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   02-SEP-2026, entry version 170.
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; DOI=10.1038/387s093;
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=5; IntAct=EBI-13638, EBI-13621;
CC       P53833; P38336: POP4; NbExp=3; IntAct=EBI-13638, EBI-13646;
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   AlphaFoldDB; P53833; -.
DR   EMDB; EMD-30296; -.
DR   EMDB; EMD-30297; -.
DR   EMDB; EMD-9616; -.
DR   EMDB; EMD-9622; -.
DR   SMR; P53833; -.
DR   BioGRID; 35559; 327.
DR   ComplexPortal; CPX-1873; Nucleolar ribonuclease P complex.
DR   ComplexPortal; CPX-3284; Ribonuclease MRP complex.
DR   DIP; DIP-4997N; -.
DR   FunCoup; P53833; 146.
DR   IntAct; P53833; 14.
DR   MINT; P53833; -.
DR   STRING; 4932.YNL282W; -.
DR   PaxDb; 4932-YNL282W; -.
DR   PeptideAtlas; P53833; -.
DR   EnsemblFungi; YNL282W_mRNA; YNL282W; YNL282W.
DR   GeneID; 855439; -.
DR   KEGG; sce:YNL282W; -.
DR   AGR; SGD:S000005226; -.
DR   SGD; S000005226; POP3.
DR   VEuPathDB; FungiDB:YNL282W; -.
DR   eggNOG; ENOG502RZX7; Eukaryota.
DR   HOGENOM; CLU_047273_0_0_1; -.
DR   InParanoid; P53833; -.
DR   OMA; XHIQSKE; -.
DR   OrthoDB; 20109at2759; -.
DR   BioCyc; YEAST:G3O-33273-MONOMER; -.
DR   BioGRID-ORCS; 855439; 9 hits in 10 CRISPR screens.
DR   CD-CODE; 7CAF9006; Tam body.
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 snoRNA 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, RNase MRP-dependent; IDA:SGD.
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; RIBONUCLEASES P/MRP PROTEIN SUBUNIT POP3; 1.
DR   PANTHER; PTHR28272:SF1; RIBONUCLEASES P_MRP PROTEIN SUBUNIT POP3; 1.
DR   Pfam; PF08228; RNase_P_pop3; 1.
DR   PDBsum; 6AGB; -.
DR   PDBsum; 6AH3; -.
DR   PDBsum; 7C79; -.
DR   PDBsum; 7C7A; -.
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   HELIX           34..36
FT                   /evidence="ECO:0007829|PDB:6AGB"
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
//