P22276 (RPC2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA-directed RNA polymerase III subunit RPC2
Short name=RNA polymerase III subunit C2
EC=2.7.7.6

Alternative name(s):
C128
DNA-directed RNA polymerase III 130 kDa polypeptide

Gene names

Name:	RET1
Synonyms:	RPC128, RPC2
Ordered Locus Names:	YOR207C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1149 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. Second largest core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol III is composed of mobile elements and RPC2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft By similarity.
Catalytic activity	Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
Subunit structure	Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits.
Subcellular location	Nucleus Ref.5.
Miscellaneous	Present with 1950 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the RNA polymerase beta chain family.

Ontologies

Keywords
Biological process	Transcription
Cellular component	DNA-directed RNA polymerase Nucleus
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Nucleotidyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	tRNA transcription from RNA polymerase III promoter Inferred from direct assay. Source: SGD
Cellular component	DNA-directed RNA polymerase III complex Inferred from direct assay. Source: SGD
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW ribonucleoside binding 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 – 1149	1149	DNA-directed RNA polymerase III subunit RPC2		PRO_0000048096
Regions
	Zinc finger	1095 – 1110	16	C4-type By similarity
Sites
	Metal binding	1095	1	Zinc By similarity
	Metal binding	1098	1	Zinc By similarity
	Metal binding	1107	1	Zinc By similarity
	Metal binding	1110	1	Zinc By similarity
Experimental info
	Sequence conflict	213	1	K → E in AAB59324. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P22276 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 6AC52354F34CF090	FASTA	1,149	129,456
	10 20 30 40 50 60 MVAATKRRKT HIHKHVKDEA FDDLLKPVYK GKKLTDEINT AQDKWHLLPA FLKVKGLVKQ 70 80 90 100 110 120 HLDSFNYFVD TDLKKIIKAN QLILSDVDPE FYLKYVDIRV GKKSSSSTKD YLTPPHECRL 130 140 150 160 170 180 RDMTYSAPIY VDIEYTRGRN IIMHKDVEIG RMPIMLRSNK CILYDADESK MAKLNECPLD 190 200 210 220 230 240 PGGYFIVNGT EKVILVQEQL SKNRIIVEAD EKKGIVQASV TSSTHERKSK TYVITKNGKI 250 260 270 280 290 300 YLKHNSIAEE IPIAIVLKAC GILSDLEIMQ LVCGNDSSYQ DIFAVNLEES SKLDIYTQQQ 310 320 330 340 350 360 ALEYIGAKVK TMRRQKLTIL QEGIEAIATT VIAHLTVEAL DFREKALYIA MMTRRVVMAM 370 380 390 400 410 420 YNPKMIDDRD YVGNKRLELA GQLISLLFED LFKKFNNDFK LSIDKVLKKP NRAMEYDALL 430 440 450 460 470 480 SINVHSNNIT SGLNRAISTG NWSLKRFKME RAGVTHVLSR LSYISALGMM TRISSQFEKS 490 500 510 520 530 540 RKVSGPRALQ PSQFGMLCTA DTPEGEACGL VKNLALMTHI TTDDEEEPIK KLCYVLGVED 550 560 570 580 590 600 ITLIDSASLH LNYGVYLNGT LIGSIRFPTK FVTQFRHLRR TGKVSEFISI YSNSHQMAVH 610 620 630 640 650 660 IATDGGRICR PLIIVSDGQS RVKDIHLRKL LDGELDFDDF LKLGLVEYLD VNEENDSYIA 670 680 690 700 710 720 LYEKDIVPSM THLEIEPFTI LGAVAGLIPY PHHNQSPRNT YQCAMGKQAI GAIAYNQFKR 730 740 750 760 770 780 IDTLLYLMTY PQQPMVKTKT IELIDYDKLP AGQNATVAVM SYSGYDIEDA LVLNKSSIDR 790 800 810 820 830 840 GFGRCETRRK TTTVLKRYAN HTQDIIGGMR VDENGDPIWQ HQSLGPDGLG EVGMKVQSGQ 850 860 870 880 890 900 IYINKSVPTN SADAPNPNNV NVQTQYREAP VIYRGPEPSH IDQVMMSVSD NDQALIKVLL 910 920 930 940 950 960 RQNRRPELGD