P05453 (ERF3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Eukaryotic peptide chain release factor GTP-binding subunit

Alternative name(s):
ERF-3
Short name=ERF3
ERF2
G1 to S phase transition protein 1
Omnipotent suppressor protein 2
PSI no more protein 2
Polypeptide release factor 3
Translation release factor 3

Gene names

Name:	SUP35
Synonyms:	GST1, PNM2, SAL3, SUF12, SUP2
Ordered Locus Names:	YDR172W
ORF Names:	YD9395.05

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

General annotation (Comments)

Function	Involved in translation termination. Stimulates the activity of ERF1. Binds guanine nucleotides. Recruited by polyadenylate-binding protein PAB1 to poly(A)-tails of mRNAs. Interaction with PAB1 is also required for regulation of normal mRNA decay through translation termination-coupled poly(A) shortening. Ref.7 Ref.13 Ref.15
Subunit structure	Heterodimer of two subunits, one of which binds GTP. Interacts with polyadenylate-binding protein PAB1, and TPA1. Ref.12 Ref.13 Ref.15 Ref.18 Ref.19
Subcellular location	Cytoplasm Probable.
Domain	The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain, which is unstructured in its native, soluble form, and which forms a parallel in-register beta-sheet in its amyloid form.
Miscellaneous	[PSI+] is the prion form of SUP35 (Ref.9). [PSI+] is the result of a conformational change of the cellular SUP35 protein that becomes self-propagating and infectious. This conformational change generates a form of SUP35 that assembles into amyloid fibrils. [PSI+] aggregates sequester soluble SUP35, resulting in defects in faithful translation termination by read-through of translation termination codons (Ref.8). [PSI+] can be cured by GdnHCl and by deletion of the molecular chaperone HSP104, which is required for [PSI+] propagation (Ref.10). It is speculated that the prion form would be at least mildly deleterious in most environments, but it might sometimes increases evolvability in certain harsh environments (Ref.23). Present with 78900 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the GTP-binding elongation factor family. ERF3 subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Amyloid Cytoplasm
Domain	Repeat
Ligand	GTP-binding Nucleotide-binding
Molecular function	Prion
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	GTP catabolic process Inferred from electronic annotation. Source: GOC nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Inferred from mutant phenotype Ref.13. Source: SGD
Cellular_component	cytosol Traceable author statement. Source: Reactome translation release factor complex Inferred from direct assay Ref.7. Source: SGD
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro translation release factor activity Inferred from direct assay PubMed 20947765. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ECM32	P32644	3	EBI-6540,EBI-22223
GLE1	Q12315	2	EBI-6540,EBI-7635
ITT1	Q04638	3	EBI-6540,EBI-27858

