ID IF2P_HUMAN Reviewed; 1220 AA.
AC O60841; O95805; Q53RV7; Q53SI8; Q9UF81; Q9UMN7;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 4.
DT 27-MAR-2024, entry version 215.
DE RecName: Full=Eukaryotic translation initiation factor 5B;
DE Short=eIF-5B;
DE EC=3.6.5.3;
DE AltName: Full=Translation initiation factor IF-2;
GN Name=EIF5B; Synonyms=IF2, KIAA0741;
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], AND VARIANT THR-522.
RC TISSUE=Cervix carcinoma;
RX PubMed=10432305; DOI=10.1042/bj3420097;
RA Wilson S.A., Sieiro-Vazquez C., Edwards N.J., Iourin O., Byles E.D.,
RA Kotsopoulou E., Adamson C.S., Kingsman S.M., Kingsman A.J.,
RA Martin-Rendon E.;
RT "Cloning and characterization of hIF2, a human homologue of bacterial
RT translation initiation factor 2 and its interaction with HIV-1 matrix.";
RL Biochem. J. 342:97-103(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF VAL-640; HIS-706 AND ASP-759,
RP CHARACTERIZATION, AND VARIANT THR-522.
RC TISSUE=Testis;
RX PubMed=10200264; DOI=10.1073/pnas.96.8.4342;
RA Lee J.H., Choi S.K., Roll-Mecak A., Burley S.K., Dever T.E.;
RT "Universal conservation in translation initiation revealed by human and
RT archaeal homologs of bacterial translation initiation factor IF2.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:4342-4347(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP PROTEIN SEQUENCE OF 9-33; 77-94; 106-122; 180-197; 206-224; 285-298;
RP 425-436; 629-644; 653-683; 695-713; 749-757; 766-777; 882-902; 1000-1015;
RP 1044-1055; 1096-1120 AND 1175-1185, PHOSPHORYLATION AT SER-190, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-1220.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 833-1220.
RX PubMed=11124703;
RX DOI=10.1002/1097-0061(200101)18:1<69::aid-yea647>3.0.co;2-h;
RA Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B., Cannata N.,
RA Zimbello R., Lanfranchi G., Valle G.;
RT "Characterization of 16 novel human genes showing high similarity to yeast
RT sequences.";
RL Yeast 18:69-80(2001).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10659855; DOI=10.1038/35002118;
RA Pestova T.V., Lomakin I.B., Lee J.H., Choi S.K., Dever T.E., Hellen C.U.;
RT "The joining of ribosomal subunits in eukaryotes requires eIF5B.";
RL Nature 403:332-335(2000).
RN [9]
RP INTERACTION WITH EIF1AX.
RX PubMed=12569173; DOI=10.1073/pnas.0437845100;
RA Marintchev A., Kolupaeva V.G., Pestova T.V., Wagner G.;
RT "Mapping the binding interface between human eukaryotic initiation factors
RT 1A and 5B: a new interaction between old partners.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1535-1540(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-113; SER-164 AND
RP SER-214, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate cancer
RT cells: identification of phosphoproteins in the LNCaP cell line.";
RL Electrophoresis 28:2027-2034(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-113; TYR-134;
RP SER-135; SER-137; SER-164; SER-182; SER-183; SER-186; SER-190; THR-301;
RP SER-547; SER-560; SER-588 AND SER-595, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-113 AND SER-164, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [17]
RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION).
RX PubMed=18572216; DOI=10.1016/j.virol.2008.05.019;
RA de Breyne S., Bonderoff J.M., Chumakov K.M., Lloyd R.E., Hellen C.U.;
RT "Cleavage of eukaryotic initiation factor eIF5B by enterovirus 3C
RT proteases.";
RL Virology 378:118-122(2008).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; TYR-134; SER-135;
RP SER-137; SER-164; SER-182; SER-183; SER-186 AND SER-214, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-135; SER-137;
RP SER-164; SER-182; SER-186; SER-190; SER-214; THR-301; SER-588; SER-589;
RP SER-591 AND SER-595, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-113; TYR-134;
RP SER-135; SER-137; SER-164; SER-171; SER-214 AND THR-498, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-107; SER-113;
RP SER-135; SER-137; SER-164; SER-186; SER-214; SER-222; SER-438 AND SER-1168,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-113; SER-135;
RP SER-137; SER-164; SER-182; SER-190 AND SER-214, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [24]
RP INTERACTION WITH EIF5 AND EIF1AX.
