ENDOV_HUMAN
ID ENDOV_HUMAN Reviewed; 282 AA.
AC Q8N8Q3; I3L3S4; Q6P2G2; Q86X99; Q8NAK0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Endonuclease V;
DE Short=hEndoV;
DE EC=3.1.26.- {ECO:0000269|PubMed:23912683, ECO:0000269|PubMed:23912718, ECO:0000269|PubMed:25195743, ECO:0000269|PubMed:27573237, ECO:0000269|PubMed:31703097};
DE AltName: Full=Inosine-specific endoribonuclease;
GN Name=ENDOV;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 5).
RC TISSUE=Prostate;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-29; GLN-112; ARG-114;
RP TYR-141 AND ASN-201.
RG NIEHS SNPs program;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Brain, and Duodenum;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PRELIMINARY ACTIVITY.
RX PubMed=22664237; DOI=10.1016/j.mrfmmm.2012.05.003;
RA Mi R., Alford-Zappala M., Kow Y.W., Cunningham R.P., Cao W.;
RT "Human endonuclease V as a repair enzyme for DNA deamination.";
RL Mutat. Res. 735:12-18(2012).
RN [7]
RP FUNCTION (ISOFORM 1), AND SUBCELLULAR LOCATION (ISOFORM 1).
RX PubMed=23139746; DOI=10.1371/journal.pone.0047466;
RA Fladeby C., Vik E.S., Laerdahl J.K., Gran Neurauter C., Heggelund J.E.,
RA Thorgaard E., Strom-Andersen P., Bjoras M., Dalhus B., Alseth I.;
RT "The human homolog of Escherichia coli endonuclease V is a nucleolar
RT protein with affinity for branched DNA structures.";
RL PLoS ONE 7:E47466-E47466(2012).
RN [8]
RP FUNCTION (ISOFORM 1), CATALYTIC ACTIVITY (ISOFORM 1), COFACTOR, AND
RP MUTAGENESIS OF ASP-52; 90-PRO--SER-93; TYR-91 AND 248-ARG-LYS-249.
RX PubMed=23912683; DOI=10.1038/ncomms3271;
RA Sebastian Vik E., Sameen Nawaz M., Strom Andersen P., Fladeby C.,
RA Bjoras M., Dalhus B., Alseth I.;
RT "Endonuclease V cleaves at inosines in RNA.";
RL Nat. Commun. 4:2271-2271(2013).
RN [9]
RP FUNCTION (ISOFORM 1), CATALYTIC ACTIVITY (ISOFORM 1), SUBCELLULAR LOCATION
RP (ISOFORM 1), AND MUTAGENESIS OF ASP-52; TYR-91 AND GLU-100.
RX PubMed=23912718; DOI=10.1038/ncomms3273;
RA Morita Y., Shibutani T., Nakanishi N., Nishikura K., Iwai S., Kuraoka I.;
RT "Human endonuclease V is a ribonuclease specific for inosine-containing
RT RNA.";
RL Nat. Commun. 4:2273-2273(2013).
RN [10]
RP FUNCTION (ISOFORM 1), CATALYTIC ACTIVITY (ISOFORM 1), ACTIVITY REGULATION
RP (ISOFORM 1), INTERACTION WITH PABPC1, SUBCELLULAR LOCATION (ISOFORM 1), AND
RP MUTAGENESIS OF ASP-52.
RX PubMed=27573237; DOI=10.1074/jbc.m116.730911;
RA Nawaz M.S., Vik E.S., Berges N., Fladeby C., Bjoeraas M., Dalhus B.,
RA Alseth I.;
RT "Regulation of Human Endonuclease V Activity and Relocalization to
RT Cytoplasmic Stress Granules.";
RL J. Biol. Chem. 291:21786-21801(2016).
RN [11]
RP ALTERNATIVE SPLICING (ISOFORMS 1; 6 AND 7), FUNCTION (ISOFORMS 1; 6 AND 7),
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION (ISOFORMS 1; 6 AND 7),
RP IDENTIFICATION BY MASS SPECTROMETRY (ISOFORM 7), AND MUTAGENESIS OF GLU-171
RP AND ARG-174.
RX PubMed=31703097; DOI=10.1371/journal.pone.0225081;
RA Berges N., Nawaz M.S., Boerresdatter Dahl T., Hagen L., Bjoeraas M.,
RA Laerdahl J.K., Alseth I.;
RT "Complex alternative splicing of human Endonuclease V mRNA, but evidence
RT for only a single protein isoform.";
RL PLoS ONE 14:e0225081-e0225081(2019).