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 685	685	Eukaryotic peptide chain release factor GTP-binding subunit		PRO_0000091482
Regions
	Nucleotide binding	267 – 274	8	GTP By similarity
	Nucleotide binding	344 – 348	5	GTP By similarity
	Nucleotide binding	406 – 409	4	GTP By similarity
	Region	1 – 239	239	Interaction with PAB1
	Region	5 – 135	131	Prion domain (PrD)
	Region	139 – 249	111	Charged
Sites
	Site	273	1	Interacts with GTP/GDP By similarity
	Site	407	1	Interacts with GTP/GDP By similarity
Amino acid modifications
	Modified residue	221	1	Phosphoserine Ref.22
	Modified residue	341	1	Phosphothreonine By similarity
	Modified residue	571	1	Phosphoserine Ref.20 Ref.21 Ref.22
Experimental info
	Sequence conflict	53	1	S → C in CAA68760. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P05453 [UniParc]. Last modified November 1, 1988. Version 1. Checksum: 43912A6D77DFA153	FASTA	685	76,551
	10 20 30 40 50 60 MSDSNQGNNQ QNYQQYSQNG NQQQGNNRYQ GYQAYNAQAQ PAGGYYQNYQ GYSGYQQGGY 70 80 90 100 110 120 QQYNPDAGYQ QQYNPQGGYQ QYNPQGGYQQ QFNPQGGRGN YKNFNYNNNL QGYQAGFQPQ 130 140 150 160 170 180 SQGMSLNDFQ KQQKQAAPKP KKTLKLVSSS GIKLANATKK VGTKPAESDK KEEEKSAETK 190 200 210 220 230 240 EPTKEPTKVE EPVKKEEKPV QTEEKTEEKS ELPKVEDLKI SESTHNTNNA NVTSADALIK 250 260 270 280 290 300 EQEEEVDDEV VNDMFGGKDH VSLIFMGHVD AGKSTMGGNL LYLTGSVDKR TIEKYEREAK 310 320 330 340 350 360 DAGRQGWYLS WVMDTNKEER NDGKTIEVGK AYFETEKRRY TILDAPGHKM YVSEMIGGAS 370 380 390 400 410 420 QADVGVLVIS ARKGEYETGF ERGGQTREHA LLAKTQGVNK MVVVVNKMDD PTVNWSKERY 430 440 450 460 470 480 DQCVSNVSNF LRAIGYNIKT DVVFMPVSGY SGANLKDHVD PKECPWYTGP TLLEYLDTMN 490 500 510 520 530 540 HVDRHINAPF MLPIAAKMKD LGTIVEGKIE SGHIKKGQST LLMPNKTAVE IQNIYNETEN 550 560 570 580 590 600 EVDMAMCGEQ VKLRIKGVEE EDISPGFVLT SPKNPIKSVT KFVAQIAIVE LKSIIAAGFS 610 620 630 640 650 660 CVMHVHTAIE EVHIVKLLHK LEKGTNRKSK KPPAFAKKGM KVIAVLETEA PVCVETYQDY 670 680 PQLGRFTLRD QGTTIAIGKI VKIAE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the SUP2 (SUP35) gene of Saccharomyces cerevisiae." Kushnirov V.V., Ter-Avanesyan M.D., Telckov M.V., Surguchov A.P., Smirnov V.N., Inge-Vechtomov S.G. Gene 66:45-54(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Localization of possible functional domains in sup2 gene product of the yeast Saccharomyces cerevisiae." Kushnirov V.V., Ter-Avanesyan M.D., Surguchov A.P., Smirnov V.N., Inge-Vechtomov S.G. FEBS Lett. 215:257-260(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"SUF12 suppressor protein of yeast. A fusion protein related to the EF-1 family of elongation factors." Wilson P.G., Culbertson M.R. J. Mol. Biol. 199:559-573(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"A yeast gene required for the G1-to-S transition encodes a protein containing an A-kinase target site and GTPase domain." Kukuchi Y., Shimatake H., Kikuchi A. EMBO J. 7:1175-1182(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[6]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[7]	"The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae." Stansfield I., Jones K.M., Kushnirov V.V., Dagkesamanskaya A.R., Poznyakovski A.I., Paushkin S.V., Nierras C.R., Cox B.S., Ter-Avanesyan M.D., Tuite M.F. EMBO J. 14:4365-4373(1995) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor." Paushkin S.V., Kushnirov V.V., Smirnov V.N., Ter-Avanesyan M.D. EMBO J. 15:3127-3134(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PRION FORMATION, AGGREGATION.
[9]	"Genesis and variability of [PSI] prion factors in Saccharomyces cerevisiae." Derkatch I.L., Chernoff Y.O., Kushnirov V.V., Inge-Vechtomov S.G., Liebman S.W. Genetics 144:1375-1386(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PRION FORMATION.
[10]	"Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae." Derkatch I.L., Bradley M.E., Zhou P., Chernoff Y.O., Liebman S.W. Genetics 147:507-519(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PRION FORMATION, PRION CURING.
[11]	"Prions affect the appearance of other prions: the story of [PIN(+)]." Derkatch I.L., Bradley M.E., Hong J.Y., Liebman S.W. Cell 106:171-182(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PRION FORMATION.
[12]	"Poly(A)-binding protein acts in translation termination via eukaryotic release factor 3 interaction and does not influence [PSI(+)] propagation." Cosson B., Couturier A., Chabelskaya S., Kiktev D., Inge-Vechtomov S.G., Philippe M., Zhouravleva G. Mol. Cell. Biol. 22:3301-3315(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PAB1.
[13]	"Translation termination factor eRF3 mediates mRNA decay through the regulation of deadenylation." Hosoda N., Kobayashi T., Uchida N., Funakoshi Y., Kikuchi Y., Hoshino S., Katada T. J. Biol. Chem. 278:38287-38291(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN MRNA DECAY, INTERACTION WITH PAB1.
[14]	"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].
[15]	"The GTP-binding release factor eRF3 as a key mediator coupling translation termination to mRNA decay." Kobayashi T., Funakoshi Y., Hoshino S., Katada T. J. Biol. Chem. 279:45693-45700(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN MRNA DECAY, INTERACTION WITH PAB1.
[16]	"Protein-only transmission of three yeast prion strains." King C.Y., Diaz-Avalos R. Nature 428:319-323(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PRION PROPAGATION, AMYLOID STRUCTURE.
[17]	"Conformational variations in an infectious protein determine prion strain differences." Tanaka M., Chien P., Naber N., Cooke R., Weissman J.S. Nature 428:323-328(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PRION PROPAGATION, AMYLOID STRUCTURE.
[18]	"A faux 3'-UTR promotes aberrant termination and triggers nonsense-mediated mRNA decay." Amrani N., Ganesan R., Kervestin S., Mangus D.A., Ghosh S., Jacobson A. Nature 432:112-118(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PAB1.
[19]	"Tpa1p is part of an mRNP complex that influences translation termination, mRNA deadenylation, and mRNA turnover in Saccharomyces cerevisiae." Keeling K.M., Salas-Marco J., Osherovich L.Z., Bedwell D.M. Mol. Cell. Biol. 26:5237-5248(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TPA1.
[20]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571, MASS SPECTROMETRY. Strain: ADR376.
[21]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571, MASS SPECTROMETRY.
[22]	"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-221 AND SER-571, MASS SPECTROMETRY.
[23]	"The spontaneous appearance rate of the yeast prion [PSI+] and its implications for the evolution of the evolvability properties of the [PSI+] system." Lancaster A.K., Bardill J.P., True H.L., Masel J. Genetics 184:393-400(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PRION APPEARANCE.
[24]	"Structure of the cross-beta spine of amyloid-like fibrils." Nelson R., Sawaya M.R., Balbirnie M., Madsen A.O., Riekel C., Grothe R., Eisenberg D. Nature 435:773-778(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 7-13.
[25]	"Amyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure." Shewmaker F., Wickner R.B., Tycko R. Proc. Natl. Acad. Sci. U.S.A. 103:19754-19759(2006) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-253.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M21129 Genomic DNA. Translation: AAA35133.1.
X07163 Genomic DNA. Translation: CAA30155.1.
Y00829 Genomic DNA. Translation: CAA68760.1.
Z46727 Genomic DNA. Translation: CAA86677.1.
BK006938 Genomic DNA. Translation: DAA12014.1.

