ID   POP1_YEAST              Reviewed;         875 AA.
AC   P41812; D6W0W9;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 169.
DE   RecName: Full=Ribonucleases P/MRP protein subunit POP1;
DE            EC=3.1.26.5;
DE   AltName: Full=RNA-processing protein POP1;
DE   AltName: Full=RNases P/MRP 100.4 kDa subunit;
GN   Name=POP1; OrderedLocusNames=YNL221C; ORFNames=N1285;
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=BSY295;
RX   PubMed=7926742; DOI=10.1101/gad.8.12.1423;
RA   Lygerou Z., Mitchell P., Petfalski E., Seraphin B., Tollervey D.;
RT   "The POP1 gene encodes a protein component common to the RNase MRP and
RT   RNase P ribonucleoproteins.";
RL   Genes Dev. 8:1423-1433(1994).
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).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-524, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
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:7926742,
CC       ECO:0000269|PubMed:9620854}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides
CC         from tRNA precursor.; EC=3.1.26.5;
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:7926742,
CC       ECO:0000269|PubMed:9620854}.
CC   -!- INTERACTION:
CC       P41812; P53833: POP3; NbExp=4; IntAct=EBI-13621, EBI-13638;
CC       P41812; P38336: POP4; NbExp=5; IntAct=EBI-13621, EBI-13646;
CC       P41812; P53218: POP6; NbExp=5; IntAct=EBI-13621, EBI-13662;
CC       P41812; P38291: POP7; NbExp=4; IntAct=EBI-13621, EBI-13670;
CC       P41812; P38786: RPP1; NbExp=3; IntAct=EBI-13621, EBI-15968;
CC       P41812; P40993: SNM1; NbExp=4; IntAct=EBI-13621, EBI-15622;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 846 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X80358; CAA56589.1; -; Genomic_DNA.
DR   EMBL; Z71497; CAA96124.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10335.1; -; Genomic_DNA.
DR   PIR; A53901; A53901.
DR   RefSeq; NP_014178.1; NM_001183059.1.
DR   PDB; 6AGB; EM; 3.48 A; B=1-875.
DR   PDB; 6AH3; EM; 3.48 A; B=1-875.
DR   PDB; 6W6V; EM; 3.00 A; B=1-875.
DR   PDB; 7C79; EM; 2.50 A; B=1-875.
DR   PDB; 7C7A; EM; 2.80 A; B=1-875.
DR   PDBsum; 6AGB; -.
DR   PDBsum; 6AH3; -.
DR   PDBsum; 6W6V; -.
DR   PDBsum; 7C79; -.
DR   PDBsum; 7C7A; -.
DR   AlphaFoldDB; P41812; -.
DR   EMDB; EMD-21564; -.
DR   EMDB; EMD-30296; -.
DR   EMDB; EMD-30297; -.
DR   EMDB; EMD-9616; -.
DR   EMDB; EMD-9622; -.
DR   SMR; P41812; -.
DR   BioGRID; 35615; 340.
DR   ComplexPortal; CPX-1873; Nucleolar ribonuclease P complex.
DR   ComplexPortal; CPX-3284; Nucleolar ribonuclease MRP complex.
DR   DIP; DIP-4284N; -.
DR   IntAct; P41812; 10.
DR   MINT; P41812; -.
DR   STRING; 4932.YNL221C; -.
DR   iPTMnet; P41812; -.
DR   MaxQB; P41812; -.
DR   PaxDb; 4932-YNL221C; -.
DR   PeptideAtlas; P41812; -.
DR   EnsemblFungi; YNL221C_mRNA; YNL221C; YNL221C.
DR   GeneID; 855500; -.
DR   KEGG; sce:YNL221C; -.
DR   AGR; SGD:S000005165; -.
DR   SGD; S000005165; POP1.
DR   VEuPathDB; FungiDB:YNL221C; -.
DR   eggNOG; KOG3322; Eukaryota.
DR   GeneTree; ENSGT00390000017478; -.
DR   HOGENOM; CLU_007205_0_1_1; -.
DR   InParanoid; P41812; -.
DR   OMA; WNAKRSH; -.
DR   OrthoDB; 5475902at2759; -.
DR   BioCyc; YEAST:YNL221C-MONOMER; -.
DR   BioGRID-ORCS; 855500; 8 hits in 10 CRISPR screens.
DR   PRO; PR:P41812; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P41812; Protein.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005655; C:nucleolar ribonuclease P complex; IDA:SGD.
DR   GO; GO:0000172; C:ribonuclease MRP complex; IDA:SGD.
DR   GO; GO:0005697; C:telomerase holoenzyme complex; IDA:SGD.
DR   GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; 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, 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; IPR039182; Pop1.
DR   InterPro; IPR009723; Pop1_N.
DR   InterPro; IPR012590; POPLD_dom.
DR   PANTHER; PTHR22731; RIBONUCLEASES P/MRP PROTEIN SUBUNIT POP1; 1.
DR   PANTHER; PTHR22731:SF3; RIBONUCLEASES P_MRP PROTEIN SUBUNIT POP1; 1.
DR   Pfam; PF06978; POP1_N; 1.
DR   Pfam; PF08170; POPLD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Hydrolase; Nucleus; Phosphoprotein;
KW   Reference proteome; rRNA processing; tRNA processing.
