APOBEC3D

APOBEC3D
Identifiers
Aliases	APOBEC3D, A3D, APOBEC3DE, APOBEC3E, ARP6, apolipoprotein B mRNA editing enzyme catalytic subunit 3D, A3DE
External IDs	OMIM: 609900; HomoloGene: 122788; GeneCards: APOBEC3D; OMA:APOBEC3D - orthologs
Gene location (Human)
Chr.	Chromosome 22 (human)
End	39,033,277 bp
RNA expression pattern
	Top expressed in
	granulocyte; ; lymph node; ; spleen; ; bone marrow cell; ; blood; ; appendix; ; right uterine tube; ; monocyte; ; gallbladder; ; rectum;
	n/a
	More reference expression data
	n/a
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; RNA binding; cytidine deaminase activity;
Cellular component	cytoplasm; P-body; nucleus;
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; cytidine deamination; cytidine to uridine editing; DNA demethylation;
	Sources:Amigo / QuickGO
Orthologs
	140564
	n/a
	ENSG00000243811
	n/a
	B2CML4
	n/a
	NM_152426; NM_001363781
	n/a
	NP_689639; NP_001350710
	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.^[3]^[4]

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.^[4]

Function

APOBEC3D is one of the human APOBEC3 enzymes involved in restriction of HIV-1.^[5]^[6] HIV-1 Vif counteracts APOBEC3D by recruiting ubiquitin-ligase machinery that leads to its polyubiquitination and proteasomal degradation in virus-producing cells.^[5]^[6]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000243811 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Jarmuz A, Chester A, Bayliss J, Gisbourne J, Dunham I, Scott J, et al. (February 2002). "An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22". Genomics. 79 (3): 285–296. doi:10.1006/geno.2002.6718. PMID 11863358.
1 2 "Entrez Gene: APOBEC3D apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3D (putative)".
1 2 Delviks-Frankenberry KA, Desimmie BA, Pathak VK (May 2020). "Structural Insights into APOBEC3-Mediated Lentiviral Restriction". Viruses. 12 (6): 587. doi:10.3390/v12060587. PMC 7354603. PMID 32471198.
1 2 Feng Y, Baig TT, Love RP, Chelico L (2014). "Suppression of APOBEC3-mediated restriction of HIV-1 by Vif". Frontiers in Microbiology. 5 450. doi:10.3389/fmicb.2014.00450. PMC 4144255. PMID 25206352.

External links

Human APOBEC3D genome location and APOBEC3D gene details page in the UCSC Genome Browser.

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 in Genetics. 19 (4): 207–216. doi:10.1016/S0168-9525(03)00054-4. PMID 12683974.
Harris RS, Liddament MT (2004). "Retroviral restriction by APOBEC proteins". Nature Reviews. Immunology. 4 (11): 868–877. doi:10.1038/nri1489. PMID 15516966. S2CID 10789405.
Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, et al. (December 1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–495. Bibcode:1999Natur.402..489D. doi:10.1038/990031. PMID 10591208.
Dias Neto E, Correa RG, Verjovski-Almeida S, Briones MR, Nagai MA, da Silva W, et al. (March 2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags". Proceedings of the National Academy of Sciences of the United States of America. 97 (7): 3491–3496. Bibcode:2000PNAS...97.3491D. doi:10.1073/pnas.97.7.3491. PMC 16267. PMID 10737800.
Mariani R, Chen D, Schröfelbauer B, Navarro F, König R, Bollman B, et al. (July 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 Biology. 2 (9): E275. doi:10.1371/journal.pbio.0020275. PMC 479043. PMID 15269786.
Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, et al. (2004). "A genome annotation-driven approach to cloning the human ORFeome". Genome Biology. 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". Journal of Virology. 80 (21): 10522–10533. doi:10.1128/JVI.01123-06. PMC 1641744. PMID 16920826.
Kinomoto M, Kanno T, Shimura M, Ishizaka Y, Kojima A, Kurata T, et al. (2007). "All APOBEC3 family proteins differentially inhibit LINE-1 retrotransposition". Nucleic Acids Research. 35 (9): 2955–2964. doi:10.1093/nar/gkm181. PMC 1888823. PMID 17439959.

This article on a gene on human chromosome 22 is a stub. You can help Wikipedia by adding missing information.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000243811 – Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid11863358-3] Jarmuz A, Chester A, Bayliss J, Gisbourne J, Dunham I, Scott J, et al. (February 2002). "An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22". Genomics. 79 (3): 285–296. doi:10.1006/geno.2002.6718. PMID 11863358.

[entrez-4] 1 2 "Entrez Gene: APOBEC3D apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3D (putative)".

[A3Restriction-5] 1 2 Delviks-Frankenberry KA, Desimmie BA, Pathak VK (May 2020). "Structural Insights into APOBEC3-Mediated Lentiviral Restriction". Viruses. 12 (6): 587. doi:10.3390/v12060587. PMC 7354603. PMID 32471198.

[VifReview-6] 1 2 Feng Y, Baig TT, Love RP, Chelico L (2014). "Suppression of APOBEC3-mediated restriction of HIV-1 by Vif". Frontiers in Microbiology. 5 450. doi:10.3389/fmicb.2014.00450. PMC 4144255. PMID 25206352.

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v t e Hydrolases: carbon-nitrogen non-peptide (EC 3.5)
3.5.1: Linear amides / Amidohydrolases	Asparaginase Glutaminase Urease Biotinidase Aminoacylase ACY1 Aspartoacylase(ACY2) ACY3 Ceramidase Aspartylglucosaminidase Fatty acid amide hydrolase Histone deacetylase Sirtuin
3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase Beta-lactamase Dihydroorotase
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

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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APOBEC3D

Function

References

External links

Further reading