RNH1_MOUSE
ID RNH1_MOUSE Reviewed; 285 AA.
AC O70338; Q8VCR6;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Ribonuclease H1;
DE Short=RNase H1;
DE EC=3.1.26.4;
GN Name=Rnaseh1; Synonyms=Rnh1;
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].
RC TISSUE=Carcinoma;
RX PubMed=9799596; DOI=10.1006/geno.1998.5497;
RA Cerritelli S.M., Crouch R.J.;
RT "Cloning, expression, and mapping of ribonucleases H of human and mouse
RT related to bacterial RNase HI.";
RL Genomics 53:300-307(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids. Plays a role in RNA polymerase II (RNAp II) transcription
CC termination by degrading R-loop RNA-DNA hybrid formation at G-rich
CC pause sites located downstream of the poly(A) site and behind the
CC elongating RNAp II. {ECO:0000250|UniProtKB:O60930}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00408};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a
CC regulatory site, or after substrate binding. {ECO:0000250};
CC -!- ACTIVITY REGULATION: In the presence of magnesium, manganese is
CC inhibitory. {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RNase H family. {ECO:0000305}.
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DR EMBL; AF048993; AAC78562.1; -; mRNA.
DR EMBL; BC019411; AAH19411.1; -; mRNA.
DR CCDS; CCDS25852.1; -.
DR AlphaFoldDB; O70338; -.
DR SMR; O70338; -.
DR STRING; 10090.ENSMUSP00000020959; -.
DR iPTMnet; O70338; -.
DR PhosphoSitePlus; O70338; -.
DR EPD; O70338; -.
DR MaxQB; O70338; -.
DR PaxDb; O70338; -.
DR PeptideAtlas; O70338; -.
DR PRIDE; O70338; -.
DR ProteomicsDB; 300429; -.
DR MGI; MGI:1335073; Rnaseh1.
DR eggNOG; KOG3752; Eukaryota.
DR InParanoid; O70338; -.
DR PhylomeDB; O70338; -.
DR ChiTaRS; Rnaseh1; mouse.
DR PRO; PR:O70338; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O70338; protein.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IDA:MGI.
DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IBA:GO_Central.
DR GO; GO:0006264; P:mitochondrial DNA replication; IMP:MGI.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GO_Central.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.40.970.10; -; 1.
DR InterPro; IPR009027; Ribosomal_L9/RNase_H1_N.
DR InterPro; IPR017067; RNase_H1_euk.
DR InterPro; IPR011320; RNase_H1_N.
DR InterPro; IPR037056; RNase_H1_N_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF01693; Cauli_VI; 1.
DR Pfam; PF00075; RNase_H; 1.
DR PIRSF; PIRSF036852; Ribonuclease_H1_euk; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF55658; SSF55658; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome.
FT CHAIN 1..285
FT /note="Ribonuclease H1"
FT /id="PRO_0000195434"
FT DOMAIN 135..281
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT REGION 72..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 185
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 209
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 273
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT CONFLICT 93
FT /note="A -> V (in Ref. 2; AAH19411)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 285 AA; 31805 MW; 92B09F8EFAFA822F CRC64;
MRWLLPLSRT VTLAVVRLRR GICGLGMFYA VRRGRRTGVF LSWSECKAQV DRFPAARFKK
FATEDEAWAF VRSSSSPDGS KGQESAHEQK SQAKTSKRPR EPLGEGEELP EPGPKHTRQD
TEPAAVVSKD TFSYMGESVI VYTDGCCSSN GRKRARAGIG VYWGPGHPLN VGIRLPGRQT
NQRAEIHAAC KAIMQAKAQN ISKLVLYTDS MFTINGITNW VQGWKKNGWR TSTGKDVINK
EDFMELDELT QGMDIQWMHI PGHSGFVGNE EADRLAREGA KQSED
