Reviewed, UniProtKB/Swiss-Prot P02994 (EF1A_YEAST)

Names and origin

Protein names

Recommended name:
    Elongation factor 1-alpha
      Short name=EF-1-alpha
Alternative name(s):
    Translation elongation factor 1A
    Eukaryotic elongation factor 1A
      Short name=eEF1A

Gene names

Name:	TEF1
Ordered Locus Names:	YPR080W
ORF Names:	P9513.7
AND
Name:	TEF2
Ordered Locus Names:	YBR118W
ORF Names:	YBR0913

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	458 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	GTP-binding component of the eukaryotic elongation factor 1 complex (eEF1). In its active GTP-bound form, binds to and delivers aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. In the presence of a correct codon-anticodon match between the aminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, the ribosome acts as a GTPase activator and the GTP is hydrolyzed. The inactive GDP-bound form leaves the ribosome and must be recycled by its guanine nucleotide exchange factor (GEF) (eEF1B subcomplex) before binding another molecule of aminoacyl-tRNA. Required for nuclear export of aminoacyl-tRNAs. May also be involved in translational quality control by targeting cotranslationally damaged proteins to the proteasome. Also exhibits actin filament-binding and -bundling activities and is involved in cytoskeleton organization.
Pathway	Protein biosynthesis; polypeptide chain elongation.
Subunit structure	The eukaryotic elongation factor 1 complex (eEF1) is probably a heterohexamer. Two trimeric complexes, each composed of eEF1A (TEF1 or TEF2), eEF1Balpha (EFB1) and eEF1Bgamma (CAM1 or TEF4), are probably dimerized via the eF1Bgamma subunits. eEF1A interacts directly with eEF1Balpha. Interacts with elongation factor 3 (YEF3 or HEF3), BNI1, SRV2 and ZPR1. Binds to actin and forms a ternary complex with BNI1 and profilin. Interacts with the proteasome, probably via RPT1.
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton.
Post-translational modification	S-thiolated in response to oxidative stress, probably inhibiting the protein and causing a reduction in protein synthesis.
Miscellaneous	Present with 827 molecules/cell in log phase SD medium. There are two genes for eEF1A in yeast.
Sequence similarities	Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A subfamily.
Biophysicochemical properties	Kinetic parameters: KM=0.14 mM for GTP

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm Cytoskeleton
Ligand	Actin-binding GTP-binding Nucleotide-binding
Molecular function	Elongation factor
PTM	Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	tRNA export from nucleus Ref.21 Inferred from genetic interaction. Source: SGD translational elongation Ref.20 Inferred from electronic annotation. Source: InterPro
Cellular component	cytoskeleton Inferred from electronic annotation. Source: UniProtKB-KW mitochondrion Inferred from physical interaction. Source: SGD ribosome Traceable author statement. Source: SGD
Molecular function	GTP binding Inferred from electronic annotation. Source: InterPro GTPase activity Inferred from electronic annotation. Source: InterPro actin binding Inferred from electronic annotation. Source: UniProtKB-KW translation elongation factor activity Ref.20 Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P40093	1	EBI-6314,EBI-22730
	P53144	1	EBI-6314,EBI-23891
	Q08977	1	EBI-6314,EBI-35762
	Q12139	1	EBI-6314,EBI-30624
	Q12292	1	EBI-6314,EBI-36362
APT2	P36973	1	EBI-6314,EBI-2738
ATG4	P53867	1	EBI-6314,EBI-29160
BUD27	P43573	1	EBI-6314,EBI-22787
FAR8	Q05040	1	EBI-6314,EBI-28053
HIR1	P32479	1	EBI-6314,EBI-8316
HIR2	P32480	1	EBI-6314,EBI-8323
JHD2	P47156	1	EBI-6314,EBI-25646
KIP1	P28742	1	EBI-6314,EBI-9740
MTQ2	Q03920	1	EBI-6314,EBI-31378
POM152	P39685	1	EBI-6314,EBI-12739
PUS4	P48567	1	EBI-6314,EBI-14291
SDO1	Q07953	1	EBI-6314,EBI-27124
SRV2	P17555	2	EBI-6314,EBI-4024
TVP38	P36164	1	EBI-6314,EBI-26527
YPT7	P32939	1	EBI-6314,EBI-29509
ZPR1	P53303	1	EBI-6314,EBI-29657

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 458

458

Elongation factor 1-alpha

PRO_0000090973

Regions

Nucleotide binding

14 – 21

8

GTP

Nucleotide binding

91 – 95

5

GTP

Nucleotide binding

153 – 156

4

GTP

Sites

Site

298

1

Not modified

Site

372

1

Not modified

Amino acid modifications

Modified residue

1

1

Blocked amino end (Met)

