RNH2A_MOUSE
ID RNH2A_MOUSE Reviewed; 301 AA.
AC Q9CWY8; Q8CHY8;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Ribonuclease H2 subunit A;
DE Short=RNase H2 subunit A;
DE EC=3.1.26.4;
DE AltName: Full=Ribonuclease HI large subunit;
DE Short=RNase HI large subunit;
DE AltName: Full=Ribonuclease HI subunit A;
GN Name=Rnaseh2a; Synonyms=Rnasehi;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, and Kidney;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Spleen;
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 [5]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP SUBUNIT, COFACTOR, AND MUTAGENESIS OF ASP-34; GLU-35; GLY-37; ASP-142 AND
RP ASP-170.
RX PubMed=19923215; DOI=10.1074/jbc.m109.059048;
RA Shaban N.M., Harvey S., Perrino F.W., Hollis T.;
RT "The structure of the mammalian RNase H2 complex provides insight into
RT RNA.NA hybrid processing to prevent immune dysfunction.";
RL J. Biol. Chem. 285:3617-3624(2010).
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:0000269|PubMed:19923215}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000269|PubMed:19923215};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
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:0000250};
CC -!- SUBUNIT: The RNase H2 complex is a heterotrimer composed of the
CC catalytic subunit RNASEH2A and the non-catalytic subunits RNASEH2B and
CC RNASEH2C. {ECO:0000269|PubMed:19923215}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNase HII family. Eukaryotic subfamily.
CC {ECO:0000305}.
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DR EMBL; AK010292; BAB26828.1; -; mRNA.
DR EMBL; AK146518; BAE27230.1; -; mRNA.
DR EMBL; BC038158; AAH38158.1; -; mRNA.
DR CCDS; CCDS22486.1; -.
DR RefSeq; NP_081463.1; NM_027187.3.
DR RefSeq; XP_011246799.1; XM_011248497.2.
DR RefSeq; XP_011246800.1; XM_011248498.2.
DR PDB; 3KIO; X-ray; 2.90 A; A=1-301.
DR PDB; 3P5J; X-ray; 2.90 A; A=1-301.
DR PDBsum; 3KIO; -.
DR PDBsum; 3P5J; -.
DR AlphaFoldDB; Q9CWY8; -.
DR SMR; Q9CWY8; -.
DR BioGRID; 213639; 3.
DR ComplexPortal; CPX-2875; RNase H2 complex.
DR STRING; 10090.ENSMUSP00000105358; -.
DR iPTMnet; Q9CWY8; -.
DR PhosphoSitePlus; Q9CWY8; -.
DR EPD; Q9CWY8; -.
DR jPOST; Q9CWY8; -.
DR MaxQB; Q9CWY8; -.
DR PaxDb; Q9CWY8; -.
DR PeptideAtlas; Q9CWY8; -.
DR PRIDE; Q9CWY8; -.
DR ProteomicsDB; 299855; -.
DR Antibodypedia; 13379; 185 antibodies from 28 providers.
DR DNASU; 69724; -.
DR Ensembl; ENSMUST00000109736; ENSMUSP00000105358; ENSMUSG00000052926.
DR Ensembl; ENSMUST00000109738; ENSMUSP00000105360; ENSMUSG00000052926.
DR Ensembl; ENSMUST00000147812; ENSMUSP00000120374; ENSMUSG00000052926.
DR GeneID; 69724; -.
DR KEGG; mmu:69724; -.
DR UCSC; uc009mok.1; mouse.
DR CTD; 10535; -.
DR MGI; MGI:1916974; Rnaseh2a.
DR VEuPathDB; HostDB:ENSMUSG00000052926; -.
DR eggNOG; KOG2299; Eukaryota.
DR GeneTree; ENSGT00390000010768; -.
DR InParanoid; Q9CWY8; -.
DR OMA; REECRFF; -.
DR OrthoDB; 1354466at2759; -.
DR PhylomeDB; Q9CWY8; -.
DR TreeFam; TF314302; -.
DR BRENDA; 3.1.26.4; 3474.
DR BioGRID-ORCS; 69724; 40 hits in 110 CRISPR screens.
DR ChiTaRS; Rnaseh2a; mouse.
DR EvolutionaryTrace; Q9CWY8; -.
DR PRO; PR:Q9CWY8; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9CWY8; protein.
DR Bgee; ENSMUSG00000052926; Expressed in seminiferous tubule of testis and 230 other tissues.
DR ExpressionAtlas; Q9CWY8; baseline and differential.
DR Genevisible; Q9CWY8; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0032299; C:ribonuclease H2 complex; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; ISS:UniProtKB.
DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IBA:GO_Central.
DR GO; GO:0006298; P:mismatch repair; IMP:MGI.
DR GO; GO:0006401; P:RNA catabolic process; ISS:UniProtKB.
DR Gene3D; 1.10.10.460; -; 1.
DR Gene3D; 3.30.420.10; -; 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 PANTHER; PTHR10954; PTHR10954; 1.
DR Pfam; PF01351; RNase_HII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR TIGRFAMs; TIGR00729; TIGR00729; 1.
DR PROSITE; PS51975; RNASE_H_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Endonuclease; Hydrolase; Metal-binding;
KW Nuclease; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..301
FT /note="Ribonuclease H2 subunit A"
FT /id="PRO_0000111711"
FT DOMAIN 28..251
FT /note="RNase H type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT REGION 255..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 34
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000305"
FT BINDING 35
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000305"
FT BINDING 142
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000305"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O75792"
FT MOD_RES 217
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75792"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MUTAGEN 34
FT /note="D->N: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:19923215"
FT MUTAGEN 35
FT /note="E->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:19923215"
FT MUTAGEN 37
FT /note="G->S: Strongly reduced in vitro enzyme activity."
FT /evidence="ECO:0000269|PubMed:19923215"
FT MUTAGEN 142
FT /note="D->N: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:19923215"
FT MUTAGEN 170
FT /note="D->N: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:19923215"
FT CONFLICT 132
FT /note="Q -> R (in Ref. 1; BAB26828)"
FT /evidence="ECO:0000305"
FT TURN 3..6
FT /evidence="ECO:0007829|PDB:3KIO"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:3KIO"
FT STRAND 11..17
FT /evidence="ECO:0007829|PDB:3KIO"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:3KIO"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:3KIO"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:3KIO"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:3KIO"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:3KIO"
FT HELIX 60..64
FT /evidence="ECO:0007829|PDB:3KIO"
FT HELIX 73..85
FT /evidence="ECO:0007829|PDB:3KIO"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:3KIO"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:3KIO"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:3KIO"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:3KIO"
FT HELIX 114..131
FT /evidence="ECO:0007829|PDB:3KIO"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:3KIO"
FT HELIX 148..156
FT /evidence="ECO:0007829|PDB:3KIO"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:3KIO"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:3KIO"
FT HELIX 174..200
FT /evidence="ECO:0007829|PDB:3KIO"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:3KIO"
FT HELIX 215..222
FT /evidence="ECO:0007829|PDB:3KIO"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:3KIO"
FT HELIX 240..249
FT /evidence="ECO:0007829|PDB:3KIO"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:3P5J"
FT HELIX 287..293
FT /evidence="ECO:0007829|PDB:3P5J"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:3P5J"
SQ SEQUENCE 301 AA; 33513 MW; 3B95211289847CBC 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 EDVIWEDSEA EEDPERPGKI TSYFSQGPQT CRPQAPHRYF QERGLEAASS
L
