ID EF1A1_HUMAN Reviewed; 462 AA.
AC P68104; P04719; P04720; Q6IQ15;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 27-MAR-2024, entry version 208.
DE RecName: Full=Elongation factor 1-alpha 1;
DE Short=EF-1-alpha-1;
DE EC=3.6.5.- {ECO:0000305|PubMed:26593721};
DE AltName: Full=Elongation factor Tu;
DE Short=EF-Tu;
DE AltName: Full=Eukaryotic elongation factor 1 A-1;
DE Short=eEF1A-1;
DE AltName: Full=Leukocyte receptor cluster member 7;
GN Name=EEF1A1; Synonyms=EEF1A, EF1A, LENG7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3512269; DOI=10.1111/j.1432-1033.1986.tb09472.x;
RA Brands J.H.G.M., Maassen J.A., van Hemert F.J., Amons R., Moeller W.;
RT "The primary structure of the alpha subunit of human elongation factor 1.
RT Structural aspects of guanine-nucleotide-binding sites.";
RL Eur. J. Biochem. 155:167-171(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2564392; DOI=10.1016/s0021-9258(18)83619-5;
RA Uetsuki T., Naito A., Nagata S., Kaziro Y.;
RT "Isolation and characterization of the human chromosomal gene for
RT polypeptide chain elongation factor-1 alpha.";
RL J. Biol. Chem. 264:5791-5798(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=2183196; DOI=10.1093/nar/18.6.1513;
RA Madsen H.O., Poulsen K., Dahl O., Clark B.F.C., Hjorth J.P.;
RT "Retropseudogenes constitute the major part of the human elongation factor
RT 1 alpha gene family.";
RL Nucleic Acids Res. 18:1513-1516(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Shimazu T., Koike K.;
RT "Postnatal expression of a novel mRNA isoform from the human elongation
RT factor-1a gene.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell, Bone marrow, Cervix, Colon, Hippocampus, Kidney, Lung,
RC Lymph, Mammary gland, Ovary, Pancreas, Placenta, Testis, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-94.
RX PubMed=3960725; DOI=10.1093/nar/14.5.2409;
RA Rao T.R., Slobin L.I.;
RT "Structure of the amino-terminal end of mammalian elongation factor Tu.";
RL Nucleic Acids Res. 14:2409-2409(1986).
RN [7]
RP PROTEIN SEQUENCE OF 6-30; 52-62; 85-96; 101-129; 135-180; 248-313; 396-423
RP AND 431-439, METHYLATION AT LYS-55 AND LYS-165, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Colon carcinoma, and Ovarian carcinoma;
RA Bienvenut W.V., Zebisch A., Kolch W.;
RL Submitted (JAN-2010) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 7-16 AND 85-96, FUNCTION, INTERACTION WITH PARP1,
RP PHOSPHORYLATION BY TXK, AND SUBCELLULAR LOCATION.
RX PubMed=17177976; DOI=10.1111/j.1365-2249.2006.03249.x;
RA Maruyama T., Nara K., Yoshikawa H., Suzuki N.;
RT "Txk, a member of the non-receptor tyrosine kinase of the Tec family, forms
RT a complex with poly(ADP-ribose) polymerase 1 and elongation factor 1alpha
RT and regulates interferon-gamma gene transcription in Th1 cells.";
RL Clin. Exp. Immunol. 147:164-175(2007).
RN [9]
RP PROTEIN SEQUENCE OF 38-44; 70-79; 85-96; 135-172; 248-290; 386-392 AND
RP 428-439.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 138-462.
RX PubMed=3346208; DOI=10.1016/s0021-9258(18)68958-6;
RA Ann D.K., Wu M.M.J., Huang T., Carlson D.M., Wu R.;
RT "Retinol-regulated gene expression in human tracheobronchial epithelial
RT cells. Enhanced expression of elongation factor EF-1 alpha.";
RL J. Biol. Chem. 263:3546-3549(1988).
RN [11]
RP ETHANOLAMINYLATION AT GLU-301 AND GLU-374.
RX PubMed=2569467; DOI=10.1016/s0021-9258(18)71682-7;
RA Whiteheart S.W., Shenbagarmurthi P., Chen L., Cotter R.J., Hart G.W.;
RT "Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally
RT modified by novel amide-linked ethanolamine-phosphoglycerol moieties.
RT Addition of ethanolamine-phosphoglycerol to specific glutamic acid residues
RT on EF-1 alpha.";
RL J. Biol. Chem. 264:14334-14341(1989).
RN [12]
RP INTERACTION WITH ZPR1, AND SUBCELLULAR LOCATION.
RX PubMed=8650580; DOI=10.1126/science.272.5269.1797;
RA Galcheva-Gargova Z., Konstantinov K.N., Wu I.-H., Klier F.G., Barrett T.,
RA Davis R.J.;
RT "Binding of zinc finger protein ZPR1 to the epidermal growth factor
RT receptor.";
RL Science 272:1797-1802(1996).
RN [13]
RP INDUCTION BY HOMOCYSTEINE.
