ENDOV_MOUSE
ID ENDOV_MOUSE Reviewed; 338 AA.
AC Q8C9A2; B1ATE4; Q3TCQ4; Q8C3Y1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Endonuclease V;
DE EC=3.1.26.- {ECO:0000250|UniProtKB:Q8N8Q3};
GN Name=Endov;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), COFACTOR, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF SER-93 AND GLN-133.
RX PubMed=12853604; DOI=10.1093/nar/gkg472;
RA Moe A., Ringvoll J., Nordstrand L.M., Eide L., Bjoras M., Seeberg E.,
RA Rognes T., Klungland A.;
RT "Incision at hypoxanthine residues in DNA by a mammalian homologue of the
RT Escherichia coli antimutator enzyme endonuclease V.";
RL Nucleic Acids Res. 31:3893-3900(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, and Heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
CC -!- FUNCTION: Endoribonuclease that specifically cleaves inosine-containing
CC RNAs: cleaves RNA at the second phosphodiester bond 3' to inosine.
CC Active against both single-stranded and double-stranded RNAs. Has
CC strong preference for single-stranded RNAs (ssRNAs) toward double-
CC stranded RNAs (dsRNAs). Cleaves mRNAs and tRNAs containing inosine.
CC Also able to cleave structure-specific dsRNA substrates containing the
CC specific sites 5'-IIUI-3' and 5'-UIUU-3'. Inosine is present in a
CC number of RNAs following editing; the function of inosine-specific
CC endoribonuclease is still unclear: it could either play a regulatory
CC role in edited RNAs, or be involved in antiviral response by removing
CC the hyperedited long viral dsRNA genome that has undergone A-to-I
CC editing. Binds branched DNA structures. {ECO:0000250|UniProtKB:Q8N8Q3}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12853604};
CC -!- SUBUNIT: Monomer. Interacts with PABPC1; the interaction is RNA-
CC dependent and stimulates ENDOV activity.
CC {ECO:0000250|UniProtKB:Q8N8Q3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N8Q3}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:Q8N8Q3}. Cytoplasm, Stress
CC granule {ECO:0000250|UniProtKB:Q8N8Q3}. Note=Relocalizes to cytoplasmic
CC stress granules upon cellular stress where it colocalizes with PABPC1.
CC {ECO:0000250|UniProtKB:Q8N8Q3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C9A2-3; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C9A2-1; Sequence=VSP_041579;
CC -!- TISSUE SPECIFICITY: Highest levels detected in liver with high levels
CC also found in heart, kidney and testis. Expressed at low levels in
CC brain. {ECO:0000269|PubMed:12853604}.
CC -!- MISCELLANEOUS: Was initially characterized as an endodeoxyribonuclease
CC involved in DNA repair (PubMed:12853604). While it shows some weak
CC endodeoxyribonuclease activity in vitro, such activity probably does
CC not exist in vivo. {ECO:0000305|PubMed:12853604}.
CC -!- SIMILARITY: Belongs to the endonuclease V family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC39216.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AK042626; BAC31310.1; -; mRNA.
DR EMBL; AK084548; BAC39216.1; ALT_SEQ; mRNA.
DR EMBL; AK170595; BAE41901.1; -; mRNA.
DR EMBL; AK172181; BAE42869.1; -; mRNA.
DR EMBL; AL645911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466558; EDL34709.1; -; Genomic_DNA.
DR EMBL; BC056486; AAH56486.1; -; mRNA.
DR CCDS; CCDS25718.1; -. [Q8C9A2-1]
DR CCDS; CCDS48999.1; -. [Q8C9A2-3]
DR RefSeq; NP_001158108.1; NM_001164636.1. [Q8C9A2-3]
DR RefSeq; NP_796368.1; NM_177394.3. [Q8C9A2-1]
DR PDB; 5AOY; X-ray; 1.75 A; A=1-250.
DR PDB; 6OZJ; X-ray; 2.25 A; A/B=1-253.
DR PDB; 6OZK; X-ray; 2.10 A; A/B=6-250.
DR PDB; 6OZL; X-ray; 2.10 A; A/B=1-253.
DR PDB; 6OZM; X-ray; 2.15 A; A/B=1-253.
DR PDB; 6OZN; X-ray; 1.90 A; A/B=1-253.
DR PDB; 6OZO; X-ray; 2.23 A; A/B=1-253.
DR PDB; 6OZP; X-ray; 1.96 A; A/B=8-252.
DR PDB; 6OZQ; X-ray; 2.15 A; A/B=1-253.
DR PDB; 6OZR; X-ray; 2.15 A; A/B=1-253.
DR PDB; 6OZS; X-ray; 2.41 A; A/B=6-252.
DR PDBsum; 5AOY; -.
DR PDBsum; 6OZJ; -.
DR PDBsum; 6OZK; -.
DR PDBsum; 6OZL; -.
DR PDBsum; 6OZM; -.
DR PDBsum; 6OZN; -.
DR PDBsum; 6OZO; -.
DR PDBsum; 6OZP; -.
DR PDBsum; 6OZQ; -.
