Endonuclease V

Available protein structures:
PDB	IPR007581 PF04493 (ECOD; PDBsum)
AlphaFold	IPR007581; PF04493;

Endonuclease V
Endonuclease V
	Crystallographic structure of Thermotoga maritima endoV (blue) in complex with DNA (green and orange). The deamidated base is shown in yellow.
Identifiers
Symbol	ENDOV
Pfam	PF04493
InterPro	IPR007581
PDB
Available protein structures:
PDB	IPR007581 PF04493 (ECOD; PDBsum)
AlphaFold	IPR007581; PF04493;

ENDOV
Identifiers
Aliases	ENDOV, endonuclease V, Endonuclease V, Endonuclease-V, IPR007581
External IDs	MGI: 2444688; GeneCards: ENDOV
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4NSP
Gene location (Human)
Chr.	Chromosome 17 (human)
End	80,438,086 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	119,402,263 bp
RNA expression pattern
	Top expressed in
	parotid gland; ; right uterine tube; ; external globus pallidus; ; vena cava; ; right hemisphere of cerebellum; ; left testis; ; right testis; ; anterior pituitary; ; nucleus accumbens; ; body of uterus;
	Top expressed in
	genital tubercle; ; tail of embryo; ; ventricular zone; ; granulocyte; ; lip; ; dentate gyrus of hippocampal formation granule cell; ; spermatocyte; ; lumbar subsegment of spinal cord; ; neural layer of retina; ; superior frontal gyrus;
	More reference expression data
	n/a
Gene ontology
Molecular function	endodeoxyribonuclease activity, producing 5'-phosphomonoesters; endonuclease activity; metal ion binding; single-stranded RNA binding; endoribonuclease activity, producing 5'-phosphomonoesters; hydrolase activity; RNA binding; nuclease activity; magnesium ion binding; DNA binding;
Cellular component	nucleus; cytoplasm; nucleolus;
Biological process	nucleic acid phosphodiester bond hydrolysis; DNA repair; RNA phosphodiester bond hydrolysis, endonucleolytic;
	Sources:Amigo / QuickGO
Orthologs
Databases	NCBI: entry; OMA: entry
	284131
	338371
	ENSG00000173818
	ENSMUSG00000039850
	Q8N8Q3
	Q8C9A2
	NM_001164637; NM_001164638; NM_173627; NM_001352760; NM_001352761
	NM_001164636; NM_177394
	NP_001158109; NP_001158110; NP_775898; NP_001339689; NP_001339690
	NP_001158108; NP_796368; NP_001388988; NP_001388989
	Wikidata
View/Edit Human	View/Edit Mouse

Endonuclease V (endoV) is a highly conserved endonuclease enzyme family. The primary function of endoV differs significantly in prokaryotes and eukaryotes, as suggested by studies on the E. coli and human orthologs.

In prokaryotes endoV is primarily a deoxyribonuclease involved in DNA repair of deoxyinosine introduced into the genome by deamidation of adenine bases (EC 3.1.21.7). However, it has broad substrate specificity and can also act on other types of DNA lesions as well as on inosine-containing RNA.

In eukaryotes endoV is primarily a ribonuclease and cleaves single-stranded RNA at the 3' position relative to an inosine base, which may be present due to RNA editing by deaminase enzymes (EC 3.1.26.-). The human endoV localizes to the cytoplasm and nucleoli, suggesting a possible role in processes involving ribosomal RNA. The human gene symbol is ENDOV.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000173818 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000039850 – 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.
↑ Dalhus B, Arvai AS, Rosnes I, Olsen ØE, Backe PH, Alseth I, Gao H, Cao W, Tainer JA, Bjørås M (February 2009). "Structures of endonuclease V with DNA reveal initiation of deaminated adenine repair". Nature Structural & Molecular Biology. 16 (2): 138–43. doi:10.1038/nsmb.1538. PMC 3560532. PMID 19136958.
1 2 Vik ES, Nawaz MS, Strøm Andersen P, Fladeby C, Bjørås M, Dalhus B, Alseth I (2013). "Endonuclease V cleaves at inosines in RNA". Nature Communications. 4 2271. Bibcode:2013NatCo...4.2271S. doi:10.1038/ncomms3271. PMC 3741635. PMID 23912683.
1 2 Fladeby C, Vik ES, Laerdahl JK, Gran Neurauter C, Heggelund JE, Thorgaard E, Strøm-Andersen P, Bjørås M, Dalhus B, Alseth I (2012). "The human homolog of Escherichia coli endonuclease V is a nucleolar protein with affinity for branched DNA structures". PLOS ONE. 7 (11) e47466. Bibcode:2012PLoSO...747466F. doi:10.1371/journal.pone.0047466. PMC 3489907. PMID 23139746.
↑ Morita Y, Shibutani T, Nakanishi N, Nishikura K, Iwai S, Kuraoka I (2013). "Human endonuclease V is a ribonuclease specific for inosine-containing RNA". Nature Communications. 4 2273. Bibcode:2013NatCo...4.2273M. doi:10.1038/ncomms3273. PMC 3741642. PMID 23912718.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000173818 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000039850 – Ensembl, May 2017

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

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

[5] Dalhus B, Arvai AS, Rosnes I, Olsen ØE, Backe PH, Alseth I, Gao H, Cao W, Tainer JA, Bjørås M (February 2009). "Structures of endonuclease V with DNA reveal initiation of deaminated adenine repair". Nature Structural & Molecular Biology. 16 (2): 138–43. doi:10.1038/nsmb.1538. PMC 3560532. PMID 19136958.

[vik-6] 1 2 Vik ES, Nawaz MS, Strøm Andersen P, Fladeby C, Bjørås M, Dalhus B, Alseth I (2013). "Endonuclease V cleaves at inosines in RNA". Nature Communications. 4 2271. Bibcode:2013NatCo...4.2271S. doi:10.1038/ncomms3271. PMC 3741635. PMID 23912683.

[Fladeby_2012-7] 1 2 Fladeby C, Vik ES, Laerdahl JK, Gran Neurauter C, Heggelund JE, Thorgaard E, Strøm-Andersen P, Bjørås M, Dalhus B, Alseth I (2012). "The human homolog of Escherichia coli endonuclease V is a nucleolar protein with affinity for branched DNA structures". PLOS ONE. 7 (11) e47466. Bibcode:2012PLoSO...747466F. doi:10.1371/journal.pone.0047466. PMC 3489907. PMID 23139746.

[morita-8] Morita Y, Shibutani T, Nakanishi N, Nishikura K, Iwai S, Kuraoka I (2013). "Human endonuclease V is a ribonuclease specific for inosine-containing RNA". Nature Communications. 4 2273. Bibcode:2013NatCo...4.2273M. doi:10.1038/ncomms3273. PMC 3741642. PMID 23912718.

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)