APOBEC4: Difference between revisions

APOBEC4
Identifiers
Aliases	APOBEC4, C1orf169, apolipoprotein B mRNA editing enzyme catalytic polypeptide like 4
External IDs	OMIM: 609908; MGI: 1918531; HomoloGene: 52415; GeneCards: APOBEC4; OMA:APOBEC4 - orthologs
Gene location (Human)
Chr.	Chromosome 1 (human)
End	183,653,316 bp
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)
End	152,633,295 bp
RNA expression pattern
	Top expressed in
	bronchial epithelial cell; ; olfactory zone of nasal mucosa; ; mucosa of paranasal sinus; ; sperm; ; right uterine tube; ; epithelium of nasopharynx; ; left testis; ; right testis; ; caput epididymis; ; right lung;
	Top expressed in
	seminiferous tubule; ; spermatid; ; spermatocyte; ; olfactory epithelium; ; islet of Langerhans;
	More reference expression data
	n/a
Orthologs
	403314
	71281
	ENSG00000173627
	ENSMUSG00000055547
	Q8WW27
	n/a
	NM_203454
	NM_001081197
	NP_982279
	n/a
	Wikidata
View/Edit Human	View/Edit Mouse

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Latest revision as of 11:32, 17 October 2022

C->U-editing enzyme APOBEC-4, also known as Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 4, is a protein that in humans is encoded by the APOBEC4 gene. It is primarily expressed in testis and found in mammals, chicken, but not fishes.^[5]^[6]

Function

This gene encodes a member of the AID / APOBEC family of polynucleotide (deoxy)cytidine deaminases, which convert cytidine to uridine. Other AID/APOBEC family members are involved in mRNA editing, somatic hypermutation and recombination of immunoglobulin genes, and innate immunity to retroviral infection.^[6]

A recent study on APOBEC4 (A4) revealed an interesting finding that A4 enhanced the replication of HIV-1 through boosting promoter activity, it also increased the expression of other relevant promoter mediated enhanced protein expression. Biochemical analysis of A4 showed the lack of cytidine deaminase activity on single stranded DNA and it binds DNA rather weak.^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000173627 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000055547 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Rogozin IB, Basu MK, Jordan IK, Pavlov YI, Koonin EV (September 2005). "APOBEC4, a new member of the AID/APOBEC family of polynucleotide (deoxy)cytidine deaminases predicted by computational analysis". Cell Cycle. 4 (9): 1281–5. doi:10.4161/cc.4.9.1994. PMID 16082223.
^ ^a ^b "Entrez Gene: apolipoprotein B mRNA editing enzyme".
^ Marino D, Perković M, Hain A, Jaguva Vasudevan AA, Hofmann H, Hanschmann KM, Mühlebach MD, Schumann GG, König R, Cichutek K, Häussinger D, Münk C (2016). "APOBEC4 Enhances the Replication of HIV-1". PLOS ONE. 11 (6): e0155422. Bibcode:2016PLoSO..1155422M. doi:10.1371/journal.pone.0155422. PMC 4889046. PMID 27249646.

External links

Human APOBEC4 genome location and APOBEC4 gene details page in the UCSC Genome Browser.

