ID   ABEC3_CRILO             Reviewed;         396 AA.
AC   P60704;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2004, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=DNA dC->dU-editing enzyme APOBEC3;
DE            EC=3.5.4.38;
GN   Name=APOBEC3;
OS   Cricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Ovarian carcinoma;
RA   Mariani R., Landau N.R.;
RL   Submitted (FEB-2004) to UniProtKB.
RN   [2]
RP   FUNCTION.
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).
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. Selectively targets single-
CC       stranded DNA and does not deaminate double-stranded DNA or single- or
CC       double-stranded RNA. {ECO:0000269|PubMed:12859895}.
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: The CMP/dCMP deaminase domain 1 confers deoxycytidine deaminase
CC       activity, whereas the CMP/dCMP deaminase domain 2 mediates RNA-
CC       dependent oligomerization and virion incorporation. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Probable human APOBEC3G ortholog.
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000305}.
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DR   AlphaFoldDB; P60704; -.
DR   SMR; P60704; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0010529; P:negative regulation of transposition; ISS: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   3: Inferred from homology;
KW   Antiviral defense; Cytoplasm; Hydrolase; Immunity; Innate immunity;
KW   Metal-binding; Repeat; Zinc.
FT   CHAIN           1..396
FT                   /note="DNA dC->dU-editing enzyme APOBEC3"
FT                   /id="PRO_0000171771"
FT   DOMAIN          38..154
FT                   /note="CMP/dCMP-type deaminase 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   DOMAIN          205..324
FT                   /note="CMP/dCMP-type deaminase 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   ACT_SITE        73
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         255
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         283
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         286
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   396 AA;  47075 MW;  BBB497D2E200E52F CRC64;
     MGPFCLGCSH RKCYSPIRNL ISQETFKFHF KNLGYAKGRK DTFLCYEVTR KDCDSPVSLH
     HGVFKNKGNI HAEVCFLYWF HDKVLKVLSP REEFKITWYM SWSPCFECAE QIVRFLATHH
     YLSLDIFSSR LYNVQDPETQ QNLCRLVQEG AQVAAMDLYE FKKCWKKFVT MVAGDSGLGK
     RLLTNFRYQD SKLQEILRRM DPLSEEEFYS QFYNQRVKHL CYYHRMKPYL CYQLEQFNGQ
     APLKGCLLSE KGKQHAEILF LDKIRSMELS QVTITCYLTW SPCPNCAWRL AAFKRDRPDL
     ILHIYTSRLY FHWKRPFQKG LCSLWQSGIL VDVMDLPQFT DCWTNFVNPK RPFWPWKGLE
     IISRRTQRRL RRIKESWGLQ DLVNDFGNLQ LGPPMS