ID EIF3B_HUMAN Reviewed; 814 AA.
AC P55884; A4D208; Q2NL77; Q9UMF9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 3.
DT 27-MAR-2024, entry version 222.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit B {ECO:0000255|HAMAP-Rule:MF_03001};
DE Short=eIF3b {ECO:0000255|HAMAP-Rule:MF_03001};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 9 {ECO:0000255|HAMAP-Rule:MF_03001};
DE AltName: Full=Prt1 homolog;
DE Short=hPrt1;
DE AltName: Full=eIF-3-eta {ECO:0000255|HAMAP-Rule:MF_03001};
DE AltName: Full=eIF3 p110 {ECO:0000255|HAMAP-Rule:MF_03001};
DE AltName: Full=eIF3 p116;
GN Name=EIF3B {ECO:0000255|HAMAP-Rule:MF_03001};
GN Synonyms=EIF3S9 {ECO:0000255|HAMAP-Rule:MF_03001};
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] (ISOFORM 1), FUNCTION, AND VARIANT PRO-64.
RC TISSUE=Skeletal muscle;
RX PubMed=9388245; DOI=10.1074/jbc.272.49.30975;
RA Chaudhuri J., Chakrabarti A., Maitra U.;
RT "Biochemical characterization of mammalian translation initiation factor 3
RT (eIF3). Molecular cloning reveals that p110 subunit is the mammalian
RT homologue of Saccharomyces cerevisiae protein Prt1.";
RL J. Biol. Chem. 272:30975-30983(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT PRO-64.
RC TISSUE=Placenta;
RX PubMed=8995410; DOI=10.1074/jbc.272.2.1110;
RA Methot N., Rom E., Olsen H., Sonenberg N.;
RT "The human homologue of the yeast Prt1 protein is an integral part of the
RT eukaryotic initiation factor 3 complex and interacts with p170.";
RL J. Biol. Chem. 272:1110-1116(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PRO-64.
RC TISSUE=Brain, 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 [7]
RP INTERACTION WITH EIF3E.
RX PubMed=11457827; DOI=10.1074/jbc.m102161200;
RA Shalev A., Valasek L., Pise-Masison C.A., Radonovich M., Phan L.,
RA Clayton J., He H., Brady J.N., Hinnebusch A.G., Asano K.;
RT "Saccharomyces cerevisiae protein Pci8p and human protein eIF3e/Int-6
RT interact with the eIF3 core complex by binding to cognate eIF3b subunits.";
RL J. Biol. Chem. 276:34948-34957(2001).
RN [8]
RP INTERACTION WITH EIF3A.
RX PubMed=11169732;
RX DOI=10.1002/1097-4644(20010315)80:4<483::aid-jcb1002>3.0.co;2-b;
RA Lin L., Holbro T., Alonso G., Gerosa D., Burger M.M.;
RT "Molecular interaction between human tumor marker protein p150, the largest
RT subunit of eIF3, and intermediate filament protein K7.";
RL J. Cell. Biochem. 80:483-490(2001).
RN [9]
RP INTERACTION WITH EIF3A; EIF3C; EIF3G; EIF3I AND EIF3K.
RX PubMed=14519125; DOI=10.1046/j.1432-1033.2003.03807.x;
RA Mayeur G.L., Fraser C.S., Peiretti F., Block K.L., Hershey J.W.B.;
RT "Characterization of eIF3k: a newly discovered subunit of mammalian
RT translation initiation factor eIF3.";
RL Eur. J. Biochem. 270:4133-4139(2003).
RN [10]
RP INTERACTION WITH EIF3A; EIF3G; EIF3I AND EIF3J.
RX PubMed=14688252; DOI=10.1074/jbc.m312745200;
RA Fraser C.S., Lee J.Y., Mayeur G.L., Bushell M., Doudna J.A.,
RA Hershey J.W.B.;
RT "The j-subunit of human translation initiation factor eIF3 is required for
RT the stable binding of eIF3 and its subcomplexes to 40 S ribosomal subunits
RT in vitro.";
RL J. Biol. Chem. 279:8946-8956(2004).