Modified residue

6

1

Phosphoserine

Modified residue

18

1

Phosphoserine

Modified residue

30

1

N6-methyllysine

Modified residue

53

1

Phosphoserine

Modified residue

72

1

Phosphothreonine

Modified residue

79

1

N6,N6,N6-trimethyllysine

Modified residue

163

1

Phosphoserine

Modified residue

259

1

Phosphothreonine

Modified residue

316

1

N6,N6-dimethyllysine

Modified residue

355

1

Phosphotyrosine

Modified residue

356

1

Phosphoserine

Modified residue

390

1

N6-methyllysine

Modified residue

394

1

Phosphoserine

Modified residue

414

1

Phosphoserine

Modified residue

430

1

Phosphothreonine

Modified residue

458

1

Lysine methyl ester

Experimental info

Mutagenesis

122

1

E → K: Reduces interaction with YEF3

Mutagenesis

153

1

N → D: Increases KM for GTP to 2.7 mM

Mutagenesis

153

1

N → T: Increases KM for GTP to 6.0 mM and reduces translation fidelity. Increases Km for GTP to 10.3 mM and reduces translation fidelity; when associated with E-156

Mutagenesis

156

1

D → E: Increases KM for GTP to 10.3 mM and reduces translation fidelity; when associated with T-152

Mutagenesis

156

1

D → N: Increases KM for GTP to 13.1 mM and reduces translation fidelity. Confers hyperresistance to canavanine

Mutagenesis

156

1

D → W: Increases KM for GTP to 4.2 mM. Preferres XTP over GTP as substrate

Mutagenesis

286

1

E → K in TEF2-1; strongly reduces translation fidelity by increasing the frequency of frameshifting and amino acid misincorporation

Mutagenesis

317

1

E → K in TEF2-2; strongly reduces translation fidelity by increasing the frequency of frameshifting and amino acid misincorporation

Sequence conflict

86

1

Q → E AA sequence Ref.13

Secondary structure

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458

Helix Strand Turn

Details...

Beta strand

6 – 14

9

Helix

20 – 31

12

Helix

36 – 45

10

Helix

46 – 49

4

Beta strand

50 – 52

3

Helix

56 – 68

13

Beta strand

78 – 81

4

Beta strand

83 – 91

9

Helix

98 – 104

7

Beta strand

105 – 107

3

Beta strand

110 – 117

8

Helix

120 – 126

7

Helix

132 – 142

11

Beta strand

147 – 153

7

Helix

155 – 158

4

Helix

162 – 179

18

Helix

183 – 185

3

Beta strand

188 – 190

3

Turn

193 – 195

3

Turn

197 – 199

3

Beta strand

212 – 215

4

Beta strand

217 – 225

9

Helix

226 – 231

6

Beta strand

245 – 254

10

Turn

255 – 257

3

Beta strand

258 – 264

7

Beta strand

275 – 279

5

Turn

280 – 282

3

Beta strand

283 – 292

10

Beta strand

305 – 312

8

Turn

315 – 317

3

Beta strand

323 – 326

4

Beta strand

336 – 344

9

Beta strand

358 – 361

4

Beta strand

364 – 377

14

Turn

379 – 381

3

Beta strand

384 – 388

5

Beta strand

397 – 406

10

Turn

413 – 415

3

Helix

417 – 419

3

Beta strand

420 – 426

7

Beta strand

429 – 440

12

Sequences

	Sequence		Length	Mass (Da)
	P02994-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 411C66D830716576	FASTA	458	50,033
	10 20 30 40 50 60 MGKEKSHINV VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAELG KGSFKYAWVL 70 80 90 100 110 120 DKLKAERERG ITIDIALWKF ETPKYQVTVI DAPGHRDFIK NMITGTSQAD CAILIIAGGV 130 140 150 160 170 180 GEFEAGISKD GQTREHALLA FTLGVRQLIV AVNKMDSVKW DESRFQEIVK ETSNFIKKVG 190 200 210 220 230 240 YNPKTVPFVP ISGWNGDNMI EATTNAPWYK GWEKETKAGV VKGKTLLEAI DAIEQPSRPT 250 260 270 280 290 300 DKPLRLPLQD VYKIGGIGTV PVGRVETGVI KPGMVVTFAP AGVTTEVKSV EMHHEQLEQG 310 320 330 340 350 360 VPGDNVGFNV KNVSVKEIRR GNVCGDAKND PPKGCASFNA TVIVLNHPGQ ISAGYSPVLD 370 380 390 400 410 420 CHTAHIACRF DELLEKNDRR SGKKLEDHPK FLKSGDAALV KFVPSKPMCV EAFSEYPPLG 430 440 450 RFAVRDMRQT VAVGVIKSVD KTEKAAKVTK AAQKAAKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Polypeptide chain elongation factor 1 alpha (EF-1 alpha) from yeast: nucleotide sequence of one of the two genes for EF-1 alpha from Saccharomyces cerevisiae." Nagata S., Nagashima K., Tsunetsugu-Yokota Y., Fujimura K., Miyazaki M., Kaziro Y. EMBO J. 3:1825-1830(1984) [PubMed: 6383821] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEF1).
[2]	"Identification of two genes coding for the translation elongation factor EF-1 alpha of S. cerevisiae." Schirmaier F., Philippsen P. EMBO J. 3:3311-3315(1984) [PubMed: 6396088] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEF2).
[3]	"Cloning, nucleotide sequence, and expression of one of two genes coding for yeast elongation factor 1 alpha." Cottrelle P., Thiele D., Price V.L., Memet S., Micouin J.-Y., Marck C., Buhler J.-M., Sentenac A., Fromageot P. J. Biol. Chem. 260:3090-3096(1985) [PubMed: 2982849] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEF1).