RX PubMed=9677419; DOI=10.1074/jbc.273.31.19840;
RA Chacko G., Ling Q., Hajjar K.A.;
RT "Induction of acute translational response genes by homocysteine.
RT Elongation factors-1alpha, -beta, and -delta.";
RL J. Biol. Chem. 273:19840-19846(1998).
RN [14]
RP IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN AND
RP TRNA, AND INTERACTION WITH XPO5.
RX PubMed=12426392; DOI=10.1093/emboj/cdf613;
RA Bohnsack M.T., Regener K., Schwappach B., Saffrich R., Paraskeva E.,
RA Hartmann E., Goerlich D.;
RT "Exp5 exports eEF1A via tRNA from nuclei and synergizes with other
RT transport pathways to confine translation to the cytoplasm.";
RL EMBO J. 21:6205-6215(2002).
RN [15]
RP IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN AND
RP TRNA, AND INTERACTION WITH XPO5.
RX PubMed=12426393; DOI=10.1093/emboj/cdf620;
RA Calado A., Treichel N., Mueller E.-C., Otto A., Kutay U.;
RT "Exportin-5-mediated nuclear export of eukaryotic elongation factor 1A and
RT tRNA.";
RL EMBO J. 21:6216-6224(2002).
RN [16]
RP ISGYLATION.
RX PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT human cells.";
RL Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN [17]
RP PHOSPHORYLATION AT THR-432, AND MUTAGENESIS OF THR-432.
RX PubMed=17595531; DOI=10.1159/000104169;
RA Eckhardt K., Troger J., Reissmann J., Katschinski D.M., Wagner K.F.,
RA Stengel P., Paasch U., Hunziker P., Borter E., Barth S., Schlafli P.,
RA Spielmann P., Stiehl D.P., Camenisch G., Wenger R.H.;
RT "Male germ cell expression of the PAS domain kinase PASKIN and its novel
RT target eukaryotic translation elongation factor eEF1A1.";
RL Cell. Physiol. Biochem. 20:227-240(2007).
RN [18]
RP INTERACTION WITH KARS1.
RX PubMed=18029264; DOI=10.1016/j.bbrc.2007.11.028;
RA Guzzo C.M., Yang D.C.H.;
RT "Lysyl-tRNA synthetase interacts with EF1alpha, aspartyl-tRNA synthetase
RT and p38 in vitro.";
RL Biochem. Biophys. Res. Commun. 365:718-723(2008).
RN [19]
RP INTERACTION WITH ERGIC2.
RX PubMed=17980171; DOI=10.1016/j.bbapap.2007.10.006;
RA Yang Y.F., Chou M.Y., Fan C.Y., Chen S.F., Lyu P.C., Liu C.C., Tseng T.L.;
RT "The possible interaction of CDA14 and protein elongation factor 1alpha.";
RL Biochim. Biophys. Acta 1784:312-318(2008).
RN [20]
RP INTERACTION WITH SPHK1 AND SPHK2.
RX PubMed=18263879; DOI=10.1074/jbc.m708782200;
RA Leclercq T.M., Moretti P.A., Vadas M.A., Pitson S.M.;
RT "Eukaryotic elongation factor 1A interacts with sphingosine kinase and
RT directly enhances its catalytic activity.";
RL J. Biol. Chem. 283:9606-9614(2008).
RN [21]
RP INTERACTION WITH DLC1, AND SUBCELLULAR LOCATION.
RX PubMed=19158340; DOI=10.1242/jcs.027482;
RA Zhong D., Zhang J., Yang S., Soh U.J., Buschdorf J.P., Zhou Y.T., Yang D.,
RA Low B.C.;
RT "The SAM domain of the RhoGAP DLC1 binds EF1A1 to regulate cell
RT migration.";
RL J. Cell Sci. 122:414-424(2009).
RN [22]
RP PHOSPHORYLATION AT SER-300.
RX PubMed=20832312; DOI=10.1016/j.cub.2010.08.017;
RA Lin K.W., Yakymovych I., Jia M., Yakymovych M., Souchelnytskyi S.;
RT "Phosphorylation of eEF1A1 at Ser300 by TbetaR-I results in inhibition of
RT mRNA translation.";
RL Curr. Biol. 20:1615-1625(2010).
RN [23]
RP METHYLATION AT LYS-318, AND MUTAGENESIS OF LYS-36; LYS-55; LYS-79; LYS-165
RP AND LYS-318.
RX PubMed=25144183; DOI=10.1371/journal.pone.0105394;
RA Shimazu T., Barjau J., Sohtome Y., Sodeoka M., Shinkai Y.;
RT "Selenium-based S-adenosylmethionine analog reveals the mammalian seven-
RT beta-strand methyltransferase METTL10 to be an EF1A1 lysine
RT methyltransferase.";
RL PLoS ONE 9:E105394-E105394(2014).
RN [24]
RP FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF ALA-399.
