RNH2C_MOUSE
ID RNH2C_MOUSE Reviewed; 166 AA.
AC Q9CQ18; Q8R1N2;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Ribonuclease H2 subunit C;
DE Short=RNase H2 subunit C;
DE AltName: Full=Ribonuclease HI subunit C;
GN Name=Rnaseh2c; Synonyms=Ayp1;
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].
RA Lim H.N., Oakenfull E.A., Hawkins J.R.;
RT "Evidence that the T6 pseudogene upstream of human SRY is derived from the
RT transcript of a novel autosomal gene, AYP1.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Spleen, and Testis;
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, AND SUBUNIT.
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: Non catalytic subunit of RNase H2, 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 -!- 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 H2 subunit C family. {ECO:0000305}.
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DR EMBL; AF346604; AAO49175.1; -; mRNA.
DR EMBL; AK018776; BAB31401.1; -; mRNA.
DR EMBL; AK011556; BAB27694.1; -; mRNA.
DR EMBL; BC024333; AAH24333.1; -; mRNA.
DR CCDS; CCDS29471.1; -.
DR RefSeq; NP_080892.1; NM_026616.2.
DR PDB; 3KIO; X-ray; 2.90 A; C=1-166.
DR PDB; 3P5J; X-ray; 2.90 A; C=1-166.
DR PDBsum; 3KIO; -.
DR PDBsum; 3P5J; -.
DR AlphaFoldDB; Q9CQ18; -.
DR SMR; Q9CQ18; -.
DR BioGRID; 212732; 2.
DR ComplexPortal; CPX-2875; RNase H2 complex.
DR STRING; 10090.ENSMUSP00000025864; -.
DR iPTMnet; Q9CQ18; -.
DR PhosphoSitePlus; Q9CQ18; -.
DR EPD; Q9CQ18; -.
DR MaxQB; Q9CQ18; -.
DR PaxDb; Q9CQ18; -.
DR PeptideAtlas; Q9CQ18; -.
DR PRIDE; Q9CQ18; -.
DR ProteomicsDB; 300507; -.
DR Antibodypedia; 44295; 141 antibodies from 24 providers.
DR DNASU; 68209; -.
DR Ensembl; ENSMUST00000025864; ENSMUSP00000025864; ENSMUSG00000024925.
DR GeneID; 68209; -.
DR KEGG; mmu:68209; -.
DR UCSC; uc008gdx.1; mouse.
DR CTD; 84153; -.
DR MGI; MGI:1915459; Rnaseh2c.
DR VEuPathDB; HostDB:ENSMUSG00000024925; -.
DR eggNOG; ENOG502SBKV; Eukaryota.
DR GeneTree; ENSGT00390000001568; -.
DR HOGENOM; CLU_097632_3_0_1; -.
DR InParanoid; Q9CQ18; -.
DR OMA; YFNNYTR; -.
DR OrthoDB; 1542008at2759; -.
DR PhylomeDB; Q9CQ18; -.
DR TreeFam; TF324370; -.
DR BioGRID-ORCS; 68209; 23 hits in 73 CRISPR screens.
DR ChiTaRS; Rnaseh2c; mouse.
DR EvolutionaryTrace; Q9CQ18; -.
DR PRO; PR:Q9CQ18; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9CQ18; protein.
DR Bgee; ENSMUSG00000024925; Expressed in internal carotid artery and 260 other tissues.
DR ExpressionAtlas; Q9CQ18; baseline and differential.
DR Genevisible; Q9CQ18; MM.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032299; C:ribonuclease H2 complex; IDA:MGI.
DR GO; GO:0006298; P:mismatch repair; IC:ComplexPortal.
DR GO; GO:0006401; P:RNA catabolic process; ISS:UniProtKB.
DR CDD; cd09271; RNase_H2-C; 1.
DR InterPro; IPR013924; RNase_H2_suC.
DR Pfam; PF08615; RNase_H2_suC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Nucleus; Reference proteome.
FT CHAIN 1..166
FT /note="Ribonuclease H2 subunit C"
FT /id="PRO_0000248386"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDP1"
FT CONFLICT 9
FT /note="D -> E (in Ref. 3; AAH24333)"
FT /evidence="ECO:0000305"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:3KIO"
FT TURN 18..23
FT /evidence="ECO:0007829|PDB:3KIO"
FT STRAND 29..38
FT /evidence="ECO:0007829|PDB:3KIO"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:3KIO"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:3KIO"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:3KIO"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:3KIO"
FT STRAND 66..74
FT /evidence="ECO:0007829|PDB:3KIO"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:3KIO"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:3KIO"
FT STRAND 92..106
FT /evidence="ECO:0007829|PDB:3KIO"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:3KIO"
FT STRAND 123..138
FT /evidence="ECO:0007829|PDB:3P5J"
FT HELIX 145..149
FT /evidence="ECO:0007829|PDB:3P5J"
FT HELIX 152..159
FT /evidence="ECO:0007829|PDB:3P5J"
SQ SEQUENCE 166 AA; 17823 MW; D631CFE252040417 CRC64;
MKNPEEAADG KQRIHLRPGS LRGAAPAKLH LLPCDVLVSR PAPVDRFFTP AVRHDADGLQ
ASFRGRGLRG EEVAVPPGFA GFVMVTEEKG EGLIGKLNFS GDAEDKADEA QEPLERDFDR
LIGATGSFSH FTLWGLETVP GPDAKVHRAL GWPSLAAAIH AQVPED
