POP3_YEAST
ID POP3_YEAST Reviewed; 195 AA.
AC P53833; D6W0R2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Ribonucleases P/MRP protein subunit POP3;
DE AltName: Full=RNA-processing protein POP3;
DE AltName: Full=RNases MRP/P 22.6 kDa subunit;
GN Name=POP3; OrderedLocusNames=YNL282W; ORFNames=N0586;
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], FUNCTION, AND SUBUNIT.
RC STRAIN=SL311;
RX PubMed=9029160; DOI=10.1093/emboj/16.2.417;
RA Dichtl B., Tollervey D.;
RT "Pop3p is essential for the activity of the RNase MRP and RNase P
RT ribonucleoproteins in vivo.";
RL EMBO J. 16:417-429(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(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 FUNCTION, AND IDENTIFICATION IN THE RNASE P COMPLEX BY MASS SPECTROMETRY.
RX PubMed=9620854; DOI=10.1101/gad.12.11.1678;
RA Chamberlain J.R., Lee Y., Lane W.S., Engelke D.R.;
RT "Purification and characterization of the nuclear RNase P holoenzyme
RT complex reveals extensive subunit overlap with RNase MRP.";
RL Genes Dev. 12:1678-1690(1998).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [6]
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 [7]
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 [8]
RP IDENTIFICATION IN THE RNASE MRP COMPLEX BY MASS SPECTROMETRY.
RX PubMed=15637077; DOI=10.1074/jbc.m409568200;
RA Salinas K., Wierzbicki S., Zhou L., Schmitt M.E.;
RT "Characterization and purification of Saccharomyces cerevisiae RNase MRP
RT reveals a new unique protein component.";
RL J. Biol. Chem. 280:11352-11360(2005).
CC -!- FUNCTION: Required for processing of 5.8S rRNA (short form) at site A3
CC and for 5'- and 3'-processing of pre-tRNA. {ECO:0000269|PubMed:9029160,
CC ECO:0000269|PubMed:9620854}.
CC -!- SUBUNIT: Component of nuclear RNase P and RNase MRP complexes. RNase P
CC consists of an RNA moiety and at least 9 protein subunits including
CC POP1, POP3, POP4, POP5, POP6, POP7, POP8, RPP1 and RPR2. RNase MRP
CC complex consists of an RNA moiety and at least 10 protein subunits
CC including POP1, POP3, POP4, POP5, POP6, POP7, POP8, RMP1, RPP1 and
CC SNM1, many of which are shared with the RNase P complex.
CC {ECO:0000269|PubMed:15637077, ECO:0000269|PubMed:9029160,
CC ECO:0000269|PubMed:9620854}.
CC -!- INTERACTION:
CC P53833; P41812: POP1; NbExp=4; IntAct=EBI-13638, EBI-13621;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1360 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the POP3 family. {ECO:0000305}.
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DR EMBL; X95844; CAA65102.1; -; Genomic_DNA.
DR EMBL; Z71558; CAA96194.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10278.1; -; Genomic_DNA.
DR PIR; S63256; S63256.
DR RefSeq; NP_014117.1; NM_001183120.1.
DR PDB; 6AGB; EM; 3.48 A; C=1-195.
DR PDB; 6AH3; EM; 3.48 A; C=1-195.
DR PDB; 7C79; EM; 2.50 A; C=1-195.
DR PDB; 7C7A; EM; 2.80 A; C=1-195.
DR PDBsum; 6AGB; -.
DR PDBsum; 6AH3; -.
DR PDBsum; 7C79; -.
DR PDBsum; 7C7A; -.
DR AlphaFoldDB; P53833; -.
DR SMR; P53833; -.
DR BioGRID; 35559; 322.
DR ComplexPortal; CPX-1873; Nucleolar ribonuclease P complex.
DR ComplexPortal; CPX-3284; Nucleolar ribonuclease MRP complex.
DR DIP; DIP-4997N; -.
DR IntAct; P53833; 12.
DR MINT; P53833; -.
DR STRING; 4932.YNL282W; -.
DR MaxQB; P53833; -.
DR PaxDb; P53833; -.
DR PRIDE; P53833; -.
DR EnsemblFungi; YNL282W_mRNA; YNL282W; YNL282W.
DR GeneID; 855439; -.
DR KEGG; sce:YNL282W; -.
DR SGD; S000005226; POP3.
DR VEuPathDB; FungiDB:YNL282W; -.
DR eggNOG; ENOG502RZX7; Eukaryota.
DR HOGENOM; CLU_047273_0_0_1; -.
DR InParanoid; P53833; -.
DR OMA; KQVYKPI; -.
DR BioCyc; YEAST:G3O-33273-MON; -.
DR PRO; PR:P53833; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53833; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005655; C:nucleolar ribonuclease P complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000172; C:ribonuclease MRP complex; IDA:SGD.
DR GO; GO:0034965; P:intronic box C/D RNA processing; IDA:SGD.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IDA:ComplexPortal.
DR GO; GO:0000294; P:nuclear-transcribed mRNA catabolic process, endonucleolytic cleavage-dependent decay; IDA:SGD.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IEA:GOC.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IDA:ComplexPortal.
DR GO; GO:0008033; P:tRNA processing; IMP:SGD.
DR InterPro; IPR013241; RNase_P_Pop3.
DR PANTHER; PTHR28272; PTHR28272; 1.
DR Pfam; PF08228; RNase_P_pop3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome; rRNA processing;
KW tRNA processing.
FT CHAIN 1..195
FT /note="Ribonucleases P/MRP protein subunit POP3"
FT /id="PRO_0000058516"
FT STRAND 15..23
FT /evidence="ECO:0007829|PDB:6AGB"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:7C7A"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:7C7A"
FT HELIX 41..55
FT /evidence="ECO:0007829|PDB:7C79"
FT TURN 59..65
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 108..114
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 131..135
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:7C79"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:7C79"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 179..187
FT /evidence="ECO:0007829|PDB:6AGB"
SQ SEQUENCE 195 AA; 22612 MW; 5091EE590BDBCBEA CRC64;
MSGSLKSLDK KIAKRRQVYK PVLDNPFTNE AHMWPRVHDQ PLIWQLLQSS IINKLIHIQS
KENYPWELYT DFNEIVQYLS GAHGNSDPVC LFVCNKDPDV PLVLLQQIPL LCYMAPMTVK
LVQLPKSAMD TFKSVSKYGM LLLRCDDRVD KKFVSQIQKN VDLLQFPWLN AIKYRPTSVK
LLKTTVPIVS KKRQK
