EIF3F_ARATH
ID EIF3F_ARATH Reviewed; 293 AA.
AC O04202; Q8W4H4;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit F {ECO:0000255|HAMAP-Rule:MF_03005};
DE Short=eIF3f {ECO:0000255|HAMAP-Rule:MF_03005};
DE AltName: Full=eIF-3-epsilon {ECO:0000255|HAMAP-Rule:MF_03005};
DE AltName: Full=eIF3 p32 subunit;
GN Name=TIF3F1; OrderedLocusNames=At2g39990; ORFNames=T29M21.15;
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].
RX PubMed=9341143; DOI=10.1074/jbc.272.43.27042;
RA Asano K., Vornlocher H.-P., Richter-Cook N.J., Merrick W.C.,
RA Hinnebusch A.G., Hershey J.W.B.;
RT "Structure of cDNAs encoding human eukaryotic initiation factor 3 subunits.
RT Possible roles in RNA binding and macromolecular assembly.";
RL J. Biol. Chem. 272:27042-27052(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INTERACTION WITH TIF3E1
RP AND TIF3H1, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Landsberg erecta, and cv. Wassilewskija;
RX PubMed=20444226; DOI=10.1111/j.1365-313x.2010.04237.x;
RA Xia C., Wang Y.-J., Li W.-Q., Chen Y.-R., Deng Y., Zhang X.-Q., Chen L.-Q.,
RA Ye D.;
RT "The Arabidopsis eukaryotic translation initiation factor 3, subunit F
RT (AteIF3f), is required for pollen germination and embryogenesis.";
RL Plant J. 63:189-202(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is involved in protein synthesis of a
CC specialized repertoire of mRNAs and, together with other initiation
CC factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S
CC ribosome. The eIF-3 complex specifically targets and initiates
CC translation of a subset of mRNAs involved in cell proliferation
CC (Potential). Involved in cell growth and differentiation, especially
CC during embryogenesis and male gametophyte germination
CC (PubMed:20444226). Regulates sensitivity to sugars (e.g. sucrose)
CC (PubMed:20444226). {ECO:0000255|HAMAP-Rule:MF_03005,
CC ECO:0000269|PubMed:20444226}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. Binds to TIF3E1 and TIF3H1 (PubMed:20444226).
CC {ECO:0000255|HAMAP-Rule:MF_03005, ECO:0000269|PubMed:20444226}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03005,
CC ECO:0000269|PubMed:20444226}.
CC -!- TISSUE SPECIFICITY: Expressed in inflorescences, leaves, stems,
CC siliques, roots and seedlings. Accumulates at highly levels in pollen
CC grains, developing embryos and root tips.
CC {ECO:0000269|PubMed:20444226}.
CC -!- DISRUPTION PHENOTYPE: Male gametophyte-defective. Disrupted pollen
CC germination and embryo development. Hypersensitivity to exogenous
CC sucrose. {ECO:0000269|PubMed:20444226}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit F family. {ECO:0000255|HAMAP-
CC Rule:MF_03005}.
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DR EMBL; U54561; AAD03463.1; -; mRNA.
DR EMBL; AF002109; AAB95284.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09760.1; -; Genomic_DNA.
DR EMBL; AY045824; AAK76498.1; -; mRNA.
DR EMBL; AY062556; AAL32634.1; -; mRNA.
DR EMBL; AY091363; AAM14302.1; -; mRNA.
DR EMBL; AY093368; AAM13367.1; -; mRNA.
DR PIR; H84823; H84823.
DR RefSeq; NP_181528.1; NM_129557.4.
DR AlphaFoldDB; O04202; -.
DR SMR; O04202; -.
DR BioGRID; 3925; 74.
DR STRING; 3702.AT2G39990.1; -.
DR MEROPS; M67.974; -.
DR iPTMnet; O04202; -.
DR PaxDb; O04202; -.
DR PRIDE; O04202; -.
DR ProteomicsDB; 221939; -.
DR EnsemblPlants; AT2G39990.1; AT2G39990.1; AT2G39990.
DR GeneID; 818587; -.
DR Gramene; AT2G39990.1; AT2G39990.1; AT2G39990.
DR KEGG; ath:AT2G39990; -.
DR Araport; AT2G39990; -.
DR TAIR; locus:2061206; AT2G39990.
DR eggNOG; KOG2975; Eukaryota.
DR HOGENOM; CLU_027018_0_1_1; -.
DR InParanoid; O04202; -.
DR OMA; MADTDSF; -.
DR OrthoDB; 1038775at2759; -.
DR PhylomeDB; O04202; -.
DR PRO; PR:O04202; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O04202; baseline and differential.
DR Genevisible; O04202; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0031369; F:translation initiation factor binding; IBA:GO_Central.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0009846; P:pollen germination; IMP:TAIR.
DR GO; GO:0009744; P:response to sucrose; IMP:UniProtKB.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR CDD; cd08064; MPN_eIF3f; 1.
DR HAMAP; MF_03005; eIF3f; 1.
DR InterPro; IPR027531; eIF3f.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR024969; Rpn11/EIF3F_C.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF13012; MitMem_reg; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Initiation factor; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..293
FT /note="Eukaryotic translation initiation factor 3 subunit
FT F"
FT /id="PRO_0000213966"
FT DOMAIN 28..159
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 261
FT /note="D -> N (in Ref. 4; AAL32634/AAM13367)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 293 AA; 31862 MW; 4742CF7E8F6F47C7 CRC64;
MAATSEHTIL QFVSPSSTAS ATTSVLTARI HPLVIFNVCD CFVRRPDSAE RVIGTLLGSI
LPDGTVDIRN SYAVPHNESS DQVAVDIDYH HNMLASHLKV NSKETIVGWY STGAGVNGGS
SLIHDFYARE VPNPIHLTVD TGFTNGEGTI KAFVSSNLSL GDRQLVAHFQ EIPVDLRMVD
AERVGFDVLK ATSVDKLPND LEGMELTMER LLTLINDVYK YVDSVVGGQI APDNNIGRFI
ADAVASLPKL PPQVFDNLVN DSLQDQLLLL YLSSITRTQL SLAEKLNTAA QML
