RNH2C_YEAST
ID RNH2C_YEAST Reviewed; 110 AA.
AC Q12338; D6VYE9; Q6Q5B9;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Ribonuclease H2 subunit C;
DE Short=RNase H2 subunit C;
DE Short=Rnh2C;
DE AltName: Full=RNase H(203);
DE AltName: Full=Ribonuclease HI subunit C;
GN Name=RNH203; OrderedLocusNames=YLR154C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7649171; DOI=10.1111/j.1432-1033.1995.tb20751.x;
RA van den Berg M.A., de Steensma H.Y.;
RT "ACS2, a Saccharomyces cerevisiae gene encoding acetyl-coenzyme A
RT synthetase, essential for growth on glucose.";
RL Eur. J. Biochem. 231:704-713(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP PROTEIN SEQUENCE OF N-TERMINUS, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP INTERACTION WITH RNH201 AND RNH202.
RX PubMed=14734815; DOI=10.1093/nar/gkh209;
RA Jeong H.-S., Backlund P.S., Chen H.-C., Karavanov A.A., Crouch R.J.;
RT "RNase H2 of Saccharomyces cerevisiae is a complex of three proteins.";
RL Nucleic Acids Res. 32:407-414(2004).
RN [8]
RP ERRATUM OF PUBMED:14734815.
RA Jeong H.-S., Backlund P.S., Chen H.-C., Karavanov A.A., Crouch R.J.;
RL Nucleic Acids Res. 32:1616-1616(2004).
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 -!- SUBUNIT: The RNase 2 complex is a heterotrimer composed of the
CC catalytic subunit RNH201 and of the non-catalytic subunits RNH202 and
CC RNH203.
CC -!- INTERACTION:
CC Q12338; P53942: RNH201; NbExp=2; IntAct=EBI-33805, EBI-15663;
CC Q12338; Q05635: RNH202; NbExp=2; IntAct=EBI-33805, EBI-33940;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 556 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RNase H2 subunit C family. Highly divergent.
CC {ECO:0000305}.
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DR EMBL; S79456; AAB35144.1; -; Genomic_DNA.
DR EMBL; Z73326; CAA97726.1; -; Genomic_DNA.
DR EMBL; U53879; AAB82388.1; -; Genomic_DNA.
DR EMBL; AY558209; AAS56535.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09465.1; -; Genomic_DNA.
DR PIR; S65003; S65003.
DR RefSeq; NP_013255.1; NM_001182041.1.
DR AlphaFoldDB; Q12338; -.
DR BioGRID; 31423; 113.
DR ComplexPortal; CPX-1720; RNase H2 complex.
DR DIP; DIP-1839N; -.
DR IntAct; Q12338; 4.
DR MINT; Q12338; -.
DR STRING; 4932.YLR154C; -.
DR iPTMnet; Q12338; -.
DR MaxQB; Q12338; -.
DR PaxDb; Q12338; -.
DR PRIDE; Q12338; -.
DR EnsemblFungi; YLR154C_mRNA; YLR154C; YLR154C.
DR GeneID; 850847; -.
DR KEGG; sce:YLR154C; -.
DR SGD; S000004144; RNH203.
DR VEuPathDB; FungiDB:YLR154C; -.
DR HOGENOM; CLU_2185453_0_0_1; -.
DR InParanoid; Q12338; -.
DR BioCyc; YEAST:G3O-32288-MON; -.
DR PRO; PR:Q12338; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12338; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0032299; C:ribonuclease H2 complex; IDA:SGD.
DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IC:SGD.
DR GO; GO:0006298; P:mismatch repair; IC:ComplexPortal.
DR GO; GO:0006401; P:RNA catabolic process; IDA:SGD.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IEA:GOC.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Nucleus; Reference proteome.
FT CHAIN 1..110
FT /note="Ribonuclease H2 subunit C"
FT /id="PRO_0000248387"
FT REGION 45..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 64
FT /note="F -> L (in Ref. 4; AAS56535)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 110 AA; 12482 MW; 87A110F6A1754426 CRC64;
MTKDAVNLDA YTVSFMPFYT EYQGPTEEFK DYKFEDTIYF RGKELKREKS ATPSSSDNTT
SNTFSNGAIL SGNTITGKIV SVNNYEREGT DRNELARLQE LISLIDVINQ
