POP1_YEAST
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 03-AUG-2022, entry version 162.
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}.
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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 SMR; P41812; -.
DR BioGRID; 35615; 337.
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; P41812; -.
DR PRIDE; P41812; -.
DR EnsemblFungi; YNL221C_mRNA; YNL221C; YNL221C.
DR GeneID; 855500; -.
DR KEGG; sce:YNL221C; -.
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 BioCyc; YEAST:YNL221C-MON; -.
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, endonucleolytic cleavage-dependent decay; IDA:SGD.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GO_Central.
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; PTHR22731; 1.
DR Pfam; PF06978; POP1; 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