RN [11]
RP INTERACTION WITH EIF4B; MTOR; RPTOR AND RPS6KB1.
RX PubMed=16286006; DOI=10.1016/j.cell.2005.10.024;
RA Holz M.K., Ballif B.A., Gygi S.P., Blenis J.;
RT "mTOR and S6K1 mediate assembly of the translation preinitiation complex
RT through dynamic protein interchange and ordered phosphorylation events.";
RL Cell 123:569-580(2005).
RN [12]
RP CHARACTERIZATION OF THE EIF-3 COMPLEX.
RX PubMed=15703437; DOI=10.1261/rna.7215305;
RA Kolupaeva V.G., Unbehaun A., Lomakin I.B., Hellen C.U.T., Pestova T.V.;
RT "Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and
RT its role in ribosomal dissociation and anti-association.";
RL RNA 11:470-486(2005).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-154 AND SER-164, AND
RP 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 [14]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16766523; DOI=10.1074/jbc.m605418200;
RA LeFebvre A.K., Korneeva N.L., Trutschl M., Cvek U., Duzan R.D.,
RA Bradley C.A., Hershey J.W.B., Rhoads R.E.;
RT "Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e
RT subunit.";
RL J. Biol. Chem. 281:22917-22932(2006).
RN [15]
RP FUNCTION, AND CHARACTERIZATION OF THE EIF-3 COMPLEX.
RX PubMed=17581632; DOI=10.1038/sj.emboj.7601765;
RA Masutani M., Sonenberg N., Yokoyama S., Imataka H.;
RT "Reconstitution reveals the functional core of mammalian eIF3.";
RL EMBO J. 26:3373-3383(2007).
RN [16]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=18056426; DOI=10.1101/gad.439507;
RA Poyry T.A., Kaminski A., Connell E.J., Fraser C.S., Jackson R.J.;
RT "The mechanism of an exceptional case of reinitiation after translation of
RT a long ORF reveals why such events do not generally occur in mammalian mRNA
RT translation.";
RL Genes Dev. 21:3149-3162(2007).
RN [17]
RP INTERACTION WITH EIF3A; EIF3C; EIF3E AND UPF2.
RX PubMed=17468741; DOI=10.1038/sj.embor.7400955;
RA Morris C., Wittmann J., Jaeck H.-M., Jalinot P.;
RT "Human INT6/eIF3e is required for nonsense-mediated mRNA decay.";
RL EMBO Rep. 8:596-602(2007).
RN [18]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX,
RP ACETYLATION AT MET-1, PHOSPHORYLATION AT SER-83; SER-85; SER-119; SER-125;
RP SER-152; SER-154 AND SER-164, AND MASS SPECTROMETRY.
RX PubMed=17322308; DOI=10.1074/mcp.m600399-mcp200;
RA Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L., Hershey J.W.B.,
RA Doudna J.A., Robinson C.V., Leary J.A.;
RT "Structural characterization of the human eukaryotic initiation factor 3
RT protein complex by mass spectrometry.";
RL Mol. Cell. Proteomics 6:1135-1146(2007).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [20]
RP SUBCELLULAR LOCATION.
RX PubMed=17984221; DOI=10.1128/mcb.01226-07;
RA Kim J.E., Ryu I., Kim W.J., Song O.K., Ryu J., Kwon M.Y., Kim J.H.,
RA Jang S.K.;
RT "Proline-rich transcript in brain protein induces stress granule
RT formation.";
RL Mol. Cell. Biol. 28:803-813(2008).
RN [21]
RP INTERACTION WITH DDX3X.
