APOBEC

File:Apobec.J.Steinfeld.D.png

Example of a member of the APOBEC family, APOBEC-2. A cytidine deaminase from Homo sapiens.

APOBEC-like N-terminal domain
Identifiers
Symbol	APOBEC_N
Pfam	PF08210
InterPro	IPR013158
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
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 proteins.

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. A recent 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.

Family members

Human genes encoding members of the APOBEC protein family include:

• APOBEC1
• APOBEC2
• APOBEC3A
• APOBEC3B
• APOBEC3C
• APOBEC3D ("APOBEC3E" now refers to this)
• APOBEC3F
• APOBEC3G
• APOBEC3H
• APOBEC4
• Activation-induced (cytidine) deaminase

References

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