RX PubMed=30211544; DOI=10.1021/acs.biochem.8b00839;
RA Lin K.Y., Nag N., Pestova T.V., Marintchev A.;
RT "Human eIF5 and eIF1A compete for binding to eIF5B.";
RL Biochemistry 57:5910-5920(2018).
RN [25] {ECO:0000312|PDB:7TQL}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) OF 602-1219 IN COMPLEX
RP WITH A GTP ANALOG, FUNCTION, CATALYTIC ACTIVITY, PROBABLE ACTIVE SITE,
RP MUTAGENESIS OF HIS-706; ARG-1105; ARG-1174; 1188-ARG-GLN-1189; ARG-1199 AND
RP 1218-GLU-ILE-1219, AND INTERACTION WITH EIF1AX.
RX PubMed=35732735; DOI=10.1038/s41586-022-04858-z;
RA Lapointe C.P., Grosely R., Sokabe M., Alvarado C., Wang J., Montabana E.,
RA Villa N., Shin B.S., Dever T.E., Fraser C.S., Fernandez I.S., Puglisi J.D.;
RT "eIF5B and eIF1A reorient initiator tRNA to allow ribosomal subunit
RT joining.";
RL Nature 607:185-190(2022).
RN [26]
RP VARIANT [LARGE SCALE ANALYSIS] THR-522, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Plays a role in translation initiation (PubMed:10659855,
CC PubMed:35732735). Ribosome-dependent GTPase that promotes the joining
CC of the 60S ribosomal subunit to the pre-initiation complex to form the
CC 80S initiation complex with the initiator methionine-tRNA in the P-site
CC base paired to the start codon (PubMed:10659855, PubMed:35732735).
CC Together with eIF1A (EIF1AX), actively orients the initiator
CC methionine-tRNA in a conformation that allows 60S ribosomal subunit
CC joining to form the 80S initiation complex (PubMed:12569173,
CC PubMed:35732735). Is released after formation of the 80S initiation
CC complex (PubMed:35732735). Its GTPase activity is not essential for
CC ribosomal subunits joining, but GTP hydrolysis is needed for eIF1A
CC (EIF1AX) ejection quickly followed by EIF5B release to form elongation-
CC competent ribosomes (PubMed:10659855, PubMed:35732735). In contrast to
CC its procaryotic homolog, does not promote recruitment of Met-rRNA to
CC the small ribosomal subunit (PubMed:10659855).
CC {ECO:0000269|PubMed:10659855, ECO:0000269|PubMed:12569173,
CC ECO:0000269|PubMed:35732735}.
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; EC=3.6.5.3;
CC Evidence={ECO:0000269|PubMed:10659855, ECO:0000305|PubMed:35732735};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000269|PubMed:10659855, ECO:0000305|PubMed:35732735};
CC -!- COFACTOR:
CC Name=a monovalent cation; Xref=ChEBI:CHEBI:60242;
CC Evidence={ECO:0000250|UniProtKB:G0S8G9};
CC Note=Binds 1 monovalent cation per monomer in the active site.
CC Structural cofactor that stabilizes the GTP-bound 'on' state. May also
CC act as a transition state stabilizer of the hydrolysis reaction.
CC {ECO:0000250|UniProtKB:G0S8G9};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=1 pmol/min/ug enzyme {ECO:0000269|PubMed:10659855};
CC Note=Obtained in the presence of 40S and 60S ribosomal subunits. 60S
CC ribosomal subunit is necessary for enzyme activation, while 40S
CC ribosomal subunit is not.;
CC -!- SUBUNIT: Interacts through its C-terminal domain (CTD) with the CTD of
CC eIF1A (EIF1AX) or with the CTD of EIF5 (mutually exclusive) through a
CC common binding site (PubMed:30211544). Interacts with eIF1A (EIF1AX)
CC from the location of the start codon by the 43S complex until the
CC formation of the 80S complex (PubMed:12569173, PubMed:35732735).