@@ Line 1: / Line 1: @@
+{{Short description|Protein-coding gene in the species Homo sapiens}}
 {{Infobox_gene}}
-'''C->U-editing enzyme APOBEC-4''', also known as '''Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 4''', is a [[protein]] that in humans is encoded by the '''''APOBEC4''''' [[gene]]. It is primarily expressed in testis and found in mammals, chicken, but not fishes.<ref name="pmid16082223">{{cite journal | vauthors = Rogozin IB, Basu MK, Jordan IK, Pavlov YI, Koonin EV | title = APOBEC4, a new member of the AID/APOBEC family of polynucleotide (deoxy)cytidine deaminases predicted by computational analysis | journal = Cell Cycle | volume = 4 | issue = 9 | pages = 1281–5 | date = September 2005 | pmid = 16082223 | doi = 10.4161/cc.4.9.1994 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: apolipoprotein B mRNA editing enzyme| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=403314| accessdate = }}</ref>
+'''C->U-editing enzyme APOBEC-4''', also known as '''Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 4''', is a [[protein]] that in humans is encoded by the '''''APOBEC4''''' [[gene]]. It is primarily expressed in testis and found in mammals, chicken, but not fishes.<ref name="pmid16082223">{{cite journal | vauthors = Rogozin IB, Basu MK, Jordan IK, Pavlov YI, Koonin EV | title = APOBEC4, a new member of the AID/APOBEC family of polynucleotide (deoxy)cytidine deaminases predicted by computational analysis | journal = Cell Cycle | volume = 4 | issue = 9 | pages = 1281–5 | date = September 2005 | pmid = 16082223 | doi = 10.4161/cc.4.9.1994 | doi-access = free }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: apolipoprotein B mRNA editing enzyme| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=403314}}</ref>
 == Function ==
@@ Line 6: / Line 7: @@
 This gene encodes a member of the AID / [[APOBEC]] family of polynucleotide (deoxy)[[cytidine deaminase]]s, which convert [[cytidine]] to [[uridine]]. Other AID/APOBEC family members are involved in mRNA editing, somatic hypermutation and recombination of immunoglobulin genes, and innate immunity to retroviral infection.<ref name="entrez"/>
-A recent study on APOBEC4 (A4) revealed an interesting finding that A4 enhanced the replication of HIV-1 through boosting promoter activity, it also increased the expression of other relevant promoter mediated enhanced protein expression. Biochemical analysis of A4 showed the lack of cytidine deaminase activity and it binds DNA rather weak.<ref>{{cite journal | vauthors = Marino D, Perković M, Hain A, Jaguva Vasudevan AA, Hofmann H, Hanschmann KM, Mühlebach MD, Schumann GG, König R, Cichutek K, Häussinger D, Münk C | title = APOBEC4 Enhances the Replication of HIV-1 | journal = PloS One | volume = 11 | issue = 6 | pages = e0155422 | date = 2016 | pmid = 27249646 | doi = 10.1371/journal.pone.0155422 }}</ref>
+A recent study on APOBEC4 (A4) revealed an interesting finding that A4 enhanced the replication of HIV-1 through boosting promoter activity, it also increased the expression of other relevant promoter mediated enhanced protein expression. Biochemical analysis of A4 showed the lack of cytidine deaminase activity on single stranded DNA and it binds DNA rather weak.<ref>{{cite journal | vauthors = Marino D, Perković M, Hain A, Jaguva Vasudevan AA, Hofmann H, Hanschmann KM, Mühlebach MD, Schumann GG, König R, Cichutek K, Häussinger D, Münk C | title = APOBEC4 Enhances the Replication of HIV-1 | journal = PLOS ONE | volume = 11 | issue = 6 | pages = e0155422 | date = 2016 | pmid = 27249646 | doi = 10.1371/journal.pone.0155422 | pmc=4889046| bibcode = 2016PLoSO..1155422M | doi-access = free }}</ref>
 == References ==
 {{reflist}}
+==External links==
+* {{UCSC gene info|APOBEC4}}
 == Further reading ==
 {{refbegin}}
-* {{cite journal | vauthors = Prochnow C, Bransteitter R, Chen XS | title = APOBEC deaminases-mutases with defensive roles for immunity | journal = Science in China. Series C, Life Sciences / Chinese Academy of Sciences | volume = 52 | issue = 10 | pages = 893–902 | date = October 2009 | pmid = 19911124 | doi = 10.1007/s11427-009-0133-1 }}
+* {{cite journal | vauthors = Prochnow C, Bransteitter R, Chen XS | title = APOBEC deaminases-mutases with defensive roles for immunity | journal = Science in China Series C: Life Sciences | volume = 52 | issue = 10 | pages = 893–902 | date = October 2009 | pmid = 19911124 | doi = 10.1007/s11427-009-0133-1 | s2cid = 22054803 }}
 {{refend}}
@@ Line 19: / Line 23: @@
 {{Carbon-nitrogen non-peptide hydrolases}}
 {{Enzymes}}
-{{Portal bar|Molecular and Cellular Biology|border=no}}
+{{Portal bar|Biology|border=no}}
 [[Category:EC 3.5.4]]

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)