AB3CA_FELCA
ID AB3CA_FELCA Reviewed; 192 AA.
AC Q4VDN5;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=DNA dC->dU-editing enzyme APOBEC-3Ca {ECO:0000305};
DE EC=3.5.4.38 {ECO:0000250|UniProtKB:A9QA56};
DE AltName: Full=Antiviral cytidine deaminase A3Ca {ECO:0000312|EMBL:ABW83272.1};
GN Name=APOBEC3CA {ECO:0000312|EMBL:ABW83272.1};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000312|EMBL:AAY40463.1};
RN [1] {ECO:0000312|EMBL:AAY40463.1}
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH FELINE FOAMY VIRUS PROTEIN
RP BET, AND ACTIVITY AGAINST BET-DEFICIENT FELINE FOAMY VIRUS.
RX PubMed=15911774; DOI=10.1073/pnas.0501445102;
RA Loechelt M., Romen F., Bastone P., Muckenfuss H., Kirchner N., Kim Y.B.,
RA Truyen U., Rosler U., Battenberg M., Saib A., Flory E., Cichutek K.,
RA Muenk C.;
RT "The antiretroviral activity of APOBEC3 is inhibited by the foamy virus
RT accessory Bet protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:7982-7987(2005).
RN [2] {ECO:0000312|EMBL:ABW83272.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND ACTIVITY AGAINST
RP BET-DEFICIENT FELINE FOAMY VIRUS.
RX PubMed=18315870; DOI=10.1186/gb-2008-9-3-r48;
RA Munk C., Beck T., Zielonka J., Hotz-Wagenblatt A., Chareza S.,
RA Battenberg M., Thielebein J., Cichutek K., Bravo I.G., O'Brien S.J.,
RA Lochelt M., Yuhki N.;
RT "Functions, structure, and read-through alternative splicing of feline
RT APOBEC3 genes.";
RL Genome Biol. 9:RESEARCH48.1-RESEARCH48.2(2008).
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 (By similarity). Selectively
CC targets single-stranded DNA and does not deaminate double-stranded DNA
CC or single- or double-stranded RNA (By similarity). Does not reduce
CC infectivity of foamy feline virus, feline immunodeficiency virus or
CC feline leukemia virus (PubMed:18315870). {ECO:0000250|UniProtKB:P60705,
CC ECO:0000269|PubMed:18315870}.
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 Evidence={ECO:0000250|UniProtKB:A9QA56};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9GZX7};
CC -!- SUBUNIT: (Microbial infection) Interacts with feline foamy virus
CC protein Bet (PubMed:15911774). This interaction does not induce
CC APOBEC3Ca degradation but prevents its dimerization and incorporation
CC into the virion (Probable). {ECO:0000269|PubMed:15911774,
CC ECO:0000305|PubMed:18315870}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NRW3}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9NRW3}.
CC -!- MISCELLANEOUS: One of 3 related APOBEC3C genes in cat, APOBEC3Ca,
CC APOBEC3Cb and APOBEC3Cc, which are likely to have been generated after
CC two consecutive gene duplications. {ECO:0000269|PubMed:18315870}.
CC -!- MISCELLANEOUS: Potent inhibitor of Bet-deficient foamy feline virus
CC (PubMed:15911774, PubMed:18315870). Does not inhibit Vif-deficient
CC feline immunodeficiency virus (PubMed:18315870).
CC {ECO:0000269|PubMed:15911774, ECO:0000269|PubMed:18315870}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
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DR EMBL; AY971954; AAY40463.1; -; mRNA.
DR EMBL; EU109281; ABW83272.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4VDN5; -.
DR SMR; Q4VDN5; -.
DR Proteomes; UP000011712; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
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; Metal-binding; Nucleus;
KW Reference proteome; Zinc.
FT CHAIN 1..192
FT /note="DNA dC->dU-editing enzyme APOBEC-3Ca"
FT /id="PRO_0000450521"
FT DOMAIN 15..141
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 71
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
SQ SEQUENCE 192 AA; 23500 MW; 3D847C6DF8F821B2 CRC64;
MEPWRPSPRN PMDRIDPNTF RFHFPNLLYA SGRKLCYLCF QVETEDYFSC DDSDRGVFRN
KVHPWARCHA EQCFLSWFRD QYPYRDEYYN VTWFLSWSPC PTCAEEVVEF LEEYRNLTLS
IFTSRLYYFW DPNYQEGLCK LWDAGVQLDI MSCDDFKHCW DNFVDHKGMR FQRRNLLKDY
DFLAAELQEI LR