CC Interacts with ANXA5 in a calcium and phospholipid-dependent manner (By
CC similarity). {ECO:0000250|UniProtKB:B2GUV7,
CC ECO:0000269|PubMed:35732735}.
CC -!- INTERACTION:
CC O60841; O14602: EIF1AY; NbExp=2; IntAct=EBI-928530, EBI-286439;
CC O60841; P14921: ETS1; NbExp=2; IntAct=EBI-928530, EBI-913209;
CC O60841; P28799: GRN; NbExp=3; IntAct=EBI-928530, EBI-747754;
CC O60841; O43933: PEX1; NbExp=3; IntAct=EBI-928530, EBI-988601;
CC O60841; O76024: WFS1; NbExp=3; IntAct=EBI-928530, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q05D44}.
CC -!- PTM: (Microbial infection) Cleaved and inactivated by the protease 3C
CC of poliovirus, Coxsackievirus B3 and Human rhinovirus 14, allowing the
CC virus to shutoff the host cell translation.
CC {ECO:0000269|PubMed:18572216}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34461.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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; AJ006776; CAB44357.1; -; mRNA.
DR EMBL; AF078035; AAD16006.1; -; mRNA.
DR EMBL; AC018690; AAY24313.1; -; Genomic_DNA.
DR EMBL; AC079447; AAX93258.1; -; Genomic_DNA.
DR EMBL; AB018284; BAA34461.2; ALT_INIT; mRNA.
DR EMBL; AL133563; CAB63717.1; -; mRNA.
DR EMBL; AJ006412; CAA07018.1; -; mRNA.
DR CCDS; CCDS42721.1; -.
DR PIR; T43483; T43483.
DR RefSeq; NP_056988.3; NM_015904.3.
DR PDB; 7TQL; EM; 3.40 A; 1=602-1219.
DR PDBsum; 7TQL; -.
DR AlphaFoldDB; O60841; -.
DR EMDB; EMD-26067; -.
DR SMR; O60841; -.
DR BioGRID; 115024; 177.
DR IntAct; O60841; 52.
DR MINT; O60841; -.
DR STRING; 9606.ENSP00000289371; -.
DR ChEMBL; CHEMBL4105852; -.
DR GlyGen; O60841; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; O60841; -.
DR MetOSite; O60841; -.
DR PhosphoSitePlus; O60841; -.
DR SwissPalm; O60841; -.
DR BioMuta; EIF5B; -.
DR EPD; O60841; -.
DR jPOST; O60841; -.
DR MassIVE; O60841; -.
DR MaxQB; O60841; -.
DR PaxDb; 9606-ENSP00000289371; -.
DR PeptideAtlas; O60841; -.
DR ProteomicsDB; 49628; -.
DR Pumba; O60841; -.
DR Antibodypedia; 32818; 202 antibodies from 27 providers.
DR DNASU; 9669; -.
DR Ensembl; ENST00000289371.11; ENSP00000289371.5; ENSG00000158417.11.
DR GeneID; 9669; -.
DR KEGG; hsa:9669; -.
DR MANE-Select; ENST00000289371.11; ENSP00000289371.5; NM_015904.4; NP_056988.3.
DR UCSC; uc002tab.4; human.
DR AGR; HGNC:30793; -.
DR CTD; 9669; -.
DR DisGeNET; 9669; -.
DR GeneCards; EIF5B; -.
DR HGNC; HGNC:30793; EIF5B.
DR HPA; ENSG00000158417; Low tissue specificity.
DR MIM; 606086; gene.
DR neXtProt; NX_O60841; -.
DR OpenTargets; ENSG00000158417; -.