RN [12] {ECO:0007744|PDB:4NSP}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 13-250, FUNCTION, CATALYTIC
RP ACTIVITY, SUBUNIT, AND MUTAGENESIS OF 35-ALA--PRO-40; 57-LYS--SER-60;
RP 115-GLU--MET-119; 161-ASP--ASN-166; CYS-225; CYS-226; CYS-227 AND CYS-228.
RX PubMed=25195743; DOI=10.1107/s139900471401356x;
RA Zhang Z., Hao Z., Wang Z., Li Q., Xie W.;
RT "Structure of human endonuclease V as an inosine-specific ribonuclease.";
RL Acta Crystallogr. D 70:2286-2294(2014).
CC -!- FUNCTION: [Isoform 1]: Endoribonuclease that specifically cleaves
CC inosine-containing RNAs: cleaves RNA at the second phosphodiester bond
CC 3' to inosine (PubMed:23912683, PubMed:23912718, PubMed:27573237,
CC PubMed:31703097, PubMed:25195743). Active against both single-stranded
CC and double-stranded RNAs (PubMed:31703097, PubMed:25195743). Has strong
CC preference for single-stranded RNAs (ssRNAs) toward double-stranded
CC RNAs (dsRNAs) (PubMed:23912718). Cleaves mRNAs and tRNAs containing
CC inosine (PubMed:23912683, PubMed:31703097). Also able to cleave
CC structure-specific dsRNA substrates containing the specific sites 5'-
CC IIUI-3' and 5'-UIUU-3' (PubMed:23912718, PubMed:27573237). Inosine is
CC present in a number of RNAs following editing; the function of inosine-
CC specific endoribonuclease is still unclear: it could either play a
CC regulatory role in edited RNAs, or be involved in antiviral response by
CC removing the hyperedited long viral dsRNA genome that has undergone A-
CC to-I editing (Probable). Binds branched DNA structures
CC (PubMed:23139746). {ECO:0000269|PubMed:23139746,
CC ECO:0000269|PubMed:23912683, ECO:0000269|PubMed:23912718,
CC ECO:0000269|PubMed:25195743, ECO:0000269|PubMed:27573237,
CC ECO:0000269|PubMed:31703097, ECO:0000305}.
CC -!- FUNCTION: [Isoform 6]: Endoribonuclease that specifically cleaves
CC inosine-containing RNAs: cleaves RNA at the second phosphodiester bond
CC 3' to inosine (PubMed:31703097). Active against both single-stranded
CC and double-stranded RNAs (PubMed:31703097). Cleaves tRNAs containing
CC inosine (PubMed:31703097). {ECO:0000269|PubMed:31703097}.
CC -!- FUNCTION: [Isoform 7]: Endoribonuclease that specifically cleaves
CC inosine-containing RNAs: cleaves RNA at the second phosphodiester bond
CC 3' to inosine (PubMed:31703097). Active against both single-stranded
CC and double-stranded RNAs (PubMed:31703097). Cleaves tRNAs containing
CC inosine (PubMed:31703097). {ECO:0000269|PubMed:31703097}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:23912683};
CC -!- ACTIVITY REGULATION: [Isoform 1]: Inhibited by normal intracellular
CC concentrations of ATP. {ECO:0000269|PubMed:27573237}.
CC -!- SUBUNIT: Monomer (PubMed:25195743). Interacts with PABPC1; the
CC interaction is RNA-dependent and stimulates ENDOV activity
CC (PubMed:27573237). {ECO:0000269|PubMed:25195743,
CC ECO:0000269|PubMed:27573237}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:23912718, ECO:0000269|PubMed:31703097}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:23139746, ECO:0000269|PubMed:31703097}.
CC Cytoplasm, Stress granule {ECO:0000269|PubMed:27573237}.
CC Note=Relocalizes to cytoplasmic stress granules upon cellular stress
CC where it colocalizes with PABPC1. {ECO:0000269|PubMed:27573237}.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm
CC {ECO:0000269|PubMed:31703097}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:31703097}. Cytoplasm, Stress granule
CC {ECO:0000269|PubMed:31703097}. Note=Relocalizes to cytoplasmic stress
CC granules upon cellular stress. {ECO:0000269|PubMed:31703097}.
