ENDOV
entrez
284131
canonical
uniprot
Q8N8Q3
canonical
ensembl
ENSG00000173818
resolver
ensp
ENSP00000317810
resolver
ensp
ENSP00000429190
resolver
ensp
ENSP00000430639
resolver
ensp
ENSP00000431036
resolver
ensp
ENSP00000528880
resolver
ensp
ENSP00000528882
resolver
ensp
ENSP00000662616
resolver
ensp
ENSP00000662621
resolver
ensp
ENSP00000662622
resolver
ensp
ENSP00000771667
resolver
ensp
ENSP00000771668
resolver
genesymbol
ENDOV
resolver
hgnc
HGNC:26640
resolver
uniprot
I3L3S4
resolver
uniprot
Q6P2G2
resolver
uniprot
Q86X99
resolver
uniprot
Q8NAK0
resolver
uniprot_entry
ENDOV_HUMAN
resolver
uniprot_sec
I3L3S4
resolver
uniprot_sec
Q6P2G2
resolver
uniprot_sec
Q86X99
resolver
uniprot_sec
Q8NAK0
resolver
activity_regulation
ACTIVITY REGULATION: [Isoform 1]: Inhibited by normal intracellular concentrations of ATP. {ECO:0000269|PubMed:27573237}.
uniprot
proteins
amino_acid_sequence
MALEAAGGPPEETLSLWKREQARLKAHVVDRDTEAWQRDPAFSGLQRVGGVDVSFVKGDSVRACASLVVLSFPELEVVYEESRMVSLTAPYVSGFLAFREVPFLLELVQQLREKEPGLMPQVLLVDGNGVLHHRGFGVACHLGVLTDLPCVGVAKKLLQVDGLENNALHKEKIRLLQTRGDSFPLLGDSGTVLGMALRSHDRSTRPLYISVGHRMSLEAAVRLTCCCCRFRIPEPVRQADICSREHIRKSLGLPGPPTPRSPKAQRPVACPKGDSGESSALC
uniprot
proteins
ec_number
3.1.26.-
uniprot
proteins
function
FUNCTION: [Isoform 1]: Endoribonuclease that specifically cleaves inosine-containing RNAs: cleaves RNA at the second phosphodiester bond 3' to inosine (PubMed:23912683, PubMed:23912718, PubMed:25195743, PubMed:27573237, PubMed:31703097). Active against both single-stranded and double-stranded RNAs (PubMed:25195743, PubMed:31703097). Has strong preference for single-stranded RNAs (ssRNAs) toward double-stranded RNAs (dsRNAs) (PubMed:23912718). Cleaves mRNAs and tRNAs containing inosine (PubMed:23912683, PubMed:31703097). Also able to cleave structure-specific dsRNA substrates containing the specific sites 5'-IIUI-3' and 5'-UIUU-3' (PubMed:23912718, PubMed:27573237). Inosine is present in a number of RNAs following editing; the function of inosine-specific endoribonuclease is still unclear: it could either play a regulatory role in edited RNAs, or be involved in antiviral response by removing the hyperedited long viral dsRNA genome that has undergone A-to-I editing (Probable). Binds branched DNA structures (PubMed:23139746). {ECO:0000269|PubMed:23139746, ECO:0000269|PubMed:23912683, ECO:0000269|PubMed:23912718, ECO:0000269|PubMed:25195743, ECO:0000269|PubMed:27573237, ECO:0000269|PubMed:31703097, ECO:0000305}.; FUNCTION: [Isoform 6]: Endoribonuclease that specifically cleaves inosine-containing RNAs: cleaves RNA at the second phosphodiester bond 3' to inosine (PubMed:31703097). Active against both single-stranded and double-stranded RNAs (PubMed:31703097). Cleaves tRNAs containing inosine (PubMed:31703097). {ECO:0000269|PubMed:31703097}.; FUNCTION: [Isoform 7]: Endoribonuclease that specifically cleaves inosine-containing RNAs: cleaves RNA at the second phosphodiester bond 3' to inosine (PubMed:31703097). Active against both single-stranded and double-stranded RNAs (PubMed:31703097). Cleaves tRNAs containing inosine (PubMed:31703097). {ECO:0000269|PubMed:31703097}.
