ABEC3_RAT
ID ABEC3_RAT Reviewed; 429 AA.
AC P60705;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=DNA dC->dU-editing enzyme APOBEC3;
DE EC=3.5.4.38;
GN Name=Apobec3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE.
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; P60705; -.
DR SMR; P60705; -.
DR iPTMnet; P60705; -.
DR PhosphoSitePlus; P60705; -.
DR PRIDE; P60705; -.
DR UCSC; RGD:1307800; rat.
DR RGD; 1307800; Apobec3.
DR InParanoid; P60705; -.
DR PhylomeDB; P60705; -.
DR Reactome; R-RNO-72200; mRNA Editing: C to U Conversion.
DR Reactome; R-RNO-75094; Formation of the Editosome.
DR PRO; PR:P60705; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0000932; C:P-body; ISO:RGD.
DR GO; GO:0004126; F:cytidine deaminase activity; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0070383; P:DNA cytosine deamination; ISO:RGD.
DR GO; GO:0080111; P:DNA demethylation; IBA:GO_Central.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0010529; P:negative regulation of transposition; ISS:UniProtKB.
DR GO; GO:0045071; P:negative regulation of viral genome replication; ISO:RGD.
DR GO; GO:0048525; P:negative regulation of viral process; ISO:RGD.
DR GO; GO:0050688; P:regulation of defense response to virus; ISO:RGD.
DR GO; GO:1903900; P:regulation of viral life cycle; ISO:RGD.
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; Reference proteome; Repeat; Zinc.
FT CHAIN 1..429
FT /note="DNA dC->dU-editing enzyme APOBEC3"
FT /id="PRO_0000171773"
FT DOMAIN 38..154
FT /note="CMP/dCMP-type deaminase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT DOMAIN 238..357
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 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 429 AA; 51084 MW; FEEEC7C49AA6C9A4 CRC64;
MGPFCLGCSH RKCYSPIRNL ISQETFKFHF KNLRYAIDRK DTFLCYEVTR KDCDSPVSLH
HGVFKNKDNI HAEICFLYWF HDKVLKVLSP REEFKITWYM SWSPCFECAE QVLRFLATHH
NLSLDIFSSR LYNIRDPENQ QNLCRLVQEG AQVAAMDLYE FKKCWKKFVD NGGRRFRPWK
KLLTNFRYQD SKLQEILRPC YIPVPSSSSS TLSNICLTKG LPETRFCVER RRVHLLSEEE
FYSQFYNQRV KHLCYYHGVK PYLCYQLEQF NGQAPLKGCL LSEKGKQHAE ILFLDKIRSM
ELSQVIITCY LTWSPCPNCA WQLAAFKRDR PDLILHIYTS RLYFHWKRPF QKGLCSLWQS
GILVDVMDLP QFTDCWTNFV NPKRPFWPWK GLEIISRRTQ RRLHRIKESW GLQDLVNDFG
NLQLGPPMS