RX PubMed=18628297; DOI=10.1093/nar/gkn454;
RA Lee C.S., Dias A.P., Jedrychowski M., Patel A.H., Hsu J.L., Reed R.;
RT "Human DDX3 functions in translation and interacts with the translation
RT initiation factor eIF3.";
RL Nucleic Acids Res. 36:4708-4718(2008).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-81; SER-83; SER-85
RP AND SER-239, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [23]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX,
RP INTERACTION WITH EIF3E; EIF3F; EIF3H; EIF3L AND EIF3M, AND MASS
RP SPECTROMETRY.
RX PubMed=18599441; DOI=10.1073/pnas.0801313105;
RA Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E.,
RA Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B.,
RA Doudna J.A., Robinson C.V.;
RT "Mass spectrometry reveals modularity and a complete subunit interaction
RT map of the eukaryotic translation factor eIF3.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008).
RN [24]
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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-154 AND SER-164, AND
RP IDENTIFICATION 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 [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-209; LYS-288 AND LYS-364, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-154; SER-164 AND
RP SER-239, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [28]
RP IDENTIFICATION BY MASS 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).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125 AND SER-154, AND
RP IDENTIFICATION 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 [30]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [31]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, AND IDENTIFICATION BY
RP 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 [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION BY
RP MASS 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 [34]
RP INTERACTION WITH HNRPD, AND RNA-BINDING.
RX PubMed=24423872; DOI=10.1093/nar/gkt1379;
RA Lee K.H., Kim S.H., Kim H.J., Kim W., Lee H.R., Jung Y., Choi J.H.,
RA Hong K.Y., Jang S.K., Kim K.T.;
RT "AUF1 contributes to Cryptochrome1 mRNA degradation and rhythmic
RT translation.";
RL Nucleic Acids Res. 42:3590-3606(2014).
RN [35]
RP FUNCTION, IDENTIFICATION IN THE EIF-3 COMPLEX, AND RNA-BINDING.
RX PubMed=25849773; DOI=10.1038/nature14267;
RA Lee A.S., Kranzusch P.J., Cate J.H.;
RT "eIF3 targets cell-proliferation messenger RNAs for translational
RT activation or repression.";
RL Nature 522:111-114(2015).
RN [36]
RP INTERACTION WITH METTL3.
RX PubMed=27117702; DOI=10.1016/j.molcel.2016.03.021;
RA Lin S., Choe J., Du P., Triboulet R., Gregory R.I.;
RT "The m(6)A methyltransferase METTL3 promotes translation in human cancer
RT cells.";
RL Mol. Cell 62:335-345(2016).
RN [37]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=27462815; DOI=10.1038/nature18954;
RA Lee A.S., Kranzusch P.J., Doudna J.A., Cate J.H.;
RT "eIF3d is an mRNA cap-binding protein that is required for specialized
RT translation initiation.";
RL Nature 536:96-99(2016).
RN [38]
RP 3D-STRUCTURE MODELING, AND ELECTRON MICROSCOPY.
RX PubMed=16322461; DOI=10.1126/science.1118977;
RA Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., Nogales E.;
RT "Structural roles for human translation factor eIF3 in initiation of
RT protein synthesis.";
RL Science 310:1513-1515(2005).
RN [39]
RP STRUCTURE BY NMR OF 170-274, AND INTERACTION WITH EIF3J.
RX PubMed=17190833; DOI=10.1074/jbc.m610860200;
RA ElAntak L., Tzakos A.G., Locker N., Lukavsky P.J.;
RT "Structure of eIF3b RNA recognition motif and its interaction with eIF3j:
RT structural insights into the recruitment of eIF3b to the 40 S ribosomal
RT subunit.";
RL J. Biol. Chem. 282:8165-8174(2007).
