0004126; F:cytidine deaminase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR   GO; GO:0070383; P:DNA cytosine deamination; ISS:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0010529; P:negative regulation of transposition; ISS:UniProtKB.
DR   GO; GO:0048525; P:negative regulation of viral process; ISS: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   2: Evidence at transcript level;
KW   Antiviral defense; Cytoplasm; Hydrolase; Immunity; Innate immunity;
KW   Metal-binding; Zinc.
FT   CHAIN           1..211
FT                   /note="DNA dC->dU-editing enzyme APOBEC-3H"
FT                   /id="PRO_0000291665"
FT   DOMAIN          4..126
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
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   211 AA;  24654 MW;  0B9812EE2AD5DD1E CRC64;
     MALLTAKTFS LQFNNKRRIK RPYYPRKALL CYQLTPQNGS TPTRGYFKNK KKCHAEIRFI
     NEIKSMGLDE TQCYQVTCYL TWSPCPSCVR ELVAFIKAHD HLNLRIFASR LYCHWCRRQQ
     EGLRLLCGSQ VPVEVMGSRE FADCWENFVD HEKPLSFNPS EMLEELDKNS RAIKRRLERI
     KQSWSVDVLE NGLRSLQLGP VSSSLSRSNS R