EIF3H_ARATH
ID EIF3H_ARATH Reviewed; 337 AA.
AC Q9C5Z2; F4I5Y8; Q9SAB9;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit H {ECO:0000255|HAMAP-Rule:MF_03007};
DE Short=eIF3h {ECO:0000255|HAMAP-Rule:MF_03007};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 3 {ECO:0000255|HAMAP-Rule:MF_03007};
DE AltName: Full=eIF-3-gamma;
DE AltName: Full=eIF3 p38 subunit;
GN Name=TIF3H1; OrderedLocusNames=At1g10840 {ECO:0000312|EMBL:AEE28653.1};
GN ORFNames=T16B5.2 {ECO:0000312|EMBL:AAD31329.1};
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].
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INTERACTION WITH
RP CSN1; CSN7; CSN8; TIF3A1; TIF3B1; TIF3C1 AND TIF3E1.
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 [7]
RP FUNCTION.
RC STRAIN=cv. Wassilewskija;
RX PubMed=17439654; DOI=10.1186/gb-2007-8-4-r60;
RA Kim B.-H., Cai X., Vaughn J.N., von Arnim A.G.;
RT "On the functions of the h subunit of eukaryotic initiation factor 3 in
RT late stages of translation initiation.";
RL Genome Biol. 8:R60.1-R60.20(2007).
RN [8]
RP INTERACTION WITH TIF3F1.
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 [9]
RP FUNCTION, DISRUPTION PHENOTYPE, PHOSPHORYLATION AT SER-178 BY ATPK1,
RP MUTAGENESIS OF SER-178, AND INTERACTION WITH ATPK1.
RX PubMed=23524850; DOI=10.1038/emboj.2013.61;
RA Schepetilnikov M., Dimitrova M., Mancera-Martinez E., Geldreich A.,
RA Keller M., Ryabova L.A.;
RT "TOR and S6K1 promote translation reinitiation of uORF-containing mRNAs via
RT phosphorylation of eIF3h.";
RL EMBO J. 32:1087-1102(2013).
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). Regulates translation initiation of specific 5' mRNAs
CC harboring multiple upstream open reading frames (uORFs) in their 5'
CC leader sequence (e.g. BETA-OHASE 2 and LHY) (PubMed:15548739,
CC PubMed:17439654, PubMed:23524850). {ECO:0000255|HAMAP-Rule:MF_03007,
CC ECO:0000269|PubMed:15548739, ECO:0000269|PubMed:17439654,
CC ECO:0000269|PubMed:23524850}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. Interacts directly with TIF3A1, TIF3B1, TIF3C1, TIF3E1
CC and TIF3F1 (PubMed:15548739, PubMed:20444226). Associates with the CSN
CC (COP9 signalosome) complex. Binds to CSN1, CSN7 and CSN8
CC (PubMed:15548739). Interacts with ATPK1 (PubMed:23524850).
CC {ECO:0000255|HAMAP-Rule:MF_03007, ECO:0000269|PubMed:15548739,
CC ECO:0000269|PubMed:20444226, ECO:0000269|PubMed:23524850}.
CC -!- INTERACTION:
CC Q9C5Z2; P42818: ATPK1; NbExp=3; IntAct=EBI-3387106, EBI-8107038;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03007}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C5Z2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C5Z2-2; Sequence=VSP_057957;
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots and flowers, and, to a
CC lower extent, in leaves, stems and siliques.
CC {ECO:0000269|PubMed:15548739}.
CC -!- PTM: In response to auxin (NAA), phosphorylated at Ser-178 by ATPK1 and
CC binds to polysomes via TOR signaling. This phosphorylation is repressed
CC by Torin-1. {ECO:0000269|PubMed:23524850}.
CC -!- DISRUPTION PHENOTYPE: Pleiotropic growth defects throughout development
CC including postembryonic growth retardation, and delayed shoot and root
CC growth, flowering, and senescence. Lethal at 80 percent at the
CC vegetative rosettes stage. Reduced fertility. Compromised translation
CC efficiency of specific 5' mRNA leader sequences. Requires exogenous
CC sugar to transit from seedling to vegetative development, but
CC hypersensitive to elevated levels of exogenous sugars (e.g. sucrose,
CC maltose and glucose). Enhanced sensitivity to abscisic acid (ABA)
CC (PubMed:15548739). Impaired uORF-RNAs polysomal association
CC (PubMed:23524850). {ECO:0000269|PubMed:15548739,
CC ECO:0000269|PubMed:23524850}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit H family. {ECO:0000255|HAMAP-
CC Rule:MF_03007}.
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DR EMBL; AF285833; AAG53614.1; -; mRNA.
DR EMBL; AC007354; AAD31329.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28653.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28654.1; -; Genomic_DNA.