KFSSRHGQKG VCGIIVKQED MPFNDQGIVP DIIMNPHGFP SRMTVGKMIE 970 980 990 1000 1010 1020 LISGKAGVLN GTLEYGTCFG GSKLEDMSKI LVDQGFNYSG KDMLYSGITG ECLQAYIFFG 1030 1040 1050 1060 1070 1080 PIYYQKLKHM VLDKMHARAR GPRAVLTRQP TEGRSRDGGL RLGEMERDCV IAYGASQLLL 1090 1100 1110 1120 1130 1140 ERLMISSDAF EVDVCDKCGL MGYSGWCTTC KSAENIIKMT IPYAAKLLFQ ELLSMNIAPR LRLEDIFQQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The RET1 gene of yeast encodes the second-largest subunit of RNA polymerase III. Structural analysis of the wild-type and ret1-1 mutant alleles." James P., Whelen S., Hall B.D. J. Biol. Chem. 266:5616-5624(1991) [PubMed: 2005101] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K. Nature 387:98-102(1997) [PubMed: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[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]	"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].
[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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"Structural biology of RNA polymerase III: subcomplex C17/25 X-ray structure and 11 subunit enzyme model." Jasiak A.J., Armache K.J., Martens B., Jansen R.P., Cramer P. Mol. Cell 23:71-81(2006) [PubMed: 16818233] [Abstract] Cited for: 3D-STRUCTURE MODELING OF THE POL III CORE COMPLEX.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M38723 Genomic DNA. Translation: AAB59324.1. Z75115 Genomic DNA. Translation: CAA99422.1. BK006948 Genomic DNA. Translation: DAA10979.1.
PIR	S67099.
RefSeq	NP_014850.1. NM_001183626.1.
3D structure databases
ProteinModelPortal	P22276.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-997N.
IntAct	P22276. 29 interactions.
MINT	MINT-644049.
STRING	P22276.
Proteomic databases
PeptideAtlas	P22276.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YOR207C; YOR207C; YOR207C.
GeneID	854382.
KEGG	sce:YOR207C.
NMPDR	fig|4932.3.peg.5962.
Organism-specific databases
CYGD	YOR207c.
SGD	S000005733. RET1.
Phylogenomic databases
eggNOG	fuNOG05271.
GeneTree	EFGT00050000004610.
HOGENOM	HBG317648.
OMA	FKMERAG.
OrthoDB	EOG4K6KC8.
Enzyme and pathway databases
Reactome	REACT_87991. Transcription.
Gene expression databases
ArrayExpress	P22276.
Genevestigator	P22276.
GermOnline	YOR207C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR015712. DNA-dir_RNA_pol_su2. IPR007120. DNA-dir_RNA_pol_su2_6. IPR007121. RNA_pol_bsu_CS. IPR007644. RNA_pol_bsu_protrusion. IPR007642. RNA_pol_Rpb2_2. IPR007645. RNA_pol_Rpb2_3. IPR007646. RNA_pol_Rpb2_4. IPR007647. RNA_pol_Rpb2_5. IPR007641. RNA_pol_Rpb2_7. IPR014724. RNA_pol_RPB2_OB-fold. [Graphical view]
Gene3D	G3DSA:2.40.270.10. G3DSA:2.40.270.10. 2 hits. G3DSA:2.40.50.150. Ribosomal_L2. 1 hit.
KO	K03021.
PANTHER	PTHR20856. RNA_pol_I_sub2. 1 hit.
Pfam	PF04563. RNA_pol_Rpb2_1. 1 hit. PF04561. RNA_pol_Rpb2_2. 1 hit. PF04565. RNA_pol_Rpb2_3. 1 hit. PF04566. RNA_pol_Rpb2_4. 1 hit. PF04567. RNA_pol_Rpb2_5. 1 hit. PF00562. RNA_pol_Rpb2_6. 1 hit. PF04560. RNA_pol_Rpb2_7. 1 hit. [Graphical view]
PROSITE	PS01166. RNA_POL_BETA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	976523.

Entry information

Entry name

RPC2_YEAST

Accession

Primary (citable) accession number: P22276
Secondary accession number(s): D6W2R3, Q12696

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	November 1, 1997
Last modified:	December 14, 2011
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program