APOBEC3D

Identifiers

APOBEC3D, A3D, APOBEC3DE, APOBEC3E, ARP6, apolipoprotein B mRNA editing enzyme catalytic subunit 3D

External IDs

Gene ontology
Molecular function	• hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines • zinc ion binding • catalytic activity • hydrolase activity • metal ion binding
Cellular component	• cytoplasm • cytoplasmic mRNA processing body
Biological process	• negative regulation of transposition • innate immune response • defense response to virus • DNA cytosine deamination • negative regulation of single stranded viral RNA replication via double stranded DNA intermediate • immune system process
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


140564


n/a

Ensembl


ENSG00000243811


n/a

UniProt


Q96AK3


n/a

RefSeq (mRNA)


NM_152426


n/a

RefSeq (protein)


n/a


n/a

Location (UCSC)

Chr 22: 39.01 – 39.03 Mb

n/a

PubMed search

^[1]

n/a

Wikidata

View/Edit Human

Probable DNA dC->dU-editing enzyme APOBEC-3D is a protein that in humans is encoded by the APOBEC3D gene.^[2]^[3]

This gene is a member of the cytidine deaminase gene family. It is one of seven related genes or pseudogenes found in a cluster, thought to result from gene duplication, on chromosome 22. Members of the cluster encode proteins that are structurally and functionally related to the C to U RNA-editing cytidine deaminase APOBEC1 and inhibit retroviruses, such as HIV, by deaminating cytosine residues in nascent retroviral cDNA.^[3]

References

↑ "Human PubMed Reference:".
↑ Jarmuz A, Chester A, Bayliss J, Gisbourne J, Dunham I, Scott J, Navaratnam N (Feb 2002). "An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22". Genomics. 79 (3): 285–96. doi:10.1006/geno.2002.6718. PMID 11863358.
1 2 "Entrez Gene: APOBEC3D apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3D (putative)".

Wedekind JE, Dance GS, Sowden MP, Smith HC (2003). "Messenger RNA editing in mammals: new members of the APOBEC family seeking roles in the family business". Trends Genet. 19 (4): 207–16. doi:10.1016/S0168-9525(03)00054-4. PMID 12683974.
Harris RS, Liddament MT (2004). "Retroviral restriction by APOBEC proteins". Nat. Rev. Immunol. 4 (11): 868–77. doi:10.1038/nri1489. PMID 15516966.
Dunham I, Shimizu N, Roe BA, et al. (1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–95. doi:10.1038/990031. PMID 10591208.
Dias Neto E, Correa RG, Verjovski-Almeida S, et al. (2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags". Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3491–6. doi:10.1073/pnas.97.7.3491. PMC 16267. PMID 10737800.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Mariani R, Chen D, Schröfelbauer B, et al. (2003). "Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif". Cell. 114 (1): 21–31. doi:10.1016/S0092-8674(03)00515-4. PMID 12859895.
Sawyer SL, Emerman M, Malik HS (2006). "Ancient adaptive evolution of the primate antiviral DNA-editing enzyme APOBEC3G". PLoS Biol. 2 (9): E275. doi:10.1371/journal.pbio.0020275. PMC 479043. PMID 15269786.
Collins JE, Wright CL, Edwards CA, et al. (2005). "A genome annotation-driven approach to cloning the human ORFeome". Genome Biol. 5 (10): R84. doi:10.1186/gb-2004-5-10-r84. PMC 545604. PMID 15461802.
Dang Y, Wang X, Esselman WJ, Zheng YH (2006). "Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family". J. Virol. 80 (21): 10522–33. doi:10.1128/JVI.01123-06. PMC 1641744. PMID 16920826.
Kinomoto M, Kanno T, Shimura M, et al. (2007). "All APOBEC3 family proteins differentially inhibit LINE-1 retrotransposition". Nucleic Acids Res. 35 (9): 2955–64. doi:10.1093/nar/gkm181. PMC 1888823. PMID 17439959.

Hydrolases: carbon-nitrogen non-peptide (EC 3.5)

3.5.1: Linear amides / Amidohydrolases	Asparaginase Glutaminase Urease Biotinidase Aspartoacylase Ceramidase Aspartylglucosaminidase Fatty acid amide hydrolase Histone deacetylase Sirtuin

3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase Beta-lactamase

3.5.3: Linear amidines/ Ureohydrolases	Arginase Agmatinase Protein-arginine deiminase

3.5.4: Cyclic amidines/ Aminohydrolases	Guanine deaminase Adenosine deaminase AMP deaminase Inosine monophosphate synthase DCMP deaminase GTP cyclohydrolase I Cytidine deaminase AICDA Activation-induced cytidine deaminase

3.5.5: Nitriles/ Aminohydrolases	Nitrilase

3.5.99: Other	Riboflavinase Thiaminase II

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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APOBEC3D

References

Further reading