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Endonuclease V (hEndoV) (EC 3.1.26.-) (Inosine-specific endoribonuclease)

 ENDOV_HUMAN             Reviewed;         282 AA.
Q8N8Q3; I3L3S4; Q6P2G2; Q86X99; Q8NAK0;
02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
27-SEP-2017, entry version 110.
RecName: Full=Endonuclease V;
Short=hEndoV;
EC=3.1.26.-;
AltName: Full=Inosine-specific endoribonuclease;
Name=ENDOV;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 5).
TISSUE=Prostate;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-29; GLN-112;
ARG-114; TYR-141 AND ASN-201.
NIEHS SNPs program;
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
TISSUE=Brain, and Duodenum;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PRELIMINARY ACTIVITY.
PubMed=22664237; DOI=10.1016/j.mrfmmm.2012.05.003;
Mi R., Alford-Zappala M., Kow Y.W., Cunningham R.P., Cao W.;
"Human endonuclease V as a repair enzyme for DNA deamination.";
Mutat. Res. 735:12-18(2012).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23139746; DOI=10.1371/journal.pone.0047466;
Fladeby C., Vik E.S., Laerdahl J.K., Gran Neurauter C.,
Heggelund J.E., Thorgaard E., Strom-Andersen P., Bjoras M., Dalhus B.,
Alseth I.;
"The human homolog of Escherichia coli endonuclease V is a nucleolar
protein with affinity for branched DNA structures.";
PLoS ONE 7:E47466-E47466(2012).
[8]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF ASP-52;
90-PRO--SER-93; TYR-91 AND 248-ARG-LYS-249.
PubMed=23912683; DOI=10.1038/ncomms3271;
Sebastian Vik E., Sameen Nawaz M., Strom Andersen P., Fladeby C.,
Bjoras M., Dalhus B., Alseth I.;
"Endonuclease V cleaves at inosines in RNA.";
Nat. Commun. 4:2271-2271(2013).
[9]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
ASP-52; TYR-91 AND GLU-100.
PubMed=23912718; DOI=10.1038/ncomms3273;
Morita Y., Shibutani T., Nakanishi N., Nishikura K., Iwai S.,
Kuraoka I.;
"Human endonuclease V is a ribonuclease specific for inosine-
containing RNA.";
Nat. Commun. 4:2273-2273(2013).
-!- FUNCTION: Endoribonuclease that specifically cleaves inosine-
containing RNAs: cleaves RNA at the second phosphodiester bond 3'
to inosine. Has strong preference for single-stranded RNAs
(ssRNAs) toward double-stranded RNAs (dsRNAs). Cleaves mRNAs and
tRNAs containing inosine. Also able to cleave structure-specific
dsRNA substrates containing the specific sites 5'-IIUI-3' and 5'-
UIUU-3'. 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. Binds
branched DNA structures. {ECO:0000269|PubMed:23139746,
ECO:0000269|PubMed:23912683, ECO:0000269|PubMed:23912718}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000305|PubMed:23912683};
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q8N8Q3-1; Sequence=Displayed;
Name=2;
IsoId=Q8N8Q3-2; Sequence=VSP_035229;
Name=3;
IsoId=Q8N8Q3-3; Sequence=VSP_035229, VSP_035231;
Name=4;
IsoId=Q8N8Q3-4; Sequence=VSP_035228, VSP_035230;
Name=5;
IsoId=Q8N8Q3-5; Sequence=VSP_035228;
-!- MISCELLANEOUS: Was initially characterized as an
endodeoxyribonuclease involved in DNA repair (PubMed:22664237).
While it shows some weak endodeoxyribonuclease activity in vitro,
such activity probably does not exist in vivo.
{ECO:0000305|PubMed:22664237}.
-!- SIMILARITY: Belongs to the endonuclease V family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/flj35220/";
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EMBL; AK092539; BAC03912.1; -; mRNA.
EMBL; AK096344; BAC04765.1; -; mRNA.
EMBL; AK096802; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; DQ500957; ABF47100.1; -; Genomic_DNA.
EMBL; AC120024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471099; EAW89607.1; -; Genomic_DNA.
EMBL; CH471099; EAW89605.1; -; Genomic_DNA.
EMBL; CH471099; EAW89615.1; -; Genomic_DNA.
EMBL; BC037889; AAH37889.1; -; mRNA.
