ID EF2_PONAB Reviewed; 858 AA.
AC Q5R8Z3; Q5RBA6;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 130.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
DE EC=3.6.5.- {ECO:0000250|UniProtKB:P13639};
GN Name=EEF2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC during translation elongation. During this step, the ribosome changes
CC from the pre-translocational (PRE) to the post-translocational (POST)
CC state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound
CC deacylated tRNA move to the P and E sites, respectively. Catalyzes the
CC coordinated movement of the two tRNA molecules, the mRNA and
CC conformational changes in the ribosome. {ECO:0000250|UniProtKB:P13639}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000250|UniProtKB:P13639};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P13639};
CC -!- SUBUNIT: Binds to 80S ribosomes. Actively translating ribosomes show
CC mutually exclusive binding of eIF5a (EIF5A or EIF5A2) and EEF2/eEF2.
CC Interacts with SERBP1; interaction sequesters EEF2/eEF2 at the A-site
CC of the ribosome, thereby blocking the interaction sites of the mRNA-
CC tRNA complex, promoting ribosome stabilization and hibernation (By
CC similarity). Interacts with HABP4; interaction takes place at the A-
CC site of hibernating ribosomes and promotes ribosome stabilization (By
CC similarity). Component of the mRNA surveillance SURF complex, at least
CC composed of ERF1, ERF3 (ERF3A or ERF3B), EEF2, UPF1/RENT1, SMG1, SMG8
CC and SMG9. Interacts with RBPMS2 (By similarity).
CC {ECO:0000250|UniProtKB:P13639, ECO:0000250|UniProtKB:Q7ZXP8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P13639}. Nucleus
CC {ECO:0000250|UniProtKB:P13639}. Note=Phosphorylation by CSK promotes
CC cleavage and SUMOylation-dependent nuclear translocation of the C-
CC terminal cleavage product. {ECO:0000250|UniProtKB:P13639}.
CC -!- PTM: Phosphorylation by EF-2 kinase completely inactivates EF-2; it
CC requires prior phosphorylation by CDK2 at Ser-595 during mitotic
CC prometaphase. Phosphorylation by CSK promotes SUMOylation, proteolytic
CC cleavage, and nuclear translocation if the C-terminal fragment.
CC {ECO:0000250|UniProtKB:P13639}.
CC -!- PTM: Diphthamide is 2-[3-carboxyamido-3-(trimethyl-
CC ammonio)propyl]histidine (By similarity).
CC {ECO:0000250|UniProtKB:P05197}.
CC -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P13639}.
CC -!- PTM: Proteolytically processed at two sites following phosphorylation
CC by CSK. {ECO:0000250|UniProtKB:P13639}.
CC -!- PTM: SUMOylated following phosphorylation by CSK, promotes proteolytic
CC cleavage. {ECO:0000250|UniProtKB:P13639}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR858745; CAH90954.1; -; mRNA.
DR EMBL; CR859604; CAH91767.1; -; mRNA.
DR RefSeq; NP_001125547.1; NM_001132075.1.
DR AlphaFoldDB; Q5R8Z3; -.
DR SMR; Q5R8Z3; -.
DR STRING; 9601.ENSPPYP00000010534; -.
DR Ensembl; ENSPPYT00000010948.3; ENSPPYP00000010534.2; ENSPPYG00000009393.3.
DR GeneID; 100172460; -.
DR KEGG; pon:100172460; -.
DR CTD; 1938; -.
DR eggNOG; KOG0469; Eukaryota.
DR GeneTree; ENSGT00940000154662; -.
DR HOGENOM; CLU_002794_11_1_1; -.
DR InParanoid; Q5R8Z3; -.
DR OrthoDB; 166721at2759; -.
DR TreeFam; TF300575; -.
DR Proteomes; UP000001595; Chromosome 19.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0003746; F:translation elongation factor activity; ISS:UniProtKB.
DR GO; GO:0006414; P:translational elongation; ISS:UniProtKB.
