P41812 (POP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonucleases P/MRP protein subunit POP1
EC=3.1.26.5

Alternative name(s):
RNA-processing protein POP1
RNases P/MRP 100.4 kDa subunit

Gene names

Name:	POP1
Ordered Locus Names:	YNL221C
ORF Names:	N1285

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	875 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for processing of 5.8S rRNA (short form) at site A3 and for 5' and 3' processing of pre-tRNA. Ref.1 Ref.4
Catalytic activity	Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Subunit structure	Component of nuclear RNase P and RNase MRP complexes. RNase P consists of an RNA moiety and at least 9 protein subunits including POP1, POP3, POP4, POP5, POP6, POP7, POP8, RPP1 and RPR2. RNase MRP complex consists of an RNA moiety and at least 10 protein subunits including POP1, POP3, POP4, POP5, POP6, POP7, POP8, RMP1, RPP1 and SNM1, many of which are shared with the RNase P complex. Ref.1 Ref.4 Ref.7
Subcellular location	Cytoplasm. Nucleus Ref.5.
Miscellaneous	Present with 846 molecules/cell in log phase SD medium.

Ontologies

Keywords
Biological process	rRNA processing tRNA processing
Cellular component	Cytoplasm Nucleus
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	intronic box C/D snoRNA processing Inferred from direct assay PubMed 18713869. Source: SGD mRNA cleavage Inferred from physical interaction PubMed 14729943. Source: SGD rRNA processing Inferred from mutant phenotype Ref.1. Source: SGD tRNA 5'-leader removal Inferred from electronic annotation. Source: InterPro tRNA processing Inferred from mutant phenotype Ref.1. Source: SGD
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolar ribonuclease P complex Inferred from direct assay Ref.4. Source: SGD ribonuclease MRP complex Traceable author statement Ref.4. Source: SGD
Molecular_function	ribonuclease P activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 875	875	Ribonucleases P/MRP protein subunit POP1		PRO_0000058514
Amino acid modifications
	Modified residue	524	1	Phosphothreonine Ref.8

Sequences

	Sequence		Length	Mass (Da)
	P41812 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: E41EA9FFD6262FA9	FASTA	875	100,395
	10 20 30 40 50 60 MSGSLSRGNG GKKVLNKNQL LKRNRIRNAR SIRAEAVAAS STKTGTPSDL SESGSKLNVD 70 80 90 100 110 120 QFISSRQFEV KQLQLAMHNS KAASSTRIFQ ALPRKLRRRT ASHNVRRIPK RMRNRALREM 130 140 150 160 170 180 RKSDQQDVLK GSSASSRKAH GLNAKQLYKA RMSIKLLRLA SKSTSMKLSM PPEVTSSNCH 190 200 210 220 230 240 VRQKIKTLKR MIKESSTANP NIKLLNNRMG SYDCTGVNEL APIPKGRVKY TKRQKHFAWL 250 260 270 280 290 300 PTHIWNAKRS HMMKRWGYQM VWAPTQKCFK LTHRLGGDTC SSDGALCMDS SYIGTIIVKD 310 320 330 340 350 360 KSNDSEGDFL KSIIGKLTAE RANLRKYREG QVLFQGLIYS FNEENGEDST KPLGPCDVFW 370 380 390 400 410 420 VQKDTAIIRL HPSIYTQVFN ILLQHKEKLT VQDCRYSLAS VTLKGAKALE SLASCLRSTE 430 440 450 460 470 480 YSKSFEQFKM VSMITDHNAL PQRCTFAFEA IDPRHLAAPK KLNDSQRKTV NSDDILSLHE 490 500 510 520 530 540 NYPQDEINAV FNELCDPESR TQSYNNQNTL KEISARRYKL LTATPNSINK TTVPFKESDD 550 560 570 580 590 600 PSIPLVIIRR LKTRDWIVVL PWFWLLPLWH LLNRIPRMYH IGLRQFQQIQ YENKQLYFPD 610 620 630 640 650 660 DYPFTQLGYI ENSFYKKEAS KTKWDRKPMG KRINFEKIKD IHNTKLPAYS GEIGDFFSSD 670 680 690 700 710 720 WRFLQILRNG IDYLQRNDKT LELMDSKKTG QFNAQGVRDI NCVNDVLEFC KDYEAKTKAM 730 740 750 760 770 780 SLSIEENIPV ALCKNRKCQF RTPDSISVNS SSFSLTFFPR CIIAVSCTLL ERGHPKDNAR 790 800 810 820 830 840 IYQVPEKDLE HWLQLAKGVY RPNGRKDHDL KIPLPEVHDL IGFITSGTYH LNCGNGMGIG 850 860 870 FIDHHAAIRQ PTRYVLIRNV GTNTYRLGEW SKISV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The POP1 gene encodes a protein component common to the RNase MRP and RNase P ribonucleoproteins." Lygerou Z., Mitchell P., Petfalski E., Seraphin B., Tollervey D. Genes Dev. 8:1423-1433(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT. Strain: BSY295.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J. Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Purification and characterization of the nuclear RNase P holoenzyme complex reveals extensive subunit overlap with RNase MRP." Chamberlain J.R., Lee Y., Lane W.S., Engelke D.R. Genes Dev. 12:1678-1690(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE RNASE P COMPLEX BY MASS SPECTROMETRY.
[5]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"Characterization and purification of Saccharomyces cerevisiae RNase MRP reveals a new unique protein component." Salinas K., Wierzbicki S., Zhou L., Schmitt M.E. J. Biol. Chem. 280:11352-11360(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE RNASE MRP COMPLEX BY MASS SPECTROMETRY.
[8]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-524, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X80358 Genomic DNA. Translation: CAA56589.1. Z71497 Genomic DNA. Translation: CAA96124.1. BK006947 Genomic DNA. Translation: DAA10335.1.
PIR	A53901.
RefSeq	NP_014178.1. NM_001183059.1.
3D structure databases
ProteinModelPortal	P41812.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4284N.
IntAct	P41812. 10 interactions.
MINT	MINT-472608.
STRING	4932.YNL221C.
Proteomic databases
PaxDb	P41812.
PeptideAtlas	P41812.
PRIDE	P41812.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YNL221C; YNL221C; YNL221C.
GeneID	855500.
KEGG	sce:YNL221C.
Organism-specific databases
CYGD	YNL221c.
SGD	S000005165. POP1.
Phylogenomic databases
eggNOG	NOG297409.
GeneTree	ENSGT00390000017478.
HOGENOM	HOG000247847.
KO	K01164.
OMA	KTWLPTH.
OrthoDB	EOG40VZXT.
Gene expression databases
Genevestigator	P41812.
GermOnline	YNL221C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR012590. POPLD. IPR009723. RNase_P/MRP_POP1. [Graphical view]
Pfam	PF06978. POP1. 1 hit. PF08170. POPLD. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	979496.

Entry information

Entry name

POP1_YEAST

Accession

Primary (citable) accession number: P41812
Secondary accession number(s): D6W0W9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	April 3, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program