CC -!- SUBCELLULAR LOCATION: [Isoform 7]: Cytoplasm
CC {ECO:0000269|PubMed:31703097}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:31703097}. Cytoplasm, Stress granule
CC {ECO:0000269|PubMed:31703097}. Note=Relocalizes to cytoplasmic stress
CC granules upon cellular stress. {ECO:0000269|PubMed:31703097}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=hENDOV 282 {ECO:0000303|PubMed:31703097};
CC IsoId=Q8N8Q3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N8Q3-2; Sequence=VSP_035229;
CC Name=3;
CC IsoId=Q8N8Q3-3; Sequence=VSP_035229, VSP_035231;
CC Name=4;
CC IsoId=Q8N8Q3-4; Sequence=VSP_035228, VSP_035230;
CC Name=5;
CC IsoId=Q8N8Q3-5; Sequence=VSP_035228;
CC Name=6; Synonyms=hENDOV 308 {ECO:0000303|PubMed:31703097};
CC IsoId=Q8N8Q3-6; Sequence=VSP_060583;
CC Name=7; Synonyms=hENDOV 309 {ECO:0000303|PubMed:31703097};
CC IsoId=Q8N8Q3-7; Sequence=VSP_035231;
CC -!- SIMILARITY: Belongs to the endonuclease V family. {ECO:0000305}.
CC -!- CAUTION: Was initially characterized as an endodeoxyribonuclease
CC involved in DNA repair (PubMed:22664237). While it shows some weak
CC endodeoxyribonuclease activity in vitro, such activity probably does
CC not exist in vivo. {ECO:0000305|PubMed:22664237}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/flj35220/";
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DR EMBL; AK092539; BAC03912.1; -; mRNA.
DR EMBL; AK096344; BAC04765.1; -; mRNA.
DR EMBL; AK096802; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; DQ500957; ABF47100.1; -; Genomic_DNA.
DR EMBL; AC120024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471099; EAW89607.1; -; Genomic_DNA.
DR EMBL; CH471099; EAW89605.1; -; Genomic_DNA.
DR EMBL; CH471099; EAW89615.1; -; Genomic_DNA.
DR EMBL; BC037889; AAH37889.1; -; mRNA.
DR EMBL; BC045824; AAH45824.1; -; mRNA.
DR EMBL; BC064545; AAH64545.1; -; mRNA.
DR CCDS; CCDS54172.1; -. [Q8N8Q3-1]
DR CCDS; CCDS54173.1; -. [Q8N8Q3-2]
DR CCDS; CCDS54174.1; -. [Q8N8Q3-3]
DR RefSeq; NP_001158109.1; NM_001164637.2. [Q8N8Q3-2]
DR RefSeq; NP_001158110.1; NM_001164638.1. [Q8N8Q3-3]
DR RefSeq; NP_775898.2; NM_173627.4. [Q8N8Q3-1]
DR RefSeq; XP_005257301.1; XM_005257244.3.
DR PDB; 4NSP; X-ray; 2.30 A; A=13-250.
DR PDB; 6OZE; X-ray; 1.50 A; A=9-254.
DR PDBsum; 4NSP; -.
DR PDBsum; 6OZE; -.
DR AlphaFoldDB; Q8N8Q3; -.
DR SMR; Q8N8Q3; -.
DR BioGRID; 129772; 16.
DR IntAct; Q8N8Q3; 9.
DR STRING; 9606.ENSP00000429190; -.
DR iPTMnet; Q8N8Q3; -.
DR PhosphoSitePlus; Q8N8Q3; -.
DR BioMuta; ENDOV; -.
DR DMDM; 74729504; -.
DR EPD; Q8N8Q3; -.
DR jPOST; Q8N8Q3; -.
DR MassIVE; Q8N8Q3; -.
DR MaxQB; Q8N8Q3; -.
DR PaxDb; Q8N8Q3; -.
DR PeptideAtlas; Q8N8Q3; -.
DR PRIDE; Q8N8Q3; -.
DR ProteomicsDB; 47312; -.
DR ProteomicsDB; 72445; -. [Q8N8Q3-1]
DR ProteomicsDB; 72446; -. [Q8N8Q3-2]
DR ProteomicsDB; 72447; -. [Q8N8Q3-3]
DR Antibodypedia; 32763; 27 antibodies from 11 providers.
DR DNASU; 284131; -.
