P38336 (POP4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
RNases MRP/P 32.9 kDa subunit

Alternative name(s):
RNA-processing protein POP4

Gene names

Name:	POP4
Ordered Locus Names:	YBR257W
ORF Names:	YBR1725

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	279 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for 5.8S rRNA and tRNA processing; associated with RNase MRP and RNase P. Ref.4 Ref.5
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.4 Ref.5 Ref.6
Subcellular location	Nucleus Potential.
Sequence similarities	Belongs to the eukaryotic/archaeal RNase P protein component 1 family.

Ontologies

Keywords
Biological process	rRNA processing tRNA processing
Cellular component	Nucleus
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.4. Source: SGD tRNA processing Inferred from mutant phenotype Ref.4. Source: SGD
Cellular_component	nucleolar ribonuclease P complex Inferred from direct assay Ref.5. Source: SGD ribonuclease MRP complex Inferred from direct assay Ref.5. Source: SGD
Molecular_function	RNA binding Inferred from electronic annotation. Source: InterPro ribonuclease activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 279	279	RNases MRP/P 32.9 kDa subunit		PRO_0000128422
Amino acid modifications
	Modified residue	64	1	Phosphoserine Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P38336 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: F19FD05B47DE83C1	FASTA	279	32,881
	10 20 30 40 50 60 MDRTQTFIKD CLFTKCLEDP EKPFNENRFQ DTLLLLPTDG GLTSRLQRQQ RKSKLNLDNL 70 80 90 100 110 120 QKVSQLESAD KQLEKRDYQR INKNSKIALR EYINNCKKNT KKCLKLAYEN KITDKEDLLH 130 140 150 160 170 180 YIEEKHPTIY ESLPQYVDFV PMYKELWINY IKELLNITKN LKTFNGSLAL LKLSMADYNG 190 200 210 220 230 240 ALLRVTKSKN KTLIGLQGIV IWDSQKFFIM IVKGNIIDEI KCIPKKGTVF QFEIPISDDD 250 260 270 DSALRYSILG DRFKYRSVDR AGRKFKSRRC DDMLYYIQN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete sequence of a 19,482 bp segment located on the right arm of chromosome II from Saccharomyces cerevisiae." Doignon F., Biteau N., Crouzet M., Aigle M. Yeast 9:189-199(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K. EMBO J. 13:5795-5809(1994) [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]	"A novel protein shared by RNase MRP and RNase P." Chu S., Zengel J.M., Lindahl L. RNA 3:382-391(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT.
[5]	"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.
[6]	"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.
[7]	"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 SER-64, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X70529 Genomic DNA. Translation: CAA49921.1. Z36126 Genomic DNA. Translation: CAA85220.1. BK006936 Genomic DNA. Translation: DAA07374.1.
PIR	S32959.
RefSeq	NP_009816.1. NM_001178605.1.
3D structure databases
ProteinModelPortal	P38336.
SMR	P38336. Positions 170-260.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6772N.
IntAct	P38336. 10 interactions.
MINT	MINT-669334.
STRING	4932.YBR257W.
Proteomic databases
PaxDb	P38336.
PeptideAtlas	P38336.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YBR257W; YBR257W; YBR257W.
GeneID	852560.
KEGG	sce:YBR257W.
Organism-specific databases
CYGD	YBR257w.
SGD	S000000461. POP4.
Phylogenomic databases
eggNOG	NOG255667.
GeneTree	ENSGT00390000010067.
HOGENOM	HOG000000736.
KO	K03538.
OMA	DSKEWNE.
OrthoDB	EOG4RBTTV.
Gene expression databases
Genevestigator	P38336.
GermOnline	YBR257W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	2.30.30.210. 1 hit.
InterPro	IPR002730. RNase_P/MRP_p29. IPR016848. RNase_P/MRP_p29-subunit. IPR023534. Rof/RNase_P-like. [Graphical view]
Pfam	PF01868. UPF0086. 1 hit. [Graphical view]
PIRSF	PIRSF027081. RNase_P/MRP_p29_subunit. 1 hit.
SMART	SM00538. POP4. 1 hit. [Graphical view]
SUPFAM	SSF101744. RNase_P_Rpp29. 1 hit.
ProtoNet	Search...
Other
NextBio	971667.

Entry information

Entry name

POP4_YEAST

Accession

Primary (citable) accession number: P38336
Secondary accession number(s): D6VQQ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program