CC -!- FUNCTION: RNA-binding component of the eukaryotic translation
CC initiation factor 3 (eIF-3) complex, which is required for several
CC steps in the initiation of protein synthesis (PubMed:9388245,
CC PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex
CC associates with the 40S ribosome and facilitates the recruitment of
CC eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-
CC initiation complex (43S PIC). The eIF-3 complex stimulates mRNA
CC recruitment to the 43S PIC and scanning of the mRNA for AUG
CC recognition. The eIF-3 complex is also required for disassembly and
CC recycling of post-termination ribosomal complexes and subsequently
CC prevents premature joining of the 40S and 60S ribosomal subunits prior
CC to initiation (PubMed:9388245, PubMed:17581632). The eIF-3 complex
CC specifically targets and initiates translation of a subset of mRNAs
CC involved in cell proliferation, including cell cycling, differentiation
CC and apoptosis, and uses different modes of RNA stem-loop binding to
CC exert either translational activation or repression (PubMed:25849773).
CC {ECO:0000255|HAMAP-Rule:MF_03001, ECO:0000269|PubMed:17581632,
CC ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815,
CC ECO:0000269|PubMed:9388245}.
CC -!- FUNCTION: (Microbial infection) In case of FCV infection, plays a role
CC in the ribosomal termination-reinitiation event leading to the
CC translation of VP2 (PubMed:18056426). {ECO:0000269|PubMed:18056426}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C,
CC EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and
CC EIF3M. The eIF-3 complex appears to include 3 stable modules: module A
CC is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of
CC EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D,
CC EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and
CC EIF3H of module B, thereby linking the three modules. EIF3J is a labile
CC subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex
CC interacts with RPS6KB1 under conditions of nutrient depletion.
CC Mitogenic stimulation leads to binding and activation of a complex
CC composed of MTOR and RPTOR, leading to phosphorylation and release of
CC RPS6KB1 and binding of EIF4B to eIF-3. Also interacts with UPF2 and
CC HNRPD. Interacts with METTL3 (PubMed:27117702). Interacts with DDX3X
CC (PubMed:18628297). {ECO:0000255|HAMAP-Rule:MF_03001,
CC ECO:0000269|PubMed:11169732, ECO:0000269|PubMed:11457827,
CC ECO:0000269|PubMed:14519125, ECO:0000269|PubMed:14688252,
CC ECO:0000269|PubMed:16286006, ECO:0000269|PubMed:16766523,
CC ECO:0000269|PubMed:17190833, ECO:0000269|PubMed:17322308,
CC ECO:0000269|PubMed:17468741, ECO:0000269|PubMed:18599441,
CC ECO:0000269|PubMed:18628297, ECO:0000269|PubMed:24423872,
CC ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27117702}.
CC -!- INTERACTION:
CC P55884; O00571: DDX3X; NbExp=5; IntAct=EBI-366696, EBI-353779;
CC P55884; Q14152: EIF3A; NbExp=9; IntAct=EBI-366696, EBI-366617;
CC P55884; P60228: EIF3E; NbExp=6; IntAct=EBI-366696, EBI-347740;
CC P55884; O00303: EIF3F; NbExp=8; IntAct=EBI-366696, EBI-711990;
CC P55884; O75821: EIF3G; NbExp=10; IntAct=EBI-366696, EBI-366632;
CC P55884; O15372: EIF3H; NbExp=6; IntAct=EBI-366696, EBI-709735;
CC P55884; Q13347: EIF3I; NbExp=7; IntAct=EBI-366696, EBI-354047;
CC P55884; O75822: EIF3J; NbExp=5; IntAct=EBI-366696, EBI-366647;
CC P55884; Q9UBQ5: EIF3K; NbExp=4; IntAct=EBI-366696, EBI-354344;
CC P55884; Q9Y262: EIF3L; NbExp=3; IntAct=EBI-366696, EBI-373519;
CC P55884; Q7L2H7: EIF3M; NbExp=4; IntAct=EBI-366696, EBI-353901;
CC P55884; P23443: RPS6KB1; NbExp=3; IntAct=EBI-366696, EBI-1775921;
CC P55884; Q9J0X9: UL54; Xeno; NbExp=4; IntAct=EBI-366696, EBI-7967856;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001}.
CC Cytoplasm, Stress granule {ECO:0000269|PubMed:17984221}. Note=Localizes
CC to stress granules following cellular stress.
