ID F6RP29_MOUSE Unreviewed; 258 AA. AC F6RP29; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 30-AUG-2017, sequence version 2. DT 27-MAR-2024, entry version 76. DE RecName: Full=Ribonuclease {ECO:0000256|RuleBase:RU003515}; DE EC=3.1.26.4 {ECO:0000256|RuleBase:RU003515}; GN Name=Rnaseh2a {ECO:0000313|Ensembl:ENSMUSP00000121864.3, GN ECO:0000313|MGI:MGI:1916974}; 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 {ECO:0000313|Ensembl:ENSMUSP00000121864.3, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000121864.3, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000121864.3, RC ECO:0000313|Proteomes:UP000000589}; 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 [2] {ECO:0007829|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [3] {ECO:0000313|Ensembl:ENSMUSP00000121864.3} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000121864.3}; RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. CC -!- FUNCTION: Catalytic subunit of RNase HII, an endonuclease that CC specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA CC replication, possibly by mediating the removal of lagging-strand CC Okazaki fragment RNA primers during DNA replication. Mediates the CC excision of single ribonucleotides from DNA:RNA duplexes. CC {ECO:0000256|ARBA:ARBA00024981}. CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA CC hybrids. {ECO:0000256|RuleBase:RU003515}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; CC Evidence={ECO:0000256|ARBA:ARBA00000077, ECO:0000256|PROSITE- CC ProRule:PRU01319, ECO:0000256|RuleBase:RU003515}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|PROSITE- CC ProRule:PRU01319}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|PROSITE- CC ProRule:PRU01319}; CC Note=Manganese or magnesium. Binds 1 divalent metal ion per monomer in CC the absence of substrate. May bind a second metal ion after substrate CC binding. {ECO:0000256|PROSITE-ProRule:PRU01319}; CC -!- SIMILARITY: Belongs to the RNase HII family. Eukaryotic subfamily. CC {ECO:0000256|ARBA:ARBA00007058}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; F6RP29; -. DR SMR; F6RP29; -. DR PeptideAtlas; F6RP29; -. DR ProteomicsDB; 320895; -. DR Antibodypedia; 13379; 199 antibodies from 28 providers. DR Ensembl; ENSMUST00000128972.9; ENSMUSP00000121864.3; ENSMUSG00000052926.17. DR AGR; MGI:1916974; -. DR MGI; MGI:1916974; Rnaseh2a. DR VEuPathDB; HostDB:ENSMUSG00000052926; -. DR GeneTree; ENSGT00390000010768; -. DR HOGENOM; CLU_036532_0_3_1; -. DR ChiTaRS; Rnaseh2a; mouse. DR Proteomes; UP000000589; Chromosome 8. DR Bgee; ENSMUSG00000052926; Expressed in seminiferous tubule of testis and 233 other cell types or tissues. DR ExpressionAtlas; F6RP29; baseline and differential. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-UniRule. DR GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule. DR CDD; cd07181; RNase_HII_eukaryota_like; 1. DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1. DR Gene3D; 1.10.10.460; Ribonuclease hii. Domain 2; 1. DR InterPro; IPR004649; RNase_H2_suA. DR InterPro; IPR001352; RNase_HII/HIII. DR InterPro; IPR024567; RNase_HII/HIII_dom. DR InterPro; IPR023160; RNase_HII_hlx-loop-hlx_cap_dom. DR InterPro; IPR012337; RNaseH-like_sf. DR InterPro; IPR036397; RNaseH_sf. DR NCBIfam; TIGR00729; ribonuclease HII; 1. DR PANTHER; PTHR10954; RIBONUCLEASE H2 SUBUNIT A; 1. DR PANTHER; PTHR10954:SF7; RIBONUCLEASE H2 SUBUNIT A; 1. DR Pfam; PF01351; RNase_HII; 1. DR SUPFAM; SSF53098; Ribonuclease H-like; 1. DR PROSITE; PS51975; RNASE_H_2; 1. PE 1: Evidence at protein level; KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|PROSITE- KW ProRule:PRU01319}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE- KW ProRule:PRU01319}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE- KW ProRule:PRU01319}; KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PROSITE- KW ProRule:PRU01319}; KW Proteomics identification {ECO:0007829|EPD:F6RP29, KW ECO:0007829|MaxQB:F6RP29}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}. FT DOMAIN 28..251 FT /note="RNase H type-2" FT /evidence="ECO:0000259|PROSITE:PS51975" FT BINDING 34 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319" FT BINDING 35 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319" FT BINDING 142 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319" SQ SEQUENCE 258 AA; 28668 MW; 3C51281E32F5679C CRC64; MDLSELERDN TGRCRLSSPV PAVCLKEPCV LGVDEAGRGP VLGPMVYAIC YCPLSRLADL EALKVADSKT LTENERERLF AKMEEDGDFV GWALDVLSPN LISTSMLGRV KYNLNSLSHD TAAGLIQYAL DQNVNVTQVF VDTVGMPETY QARLQQHFPG IEVTVKAKAD SLFPVVSAAS IFAKVARDKA VKNWQFVENL QDLDSDYGSG YPNDPKTKAW LRKHVDPVFG FPQFVRFSWS TAQAILEKEA EDVIWFVS //