RX PubMed=26651998; DOI=10.7554/elife.10222;
RA Carelli J.D., Sethofer S.G., Smith G.A., Miller H.R., Simard J.L.,
RA Merrick W.C., Jain R.K., Ross N.T., Taunton J.;
RT "Ternatin and improved synthetic variants kill cancer cells by targeting
RT the elongation factor-1A ternary complex.";
RL Elife 4:0-0(2015).
RN [25]
RP SUBCELLULAR LOCATION, INTERACTION WITH PPP1R16B, AND PHOSPHORYLATION BY
RP ROCK2.
RX PubMed=26497934; DOI=10.1016/j.biocel.2015.10.021;
RA Boratko A., Peter M., Thalwieser Z., Kovacs E., Csortos C.;
RT "Elongation factor-1A1 is a novel substrate of the protein phosphatase 1-
RT TIMAP complex.";
RL Int. J. Biochem. Cell Biol. 69:105-113(2015).
RN [26]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=26593721; DOI=10.1016/j.molcel.2015.09.013;
RA Ferguson A., Wang L., Altman R.B., Terry D.S., Juette M.F., Burnett B.J.,
RA Alejo J.L., Dass R.A., Parks M.M., Vincent C.T., Blanchard S.C.;
RT "Functional dynamics within the human ribosome regulate the rate of active
RT protein synthesis.";
RL Mol. Cell 60:475-486(2015).
RN [27]
RP METHYLATION AT GLY-2 AND LYS-79.
RX PubMed=26545399; DOI=10.1074/mcp.m115.052449;
RA Hamey J.J., Winter D.L., Yagoub D., Overall C.M., Hart-Smith G.,
RA Wilkins M.R.;
RT "Novel N-terminal and lysine methyltransferases that target translation
RT elongation factor 1A in yeast and human.";
RL Mol. Cell. Proteomics 15:164-176(2016).
RN [28]
RP METHYLATION AT LYS-165, AND MUTAGENESIS OF LYS-165.
RX PubMed=28108655; DOI=10.1093/nar/gkx002;
RA Malecki J., Aileni V.K., Ho A.Y., Schwarz J., Moen A., Soerensen V.,
RA Nilges B.S., Jakobsson M.E., Leidel S.A., Falnes P.O.;
RT "The novel lysine specific methyltransferase METTL21B affects mRNA
RT translation through inducible and dynamic methylation of Lys-165 in human
RT eukaryotic elongation factor 1 alpha (eEF1A).";
RL Nucleic Acids Res. 45:4370-4389(2017).
RN [29]
RP METHYLATION AT LYS-36, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS
RP OF LYS-36.
RX PubMed=28520920; DOI=10.1093/nar/gkx432;
RA Jakobsson M.E., Malecki J., Nilges B.S., Moen A., Leidel S.A., Falnes P.O.;
RT "Methylation of human eukaryotic elongation factor alpha (eEF1A) by a
RT member of a novel protein lysine methyltransferase family modulates mRNA
RT translation.";
RL Nucleic Acids Res. 45:8239-8254(2017).
RN [30]
RP METHYLATION AT LYS-55 BY METTL13, AND MUTAGENESIS OF LYS-55.
RX PubMed=30612740; DOI=10.1016/j.cell.2018.11.038;
RA Liu S., Hausmann S., Carlson S.M., Fuentes M.E., Francis J.W., Pillai R.,
RA Lofgren S.M., Hulea L., Tandoc K., Lu J., Li A., Nguyen N.D., Caporicci M.,
RA Kim M.P., Maitra A., Wang H., Wistuba I.I., Porco J.A. Jr., Bassik M.C.,
RA Elias J.E., Song J., Topisirovic I., Van Rechem C., Mazur P.K., Gozani O.;
RT "METTL13 methylation of eEF1A increases translational output to promote
RT tumorigenesis.";
RL Cell 0:0-0(2018).
RN [31]
RP METHYLATION AT GLY-2 AND LYS-55 BY METTL13, AND MUTAGENESIS OF LYS-55.
RX PubMed=30143613; DOI=10.1038/s41467-018-05646-y;
RA Jakobsson M.E., Malecki J.M., Halabelian L., Nilges B.S., Pinto R.,
RA Kudithipudi S., Munk S., Davydova E., Zuhairi F.R., Arrowsmith C.H.,
RA Jeltsch A., Leidel S.A., Olsen J.V., Falnes P.O.;
RT "The dual methyltransferase METTL13 targets N terminus and Lys55 of eEF1A
RT and modulates codon-specific translation rates.";
RL Nat. Commun. 9:3411-3411(2018).
RN [32]
RP FUNCTION (MICROBIAL INFECTION), ACTIVITY REGULATION, AND MUTAGENESIS OF
RP ALA-399.
RX PubMed=33495306; DOI=10.1126/science.abf4058;
RA White K.M., Rosales R., Yildiz S., Kehrer T., Miorin L., Moreno E.,
RA Jangra S., Uccellini M.B., Rathnasinghe R., Coughlan L.,
RA Martinez-Romero C., Batra J., Rojc A., Bouhaddou M., Fabius J.M.,
RA Obernier K., Dejosez M., Guillen M.J., Losada A., Aviles P., Schotsaert M.,
RA Zwaka T., Vignuzzi M., Shokat K.M., Krogan N.J., Garcia-Sastre A.;
RT "Plitidepsin has potent preclinical efficacy against SARS-CoV-2 by
RT targeting the host protein eEF1A.";
RL Science 371:926-931(2021).