CC {ECO:0000269|PubMed:17984221}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P55884-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P55884-2; Sequence=VSP_017274;
CC -!- DOMAIN: The RRM domain mediates interaction with EIF3J.
CC -!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum
CC stimulation. {ECO:0000255|HAMAP-Rule:MF_03001,
CC ECO:0000269|PubMed:17322308}.
CC -!- MASS SPECTROMETRY: Mass=93093.7; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:17322308};
CC -!- MASS SPECTROMETRY: Mass=92561; Mass_error=43.5; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18599441};
CC -!- SIMILARITY: Belongs to the eIF-3 subunit B family. {ECO:0000255|HAMAP-
CC Rule:MF_03001}.
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DR EMBL; U78525; AAC99479.1; -; mRNA.
DR EMBL; U62583; AAB42010.1; -; mRNA.
DR EMBL; AC004971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236953; EAL23951.1; -; Genomic_DNA.
DR EMBL; CH471144; EAW87237.1; -; Genomic_DNA.
DR EMBL; BC001173; AAH01173.1; -; mRNA.
DR EMBL; BC110865; AAI10866.1; -; mRNA.
DR CCDS; CCDS5332.1; -. [P55884-1]
DR PIR; T09582; T09582.
DR RefSeq; NP_001032360.1; NM_001037283.1. [P55884-1]
DR RefSeq; NP_003742.2; NM_003751.3. [P55884-1]
DR RefSeq; XP_011513901.1; XM_011515599.1. [P55884-1]
DR RefSeq; XP_011513902.1; XM_011515600.1.
DR RefSeq; XP_016868241.1; XM_017012752.1.
DR PDB; 2KRB; NMR; -; A=184-264.
DR PDB; 2NLW; NMR; -; A=170-274.
DR PDB; 5K1H; EM; 4.90 A; B=170-745.
DR PDB; 6YBT; EM; 6.00 A; 1=1-814.
DR PDB; 6ZMW; EM; 3.70 A; 1=1-814.
DR PDB; 6ZON; EM; 3.00 A; B=1-814.
DR PDB; 6ZP4; EM; 2.90 A; B=1-814.
DR PDB; 6ZVJ; EM; 3.80 A; B=180-745.
DR PDB; 7A09; EM; 3.50 A; B=1-814.
DR PDB; 7QP6; EM; 4.70 A; 1=1-813.
DR PDB; 7QP7; EM; 3.70 A; 1=1-813.
DR PDBsum; 2KRB; -.
DR PDBsum; 2NLW; -.
DR PDBsum; 5K1H; -.
DR PDBsum; 6YBT; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZON; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 6ZVJ; -.
DR PDBsum; 7A09; -.
DR PDBsum; 7QP6; -.
DR PDBsum; 7QP7; -.
DR AlphaFoldDB; P55884; -.
DR EMDB; EMD-10773; -.
DR EMDB; EMD-11302; -.
DR EMDB; EMD-11325; -.
DR EMDB; EMD-11335; -.
DR EMDB; EMD-11458; -.
DR EMDB; EMD-11602; -.
DR EMDB; EMD-14113; -.
DR EMDB; EMD-14114; -.
DR SMR; P55884; -.
DR BioGRID; 114211; 325.
DR ComplexPortal; CPX-6036; Eukaryotic translation initiation factor 3 complex.
DR CORUM; P55884; -.
DR DIP; DIP-31113N; -.
DR IntAct; P55884; 93.
DR MINT; P55884; -.
DR STRING; 9606.ENSP00000354125; -.
DR GlyGen; P55884; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P55884; -.
DR MetOSite; P55884; -.
DR PhosphoSitePlus; P55884; -.
DR SwissPalm; P55884; -.
DR BioMuta; EIF3B; -.
DR DMDM; 218512094; -.
DR EPD; P55884; -.
DR jPOST; P55884; -.
DR MassIVE; P55884; -.