EMBL; BC045824; AAH45824.1; -; mRNA.
EMBL; BC064545; AAH64545.1; -; mRNA.
CCDS; CCDS54172.1; -. [Q8N8Q3-1]
CCDS; CCDS54173.1; -. [Q8N8Q3-2]
CCDS; CCDS54174.1; -. [Q8N8Q3-3]
RefSeq; NP_001158109.1; NM_001164637.2. [Q8N8Q3-2]
RefSeq; NP_001158110.1; NM_001164638.1. [Q8N8Q3-3]
RefSeq; NP_775898.2; NM_173627.4. [Q8N8Q3-1]
UniGene; Hs.389678; -.
UniGene; Hs.728933; -.
PDB; 4NSP; X-ray; 2.30 A; A=13-250.
PDBsum; 4NSP; -.
ProteinModelPortal; Q8N8Q3; -.
SMR; Q8N8Q3; -.
BioGrid; 129772; 11.
IntAct; Q8N8Q3; 2.
MINT; MINT-1385974; -.
STRING; 9606.ENSP00000429190; -.
iPTMnet; Q8N8Q3; -.
PhosphoSitePlus; Q8N8Q3; -.
BioMuta; ENDOV; -.
DMDM; 74729504; -.
MaxQB; Q8N8Q3; -.
PaxDb; Q8N8Q3; -.
PeptideAtlas; Q8N8Q3; -.
PRIDE; Q8N8Q3; -.
DNASU; 284131; -.
Ensembl; ENST00000323854; ENSP00000317810; ENSG00000173818. [Q8N8Q3-3]
Ensembl; ENST00000517795; ENSP00000461577; ENSG00000173818. [Q8N8Q3-5]
Ensembl; ENST00000518137; ENSP00000429190; ENSG00000173818. [Q8N8Q3-1]
Ensembl; ENST00000518901; ENSP00000460685; ENSG00000173818. [Q8N8Q3-5]
Ensembl; ENST00000518907; ENSP00000458361; ENSG00000173818. [Q8N8Q3-4]
Ensembl; ENST00000520284; ENSP00000458391; ENSG00000173818. [Q8N8Q3-4]
Ensembl; ENST00000520367; ENSP00000431036; ENSG00000173818. [Q8N8Q3-2]
GeneID; 284131; -.
KEGG; hsa:284131; -.
UCSC; uc002jyk.4; human. [Q8N8Q3-1]
CTD; 284131; -.
DisGeNET; 284131; -.
EuPathDB; HostDB:ENSG00000173818.16; -.
GeneCards; ENDOV; -.
HGNC; HGNC:26640; ENDOV.
neXtProt; NX_Q8N8Q3; -.
OpenTargets; ENSG00000173818; -.
eggNOG; KOG4417; Eukaryota.
eggNOG; COG1515; LUCA.
GeneTree; ENSGT00390000011880; -.
HOVERGEN; HBG062398; -.
InParanoid; Q8N8Q3; -.
KO; K21813; -.
OMA; GYKLPEP; -.
OrthoDB; EOG091G0LHO; -.
PhylomeDB; Q8N8Q3; -.
TreeFam; TF300065; -.
GenomeRNAi; 284131; -.
PRO; PR:Q8N8Q3; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000173818; -.
ExpressionAtlas; Q8N8Q3; baseline and differential.
Genevisible; Q8N8Q3; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0016888; F:endodeoxyribonuclease activity, producing 5'-phosphomonoesters; ISS:UniProtKB.
GO; GO:0016891; F:endoribonuclease activity, producing 5'-phosphomonoesters; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
CDD; cd06559; Endonuclease_V; 1.
HAMAP; MF_00801; Endonuclease_5; 1.
InterPro; IPR007581; Endonuclease-V.
PANTHER; PTHR28511; PTHR28511; 1.
Pfam; PF04493; Endonuclease_5; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
DNA-binding; Endonuclease; Hydrolase; Magnesium; Metal-binding;
Nuclease; Nucleus; Polymorphism; Reference proteome; RNA-binding.
CHAIN 1 282 Endonuclease V.
/FTId=PRO_0000349223.
COMPBIAS 225 228 Poly-Cys.
METAL 52 52 Magnesium. {ECO:0000305}.
METAL 126 126 Magnesium. {ECO:0000250}.
SITE 91 91 Interaction with target RNA.
{ECO:0000305}.
