P25299 (RNA15_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
mRNA 3'-end-processing protein RNA15

Gene names

Name:	RNA15
Ordered Locus Names:	YGL044C

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

General annotation (Comments)

Function	RNA-binding component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with the cleavage factor NAB4/CFIB and the cleavage and polyadenylation factor (CPF) complex. Binds to A-rich RNA sequence elements. Ref.5 Ref.7
Subunit structure	Component of the CFIA complex, which is composed of RNA14, RNA15, PCF11 and CLP1. Interacts directly with RNA14. Interacts with polyadenylate-binding protein PAB1. Ref.6
Subcellular location	Nucleus.
Miscellaneous	Present with 6350 molecules/cell in log phase SD medium.
Sequence similarities	Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
Biological process	mRNA processing
Cellular component	Nucleus
Ligand	RNA-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mRNA cleavage Inferred from direct assay Ref.7. Source: SGD mRNA polyadenylation Inferred from direct assay Ref.7. Source: SGD
Cellular_component	mRNA cleavage factor complex Inferred from physical interaction Ref.7. Source: SGD
Molecular_function	mRNA binding Inferred from direct assay PubMed 17684230. Source: SGD nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PCF11	P39081	9	EBI-15640,EBI-12980
RNA14	P25298	8	EBI-15640,EBI-15632
SUB1	P54000	2	EBI-15640,EBI-18492

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 296

296

mRNA 3'-end-processing protein RNA15

PRO_0000081807

Regions

Domain

18 – 96

79

RRM

Compositional bias

104 – 109

6

Poly-Gln

Compositional bias

111 – 128

18

Asn-rich

Secondary structure

1

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296

Helix Strand Turn

Details...

Beta strand

18 – 24

7

Helix

31 – 39

9

Beta strand

44 – 48

5

Turn

53 – 55

3

Beta strand

60 – 68

9

Helix

69 – 79

11

Beta strand

85 – 87

3

Beta strand

90 – 93

4

Helix

99 – 101

3

Helix

139 – 143

5

Turn

156 – 158

3

Helix

161 – 170

10

Helix

174 – 190

17

Helix

192 – 201

10

Helix

203 – 216

14

Beta strand

217 – 219

3

Helix

221 – 224

4

Turn

225 – 227

3

Sequences

	Sequence		Length	Mass (Da)
	P25299 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 10053B8648A71ECB	FASTA	296	32,791
	10 20 30 40 50 60 MNRQSGVNAG VQNNPPSRVV YLGSIPYDQT EEQILDLCSN VGPVINLKMM FDPQTGRSKG 70 80 90 100 110 120 YAFIEFRDLE SSASAVRNLN GYQLGSRFLK CGYSSNSDIS GVSQQQQQQY NNINGNNNNN 130 140 150 160 170 180 GNNNNNSNGP DFQNSGNANF LSQKFPELPS GIDVNINMTT PAMMISSELA KKPKEVQLKF 190 200 210 220 230 240 LQKFQEWTRA HPEDAVSLLE LCPQLSFVTA ELLLTNGICK VDDLIPLASR PQEEASATNN 250 260 270 280 290 NSVNEVVDPA VLNKQKELLK QVLQLNDSQI SILPDDERMA IWDLKQKALR GEFGAF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mutations in the yeast RNA14 and RNA15 genes result in an abnormal mRNA decay rate; sequence analysis reveals an RNA-binding domain in the RNA15 protein." Minvielle-Sebastia L., Winsor B., Bonneaud N., Lacroute F. Mol. Cell. Biol. 11:3075-3087(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 28383 / FL100 / VTT C-80102.
[2]	"The characterization of two new clusters of duplicated genes suggests a 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes." Feuermann M., de Montigny J., Potier S., Souciet J.-L. Yeast 13:861-869(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"RNA14 and RNA15 proteins as components of a yeast pre-mRNA 3'-end processing factor." Minvielle-Sebastia L., Preker P.J., Keller W. Science 266:1702-1705(1994) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Yeast Pab1 interacts with Rna15 and participates in the control of the poly(A) tail length in vitro." Amrani N., Minet M., Le Gouar M., Lacroute F., Wyers F. Mol. Cell. Biol. 17:3694-3701(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PAB1.
[7]	"Five subunits are required for reconstitution of the cleavage and polyadenylation activities of Saccharomyces cerevisiae cleavage factor I." Gross S., Moore C. Proc. Natl. Acad. Sci. U.S.A. 98:6080-6085(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE CFIA COMPLEX.
[8]	"Rna15 interaction with the A-rich yeast polyadenylation signal is an essential step in mRNA 3'-end formation." Gross S., Moore C.L. Mol. Cell. Biol. 21:8045-8055(2001) [PubMed] [Europe PMC] [Abstract] Cited for: RNA-BINDING.
[9]	"Purification of the Saccharomyces cerevisiae cleavage/polyadenylation factor I. Separation into two components that are required for both cleavage and polyadenylation of mRNA 3' ends." Kessler M.M., Zhao J., Moore C.L. J. Biol. Chem. 271:27167-27175(1996) [PubMed] [Europe PMC] [Abstract] Cited for: COMPOSITION OF THE CFIA COMPLEX.
[10]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M73462 Genomic DNA. Translation: AAA34984.1.
Z72566 Genomic DNA. Translation: CAA96746.1.
BK006941 Genomic DNA. Translation: DAA08056.1.

PIR

B40257.

RefSeq

NP_011471.1. NM_001180909.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KM8	NMR	-	B	14-97	[»]
2L9B	NMR	-	A	127-232	[»]
2X1A	X-ray	2.05	A	16-111	[»]
2X1B	X-ray	1.80	A	16-111	[»]
2X1F	X-ray	1.60	A	16-103	[»]

ProteinModelPortal

P25299.

SMR

P25299. Positions 16-101, 138-228.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1489N.

IntAct

P25299. 11 interactions.

MINT

MINT-389896.

STRING

4932.YGL044C.

Proteomic databases

PaxDb

P25299.

PeptideAtlas

P25299.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YGL044C; YGL044C; YGL044C.

GeneID

852838.

KEGG

sce:YGL044C.

Organism-specific databases

CYGD

YGL044c.

SGD

S000003012. RNA15.

Phylogenomic databases

eggNOG

NOG246793.

GeneTree

ENSGT00550000074641.

HOGENOM

HOG000247912.

KO

K14407.

OMA

NINMTTP.

OrthoDB

EOG4GQTF6.

Enzyme and pathway databases

BioCyc

YEAST:G3O-30555-MONOMER.

Gene expression databases

Genevestigator

P25299.

GermOnline

YGL044C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.30.70.330. 1 hit.

InterPro

IPR026896. CSTF_C.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

Pfam

PF14304. CSTF_C. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]

SMART

SM00360. RRM. 1 hit.
[Graphical view]

PROSITE

PS50102. RRM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P25299.

NextBio

972414.

Entry information

Entry name

RNA15_YEAST

Accession

Primary (citable) accession number: P25299
Secondary accession number(s): D6VU95

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	May 29, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program