RN [33]
RP FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF ALA-399.
RX PubMed=36264623; DOI=10.7554/elife.81608;
RA Juette M.F., Carelli J.D., Rundlet E.J., Brown A., Shao S., Ferguson A.,
RA Wasserman M.R., Holm M., Taunton J., Blanchard S.C.;
RT "Didemnin B and ternatin-4 differentially inhibit conformational changes in
RT eEF1A required for aminoacyl-tRNA accommodation into mammalian ribosomes.";
RL Elife 11:0-0(2022).
RN [34]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=36123449; DOI=10.1038/s41557-022-01039-3;
RA Wang H.Y., Yang H., Holm M., Tom H., Oltion K., Al-Khdhairawi A.A.Q.,
RA Weber J.F., Blanchard S.C., Ruggero D., Taunton J.;
RT "Synthesis and single-molecule imaging reveal stereospecific enhancement of
RT binding kinetics by the antitumour eEF1A antagonist SR-A3.";
RL Nat. Chem. 14:1443-1450(2022).
RN [35]
RP FUNCTION, ACTIVITY REGULATION, UBIQUITINATION AT LYS-385, AND MUTAGENESIS
RP OF LYS-385.
RX PubMed=36638793; DOI=10.1016/j.cell.2022.12.025;
RA Oltion K., Carelli J.D., Yang T., See S.K., Wang H.Y., Kampmann M.,
RA Taunton J.;
RT "An E3 ligase network engages GCN1 to promote the degradation of
RT translation factors on stalled ribosomes.";
RL Cell 0:0-0(2023).
CC -!- FUNCTION: Translation elongation factor that catalyzes the GTP-
CC dependent binding of aminoacyl-tRNA (aa-tRNA) to the A-site of
CC ribosomes during the elongation phase of protein synthesis
CC (PubMed:26651998, PubMed:26593721, PubMed:36264623, PubMed:36123449,
CC PubMed:36638793). Base pairing between the mRNA codon and the aa-tRNA
CC anticodon promotes GTP hydrolysis, releasing the aa-tRNA from EEF1A1
CC and allowing its accommodation into the ribosome (PubMed:26651998,
CC PubMed:26593721, PubMed:36264623, PubMed:36123449, PubMed:36638793).
CC The growing protein chain is subsequently transferred from the P-site
CC peptidyl tRNA to the A-site aa-tRNA, extending it by one amino acid
CC through ribosome-catalyzed peptide bond formation (PubMed:26651998,
CC PubMed:26593721, PubMed:36264623, PubMed:36123449). Also plays a role
CC in the positive regulation of IFNG transcription in T-helper 1 cells as
CC part of an IFNG promoter-binding complex with TXK and PARP1
CC (PubMed:17177976). {ECO:0000269|PubMed:17177976,
CC ECO:0000269|PubMed:26593721, ECO:0000269|PubMed:26651998,
CC ECO:0000269|PubMed:36123449, ECO:0000269|PubMed:36264623,
CC ECO:0000269|PubMed:36638793}.
CC -!- FUNCTION: (Microbial infection) Required for the translation of viral
CC proteins and viral replication during human coronavirus SARS-CoV-2
CC infection. {ECO:0000269|PubMed:33495306}.
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:0000305|PubMed:26593721};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000305|PubMed:26593721};
CC -!- ACTIVITY REGULATION: Inhibited by plitidepsin, a chemical compound
CC extracted from the ascidian Aplidium albicans (PubMed:33495306).
CC Specifically inhibited by didemnin B, a natural product that triggers
CC ribosome stalling by preventing aminoacyl-tRNA (aa-tRNA) release from
CC EEF1A1 on the ribosome (PubMed:26651998, PubMed:36264623). Specifically
CC inhibited by ternatin-4, a small-molecule inhibitor that triggers
CC ribosome stalling by traping EEF1A1 on the ribosome and preventing
CC aminoacyl-tRNA (aa-tRNA) accommodation (PubMed:26651998,
CC PubMed:36264623, PubMed:36123449, PubMed:36638793). Ribosome stalling
CC by ternatin-4 causes ubiquitination and degradation of EEF1A1
CC (PubMed:36638793). Specifically inhibited by ternatin SR-A3, which
CC differs from ternatin-4 by the addition of a single oxygen atom into
CC the side chain of N-Me-Leu (PubMed:36123449). Inhibition by ternatin-4
CC can be reversed, while it is not the case for didemnin B
CC (PubMed:36264623). {ECO:0000269|PubMed:26651998,
CC ECO:0000269|PubMed:33495306, ECO:0000269|PubMed:36123449,
CC ECO:0000269|PubMed:36264623, ECO:0000269|PubMed:36638793}.