DR PDBsum; 6OZR; -.
DR PDBsum; 6OZS; -.
DR AlphaFoldDB; Q8C9A2; -.
DR SMR; Q8C9A2; -.
DR STRING; 10090.ENSMUSP00000101851; -.
DR PhosphoSitePlus; Q8C9A2; -.
DR EPD; Q8C9A2; -.
DR MaxQB; Q8C9A2; -.
DR PaxDb; Q8C9A2; -.
DR PRIDE; Q8C9A2; -.
DR ProteomicsDB; 277834; -. [Q8C9A2-3]
DR ProteomicsDB; 277835; -. [Q8C9A2-1]
DR Antibodypedia; 32763; 27 antibodies from 11 providers.
DR Ensembl; ENSMUST00000106244; ENSMUSP00000101851; ENSMUSG00000039850. [Q8C9A2-3]
DR Ensembl; ENSMUST00000106245; ENSMUSP00000132755; ENSMUSG00000039850. [Q8C9A2-1]
DR Ensembl; ENSMUST00000129327; ENSMUSP00000119599; ENSMUSG00000039850. [Q8C9A2-1]
DR GeneID; 338371; -.
DR KEGG; mmu:338371; -.
DR UCSC; uc007mqt.2; mouse. [Q8C9A2-3]
DR CTD; 284131; -.
DR MGI; MGI:2444688; Endov.
DR VEuPathDB; HostDB:ENSMUSG00000039850; -.
DR eggNOG; KOG4417; Eukaryota.
DR GeneTree; ENSGT00390000011880; -.
DR InParanoid; Q8C9A2; -.
DR OrthoDB; 1416056at2759; -.
DR PhylomeDB; Q8C9A2; -.
DR TreeFam; TF300065; -.
DR BRENDA; 3.1.21.7; 3474.
DR BioGRID-ORCS; 338371; 3 hits in 107 CRISPR screens.
DR ChiTaRS; Endov; mouse.
DR PRO; PR:Q8C9A2; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8C9A2; protein.
DR Bgee; ENSMUSG00000039850; Expressed in embryonic brain and 110 other tissues.
DR ExpressionAtlas; Q8C9A2; baseline and differential.
DR Genevisible; Q8C9A2; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0016888; F:endodeoxyribonuclease activity, producing 5'-phosphomonoesters; IDA:UniProtKB.
DR GO; GO:0016891; F:endoribonuclease activity, producing 5'-phosphomonoesters; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IDA: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..338
FT /note="Endonuclease V"
FT /id="PRO_0000349224"
FT REGION 253..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
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 DNA"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..83
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_041579"
FT MUTAGEN 93
FT /note="S->P: No effect on activity."
FT /evidence="ECO:0000269|PubMed:12853604"
FT MUTAGEN 133
FT /note="Q->P: No effect on activity."
FT /evidence="ECO:0000269|PubMed:12853604"
FT CONFLICT 285
FT /note="Q -> R (in Ref. 2; BAE41901)"
FT /evidence="ECO:0000305"
FT HELIX 10..25
FT /evidence="ECO:0007829|PDB:5AOY"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:5AOY"
FT STRAND 47..56
FT /evidence="ECO:0007829|PDB:5AOY"
FT STRAND 58..71
FT /evidence="ECO:0007829|PDB:5AOY"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:5AOY"
FT STRAND 77..87
FT /evidence="ECO:0007829|PDB:5AOY"
FT HELIX 97..114
FT /evidence="ECO:0007829|PDB:5AOY"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:5AOY"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:5AOY"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:5AOY"
FT HELIX 138..146
FT /evidence="ECO:0007829|PDB:5AOY"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:5AOY"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:6OZR"
FT HELIX 167..174
FT /evidence="ECO:0007829|PDB:5AOY"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:5AOY"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:5AOY"
FT STRAND 207..215
FT /evidence="ECO:0007829|PDB:5AOY"
FT HELIX 217..226
FT /evidence="ECO:0007829|PDB:5AOY"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:5AOY"
FT HELIX 234..245
FT /evidence="ECO:0007829|PDB:5AOY"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:6OZP"
SQ SEQUENCE 338 AA; 37174 MW; A3760F16199F00E4 CRC64;
MAHTAAERPP EETLSLWKGE QARLKARVVD RDTEAWQRDP SFSGLQKVGG VDVSFVKGDS
VRACASLVVL SYPELKVVYE DSRMVGLKAP YVSGFLAFRE VPFLVELVQR LQEKEPDLMP
QVVLVDGNGV LHQRGFGVAC HLGVLTELPC IGVAKKLLQV DGLENNALHK EKIVLLQAGG
DTFPLIGSSG TVLGMALRSH DHSTKPLYVS VGHRISLEVA VRLTHHCCRF RIPEPIRQAD
IRSREYIRRT LGQLGVAPAQ RKDRSQKEQR PNACPQGGPG ALADQGRPPE CDGRDSSSDR
KAPEPGFQEQ KDQQLEGTGH QEDSDLWPPS PAWVQSPP