PIR

EFBYS2. S00733.

RefSeq

NP_010457.3. NM_001180479.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YJO	X-ray	1.30	A	8-13	[»]
1YJP	X-ray	1.80	A	7-13	[»]

ProteinModelPortal

P05453.

SMR

P05453. Positions 243-685.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-376N.

IntAct

P05453. 34 interactions.

MINT

MINT-516826.

Proteomic databases

PaxDb

P05453.

PeptideAtlas

P05453.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDR172W; YDR172W; YDR172W.

GeneID

851752.

KEGG

sce:YDR172W.
sce:YDR176W.

Organism-specific databases

CYGD

YDR172w.

SGD

S000002579. SUP35.

Phylogenomic databases

eggNOG

COG5256.

GeneTree

ENSGT00620000087924.

HOGENOM

HOG000229291.

KO

K03267.
K11315.

OMA

GWYLSWV.

OrthoDB

EOG4SXRMS.

Enzyme and pathway databases

Reactome

REACT_1034. Eukaryotic Translation Termination.
REACT_83470. Gene Expression.
REACT_85873. Metabolism of proteins.

Gene expression databases

ArrayExpress

P05453.

Genevestigator

P05453.

GermOnline

YDR172W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR000795. EF_GTP-bd_dom.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR004160. Transl_elong_EFTu/EF1A_C.
IPR009000. Transl_elong_init/rib_B-barrel.
IPR003285. Yeast_ERF.
[Graphical view]

Pfam

PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]

PRINTS

PR00315. ELONGATNFCT.
PR01343. YEASTERF.

SUPFAM

SSF50465. Elong_init_C. 1 hit.
SSF50447. Translat_factor. 1 hit.

PROSITE

PS00301. EFACTOR_GTP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P05453.

NextBio

969510.

Entry information

Entry name

ERF3_YEAST

Accession

Primary (citable) accession number: P05453
Secondary accession number(s): D6VSF4, P05420

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1988
Last modified:	May 1, 2013
This is version 146 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program