CC -!- SUBUNIT: Found in a nuclear export complex with XPO5, EEF1A1, Ran and
CC aminoacylated tRNA (PubMed:12426392, PubMed:12426393). Interacts with
CC PARP1 (PubMed:17177976). Interacts with KARS1 (PubMed:18029264). May
CC interact with ERGIC2 (PubMed:17980171). Interacts with IFIT1 (via TPR
CC repeats 4-7) (By similarity). Interacts with DLC1, facilitating
CC distribution to the membrane periphery and ruffles upon growth factor
CC stimulation (PubMed:19158340). Interacts with ZPR1; the interaction
CC occurs in a epidermal growth factor (EGF)-dependent manner
CC (PubMed:8650580). Interacts with PPP1R16B (PubMed:26497934). Interacts
CC with SPHK1 and SPHK2; both interactions increase SPHK1 and SPHK2 kinase
CC activity (PubMed:18263879). {ECO:0000250|UniProtKB:P10126,
CC ECO:0000269|PubMed:12426392, ECO:0000269|PubMed:12426393,
CC ECO:0000269|PubMed:17177976, ECO:0000269|PubMed:17980171,
CC ECO:0000269|PubMed:18029264, ECO:0000269|PubMed:18263879,
CC ECO:0000269|PubMed:19158340, ECO:0000269|PubMed:26497934,
CC ECO:0000269|PubMed:8650580}.
CC -!- INTERACTION:
CC P68104; Q8NFJ9: BBS1; NbExp=3; IntAct=EBI-352162, EBI-1805484;
CC P68104; Q96IK1-2: BOD1; NbExp=3; IntAct=EBI-352162, EBI-18924329;
CC P68104; Q16539: MAPK14; NbExp=3; IntAct=EBI-352162, EBI-73946;
CC P68104; Q00987: MDM2; NbExp=9; IntAct=EBI-352162, EBI-389668;
CC P68104; Q9NZ94-2: NLGN3; NbExp=4; IntAct=EBI-352162, EBI-16423037;
CC P68104; P12004: PCNA; NbExp=2; IntAct=EBI-352162, EBI-358311;
CC P68104; P54725: RAD23A; NbExp=2; IntAct=EBI-352162, EBI-746453;
CC P68104; Q9NYA1: SPHK1; NbExp=2; IntAct=EBI-352162, EBI-985303;
CC P68104; Q14166: TTLL12; NbExp=4; IntAct=EBI-352162, EBI-923010;
CC P68104; P63104: YWHAZ; NbExp=2; IntAct=EBI-352162, EBI-347088;
CC P68104; Q05516: ZBTB16; NbExp=4; IntAct=EBI-352162, EBI-711925;
CC P68104; Q8IUH5: ZDHHC17; NbExp=2; IntAct=EBI-352162, EBI-524753;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19158340,
CC ECO:0000269|PubMed:8650580}. Nucleus {ECO:0000269|PubMed:17177976,
CC ECO:0000269|PubMed:8650580}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:8650580}. Cell membrane
CC {ECO:0000269|PubMed:26497934}. Note=Colocalizes with DLC1 at actin-rich
CC regions in the cell periphery (PubMed:19158340). Translocates together
CC with ZPR1 from the cytoplasm to the nucleus and nucleolus after
CC treatment with mitogens (PubMed:8650580). Localization at the cell
CC membrane depends on EEF1A1 phosphorylation status and the presence of
CC PPP1R16B (PubMed:26497934). {ECO:0000269|PubMed:19158340,
CC ECO:0000269|PubMed:26497934, ECO:0000269|PubMed:8650580}.
CC -!- INDUCTION: By homocysteine (HC), may mediate accelerated synthesis of
CC free thiol-containing proteins in response to HC-induced oxidative
CC stress. {ECO:0000269|PubMed:9677419}.
CC -!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
CC -!- PTM: Phosphorylated by TXK (PubMed:17177976). Phosphorylation by PASK
CC increases translation efficiency (PubMed:17595531). Phosphorylated by
CC ROCK2 (PubMed:26497934). Phosphorylation by TGFBR1 inhibits translation
CC elongation (PubMed:20832312). {ECO:0000269|PubMed:17177976,
CC ECO:0000269|PubMed:17595531, ECO:0000269|PubMed:20832312,
CC ECO:0000269|PubMed:26497934}.
CC -!- PTM: Trimethylated at Lys-79 by EEF1AKMT1 (PubMed:26545399). Methylated
CC at Lys-165 by EEF1AKMT3, methylation by EEF1AKMT3 is dynamic as well as
CC inducible by stress conditions, such as ER-stress, and plays a
CC regulatory role on mRNA translation (PubMed:28108655). Trimethylated at
CC Lys-318 by EEF1AKMT2 (PubMed:25144183). Mono-, di-, and trimethylated
CC at Lys-36 by EEF1AKMT4; trimethylated form is predominant. Methylation
CC by EEF1AKMT4 contributes to the fine-tuning of translation rates for a
CC subset of tRNAs (PubMed:28520920). Trimethylated at Gly-2 by METTL13
CC (PubMed:30143613). Mono- and dimethylated at Lys-55 by METTL13;
CC dimethylated form is predominant (PubMed:30143613, PubMed:30612740).
