APOBEC
| APOBEC-like N-terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | APOBEC_N | ||||||||
| Pfam | PF08210 | ||||||||
| InterPro | IPR013158 | ||||||||
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| Available protein structures: | |
|---|---|
| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
| APOBEC-like C-terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | APOBEC_C | ||||||||
| Pfam | PF05240 | ||||||||
| InterPro | IPR007904 | ||||||||
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| Available protein structures: | |
|---|---|
| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
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.
In humans/mammals they help protect from viral infections. These enzymes, when misregulated, are a major source of mutation in numerous cancer types.
A 2013 review discussed the structural and biophysical aspects of APOBEC3 family enzymes. Much of the APOBEC protein features are described in the widely studied APOBEC3G's page.
Human genes encoding members of the APOBEC protein family include:
This article incorporates text from the public domain Pfam and InterPro IPR013158
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