DR PharmGKB; PA134864457; -.
DR VEuPathDB; HostDB:ENSG00000158417; -.
DR eggNOG; KOG1144; Eukaryota.
DR GeneTree; ENSGT00940000162583; -.
DR HOGENOM; CLU_002656_0_1_1; -.
DR InParanoid; O60841; -.
DR OMA; EFAVMLC; -.
DR OrthoDB; 169393at2759; -.
DR PhylomeDB; O60841; -.
DR TreeFam; TF101535; -.
DR BRENDA; 3.6.5.3; 2681.
DR PathwayCommons; O60841; -.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR SignaLink; O60841; -.
DR SIGNOR; O60841; -.
DR BioGRID-ORCS; 9669; 442 hits in 1150 CRISPR screens.
DR ChiTaRS; EIF5B; human.
DR GeneWiki; EIF5B; -.
DR GenomeRNAi; 9669; -.
DR Pharos; O60841; Tchem.
DR PRO; PR:O60841; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O60841; Protein.
DR Bgee; ENSG00000158417; Expressed in tendon of biceps brachii and 209 other cell types or tissues.
DR ExpressionAtlas; O60841; baseline and differential.
DR Genevisible; O60841; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IDA:UniProtKB.
DR GO; GO:0006446; P:regulation of translational initiation; IDA:UniProtKB.
DR GO; GO:0042255; P:ribosome assembly; IDA:UniProtKB.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR CDD; cd03703; aeIF5B_II; 1.
DR CDD; cd16266; IF2_aeIF5B_IV; 1.
DR CDD; cd01887; IF2_eIF5B; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR InterPro; IPR029459; EFTU-type.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR015760; TIF_IF2.
DR InterPro; IPR023115; TIF_IF2_dom3.
DR InterPro; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF4; EUKARYOTIC TRANSLATION INITIATION FACTOR 5B; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF14578; GTP_EFTU_D4; 1.
DR Pfam; PF11987; IF-2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; GTP-binding; Hydrolase;
KW Initiation factor; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..1220
FT /note="Eukaryotic translation initiation factor 5B"
FT /id="PRO_0000137294"
FT DOMAIN 629..846
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 1..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..645
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 663..667
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 702..705
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 756..759
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 824..826
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..512
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..569
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 706
FT /evidence="ECO:0000305|PubMed:35732735"
FT BINDING 640..646
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|PubMed:35732735,
FT ECO:0007744|PDB:7TQL"
FT BINDING 663..665
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|PubMed:35732735,
FT ECO:0007744|PDB:7TQL"
FT BINDING 756..757
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|PubMed:35732735,
FT ECO:0007744|PDB:7TQL"
FT BINDING 759..760
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|PubMed:35732735,
FT ECO:0007744|PDB:7TQL"
FT BINDING 825..826
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|PubMed:35732735,
FT ECO:0007744|PDB:7TQL"
FT SITE 478..479
FT /note="(Microbial infection) Cleavage; by viral protease 3C
FT of poliovirus, Coxsackievirus B3 and Human rhinovirus 14"
FT /evidence="ECO:0000269|PubMed:18572216"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 134
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17487921, ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 301
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 498
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2GUV7"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 589
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 1168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 337
FT /note="S -> G (in dbSNP:rs10642)"
FT /id="VAR_055954"
FT VARIANT 360
FT /note="R -> G (in dbSNP:rs3205296)"
FT /id="VAR_055955"
FT VARIANT 522
FT /note="K -> T (in dbSNP:rs7558074)"
FT /evidence="ECO:0000269|PubMed:10200264,
FT ECO:0000269|PubMed:10432305, ECO:0007744|PubMed:21269460"
FT /id="VAR_060587"
FT MUTAGEN 640
FT /note="V->G: Loss of activity in vivo. Retains full
FT activity in vitro."
FT /evidence="ECO:0000269|PubMed:10200264"
FT MUTAGEN 706
FT /note="H->E: Loss of activity; both in vivo and in vitro.