CC {ECO:0000269|PubMed:25144183, ECO:0000269|PubMed:26545399,
CC ECO:0000269|PubMed:28108655, ECO:0000269|PubMed:28520920,
CC ECO:0000269|PubMed:30143613, ECO:0000269|PubMed:30612740}.
CC -!- PTM: Ubiquitinated at Lys-385 by RNF14 in response to ribosome
CC collisions (ribosome stalling), leading to its degradation by the
CC proteasome and rescue of stalled ribosomes.
CC {ECO:0000269|PubMed:36638793}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA52367.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH71619.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="https://atlasgeneticsoncology.org/gene/40407/EEF1A1";
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DR EMBL; X03558; CAA27245.1; -; mRNA.
DR EMBL; J04617; AAA52343.1; -; Genomic_DNA.
DR EMBL; X16869; CAA34756.1; -; mRNA.
DR EMBL; AY043301; AAK95378.1; -; mRNA.
DR EMBL; BC008587; AAH08587.1; -; mRNA.
DR EMBL; BC009733; AAH09733.1; -; mRNA.
DR EMBL; BC009875; AAH09875.1; -; mRNA.
DR EMBL; BC010735; AAH10735.1; -; mRNA.
DR EMBL; BC012891; AAH12891.1; -; mRNA.
DR EMBL; BC014224; AAH14224.1; -; mRNA.
DR EMBL; BC018150; AAH18150.1; -; mRNA.
DR EMBL; BC018641; AAH18641.1; -; mRNA.
DR EMBL; BC021686; AAH21686.1; -; mRNA.
DR EMBL; BC028674; AAH28674.1; -; mRNA.
DR EMBL; BC038339; AAH38339.1; -; mRNA.
DR EMBL; BC057391; AAH57391.1; -; mRNA.
DR EMBL; BC066893; AAH66893.1; -; mRNA.
DR EMBL; BC071619; AAH71619.1; ALT_SEQ; mRNA.
DR EMBL; BC072385; AAH72385.1; -; mRNA.
DR EMBL; BC082268; AAH82268.1; -; mRNA.
DR EMBL; X03689; CAA27325.1; -; mRNA.
DR EMBL; M29548; AAA52367.1; ALT_INIT; mRNA.
DR CCDS; CCDS4980.1; -.
DR PIR; B24977; EFHU1.
DR RefSeq; NP_001393.1; NM_001402.5.
DR RefSeq; XP_011533816.1; XM_011535514.2.
DR PDB; 3C5J; X-ray; 1.80 A; C=343-355.
DR PDB; 6ZMO; EM; 3.10 A; CD=1-462.
DR PDB; 8G60; EM; 2.54 A; EF=1-462.
DR PDB; 8G6J; EM; 2.80 A; EF=1-462.
DR PDBsum; 3C5J; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 8G60; -.
DR PDBsum; 8G6J; -.
DR AlphaFoldDB; P68104; -.
DR EMDB; EMD-11299; -.
DR EMDB; EMD-29759; -.
DR EMDB; EMD-29771; -.
DR SMR; P68104; -.
DR BioGRID; 108237; 681.
DR CORUM; P68104; -.
DR DIP; DIP-31277N; -.
DR IntAct; P68104; 259.
DR MINT; P68104; -.
DR STRING; 9606.ENSP00000339063; -.
DR BindingDB; P68104; -.
DR ChEMBL; CHEMBL1795120; -.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR MoonProt; P68104; -.
DR GlyGen; P68104; 6 sites, 1 O-linked glycan (5 sites).
DR iPTMnet; P68104; -.
DR MetOSite; P68104; -.
DR PhosphoSitePlus; P68104; -.
DR SwissPalm; P68104; -.
DR BioMuta; EEF1A1; -.
DR DMDM; 55584035; -.
DR OGP; P68104; -.
DR SWISS-2DPAGE; P68104; -.
DR UCD-2DPAGE; P68104; -.
DR EPD; P68104; -.
DR jPOST; P68104; -.
DR MassIVE; P68104; -.
DR PaxDb; 9606-ENSP00000339063; -.
DR PeptideAtlas; P68104; -.
DR PRIDE; P68104; -.
DR ProteomicsDB; 66470; -.
DR Pumba; P68104; -.
DR TopDownProteomics; P68104; -.
DR ABCD; P68104; 1 sequenced antibody.
DR Antibodypedia; 31353; 395 antibodies from 35 providers.
DR DNASU; 1915; -.
DR Ensembl; ENST00000309268.11; ENSP00000339053.4; ENSG00000156508.19.
DR Ensembl; ENST00000316292.13; ENSP00000339063.7; ENSG00000156508.19.
DR Ensembl; ENST00000331523.7; ENSP00000330054.2; ENSG00000156508.19.
DR Ensembl; ENST00000356303.7; ENSP00000348651.3; ENSG00000156508.19.