DR EMBL; AY054641; AAK96832.1; -; mRNA.
DR EMBL; AY081546; AAM10108.1; -; mRNA.
DR EMBL; BT000765; AAN31904.1; -; mRNA.
DR EMBL; AY087338; AAM64888.1; -; mRNA.
DR PIR; B86242; B86242.
DR RefSeq; NP_563880.1; NM_100960.3. [Q9C5Z2-1]
DR RefSeq; NP_973808.1; NM_202079.1. [Q9C5Z2-2]
DR AlphaFoldDB; Q9C5Z2; -.
DR SMR; Q9C5Z2; -.
DR BioGRID; 22867; 34.
DR IntAct; Q9C5Z2; 4.
DR MINT; Q9C5Z2; -.
DR STRING; 3702.AT1G10840.1; -.
DR MEROPS; M67.971; -.
DR iPTMnet; Q9C5Z2; -.
DR PaxDb; Q9C5Z2; -.
DR PRIDE; Q9C5Z2; -.
DR ProteomicsDB; 220755; -. [Q9C5Z2-1]
DR EnsemblPlants; AT1G10840.1; AT1G10840.1; AT1G10840. [Q9C5Z2-1]
DR EnsemblPlants; AT1G10840.2; AT1G10840.2; AT1G10840. [Q9C5Z2-2]
DR GeneID; 837627; -.
DR Gramene; AT1G10840.1; AT1G10840.1; AT1G10840. [Q9C5Z2-1]
DR Gramene; AT1G10840.2; AT1G10840.2; AT1G10840. [Q9C5Z2-2]
DR KEGG; ath:AT1G10840; -.
DR Araport; AT1G10840; -.
DR TAIR; locus:2196469; AT1G10840.
DR eggNOG; KOG1560; Eukaryota.
DR HOGENOM; CLU_044094_0_0_1; -.
DR InParanoid; Q9C5Z2; -.
DR OMA; KFNRYQQ; -.
DR PhylomeDB; Q9C5Z2; -.
DR PRO; PR:Q9C5Z2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C5Z2; baseline and differential.
DR Genevisible; Q9C5Z2; AT.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IBA:GO_Central.
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:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0042788; C:polysomal ribosome; IDA:UniProtKB.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0045948; P:positive regulation of translational initiation; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IMP:UniProtKB.
DR GO; GO:0009733; P:response to auxin; IMP:UniProtKB.
DR GO; GO:0009749; P:response to glucose; IMP:UniProtKB.
DR GO; GO:0034286; P:response to maltose; IMP:UniProtKB.
DR GO; GO:0009744; P:response to sucrose; IMP:UniProtKB.
DR CDD; cd08065; MPN_eIF3h; 1.
DR HAMAP; MF_03007; eIF3h; 1.
DR InterPro; IPR027524; eIF3h.
DR InterPro; IPR045810; eIF3h_C.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR Pfam; PF19445; eIF3h_C; 1.
DR Pfam; PF01398; JAB; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Alternative splicing; Cytoplasm;
KW Initiation factor; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Translation regulation.
FT CHAIN 1..337
FT /note="Eukaryotic translation initiation factor 3 subunit
FT H"
FT /id="PRO_0000213963"
FT DOMAIN 25..158
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 267..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 178
FT /note="Phosphoserine; by ATPK1"
FT /evidence="ECO:0000269|PubMed:23524850"
FT VAR_SEQ 1..87
FT /note="Missing (in isoform 2)"
FT /id="VSP_057957"
FT MUTAGEN 178
FT /note="S->A: Impaired activation of uORF-mRNA translation."
FT /evidence="ECO:0000269|PubMed:23524850"
FT MUTAGEN 178
FT /note="S->D: Phosphorylation mimic mutant, up-regulation of
FT uORF-mRNA translation."
FT /evidence="ECO:0000269|PubMed:23524850"
FT CONFLICT 146
FT /note="V -> L (in Ref. 1; AAG53614)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 38373 MW; F9965DA546AC977C CRC64;
MATMARSFLQ AISKDEAVAP PLRVVQIEGL AVLKIIKHCK EFSPTLVTGQ LLGLDVGSVL
EVTNCFPFPV RDDDEEIEAD GANYQLEMMR CLREVNVDNN TVGWYQSTVL GSYQTVELIE
TFMNYQENIK RCVCIIYDPS KADLGVLALK ALKLSDSFME LYRGGNFTGE KLREKNFSWM
DIFEEIPIKV SNSALVSAFM TELETDTPVS QGDYDRLHSS TTPFLENNME FLIKCMDDLS
MEQQKFQYYY RNLSRQQAQQ QAWLQKRRTE NMARKSAGEE PLPEEDPSNP IFKAIPEPSR
LESFLITNQV SNFCGQINGV AGQNFSRLYL TKALHDN
