Reviewed, UniProtKB/Swiss-Prot P25441 (RPC4_YEAST)

Names and origin

Protein names

Recommended name:
    DNA-directed RNA polymerase III subunit RPC4
      Short name=RNA polymerase III subunit C4
Alternative name(s):
    DNA-directed RNA polymerase III 47 kDa polypeptide
    C53

Gene names

Name:	RPC53
Synonyms:	RPC4
Ordered Locus Names:	YDL150W
ORF Names:	D1557

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	422 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Essential for tRNA synthesis. The RPC53/RPC4-RPC37/RPC5 subcomplex is required for terminator recognition and reinitiation. Ref.9
Subunit structure	Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits. Interacts with RPC37/RPC5. RPC53/RPC4, RPC37/RPC5 and RPC11/RPC10 probably form a Pol III subcomplex. Ref.5
Subcellular location	Nucleus Ref.6.
Miscellaneous	Present with 998 molecules/cell in log phase SD medium. Ref.7
Sequence similarities	Belongs to the eukaryotic RPC4/POLR3D RNA polymerase subunit family.

Ontologies

Keywords
Biological process	Transcription
Cellular component	DNA-directed RNA polymerase Nucleus
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	transcription from RNA polymerase III promoter Inferred from electronic annotation. Source: InterPro
Cellular component	DNA-directed RNA polymerase III complex Traceable author statement. Source: SGD
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed RNA polymerase activity Traceable author statement. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BOI1	P38041	1	EBI-15826,EBI-3719
LSB3	P43603	1	EBI-15826,EBI-22980

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 422	422	DNA-directed RNA polymerase III subunit RPC4		PRO_0000073969
Regions
	Motif	25 – 29	5	Nuclear localization signal Potential
Amino acid modifications
	Modified residue	119	1	Phosphoserine Ref.13
	Modified residue	137	1	Phosphoserine Ref.13
	Modified residue	138	1	Phosphoserine Ref.13
	Modified residue	178	1	Phosphoserine Ref.10
	Modified residue	182	1	Phosphoserine Ref.10
	Modified residue	224	1	Phosphoserine Ref.13 Ref.10 Ref.11 Ref.12
	Modified residue	228	1	Phosphothreonine Ref.10 Ref.11 Ref.12
	Modified residue	232	1	Phosphothreonine Ref.13 Ref.10 Ref.11 Ref.8
Experimental info
	Sequence conflict	42	1	E → K in CAA45073. Ref.1
	Sequence conflict	264	1	L → LGL Ref.1
	Sequence conflict	284 – 285	2	NA → KR in CAA45073. Ref.1
	Sequence conflict	392	1	Q → H in CAA45073. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P25441-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 206FBAC274BC72D5	FASTA	422	46,667
	10 20 30 40 50 60 MSSNKGNGRL PSLKDSSSNG GGSAKPSLKF KPKAVARKSK EEREAAASKV KLEEESKRGN 70 80 90 100 110 120 DKKHFNNKNK RVTGAGGQQR RMAKYLNNTH VISSGPLAAG NFVSEKGDLR RGFIKSEGSG 130 140 150 160 170 180 SSLVQKGLET IDNGAESSEN EAEDDDNEGV ASKSKKKFNM GKEFEARNLI EDEDDGESEK 190 200 210 220 230 240 SSDVDMDDEE WRSKRIEQLF PVRPVRVRHE DVETVKREIQ EALSEKPTRE PTPSVKTEPV 250 260 270 280 290 300 GTGLQSYLEE RERQVNEKLA DLGLEKEFQS VDGKEAAAEL ELLNADHQHI LRKLKKMNNK 310 320 330 340 350 360 PERFMVFQLP TRLPAFERPA VKEEKEDMET QASDPSKKKK NIKKKDTKDA LSTRELAGKV 370 380 390 400 410 420 GSIRVHKSGK LSVKIGNVVM DIGKGAETTF LQDVIALSIA DDASSAELLG RVDGKIVVTP QI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"RPC53 encodes a subunit of Saccharomyces cerevisiae RNA polymerase C (III) whose inactivation leads to a predominantly G1 arrest." Mann C., Micouin J.-Y., Chiannilkulchai N., Treich I., Buhler J.-M., Sentenac A. Mol. Cell. Biol. 12:4314-4326(1992) [PubMed: 1406624] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Analysis of a 23 kb region on the left arm of yeast chromosome IV." Delaveau T.T.D., Blugeon C., Jacq C., Perea J. Yeast 12:1587-1592(1996) [PubMed: 8972581] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	"The yeast RNA polymerase III transcription machinery: a paradigm for eukaryotic gene activation." Chedin S., Ferri M.L., Peyroche G., Andrau J.-C., Jourdain S., Lefebvre O., Werner M., Carles C., Sentenac A. Cold Spring Harb. Symp. Quant. Biol. 63:381-389(1998) [PubMed: 10384303] [Abstract] Cited for: REVIEW ON THE RNA POL III COMPLEX.
[5]	"A protein-protein interaction map of yeast RNA polymerase III." Flores A., Briand J.-F., Gadal O., Andrau J.-C., Rubbi L., Van Mullem V., Boschiero C., Goussot M., Marck C., Carles C., Thuriaux P., Sentenac A., Werner M. Proc. Natl. Acad. Sci. U.S.A. 96:7815-7820(1999) [PubMed: 10393904] [Abstract] Cited for: INTERACTION WITH RPC4.
[6]	"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: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-232, MASS SPECTROMETRY.
[9]	"A subcomplex of RNA polymerase III subunits involved in transcription termination and reinitiation." Landrieux E., Alic N., Ducrot C., Acker J., Riva M., Carles C. EMBO J. 25:118-128(2006) [PubMed: 16362040] [Abstract] Cited for: FUNCTION OF THE RPC53-RPC37 SUBCOMPLEX.
[10]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-182; SER-224; THR-228 AND THR-232, MASS SPECTROMETRY.
[11]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; THR-228 AND THR-232, MASS SPECTROMETRY.
[12]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND THR-228, MASS SPECTROMETRY.
[13]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119; SER-137; SER-138; SER-224 AND THR-232, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X63501 Genomic DNA. Translation: CAA45073.1. X97751 Genomic DNA. Translation: CAA66340.1. Z74199 Genomic DNA. Translation: CAA98725.1.
PIR	S67698.
RefSeq	NP_010131.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1003N.
IntAct	P25441. 21 interactions.
STRING	P25441.
Proteomic databases
PRIDE	P25441.
Genome annotation databases
Ensembl	YDL150W; YDL150W; YDL150W; Saccharomyces cerevisiae. [Genome view]
GeneID	851404.
KEGG	sce:YDL150W.
NMPDR	fig|4932.3.peg.868.
Organism-specific databases
CYGD	YDL150w.
SGD	S000002309. RPC53.
Phylogenomic databases
eggNOG	fuNOG08452.
HOGENOM	HBG203353.
OMA	LKFKPKV.
OrthoDB	EOG92Z66P.
PhylomeDB	P25441.
Gene expression databases
ArrayExpress	P25441.
Genevestigator	P25441.
GermOnline	YDL150W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR007811. RNA_pol_Rpc4. [Graphical view]
PANTHER	PTHR13408. RNA_pol_Rpc4. 1 hit.
Pfam	PF05132. RNA_pol_Rpc4. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	968576.

Entry information

Entry name

RPC4_YEAST

Accession

Primary (citable) accession number: P25441
Secondary accession number(s): Q12073

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	November 1, 1997
Last modified:	January 19, 2010
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)