DR CDD; cd01681; aeEF2_snRNP_like_IV; 1.
DR CDD; cd04096; eEF2_snRNP_like_C; 1.
DR CDD; cd01885; EF2; 1.
DR CDD; cd16261; EF2_snRNP_III; 1.
DR CDD; cd03700; EF2_snRNP_like_II; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR42908:SF10; ELONGATION FACTOR 2; 1.
DR PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Elongation factor; GTP-binding; Hydrolase;
KW Isopeptide bond; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Ubl conjugation.
FT CHAIN 1..858
FT /note="Elongation factor 2"
FT /id="PRO_0000223487"
FT DOMAIN 17..362
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 26..33
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32324"
FT BINDING 158..161
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32324"
FT BINDING 216..218
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32324"
FT SITE 586..587
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT SITE 605..606
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 54
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 57
FT /note="Phosphothreonine; by EEF2K"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 152
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P58252"
FT MOD_RES 235
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 239
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 265
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 272
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 272
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P58252"
FT MOD_RES 275
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05197"
FT MOD_RES 373
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 435
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 439
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P58252"
FT MOD_RES 445
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 525
FT /note="N6,N6,N6-trimethyllysine; by EEF2KMT"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 572
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P58252"
FT MOD_RES 595
FT /note="Phosphoserine; by CDK2"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 619
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P58252"
FT MOD_RES 715
FT /note="Diphthamide"
FT /evidence="ECO:0000250|UniProtKB:P05197"
FT CROSSLNK 239
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT CROSSLNK 322
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT CROSSLNK 529
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT CONFLICT 233
FT /note="V -> A (in Ref. 1; CAH90954)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="P -> A (in Ref. 1; CAH91767)"
FT /evidence="ECO:0000305"
FT CONFLICT 794
FT /note="F -> L (in Ref. 1; CAH91767)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 858 AA; 95338 MW; 78BD1710236C0D9C CRC64;
MVNFTVDQIR AIMDKKANIR NMSVIAHVDH GKSTLTDSLV CKAGIIASAR AGETRFTDTR
KDEQERCITI KSTAISLFYE LSENDLNFIK QSKDGAGFLI NLIDSPGHVD FSSEVTAALR
VTDGALVVVD CVSGVCVQTE TVLRQAIAER IKPVLMMNKM DRALLELQLE PEELYQTFQR
IVENVNVIIS TYGEGESGPM GNIMIDPVLG TVGFGSGLHG WAFTLKQFAE MYVAKFAAKG
EGQLGPAERA KKVEDMMKKL WGDRYFDPAN GKFSKSATSP EGKKLPRTFC QLILDPIFKV
FDAIMNFKKE ETAKLIEKLD IKLDSEDKDK EGKPLLKAVM RRWLPAGDAL LQMITIHLPS
PVTAQKYRCE LLYEGPPDDE AAMGIKSCDP KGPLMMYISK MVPTSDKGRF YAFGRVFSGL
VSTGLKVRIM GPNYTPGKKE DLYLKPIQRT ILMMGRYVEP IEDVPCGNIV GLVGVDQFLV
KTGTITTFEH AHNMRVMKFS VSPVVRVAVE AKNPADLPKL VEGLKRLAKS DPMVQCIIEE
SGEHIIAGAG ELHLEICLKD LEEDHACIPI KKSDPVVSYR ETVSEESNVL CLSKSPNKHN
RLYMKARPFP DGLAEDIDKG EVSARQELKQ RARYLAEKYE WDVAEARKIW CFGPDGTGPN
ILTDITKGVQ YLNEIKDSVV AGFQWATKEG ALCEENMRGV RFDVHDVTLH ADAIHRGGGQ
IIPTARRCLY ASVLTAQPRL MEPIYLVEIQ CPEQVVGGIY GVLNRKRGHV FEESQVAGTP
MFVVKAYLPV NESFGFTADL RSNTGGQAFP QCVFDHWQIL PGDPFDNSSR PSQVVAETRK
RKGLKEGIPA LDNFLDKL
//