DR Ensembl; ENST00000323854.9; ENSP00000317810.5; ENSG00000173818.17. [Q8N8Q3-3]
DR Ensembl; ENST00000517795.5; ENSP00000461577.1; ENSG00000173818.17. [Q8N8Q3-5]
DR Ensembl; ENST00000518137.6; ENSP00000429190.1; ENSG00000173818.17. [Q8N8Q3-1]
DR Ensembl; ENST00000518901.5; ENSP00000460685.1; ENSG00000173818.17. [Q8N8Q3-5]
DR Ensembl; ENST00000518907.5; ENSP00000458361.1; ENSG00000173818.17. [Q8N8Q3-4]
DR Ensembl; ENST00000520284.5; ENSP00000458391.1; ENSG00000173818.17. [Q8N8Q3-4]
DR Ensembl; ENST00000520367.5; ENSP00000431036.1; ENSG00000173818.17. [Q8N8Q3-2]
DR GeneID; 284131; -.
DR KEGG; hsa:284131; -.
DR MANE-Select; ENST00000518137.6; ENSP00000429190.1; NM_173627.5; NP_775898.2.
DR UCSC; uc002jyk.4; human. [Q8N8Q3-1]
DR CTD; 284131; -.
DR DisGeNET; 284131; -.
DR GeneCards; ENDOV; -.
DR HGNC; HGNC:26640; ENDOV.
DR HPA; ENSG00000173818; Low tissue specificity.
DR MIM; 619821; gene.
DR neXtProt; NX_Q8N8Q3; -.
DR OpenTargets; ENSG00000173818; -.
DR VEuPathDB; HostDB:ENSG00000173818; -.
DR eggNOG; KOG4417; Eukaryota.
DR GeneTree; ENSGT00390000011880; -.
DR HOGENOM; CLU_047631_0_1_1; -.
DR InParanoid; Q8N8Q3; -.
DR OMA; RIHFRQA; -.
DR OrthoDB; 1416056at2759; -.
DR PhylomeDB; Q8N8Q3; -.
DR TreeFam; TF300065; -.
DR BRENDA; 3.1.21.7; 2681.
DR BRENDA; 3.1.27.8; 2681.
DR PathwayCommons; Q8N8Q3; -.
DR SignaLink; Q8N8Q3; -.
DR BioGRID-ORCS; 284131; 16 hits in 1073 CRISPR screens.
DR GenomeRNAi; 284131; -.
DR Pharos; Q8N8Q3; Tbio.
DR PRO; PR:Q8N8Q3; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8N8Q3; protein.
DR Bgee; ENSG00000173818; Expressed in parotid gland and 161 other tissues.
DR ExpressionAtlas; Q8N8Q3; baseline and differential.
DR Genevisible; Q8N8Q3; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0016888; F:endodeoxyribonuclease activity, producing 5'-phosphomonoesters; ISS:UniProtKB.
DR GO; GO:0016891; F:endoribonuclease activity, producing 5'-phosphomonoesters; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR CDD; cd06559; Endonuclease_V; 1.
DR HAMAP; MF_00801; Endonuclease_5; 1.
DR InterPro; IPR007581; Endonuclease-V.
DR PANTHER; PTHR28511; PTHR28511; 1.
DR Pfam; PF04493; Endonuclease_5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; DNA-binding; Endonuclease;
KW Hydrolase; Magnesium; Metal-binding; Nuclease; Nucleus; Reference proteome;
KW RNA-binding.
FT CHAIN 1..282
FT /note="Endonuclease V"
FT /id="PRO_0000349223"
FT REGION 250..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305"
FT BINDING 126
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 91
FT /note="Interaction with target RNA"
FT /evidence="ECO:0000305"
FT VAR_SEQ 1..194
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_035228"
FT VAR_SEQ 77..121
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_035229"
FT VAR_SEQ 239..282
FT /note="ADICSREHIRKSLGLPGPPTPRSPKAQRPVACPKGDSGESSALC -> HFVE
FT RGGESTRPRLIPDRTRW (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035230"
FT VAR_SEQ 280..282
FT /note="ALC -> GEGQPPQDHSPGPRTAPRPGSQEQAGKDWQ (in isoform 3
FT and isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035231"
FT VAR_SEQ 280..282
FT /note="ALC -> GGAPSPQRQADRTTPGGRRSTAQHQVGQR (in isoform 6)"
FT /id="VSP_060583"
FT VARIANT 29
FT /note="V -> I (in dbSNP:rs35549084)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_046285"
FT VARIANT 112
FT /note="R -> Q (in dbSNP:rs34933300)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_046286"
FT VARIANT 114
FT /note="K -> R (in dbSNP:rs41298706)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_046287"
FT VARIANT 141
FT /note="H -> Y (in dbSNP:rs41299812)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_046288"
FT VARIANT 201
FT /note="D -> N (in dbSNP:rs35929621)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_046289"
FT MUTAGEN 35..40
FT /note="Missing: Does not gain activity against single- or
FT double-stranded DNA."