DR MaxQB; P55884; -.
DR PaxDb; 9606-ENSP00000354125; -.
DR PeptideAtlas; P55884; -.
DR ProteomicsDB; 56875; -. [P55884-1]
DR ProteomicsDB; 56876; -. [P55884-2]
DR Pumba; P55884; -.
DR Antibodypedia; 4313; 184 antibodies from 30 providers.
DR DNASU; 8662; -.
DR Ensembl; ENST00000360876.9; ENSP00000354125.4; ENSG00000106263.19. [P55884-1]
DR Ensembl; ENST00000397011.2; ENSP00000380206.2; ENSG00000106263.19. [P55884-1]
DR GeneID; 8662; -.
DR KEGG; hsa:8662; -.
DR MANE-Select; ENST00000360876.9; ENSP00000354125.4; NM_001037283.2; NP_001032360.1.
DR UCSC; uc003slx.4; human. [P55884-1]
DR AGR; HGNC:3280; -.
DR CTD; 8662; -.
DR DisGeNET; 8662; -.
DR GeneCards; EIF3B; -.
DR HGNC; HGNC:3280; EIF3B.
DR HPA; ENSG00000106263; Low tissue specificity.
DR MIM; 603917; gene.
DR neXtProt; NX_P55884; -.
DR OpenTargets; ENSG00000106263; -.
DR PharmGKB; PA162384603; -.
DR VEuPathDB; HostDB:ENSG00000106263; -.
DR eggNOG; KOG2314; Eukaryota.
DR GeneTree; ENSGT00550000074913; -.
DR HOGENOM; CLU_011152_1_0_1; -.
DR InParanoid; P55884; -.
DR OMA; LWGGPQF; -.
DR OrthoDB; 5479191at2759; -.
DR PhylomeDB; P55884; -.
DR TreeFam; TF101521; -.
DR PathwayCommons; P55884; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-72649; Translation initiation complex formation.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR SignaLink; P55884; -.
DR SIGNOR; P55884; -.
DR BioGRID-ORCS; 8662; 831 hits in 1156 CRISPR screens.
DR ChiTaRS; EIF3B; human.
DR EvolutionaryTrace; P55884; -.
DR GeneWiki; EIF3B; -.
DR GenomeRNAi; 8662; -.
DR Pharos; P55884; Tbio.
DR PRO; PR:P55884; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P55884; Protein.
DR Bgee; ENSG00000106263; Expressed in body of pancreas and 205 other cell types or tissues.
DR ExpressionAtlas; P55884; baseline and differential.
DR Genevisible; P55884; HS.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
DR GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0060090; F:molecular adaptor activity; TAS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
DR GO; GO:0031369; F:translation initiation factor binding; IEA:InterPro.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; NAS:ComplexPortal.
DR GO; GO:0075522; P:IRES-dependent viral translational initiation; IDA:UniProtKB.
DR GO; GO:0006446; P:regulation of translational initiation; IDA:UniProtKB.
DR GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
DR GO; GO:0075525; P:viral translational termination-reinitiation; IDA:UniProtKB.
DR CDD; cd12278; RRM_eIF3B; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR HAMAP; MF_03001; eIF3b; 1.
DR InterPro; IPR011400; EIF3B.
DR InterPro; IPR034363; eIF3B_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR013979; TIF_beta_prop-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR14068; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 EIF3 -RELATED; 1.
DR PANTHER; PTHR14068:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT B; 1.
DR Pfam; PF08662; eIF2A; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF036424; eIF3b; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR SUPFAM; SSF69322; Tricorn protease domain 2; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Initiation factor; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Repeat; RNA-binding; WD repeat.
