EIF3B_ARATH
ID EIF3B_ARATH Reviewed; 712 AA.
AC Q9C5Z1;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
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=eIF-3-eta {ECO:0000255|HAMAP-Rule:MF_03001};
DE AltName: Full=eIF3 p110 {ECO:0000255|HAMAP-Rule:MF_03001};
DE AltName: Full=p82;
GN Name=TIF3B1; OrderedLocusNames=At5g27640; ORFNames=F15A18_100;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=11042177; DOI=10.1074/jbc.m007236200;
RA Burks E.A., Bezerra P.P., Le H., Gallie D.R., Browning K.S.;
RT "Plant initiation factor 3 subunit composition resembles mammalian
RT initiation factor 3 and has a novel subunit.";
RL J. Biol. Chem. 276:2122-2131(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP INTERACTION WITH TIF3H1.
RX PubMed=15548739; DOI=10.1105/tpc.104.026880;
RA Kim T.-H., Kim B.-H., Yahalom A., Chamovitz D.A., von Arnim A.G.;
RT "Translational regulation via 5' mRNA leader sequences revealed by
RT mutational analysis of the Arabidopsis translation initiation factor
RT subunit eIF3h.";
RL Plant Cell 16:3341-3356(2004).
RN [6]
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).
CC -!- FUNCTION: RNA-binding component of the eukaryotic translation
CC initiation factor 3 (eIF-3) complex, which is involved in protein
CC synthesis of a specialized repertoire of mRNAs and, together with other
CC initiation factors, stimulates binding of mRNA and methionyl-tRNAi to
CC the 40S ribosome. The eIF-3 complex specifically targets and initiates
CC translation of a subset of mRNAs involved in cell proliferation.
CC {ECO:0000255|HAMAP-Rule:MF_03001}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is composed of at least 13 different subunits.
CC Binds to the translation initiation factor TIF3H1 (PubMed:15548739).
CC {ECO:0000255|HAMAP-Rule:MF_03001, ECO:0000269|PubMed:11042177,
CC ECO:0000269|PubMed:15548739}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9C5Z1-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the eIF-3 subunit B family. {ECO:0000255|HAMAP-
CC Rule:MF_03001}.
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DR EMBL; AF285834; AAG53615.1; -; mRNA.
DR EMBL; AC007478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93709.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68848.1; -; Genomic_DNA.
DR EMBL; AF378883; AAK55686.1; -; mRNA.
DR EMBL; AY102149; AAM26716.1; -; mRNA.
DR RefSeq; NP_001330567.1; NM_001344024.1. [Q9C5Z1-1]
DR RefSeq; NP_568498.1; NM_122646.4. [Q9C5Z1-1]
DR AlphaFoldDB; Q9C5Z1; -.
DR SMR; Q9C5Z1; -.
DR BioGRID; 18100; 44.
DR IntAct; Q9C5Z1; 2.
DR STRING; 3702.AT5G27640.2; -.
DR iPTMnet; Q9C5Z1; -.
DR PaxDb; Q9C5Z1; -.
DR PRIDE; Q9C5Z1; -.
DR ProteomicsDB; 222317; -. [Q9C5Z1-1]
DR DNASU; 832826; -.
DR EnsemblPlants; AT5G27640.1; AT5G27640.1; AT5G27640. [Q9C5Z1-1]
DR EnsemblPlants; AT5G27640.3; AT5G27640.3; AT5G27640. [Q9C5Z1-1]
DR GeneID; 832826; -.
DR Gramene; AT5G27640.1; AT5G27640.1; AT5G27640. [Q9C5Z1-1]
DR Gramene; AT5G27640.3; AT5G27640.3; AT5G27640. [Q9C5Z1-1]
DR KEGG; ath:AT5G27640; -.
DR Araport; AT5G27640; -.
DR eggNOG; KOG2314; Eukaryota.
DR HOGENOM; CLU_011152_2_0_1; -.
DR InParanoid; Q9C5Z1; -.
DR OMA; NVADCKI; -.
DR PhylomeDB; Q9C5Z1; -.
DR PRO; PR:Q9C5Z1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9C5Z1; baseline and differential.
DR Genevisible; Q9C5Z1; AT.
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; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0031369; F:translation initiation factor binding; IEA:InterPro.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR CDD; cd12278; RRM_eIF3B; 1.
DR Gene3D; 2.130.10.10; -; 2.
DR Gene3D; 3.30.70.330; -; 1.
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; PTHR14068; 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; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Initiation factor;
KW Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..712
FT /note="Eukaryotic translation initiation factor 3 subunit
FT B"
FT /id="PRO_0000123532"
FT DOMAIN 56..143
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 712 AA; 81876 MW; 56AC3DECD9F0EFF9 CRC64;
MEVVDIDARA AKLGIDWSQV NFDSIQLPPG EDFGIESDDE AVYQDDQSEF DTGFGNIIVV
DHLPVVPKEK FEKLEGVVKK IYNQLGVIKE NGLWMPVDPD TKMTLGYCFI EFNTPQEAQN
AKEKSHGYKL DKSHIFAVNM FDDFDRLMNV KEEWEPPQAR PYVPGENLQK WLTDEKARDQ
LVIRSGPDTE VFWNDTRQKA PEPVHKRPYW TESYVQWSPL GTYLVTLHKQ GAAVWGGADT
FTRLMRYQHS MVKLVDFSPG EKYLVTYHSQ EPSNPRDASK VEIKVFDVRT GRMMRDFKGS
ADEFSIGGPG GVAGASWPVF RWAGGKDDKY FAKLSKNTIS VYETETFSLI DKKSMKVDNV
VDICWSPTDS ILSLFVPEQG GGNQPAKVAL VQIPSKVELR QKNLFSVSDC KMYWQSSGEY
LAVKVDRYTK TKKSTYSGFE LFRIKERDIP IEVLELDNKN DKIIAFAWEP KGHRFAVIHG
DQPRPDVSFY SMKTAQNTGR VSKLATLKAK QANALFWSPT GKYIILAGLK GFNGQLEFFN
VDELETMATA EHFMATDIEW DPTGRYVATA VTSVHEMENG FTIWSFNGIM LYRILKDHFF
QLAWRPRPPS FLTAEKEEEI AKTLKKYSKK YEAEDQDVSL LLSEQDREKR KALKEEWEKW
VMQWKSLHEE EKLVRQNLRD GEVSDVEEDE YEAKEVEFED LIDVTEEIVQ ES