FT /evidence="ECO:0000269|PubMed:25195743"
FT MUTAGEN 52
FT /note="D->A: Abolishes ribonuclease activity."
FT /evidence="ECO:0000269|PubMed:23912683,
FT ECO:0000269|PubMed:23912718, ECO:0000269|PubMed:27573237"
FT MUTAGEN 57..60
FT /note="KGDS->QGGE: Does not gain activity against
FT single- or double-stranded DNA."
FT /evidence="ECO:0000269|PubMed:25195743"
FT MUTAGEN 90..93
FT /note="PYVS->GGGG: Abolishes ability to bind branched DNA
FT and RNA."
FT /evidence="ECO:0000269|PubMed:23912683"
FT MUTAGEN 91
FT /note="Y->A: Abolishes ribonuclease activity without
FT affecting ability to bind branched DNA."
FT /evidence="ECO:0000269|PubMed:23912683,
FT ECO:0000269|PubMed:23912718"
FT MUTAGEN 100
FT /note="E->A: Abolishes ribonuclease activity."
FT /evidence="ECO:0000269|PubMed:23912718"
FT MUTAGEN 115..119
FT /note="Missing: Does not gain activity against single- or
FT double-stranded DNA."
FT /evidence="ECO:0000269|PubMed:25195743"
FT MUTAGEN 161..166
FT /note="Missing: Does not gain activity against single- or
FT double-stranded DNA."
FT /evidence="ECO:0000269|PubMed:25195743"
FT MUTAGEN 171
FT /note="E->A: No effect on subcellular location or activity;
FT when associated with A-174."
FT /evidence="ECO:0000269|PubMed:31703097"
FT MUTAGEN 174
FT /note="R->A: No effect on subcellular location or activity;
FT when associated with A-171."
FT /evidence="ECO:0000269|PubMed:31703097"
FT MUTAGEN 225
FT /note="C->S: No significant effect on activity."
FT /evidence="ECO:0000269|PubMed:25195743"
FT MUTAGEN 226
FT /note="C->S: No significant effect on activity."
FT /evidence="ECO:0000269|PubMed:25195743"
FT MUTAGEN 227
FT /note="C->S: 68% decrease in activity."
FT /evidence="ECO:0000269|PubMed:25195743"
FT MUTAGEN 228
FT /note="C->S: 46% decrease in activity."
FT /evidence="ECO:0000269|PubMed:25195743"
FT MUTAGEN 248..249
FT /note="RK->AA: Abolishes ability to bind branched DNA and
FT RNA."
FT /evidence="ECO:0000269|PubMed:23912683"
FT CONFLICT 19
FT /note="R -> W (in Ref. 1; BAC03912)"
FT /evidence="ECO:0000305"
FT HELIX 11..25
FT /evidence="ECO:0007829|PDB:6OZE"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:6OZE"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:6OZE"
FT STRAND 60..71
FT /evidence="ECO:0007829|PDB:6OZE"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:6OZE"
FT STRAND 77..86
FT /evidence="ECO:0007829|PDB:6OZE"
FT HELIX 97..114
FT /evidence="ECO:0007829|PDB:6OZE"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:6OZE"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:6OZE"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:6OZE"
FT HELIX 138..146
FT /evidence="ECO:0007829|PDB:6OZE"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:6OZE"
FT HELIX 167..175
FT /evidence="ECO:0007829|PDB:6OZE"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:6OZE"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:6OZE"
FT STRAND 207..215
FT /evidence="ECO:0007829|PDB:6OZE"
FT HELIX 217..226
FT /evidence="ECO:0007829|PDB:6OZE"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:6OZE"
FT HELIX 234..250
FT /evidence="ECO:0007829|PDB:6OZE"
SQ 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