FT   CHAIN           1..875
FT                   /note="Ribonucleases P/MRP protein subunit POP1"
FT                   /id="PRO_0000058514"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          35..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          119..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         524
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   STRAND          48..50
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          55..58
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   HELIX           59..65
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   HELIX           68..77
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          79..84
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   HELIX           89..91
FT                   /evidence="ECO:0007829|PDB:6AGB"
FT   TURN            94..96
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   HELIX           100..102
FT                   /evidence="ECO:0007829|PDB:6AGB"
FT   HELIX           105..107
FT                   /evidence="ECO:0007829|PDB:6AH3"
FT   HELIX           110..121
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   HELIX           144..162
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   HELIX           164..169
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   HELIX           176..179
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   HELIX           181..194
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   TURN            200..202
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          206..209
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          217..219
FT                   /evidence="ECO:0007829|PDB:7C7A"
FT   HELIX           228..234
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          235..238
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   HELIX           243..249
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          250..254
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          256..266
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   HELIX           269..276
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          277..280
FT                   /evidence="ECO:0007829|PDB:6AGB"
FT   STRAND          284..289
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          293..299
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          304..306
FT                   /evidence="ECO:0007829|PDB:6AGB"
FT   HELIX           308..317
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   TURN            320..322
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   HELIX           325..329
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          334..346
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          348..361
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   TURN            362..364
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          365..370
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   HELIX           372..383
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   TURN            386..388
FT                   /evidence="ECO:0007829|PDB:6W6V"
FT   STRAND          390..407
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   HELIX           408..415
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          418..420
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   HELIX           423..431
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   TURN            432..434
FT                   /evidence="ECO:0007829|PDB:7C7A"
FT   TURN            437..439
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          445..450
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   HELIX           453..455
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          456..458
FT                   /evidence="ECO:0007829|PDB:6W6V"
FT   STRAND          465..468
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   HELIX           472..478
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   HELIX           484..495
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   HELIX           497..502
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   TURN            503..506
FT                   /evidence="ECO:0007829|PDB:6W6V"
FT   HELIX           510..519
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          537..540
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          543..549
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          551..553
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          556..561
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   TURN            562..564
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   HELIX           565..573
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          578..580
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   HELIX           583..592
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   TURN            598..601
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   HELIX           606..626
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   TURN            629..631
FT                   /evidence="ECO:0007829|PDB:6AGB"
FT   STRAND          635..637
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          640..644
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   TURN            647..649
FT                   /evidence="ECO:0007829|PDB:7C7A"
FT   STRAND          656..658
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   HELIX           661..677
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   HELIX           703..717
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   HELIX           734..737
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          755..758
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          762..769
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          777..783
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          786..788
FT                   /evidence="ECO:0007829|PDB:6AGB"
FT   HELIX           790..797
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          804..806
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   HELIX           817..819
FT                   /evidence="ECO:0007829|PDB:6W6V"
FT   STRAND          820..830
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   TURN            831..834
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          835..843
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   HELIX           844..849
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          850..852
FT                   /evidence="ECO:0007829|PDB:6AGB"
FT   STRAND          854..858
FT                   /evidence="ECO:0007829|PDB:7C79"
FT   STRAND          865..872
FT                   /evidence="ECO:0007829|PDB:7C79"
SQ   SEQUENCE   875 AA;  100395 MW;  E41EA9FFD6262FA9 CRC64;
     MSGSLSRGNG GKKVLNKNQL LKRNRIRNAR SIRAEAVAAS STKTGTPSDL SESGSKLNVD
     QFISSRQFEV KQLQLAMHNS KAASSTRIFQ ALPRKLRRRT ASHNVRRIPK RMRNRALREM
     RKSDQQDVLK GSSASSRKAH GLNAKQLYKA RMSIKLLRLA SKSTSMKLSM PPEVTSSNCH
     VRQKIKTLKR MIKESSTANP NIKLLNNRMG SYDCTGVNEL APIPKGRVKY TKRQKHFAWL
     PTHIWNAKRS HMMKRWGYQM VWAPTQKCFK LTHRLGGDTC SSDGALCMDS SYIGTIIVKD
     KSNDSEGDFL KSIIGKLTAE RANLRKYREG QVLFQGLIYS FNEENGEDST KPLGPCDVFW
     VQKDTAIIRL HPSIYTQVFN ILLQHKEKLT VQDCRYSLAS VTLKGAKALE SLASCLRSTE
     YSKSFEQFKM VSMITDHNAL PQRCTFAFEA IDPRHLAAPK KLNDSQRKTV NSDDILSLHE
     NYPQDEINAV FNELCDPESR TQSYNNQNTL KEISARRYKL LTATPNSINK TTVPFKESDD
     PSIPLVIIRR LKTRDWIVVL PWFWLLPLWH LLNRIPRMYH IGLRQFQQIQ YENKQLYFPD
     DYPFTQLGYI ENSFYKKEAS KTKWDRKPMG KRINFEKIKD IHNTKLPAYS GEIGDFFSSD
     WRFLQILRNG IDYLQRNDKT LELMDSKKTG QFNAQGVRDI NCVNDVLEFC KDYEAKTKAM
     SLSIEENIPV ALCKNRKCQF RTPDSISVNS SSFSLTFFPR CIIAVSCTLL ERGHPKDNAR
     IYQVPEKDLE HWLQLAKGVY RPNGRKDHDL KIPLPEVHDL IGFITSGTYH LNCGNGMGIG
     FIDHHAAIRQ PTRYVLIRNV GTNTYRLGEW SKISV
//