VAR_SEQ 1 194 Missing (in isoform 4 and isoform 5).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_035228.
VAR_SEQ 77 121 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_035229.
VAR_SEQ 239 282 ADICSREHIRKSLGLPGPPTPRSPKAQRPVACPKGDSGESS
ALC -> HFVERGGESTRPRLIPDRTRW (in isoform
4). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_035230.
VAR_SEQ 280 282 ALC -> GEGQPPQDHSPGPRTAPRPGSQEQAGKDWQ (in
isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_035231.
VARIANT 29 29 V -> I (in dbSNP:rs35549084).
{ECO:0000269|Ref.2}.
/FTId=VAR_046285.
VARIANT 112 112 R -> Q (in dbSNP:rs34933300).
{ECO:0000269|Ref.2}.
/FTId=VAR_046286.
VARIANT 114 114 K -> R (in dbSNP:rs41298706).
{ECO:0000269|Ref.2}.
/FTId=VAR_046287.
VARIANT 141 141 H -> Y (in dbSNP:rs41299812).
{ECO:0000269|Ref.2}.
/FTId=VAR_046288.
VARIANT 201 201 D -> N (in dbSNP:rs35929621).
{ECO:0000269|Ref.2}.
/FTId=VAR_046289.
MUTAGEN 52 52 D->A: Abolishes ribonuclease activity.
{ECO:0000269|PubMed:23912683,
ECO:0000269|PubMed:23912718}.
MUTAGEN 90 93 PYVS->GGGG: Abolishes ability to bind
branched DNA and RNA.
{ECO:0000269|PubMed:23912683}.
MUTAGEN 91 91 Y->A: Abolishes ribonuclease activity
without affecting ability to bind
branched DNA.
{ECO:0000269|PubMed:23912683,
ECO:0000269|PubMed:23912718}.
MUTAGEN 100 100 E->A: Abolishes ribonuclease activity.
{ECO:0000269|PubMed:23912718}.
MUTAGEN 248 249 RK->AA: Abolishes ability to bind
branched DNA and RNA.
{ECO:0000269|PubMed:23912683}.
CONFLICT 19 19 R -> W (in Ref. 1; BAC03912).
{ECO:0000305}.
HELIX 15 25 {ECO:0000244|PDB:4NSP}.
HELIX 35 38 {ECO:0000244|PDB:4NSP}.
STRAND 47 55 {ECO:0000244|PDB:4NSP}.
STRAND 61 71 {ECO:0000244|PDB:4NSP}.
TURN 72 74 {ECO:0000244|PDB:4NSP}.
STRAND 77 86 {ECO:0000244|PDB:4NSP}.
HELIX 97 114 {ECO:0000244|PDB:4NSP}.
HELIX 116 118 {ECO:0000244|PDB:4NSP}.
STRAND 121 127 {ECO:0000244|PDB:4NSP}.
STRAND 129 132 {ECO:0000244|PDB:4NSP}.
HELIX 138 146 {ECO:0000244|PDB:4NSP}.
STRAND 150 156 {ECO:0000244|PDB:4NSP}.
HELIX 167 175 {ECO:0000244|PDB:4NSP}.
STRAND 182 186 {ECO:0000244|PDB:4NSP}.
STRAND 192 197 {ECO:0000244|PDB:4NSP}.
STRAND 207 215 {ECO:0000244|PDB:4NSP}.
HELIX 217 226 {ECO:0000244|PDB:4NSP}.
STRAND 229 232 {ECO:0000244|PDB:4NSP}.
HELIX 234 250 {ECO:0000244|PDB:4NSP}.
SEQUENCE 282 AA; 30792 MW; EDB10210FB508A51 CRC64;
MALEAAGGPP EETLSLWKRE QARLKAHVVD RDTEAWQRDP AFSGLQRVGG VDVSFVKGDS
VRACASLVVL SFPELEVVYE ESRMVSLTAP YVSGFLAFRE VPFLLELVQQ LREKEPGLMP
QVLLVDGNGV LHHRGFGVAC HLGVLTDLPC VGVAKKLLQV DGLENNALHK EKIRLLQTRG
DSFPLLGDSG TVLGMALRSH DRSTRPLYIS VGHRMSLEAA VRLTCCCCRF RIPEPVRQAD
ICSREHIRKS LGLPGPPTPR SPKAQRPVAC PKGDSGESSA LC


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