EF2K_CAEEL
ID EF2K_CAEEL Reviewed; 768 AA.
AC O01991; O01992; Q20309; Q8MYP9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Eukaryotic elongation factor 2 kinase {ECO:0000303|PubMed:9144159};
DE Short=eEF-2 kinase {ECO:0000303|PubMed:9144159};
DE Short=eEF-2K;
DE EC=2.7.11.20 {ECO:0000269|PubMed:9144159};
DE AltName: Full=Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase;
GN Name=efk-1; ORFNames=F42A10.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, CATALYTIC
RP ACTIVITY, AND ACTIVITY REGULATION.
RC STRAIN=Bristol N2;
RX PubMed=9144159; DOI=10.1073/pnas.94.10.4884;
RA Ryazanov A.G., Ward M.D., Mendola C.E., Pavur K.S., Dorovkov M.V.,
RA Wiedmann M., Erdjument-Bromage H., Tempst P., Parmer T.G., Prostko C.R.,
RA Germino F.J., Hait W.N.;
RT "Identification of a new class of protein kinases represented by eukaryotic
RT elongation factor-2 kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:4884-4889(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP INTERACTION WITH CMD-1.
RX PubMed=17854888; DOI=10.1016/j.ceca.2007.07.008;
RA Shen X., Valencia C.A., Gao W., Cotten S.W., Dong B., Huang B.C., Liu R.;
RT "Ca(2+)/Calmodulin-binding proteins from the C. elegans proteome.";
RL Cell Calcium 43:444-456(2008).
CC -!- FUNCTION: Phosphorylates elongation factor-2 (eEF-2) at two threonine
CC residues that are conserved in all eukaryotes and are located within a
CC GTP-binding domain (PubMed:9144159). Calcium(2+)/calmodulin dependent
CC activity (PubMed:9144159). Inactivates eEF-2 by catalyzing its
CC phosphorylation (PubMed:9144159). eEF-2 catalyzes the movement of the
CC ribosome along mRNA during translation in eukaryotic cells
CC (PubMed:9144159). {ECO:0000269|PubMed:9144159,
CC ECO:0000303|PubMed:9144159}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[translation elongation factor 2] + ATP = [translation
CC elongation factor 2]-phosphate + ADP + H(+); Xref=Rhea:RHEA:21436,
CC Rhea:RHEA-COMP:11268, Rhea:RHEA-COMP:11269, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
CC ChEBI:CHEBI:456216; EC=2.7.11.20;
CC Evidence={ECO:0000269|PubMed:9144159};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21437;
CC Evidence={ECO:0000269|PubMed:9144159};
CC -!- ACTIVITY REGULATION: Calcium(2+)/calmodulin dependent activity
CC (PubMed:9144159). Undergoes calcium/calmodulin-dependent intramolecular
CC autophosphorylation, and this results in it becoming partially
CC calcium/calmodulin-independent. {ECO:0000250,
CC ECO:0000269|PubMed:9144159}.
CC -!- SUBUNIT: Monomer or homodimer (Probable). Interacts with cmd-1 in the
CC presence of Ca(2+) (PubMed:17854888). {ECO:0000269|PubMed:17854888,
CC ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=O01991-1; Sequence=Displayed;
CC Name=b;
CC IsoId=O01991-2; Sequence=VSP_004231;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Alpha-type
CC protein kinase family. {ECO:0000305}.
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DR EMBL; U93846; AAB58268.1; -; mRNA.
DR EMBL; U93847; AAB58269.1; -; mRNA.
DR EMBL; FO080631; CCD65313.1; -; Genomic_DNA.
DR EMBL; FO080631; CCD65314.1; -; Genomic_DNA.
DR RefSeq; NP_001022572.1; NM_001027401.2. [O01991-1]
DR RefSeq; NP_001022573.1; NM_001027402.3. [O01991-2]
DR AlphaFoldDB; O01991; -.
DR SMR; O01991; -.
DR BioGRID; 41092; 3.
DR IntAct; O01991; 2.
