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Example of a member of the APOBEC family, APOBEC-2. A cytidine deaminase from Homo sapiens.[1]
APOBEC-like N-terminal domain
Pfam PF08210
InterPro IPR013158
APOBEC-like C-terminal domain
Pfam PF05240
InterPro IPR007904

APOBEC ("apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like") is a family of evolutionarily conserved cytidine deaminases.

A mechanism of generating protein diversity is mRNA editing. Members of this family are C-to-U editing enzymes. The N-terminal domain of APOBEC like proteins is the catalytic domain, while the C-terminal domain is a pseudocatalytic domain. More specifically, the catalytic domain is a zinc dependent cytidine deaminase domain and is essential for cytidine deamination. RNA editing by APOBEC-1 requires homodimerisation and this complex interacts with RNA binding proteins to form the editosome.[2]

In humans/mammals they help protect from viral infections.[3] These enzymes, when misregulated, are a major source of mutation in numerous cancer types.[3]

A 2013 review discussed the structural and biophysical aspects of APOBEC3 family enzymes.[4] Much of the APOBEC protein features are described in the widely studied APOBEC3G's page.

Family members[edit]

Human genes encoding members of the APOBEC protein family include:


  1. ^ PDB: 2NYT​; Prochnow, C.; Bransteitter, R.; Klein, M.G.; Goodman, M.F.; Chen, X.S.; functional implications for the deaminase AID. (2007). "The APOBEC-2 crystal structure". Nature. 445 (7126): 447–451. PMID 17187054. doi:10.1038/nature05492. ; rendered using PyMOL.
  2. ^ Wedekind JE, Dance GS, Sowden MP, Smith HC (April 2003). "Messenger RNA editing in mammals: new members of the APOBEC family seeking roles in the family business". Trends Genet. 19 (4): 207–16. PMID 12683974. doi:10.1016/S0168-9525(03)00054-4. 
  3. ^ a b Unexpected DNA-Binding Mechanism Suggests Ways to Block Enzyme Activity in Cancer
  4. ^ Jaguva Vasudevan, AA; Smits SH; Höppner A; Häussinger D; Koenig BW; Münk C. (June 2013). "Structural features of antiviral DNA cytidine deaminases". Biol Chem. 394 (11): 1357–1370. PMID 23787464. doi:10.1515/hsz-2013-0165. 

This article incorporates text from the public domain Pfam and InterPro IPR013158