APOBEC3G

Available structures

Human UniProt search: PDBe RCSB

List of PDB id codes
2JYW, 2KBO, 2KEM, 3E1U, 3IQS, 3IR2, 3V4J, 3V4K, 4ROV, 4ROW

Identifiers

Aliases

APOBEC3G, A3G, ARCD, ARP-9, ARP9, CEM-15, CEM15, MDS019, bK150C2.7, dJ494G10.1, apolipoprotein B mRNA editing enzyme catalytic subunit 3G

External IDs

OMIM: 607113 HomoloGene: 128348 GeneCards: APOBEC3G

Gene ontology
Molecular function	• protein homodimerization activity • cytidine deaminase activity • protein binding • catalytic activity • hydrolase activity • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines • metal ion binding • deoxycytidine deaminase activity • RNA binding • zinc ion binding • dCTP deaminase activity
Cellular component	• intracellular ribonucleoprotein complex • nucleus • apolipoprotein B mRNA editing enzyme complex • cytosol • cytoplasm • P-body
Biological process	• cytidine deamination • negative regulation of single stranded viral RNA replication via double stranded DNA intermediate • negative regulation of transposition • base conversion or substitution editing • immune system process • DNA cytosine deamination • positive regulation of defense response to virus by host • negative regulation of viral genome replication • negative regulation of viral process • defense response to virus • innate immune response • viral process
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


60489


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Ensembl


ENSG00000239713


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UniProt


Q9HC16


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RefSeq (mRNA)


NM_021822


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RefSeq (protein)


NP_068594


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Location (UCSC)

Chr 22: 39.04 – 39.09 Mb

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PubMed search

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2JYW, 2KBO, 2KEM, 3E1U, 3IQS, 3IR2, 3V4J, 3V4K, 4ROV, 4ROW

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APOBEC3G (apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3G) is a human enzyme encoded by the APOBEC3G gene that belongs to the APOBEC superfamily of proteins. This family of proteins has been suggested to play an important role in innate anti-viral immunity. APOBEC3G belongs to the family of cytidine deaminases that catalyze the deamination of cytidine to uridine in the single stranded DNA substrate. The C-terminal domain of A3G renders catalytic activity, several NMR and crystal structures explain the substrate specificity and catalytic activity

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