FT Loss of EIF5B release from the 80S initiation complex,
FT certainly due to loss of ability to hydrolyze GTP."
FT /evidence="ECO:0000269|PubMed:10200264,
FT ECO:0000269|PubMed:35732735"
FT MUTAGEN 706
FT /note="H->Q: Loss of activity in vivo. Partial activity in
FT vitro."
FT /evidence="ECO:0000269|PubMed:10200264"
FT MUTAGEN 759
FT /note="D->N: Loss of activity; both in vivo and in vitro."
FT /evidence="ECO:0000269|PubMed:10200264"
FT MUTAGEN 1105
FT /note="R->A: Disruption of contacts with the Met-tRNA
FT acceptor stem; when associated with A-1174."
FT /evidence="ECO:0000269|PubMed:35732735"
FT MUTAGEN 1174
FT /note="R->A: Disruption of contacts with the Met-tRNA
FT acceptor stem; when associated with A-1105."
FT /evidence="ECO:0000269|PubMed:35732735"
FT MUTAGEN 1188..1189
FT /note="RQ->ER: Disruption of contacts with eIF1A (EIF1AX);
FT when associated with E-1199 and 1218-R-R-1219."
FT /evidence="ECO:0000269|PubMed:35732735"
FT MUTAGEN 1199
FT /note="R->E: Disruption of contacts with eIF1A (EIF1AX);
FT when associated with 1188-E-E-1189 and 1218-R-R-1219."
FT /evidence="ECO:0000269|PubMed:35732735"
FT MUTAGEN 1218..1219
FT /note="EI->RR: Disruption of contacts with eIF1A (EIF1AX);
FT when associated with 1188-E-R-1189 and E-1199."
FT /evidence="ECO:0000269|PubMed:35732735"
FT CONFLICT 64
FT /note="E -> G (in Ref. 3; BAA34461)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="T -> I (in Ref. 1; CAB44357)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="I -> M (in Ref. 2; AAD16006)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="K -> R (in Ref. 2; AAD16006)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="E -> V (in Ref. 2; AAD16006)"
FT /evidence="ECO:0000305"
FT CONFLICT 669
FT /note="G -> W (in Ref. 2; AAD16006)"
FT /evidence="ECO:0000305"
FT CONFLICT 894
FT /note="E -> K (in Ref. 1; CAB44357)"
FT /evidence="ECO:0000305"
FT HELIX 603..622
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 633..637
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 639..646
FT /evidence="ECO:0007829|PDB:7TQL"
FT HELIX 647..652
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 661..664
FT /evidence="ECO:0007829|PDB:7TQL"
FT HELIX 676..685
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 699..702
FT /evidence="ECO:0007829|PDB:7TQL"
FT HELIX 708..711
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 721..726
FT /evidence="ECO:0007829|PDB:7TQL"
FT HELIX 729..731
FT /evidence="ECO:0007829|PDB:7TQL"
FT HELIX 735..746
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 751..755
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 757..759
FT /evidence="ECO:0007829|PDB:7TQL"
FT HELIX 772..777
FT /evidence="ECO:0007829|PDB:7TQL"
FT HELIX 781..799
FT /evidence="ECO:0007829|PDB:7TQL"
FT TURN 800..802
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 808..811
FT /evidence="ECO:0007829|PDB:7TQL"
FT TURN 814..816
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 818..822
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 824..827
FT /evidence="ECO:0007829|PDB:7TQL"
FT HELIX 831..844
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 857..866
FT /evidence="ECO:0007829|PDB:7TQL"
FT TURN 867..869
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 870..879