DR STRING; 6239.F42A10.4a; -.
DR iPTMnet; O01991; -.
DR EPD; O01991; -.
DR PaxDb; O01991; -.
DR PeptideAtlas; O01991; -.
DR EnsemblMetazoa; F42A10.4a.1; F42A10.4a.1; WBGene00001160. [O01991-1]
DR EnsemblMetazoa; F42A10.4b.1; F42A10.4b.1; WBGene00001160. [O01991-2]
DR GeneID; 175871; -.
DR KEGG; cel:CELE_F42A10.4; -.
DR UCSC; F42A10.4a.1; c. elegans. [O01991-1]
DR CTD; 175871; -.
DR WormBase; F42A10.4a; CE32415; WBGene00001160; efk-1. [O01991-1]
DR WormBase; F42A10.4b; CE32416; WBGene00001160; efk-1. [O01991-2]
DR eggNOG; ENOG502QVA3; Eukaryota.
DR GeneTree; ENSGT00940000157839; -.
DR InParanoid; O01991; -.
DR OMA; CNDICET; -.
DR OrthoDB; 741011at2759; -.
DR PhylomeDB; O01991; -.
DR BRENDA; 2.7.11.20; 1045.
DR Reactome; R-CEL-166208; mTORC1-mediated signalling.
DR PRO; PR:O01991; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001160; Expressed in embryo and 4 other tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0004686; F:elongation factor-2 kinase activity; IDA:WormBase.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:WormBase.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR017400; eEF-2K.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR004166; MHCK_EF2_kinase.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF02816; Alpha_kinase; 1.
DR PIRSF; PIRSF038139; Elongation_factor_2_kinase; 1.
DR SMART; SM00811; Alpha_kinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51158; ALPHA_KINASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Calcium; Calmodulin-binding; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..768
FT /note="Eukaryotic elongation factor 2 kinase"
FT /id="PRO_0000086935"
FT DOMAIN 102..309
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00501"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 279..284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 625..632
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:9144159"
FT /id="VSP_004231"
SQ SEQUENCE 768 AA; 87825 MW; 9333F3B13F0C14C5 CRC64;
MTIDTTNESD NSPTNSPGLE ASARTFSLNA SKMVRITDDY ADEVFIEQND VVIEKPRMDP
LHVRKLMETW RKAARRARTN YIDPWDEFNI HEYPVQRAKR YRYSAIRKQW TEDIVDVRLH
PDSFARGAMR ECYRLKKCSK HGTSQDWSSN YVAKRYICQV DRRVLFDDVR LQMDAKLWAE
EYNRYNPPKK IDIVQMCVIE MIDVKGSPLY HLEHFIEGKY IKYNSNSGFV SNAARLTPQA
FSHFTFERSG HQMMVVDIQG VGDLYTDPQI HTVVGTDYGD GNLGTRGMAL FFHSHRCNDI
CETMDLSNFE LSPPEIEATE VAMEVAAKQK KSCIVPPTVF EARRNRISSE CVHVEHGISM
DQLRKRKTLN QSSTDLSAKS HNEDCVCPEC IPVVEQLCEP CSEDEEDEEE DYPRSEKSGN
SQKSRRSRMS ISTRSSGDES ASRPRKCGFV DLNSLRQRHD SFRSSVGTYS MNSSRQTRDT
EKDEFWKVLR KQSVPANILS LQLQQMAANL ENDEDVPQVT GHQFSVLGQI HIDLSRYHEL
GRFVEVDSEH KEMLEGSEND ARVPIKYDKQ SAIFHLDIAR KCGILEAVLT SAHIVLGLPH
ELLKEVTVDD LFPNGFGEQE NGIRADKGQK PCDLEEFGSD LMEIAAEMGD KGAMLYMAHA
YETGQHLGPN RRTDYKKSID WYQRVVGFQE EEELDSDCGK TTFSSFAPLT RHEILAKMAE
MYKEGGYGLN QDFERAYGLF NEAAEAAMEA MNGKLANKYY EKAEMCGE
