Reviewed, UniProtKB/Swiss-Prot P26642 (EF1GA_XENLA)

Names and origin

Protein names

Recommended name:
    Elongation factor 1-gamma-A
      Short name=EF-1-gamma-A
Alternative name(s):
    eEF-1B gamma-A
    p47

Gene names

Name:

eef1g-A

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	436 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Probably plays a role in anchoring the complex to other cellular components.
Subunit structure	EF-1 is composed of four subunits: alpha, beta, delta, and gamma.
Post-translational modification	Phosphorylated by CDC2. Ref.4 The N-terminus is blocked Probable.
Sequence similarities	Contains 1 EF-1-gamma C-terminal domain. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Biological process	Protein biosynthesis
Molecular function	Elongation factor
PTM	Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	translational elongation Inferred from electronic annotation. Source: InterPro
Cellular component	eukaryotic translation elongation factor 1 complex Inferred from electronic annotation. Source: InterPro
Molecular function	translation elongation factor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 436	436	Elongation factor 1-gamma-A		PRO_0000208820
Regions
	Domain	2 – 87	86	GST N-terminal
	Domain	88 – 221	134	GST C-terminal
	Domain	275 – 436	162	EF-1-gamma C-terminal
Experimental info
	Sequence conflict	77	1	H → A AA sequence Ref.3
	Sequence conflict	134	1	G → E in AAB29957. Ref.2
	Sequence conflict	270	1	Missing AA sequence Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P26642-1 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 8785C1E80578B131	FASTA	436	49,791
	10 20 30 40 50 60 MAGGTLYTYP DNWRAYKPLI AAQYSGFPIK VASSAPEFQF GVTNKTPEFL KKFPLGKVPA 70 80 90 100 110 120 FEGKDGFCLF ESSAIAHYVG NDELRGTTRL HQAQVIQWVS FSDSHIVPPA SAWVFPTLGI 130 140 150 160 170 180 MQYNKQATEQ AKEGIKTVLG VLDSHLQTRT FLVGERITLA DITVTCSLLW LYKQVLEPSF 190 200 210 220 230 240 RQPFGNVTRW FVTCVNQPEF RAVLGEVKLC DKMAQFDAKK FAEMQPKKET PKKEKPAKEP 250 260 270 280 290 300 KKEKEEKKKA APTPAPAPED DLDESEKALA AEPKSKDPYA HLPKSSFIMD EFKRKYSNED 310 320 330 340 350 360 TLTVALPYFW EHFDKEGWSI WYAEYKFPEE LTQAFMSCNL ITGMFQRLDK LRKTGFASVI 370 380 390 400 410 420 LFGTNNNSSI SGVWVFRGQD LAFTLSEDWQ IDYESYNWRK LDSGSEECKT LVKEYFAWEG 430 EFKNVGKPFN QGKIFK

References

[1]	"Molecular cloning of Xenopus elongation factor 1 gamma, major M-phase promoting factor substrate." Cormier P., Osborne H.B., Morales J., Bassez T., Poulhe R., Mazabraud A., Mulner-Lorillon O., Belle R. Nucleic Acids Res. 19:6644-6644(1991) [PubMed: 1754404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Ovary.
[2]	"Expression of elongation factor 1 alpha (EF-1 alpha) and 1 beta gamma (EF-1 beta gamma) are uncoupled in early Xenopus embryos." Morales J., Bassez T., Cormier P., Mulner-Lorillon O., Belle R., Osborne H.B. Dev. Genet. 14:440-448(1993) [PubMed: 8111972] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Oocyte.
[3]	"A purified complex from Xenopus oocytes contains a p47 protein, an in vivo substrate of MPF, and a p30 protein respectively homologous to elongation factors EF-1 gamma and EF-1 beta." Belle R., Derancourt J., Poulhe R., Capony J.-P., Ozon R., Mulner-Lorillon O. FEBS Lett. 255:101-104(1989) [PubMed: 2676593] [Abstract] Cited for: PROTEIN SEQUENCE OF 38-48; 72-79; 268-274; 388-394 AND 415-419.
[4]	"Purification of a p47 phosphoprotein from Xenopus laevis oocytes and identification as an in vivo and in vitro p34cdc2 substrate." Mulner-Lorillon O., Poulhe R., Cormier P., Labbe J.C., Doree M., Belle R. FEBS Lett. 251:219-224(1989) [PubMed: 2546822] [Abstract] Cited for: PHOSPHORYLATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X62508 mRNA. Translation: CAA44367.1. S69724 mRNA. Translation: AAB29957.1.
PIR	I51237. S20060.
UniGene	Xl.7814
3D structure databases
HSSP	HSSP built from PDB template 1PBU based on UniProtKB P26641.
SMR	P26642. Positions 275-436.
ModBase	Search...
Proteomic databases
PRIDE	P26642.
Organism-specific databases
Xenbase	XB-FEAT-975012. eef1g.
Phylogenomic databases
HOVERGEN	P26642.
Family and domain databases
InterPro	IPR010987. Glutathione-S-Trfase_C-like. IPR004045. Glutathione_S-Trfase_N. IPR017933. Glutathione_S_Trfase/Cl_chnl_C. IPR004046. GST_C. IPR001662. Transl_elong_EF1_G_con. [Graphical view]
Gene3D	G3DSA:1.20.1050.10. GST_C_like. 1 hit. G3DSA:3.30.70.1010. Transl_elong_EF1_G_con. 1 hit.
Pfam	PF00647. EF1G. 1 hit. PF00043. GST_C. 1 hit. PF02798. GST_N. 1 hit. [Graphical view]
ProDom	PD006217. EF1_G. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS50040. EF1G_C. 1 hit. PS50405. GST_CTER. 1 hit. PS50404. GST_NTER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

EF1GA_XENLA

Accession

Primary (citable) accession number: P26642
Secondary accession number(s): Q91374

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	June 16, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Xenopus annotation project