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 887..890
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 897..900
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 903..906
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 913..915
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 920..923
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 927..934
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 943..949
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 952..954
FT /evidence="ECO:0007829|PDB:7TQL"
FT TURN 961..963
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 981..987
FT /evidence="ECO:0007829|PDB:7TQL"
FT HELIX 988..1001
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 1005..1013
FT /evidence="ECO:0007829|PDB:7TQL"
FT HELIX 1015..1025
FT /evidence="ECO:0007829|PDB:7TQL"
FT TURN 1029..1031
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 1033..1038
FT /evidence="ECO:0007829|PDB:7TQL"
FT HELIX 1043..1051
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 1055..1061
FT /evidence="ECO:0007829|PDB:7TQL"
FT HELIX 1062..1081
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 1086..1088
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 1092..1096
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 1105..1117
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 1125..1135
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 1138..1143
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 1157..1161
FT /evidence="ECO:0007829|PDB:7TQL"
FT TURN 1173..1175
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 1182..1184
FT /evidence="ECO:0007829|PDB:7TQL"
FT HELIX 1188..1195
FT /evidence="ECO:0007829|PDB:7TQL"
FT STRAND 1199..1202
FT /evidence="ECO:0007829|PDB:7TQL"
FT HELIX 1209..1214
FT /evidence="ECO:0007829|PDB:7TQL"
FT TURN 1215..1218
FT /evidence="ECO:0007829|PDB:7TQL"
SQ SEQUENCE 1220 AA; 138827 MW; 454C29FB90AA768E CRC64;
MGKKQKNKSE DSTKDDIDLD ALAAEIEGAG AAKEQEPQKS KGKKKKEKKK QDFDEDDILK
ELEELSLEAQ GIKADRETVA VKPTENNEEE FTSKDKKKKG QKGKKQSFDD NDSEELEDKD
SKSKKTAKPK VEMYSGSDDD DDFNKLPKKA KGKAQKSNKK WDGSEEDEDN SKKIKERSRI
NSSGESGDES DEFLQSRKGQ KKNQKNKPGP NIESGNEDDD ASFKIKTVAQ KKAEKKERER
KKRDEEKAKL RKLKEKEELE TGKKDQSKQK ESQRKFEEET VKSKVTVDTG VIPASEEKAE
TPTAAEDDNE GDKKKKDKKK KKGEKEEKEK EKKKGPSKAT VKAMQEALAK LKEEEERQKR
EEEERIKRLE ELEAKRKEEE RLEQEKRERK KQKEKERKER LKKEGKLLTK SQREARARAE
ATLKLLQAQG VEVPSKDSLP KKRPIYEDKK RKKIPQQLES KEVSESMELC AAVEVMEQGV
PEKEETPPPV EPEEEEDTED AGLDDWEAMA SDEETEKVEG NKVHIEVKEN PEEEEEEEEE
EEEDEESEEE EEEEGESEGS EGDEEDEKVS DEKDSGKTLD KKPSKEMSSD SEYDSDDDRT
KEERAYDKAK RRIEKRRLEH SKNVNTEKLR APIICVLGHV DTGKTKILDK LRHTHVQDGE
AGGITQQIGA TNVPLEAINE QTKMIKNFDR ENVRIPGMLI IDTPGHESFS NLRNRGSSLC
DIAILVVDIM HGLEPQTIES INLLKSKKCP FIVALNKIDR LYDWKKSPDS DVAATLKKQK
KNTKDEFEER AKAIIVEFAQ QGLNAALFYE NKDPRTFVSL VPTSAHTGDG MGSLIYLLVE
LTQTMLSKRL AHCEELRAQV MEVKALPGMG TTIDVILING RLKEGDTIIV PGVEGPIVTQ
IRGLLLPPPM KELRVKNQYE KHKEVEAAQG VKILGKDLEK TLAGLPLLVA YKEDEIPVLK
DELIHELKQT LNAIKLEEKG VYVQASTLGS LEALLEFLKT SEVPYAGINI GPVHKKDVMK
ASVMLEHDPQ YAVILAFDVR IERDAQEMAD SLGVRIFSAE IIYHLFDAFT KYRQDYKKQK
QEEFKHIAVF PCKIKILPQY IFNSRDPIVM GVTVEAGQVK QGTPMCVPSK NFVDIGIVTS
IEINHKQVDV AKKGQEVCVK IEPIPGESPK MFGRHFEATD ILVSKISRQS IDALKDWFRD
EMQKSDWQLI VELKKVFEII
//