FT CHAIN 1..814
FT /note="Eukaryotic translation initiation factor 3 subunit
FT B"
FT /id="PRO_0000123531"
FT DOMAIN 185..268
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT REPEAT 285..324
FT /note="WD 1"
FT REPEAT 325..365
FT /note="WD 2"
FT REPEAT 366..425
FT /note="WD 3"
FT REPEAT 426..489
FT /note="WD 4"
FT REPEAT 490..553
FT /note="WD 5"
FT REPEAT 554..598
FT /note="WD 6"
FT REPEAT 599..642
FT /note="WD 7"
FT REPEAT 643..685
FT /note="WD 8"
FT REGION 1..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..413
FT /note="Sufficient for interaction with EIF3E"
FT REGION 170..274
FT /note="Sufficient for interaction with EIF3J"
FT COMPBIAS 132..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001,
FT ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001,
FT ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:18669648"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001,
FT ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:18669648"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001,
FT ECO:0000269|PubMed:17322308"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001,
FT ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001,
FT ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001,
FT ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001,
FT ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 209
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 288
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 364
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 812..814
FT /note="NQE -> IRSDLEHCAQPCVLWSRGRPAGSRVTPASSLCSLALDCDCAWILP
FT LRHIFVPFSPWCLQWGI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8995410"
FT /id="VSP_017274"
FT VARIANT 64
FT /note="S -> P (in dbSNP:rs9690787)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8995410, ECO:0000269|PubMed:9388245"
FT /id="VAR_047972"
FT VARIANT 793
FT /note="D -> E (in dbSNP:rs1063257)"
FT /id="VAR_047973"
FT CONFLICT 115..116
FT /note="ER -> AG (in Ref. 2; AAB42010)"
FT /evidence="ECO:0000305"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:2KRB"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:2KRB"
FT HELIX 200..212
FT /evidence="ECO:0007829|PDB:2KRB"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:2KRB"
FT STRAND 232..239
FT /evidence="ECO:0007829|PDB:2KRB"
FT HELIX 240..247
FT /evidence="ECO:0007829|PDB:2KRB"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:2KRB"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:2KRB"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:2NLW"
SQ SEQUENCE 814 AA; 92482 MW; C687A986EDAE0F5E CRC64;
MQDAENVAVP EAAEERAEPG QQQPAAEPPP AEGLLRPAGP GAPEAAGTEA SSEEVGIAEA
GPESEVRTEP AAEAEAASGP SESPSPPAAE ELPGSHAEPP VPAQGEAPGE QARDERSDSR
AQAVSEDAGG NEGRAAEAEP RALENGDADE PSFSDPEDFV DDVSEEELLG DVLKDRPQEA
DGIDSVIVVD NVPQVGPDRL EKLKNVIHKI FSKFGKITND FYPEEDGKTK GYIFLEYASP
AHAVDAVKNA DGYKLDKQHT FRVNLFTDFD KYMTISDEWD IPEKQPFKDL GNLRYWLEEA
ECRDQYSVIF ESGDRTSIFW NDVKDPVSIE ERARWTETYV RWSPKGTYLA TFHQRGIALW
GGEKFKQIQR FSHQGVQLID FSPCERYLVT FSPLMDTQDD PQAIIIWDIL TGHKKRGFHC
ESSAHWPIFK WSHDGKFFAR MTLDTLSIYE TPSMGLLDKK SLKISGIKDF SWSPGGNIIA
FWVPEDKDIP ARVTLMQLPT RQEIRVRNLF NVVDCKLHWQ KNGDYLCVKV DRTPKGTQGV
VTNFEIFRMR EKQVPVDVVE MKETIIAFAW EPNGSKFAVL HGEAPRISVS FYHVKNNGKI
ELIKMFDKQQ ANTIFWSPQG QFVVLAGLRS MNGALAFVDT SDCTVMNIAE HYMASDVEWD
PTGRYVVTSV SWWSHKVDNA YWLWTFQGRL LQKNNKDRFC QLLWRPRPPT LLSQEQIKQI
KKDLKKYSKI FEQKDRLSQS KASKELVERR RTMMEDFRKY RKMAQELYME QKNERLELRG
GVDTDELDSN VDDWEEETIE FFVTEEIIPL GNQE
//