DR Ensembl; ENST00000455918.2; ENSP00000392366.2; ENSG00000156508.19.
DR Ensembl; ENST00000615060.5; ENSP00000479055.2; ENSG00000156508.19.
DR Ensembl; ENST00000676710.1; ENSP00000504335.1; ENSG00000156508.19.
DR Ensembl; ENST00000677236.1; ENSP00000503192.1; ENSG00000156508.19.
DR Ensembl; ENST00000678508.1; ENSP00000503249.1; ENSG00000156508.19.
DR Ensembl; ENST00000678702.1; ENSP00000503823.1; ENSG00000156508.19.
DR GeneID; 1915; -.
DR KEGG; hsa:1915; -.
DR MANE-Select; ENST00000309268.11; ENSP00000339053.4; NM_001402.6; NP_001393.1.
DR AGR; HGNC:3189; -.
DR CTD; 1915; -.
DR DisGeNET; 1915; -.
DR GeneCards; EEF1A1; -.
DR HGNC; HGNC:3189; EEF1A1.
DR HPA; ENSG00000156508; Low tissue specificity.
DR MIM; 130590; gene.
DR neXtProt; NX_P68104; -.
DR OpenTargets; ENSG00000156508; -.
DR PharmGKB; PA27625; -.
DR VEuPathDB; HostDB:ENSG00000156508; -.
DR eggNOG; KOG0052; Eukaryota.
DR GeneTree; ENSGT00950000183029; -.
DR InParanoid; P68104; -.
DR OMA; EMHHKSV; -.
DR OrthoDB; 5477300at2759; -.
DR PhylomeDB; P68104; -.
DR TreeFam; TF300304; -.
DR PathwayCommons; P68104; -.
DR Reactome; R-HSA-156842; Eukaryotic Translation Elongation.
DR Reactome; R-HSA-156902; Peptide chain elongation.
DR Reactome; R-HSA-3371511; HSF1 activation.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8876725; Protein methylation.
DR Reactome; R-HSA-9613829; Chaperone Mediated Autophagy.
DR Reactome; R-HSA-9735869; SARS-CoV-1 modulates host translation machinery.
DR SignaLink; P68104; -.
DR SIGNOR; P68104; -.
DR BioGRID-ORCS; 1915; 746 hits in 1099 CRISPR screens.
DR ChiTaRS; EEF1A1; human.
DR GeneWiki; Eukaryotic_translation_elongation_factor_1_alpha_1; -.
DR GenomeRNAi; 1915; -.
DR Pharos; P68104; Tchem.
DR PRO; PR:P68104; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P68104; Protein.
DR Bgee; ENSG00000156508; Expressed in ganglionic eminence and 193 other cell types or tissues.
DR ExpressionAtlas; P68104; baseline and differential.
DR Genevisible; P68104; HS.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0098574; C:cytoplasmic side of lysosomal membrane; NAS:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:UniProt.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; TAS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005840; C:ribosome; IDA:UniProt.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0005525; F:GTP binding; TAS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0060090; F:molecular adaptor activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003746; F:translation elongation factor activity; IDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IDA:UniProtKB.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0044829; P:positive regulation by host of viral genome replication; IDA:UniProtKB.
DR GO; GO:1904714; P:regulation of chaperone-mediated autophagy; NAS:ParkinsonsUK-UCL.
DR GO; GO:1900022; P:regulation of D-erythro-sphingosine kinase activity; IDA:UniProtKB.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IDA:UniProtKB.
DR CDD; cd01883; EF1_alpha; 1.
DR CDD; cd03693; EF1_alpha_II; 1.
DR CDD; cd03705; EF1_alpha_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR HAMAP; MF_00118_A; EF_Tu_A; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR NCBIfam; TIGR00483; EF-1_alpha; 1.
DR PANTHER; PTHR23115:SF222; ELONGATION FACTOR 1-ALPHA 1-RELATED; 1.
DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Elongation factor; GTP-binding;
KW Host-virus interaction; Hydrolase; Isopeptide bond; Membrane; Methylation;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:26545399"
FT CHAIN 2..462
FT /note="Elongation factor 1-alpha 1"
FT /id="PRO_0000090885"
FT DOMAIN 5..242
FT /note="tr-type G"
FT REGION 14..21
FT /note="G1"
FT /evidence="ECO:0000255"
FT REGION 70..74
FT /note="G2"
FT /evidence="ECO:0000255"
FT REGION 91..94
FT /note="G3"
FT /evidence="ECO:0000255"
FT REGION 153..156
FT /note="G4"
FT /evidence="ECO:0000255"
FT REGION 194..196
FT /note="G5"
FT /evidence="ECO:0000255"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P68105"
FT BINDING 153..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P68105"
FT BINDING 194..196
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P68105"
FT MOD_RES 2
FT /note="N,N,N-trimethylglycine"
FT /evidence="ECO:0000269|PubMed:26545399,
FT ECO:0000269|PubMed:30143613"
FT MOD_RES 36
FT /note="N6,N6,N6-trimethyllysine; alternate; by EEF1AKMT4"
FT /evidence="ECO:0000269|PubMed:28520920"
FT MOD_RES 36
FT /note="N6,N6-dimethyllysine; alternate; by EEF1AKMT4"
FT /evidence="ECO:0000269|PubMed:28520920"
FT MOD_RES 36
FT /note="N6-methyllysine; alternate; by EEF1AKMT4"
FT /evidence="ECO:0000269|PubMed:28520920"
FT MOD_RES 55
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000269|PubMed:30143613,
FT ECO:0000269|PubMed:30612740, ECO:0000269|Ref.7"
FT MOD_RES 79
FT /note="N6,N6,N6-trimethyllysine; by EEF1AKMT1"
FT /evidence="ECO:0000269|PubMed:26545399"
FT MOD_RES 165
FT /note="N6,N6,N6-trimethyllysine; alternate; by EEF1AKMT3"
FT /evidence="ECO:0000269|PubMed:28108655"
FT MOD_RES 165
FT /note="N6,N6-dimethyllysine; alternate; by EEF1AKMT3"
FT /evidence="ECO:0000269|PubMed:28108655, ECO:0000269|Ref.7"
FT MOD_RES 165
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10126"
FT MOD_RES 165
FT /note="N6-methyllysine; alternate; by EEF1AKMT3"
FT /evidence="ECO:0000269|PubMed:28108655"
FT MOD_RES 172
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10126"
FT MOD_RES 273
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10126"
FT MOD_RES 300
FT /note="Phosphoserine; by TGFBR1"
FT /evidence="ECO:0000269|PubMed:20832312"
FT MOD_RES 301
FT /note="5-glutamyl glycerylphosphorylethanolamine"
FT /evidence="ECO:0000269|PubMed:2569467"
FT MOD_RES 318
FT /note="N6,N6,N6-trimethyllysine; by EEF1AKMT2"
FT /evidence="ECO:0000269|PubMed:25144183"
FT MOD_RES 374
FT /note="5-glutamyl glycerylphosphorylethanolamine"
FT /evidence="ECO:0000269|PubMed:2569467"
FT MOD_RES 392
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10126"
FT MOD_RES 392
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10126"
FT MOD_RES 432
FT /note="Phosphothreonine; by PASK"
FT /evidence="ECO:0000269|PubMed:17595531"
FT MOD_RES 439
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10126"
FT CROSSLNK 385
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:36638793"
FT MUTAGEN 36
FT /note="K->R: No effect on methylation by EEF1AKMT2.
FT Abolishes EEF1AKMT4-mediated methylation."
FT /evidence="ECO:0000269|PubMed:25144183,
FT ECO:0000269|PubMed:28520920"
FT MUTAGEN 55
FT /note="K->R: No effect on methylation by EEF1AKMT2.
FT Abolishes methylation by METTL13."
FT /evidence="ECO:0000269|PubMed:25144183,
FT ECO:0000269|PubMed:30143613, ECO:0000269|PubMed:30612740"
FT MUTAGEN 79
FT /note="K->R: No effect on methylation by EEF1AKMT2."
FT /evidence="ECO:0000269|PubMed:25144183"
FT MUTAGEN 165
FT /note="K->A: Abolishes methylation by EEF1AKMT3."
FT /evidence="ECO:0000269|PubMed:28108655"
FT MUTAGEN 165
FT /note="K->R: No effect on methylation by EEF1AKMT2."
FT /evidence="ECO:0000269|PubMed:25144183"
FT MUTAGEN 318
FT /note="K->R: Abolishes methylation by EEF1AKMT2."
FT /evidence="ECO:0000269|PubMed:25144183"
FT MUTAGEN 385
FT /note="K->R: Impaired ubiquitination in response to
FT ribosome stalling caused by ternatin-4."
FT /evidence="ECO:0000269|PubMed:36638793"
FT MUTAGEN 399
FT /note="A->V: Resistant to inhibition by plitidepsin and
FT ternatin-4. No effect on SARS-CoV-2 proteins translation."
FT /evidence="ECO:0000269|PubMed:26651998,
FT ECO:0000269|PubMed:33495306, ECO:0000269|PubMed:36264623"
FT MUTAGEN 432
FT /note="T->A: Abolishes phosphorylation by PASK."
FT /evidence="ECO:0000269|PubMed:17595531"
FT CONFLICT 83
FT /note="S -> A (in Ref. 6; CAA27325)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="L -> V (in Ref. 3; CAA34756)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 50141 MW; D465615545AF686A CRC64;
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL
DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV
GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP PYSQKRYEEI VKEVSTYIKK
IGYNPDTVAF VPISGWNGDN MLEPSANMPW FKGWKVTRKD GNASGTTLLE ALDCILPPTR
PTDKPLRLPL QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APVNVTTEVK SVEMHHEALS
EALPGDNVGF NVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP GQISAGYAPV
LDCHTAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA IVDMVPGKPM CVESFSDYPP
LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK VTKSAQKAQK AK
//