uniprot
proteins
mass_dalton
30792
uniprot
proteins
mutagenesis
MUTAGEN 35..40; /note="Missing: Does not gain activity against single- or double-stranded DNA."; /evidence="ECO:0000269|PubMed:25195743"; MUTAGEN 52; /note="D->A: Abolishes ribonuclease activity."; /evidence="ECO:0000269|PubMed:23912683, ECO:0000269|PubMed:23912718, ECO:0000269|PubMed:27573237"; MUTAGEN 57..60; /note="KGDS->QGGE: Does not gain activity against single- or double-stranded DNA."; /evidence="ECO:0000269|PubMed:25195743"; MUTAGEN 90..93; /note="PYVS->GGGG: Abolishes ability to bind branched DNA and RNA."; /evidence="ECO:0000269|PubMed:23912683"; MUTAGEN 91; /note="Y->A: Abolishes ribonuclease activity without affecting ability to bind branched DNA."; /evidence="ECO:0000269|PubMed:23912683, ECO:0000269|PubMed:23912718"; MUTAGEN 100; /note="E->A: Abolishes ribonuclease activity."; /evidence="ECO:0000269|PubMed:23912718"; MUTAGEN 115..119; /note="Missing: Does not gain activity against single- or double-stranded DNA."; /evidence="ECO:0000269|PubMed:25195743"; MUTAGEN 161..166; /note="Missing: Does not gain activity against single- or double-stranded DNA."; /evidence="ECO:0000269|PubMed:25195743"; MUTAGEN 171; /note="E->A: No effect on subcellular location or activity; when associated with A-174."; /evidence="ECO:0000269|PubMed:31703097"; MUTAGEN 174; /note="R->A: No effect on subcellular location or activity; when associated with A-171."; /evidence="ECO:0000269|PubMed:31703097"; MUTAGEN 225; /note="C->S: No significant effect on activity."; /evidence="ECO:0000269|PubMed:25195743"; MUTAGEN 226; /note="C->S: No significant effect on activity."; /evidence="ECO:0000269|PubMed:25195743"; MUTAGEN 227; /note="C->S: 68% decrease in activity."; /evidence="ECO:0000269|PubMed:25195743"; MUTAGEN 228; /note="C->S: 46% decrease in activity."; /evidence="ECO:0000269|PubMed:25195743"; MUTAGEN 248..249; /note="RK->AA: Abolishes ability to bind branched DNA and RNA."; /evidence="ECO:0000269|PubMed:23912683
uniprot
proteins
protein_family
Endonuclease V family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
22664237
uniprot
proteins
pubmed
23139746
uniprot
proteins
pubmed
23912683
uniprot
proteins
pubmed
23912718
uniprot
proteins
pubmed
25195743
uniprot
proteins
pubmed
27573237
uniprot
proteins
pubmed
31703097
uniprot
proteins
sequence_length
282
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:23912718, ECO:0000269|PubMed:31703097}. Nucleus, nucleolus {ECO:0000269|PubMed:23139746, ECO:0000269|PubMed:31703097}. Cytoplasm, Stress granule {ECO:0000269|PubMed:27573237}. Note=Relocalizes to cytoplasmic stress granules upon cellular stress where it colocalizes with PABPC1. {ECO:0000269|PubMed:27573237}.; SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm {ECO:0000269|PubMed:31703097}. Nucleus, nucleolus {ECO:0000269|PubMed:31703097}. Cytoplasm, Stress granule {ECO:0000269|PubMed:31703097}. Note=Relocalizes to cytoplasmic stress granules upon cellular stress. {ECO:0000269|PubMed:31703097}.; SUBCELLULAR LOCATION: [Isoform 7]: Cytoplasm {ECO:0000269|PubMed:31703097}. Nucleus, nucleolus {ECO:0000269|PubMed:31703097}. Cytoplasm, Stress granule {ECO:0000269|PubMed:31703097}. Note=Relocalizes to cytoplasmic stress granules upon cellular stress. {ECO:0000269|PubMed:31703097}.
uniprot
proteins