MRF1_ARATH
ID MRF1_ARATH Reviewed; 702 AA.
AC Q94BR1; Q8LDN5; Q9FMK4;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=MA3 DOMAIN-CONTAINING TRANSLATION REGULATORY FACTOR 1 {ECO:0000303|PubMed:29084871};
DE AltName: Full=MA3 domain-containing protein 6 {ECO:0000303|PubMed:24041411};
GN Name=MRF1 {ECO:0000303|PubMed:29084871};
GN Synonyms=MAT6 {ECO:0000303|PubMed:24041411};
GN OrderedLocusNames=At5g63190 {ECO:0000312|Araport:AT5G63190};
GN ORFNames=MDC12.16 {ECO:0000312|EMBL:BAB10561.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [2]
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 [3]
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 [4]
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 [5] {ECO:0007744|PubMed:22223895}
RP IDENTIFICATION BY MASS 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 [6]
RP GENE FAMILY.
RX PubMed=24041411; DOI=10.1186/1471-2148-13-199;
RA Cheng S., Liu R., Gallie D.R.;
RT "The unique evolution of the programmed cell death 4 protein in plants.";
RL BMC Evol. Biol. 13:199-199(2013).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY DARK AND STARVATION,
RP PHOSPHORYLATION, TISSUE SPECIFICITY, INTERACTION WITH S6K1; S6K2; EIF4A1
RP AND RIBOSOMES, SUBCELLULAR LOCATION, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=29084871; DOI=10.1105/tpc.17.00563;
RA Lee D.-H., Park S.J., Ahn C.S., Pai H.-S.;
RT "MRF family genes are involved in translation control, especially under
RT energy-deficient conditions, and their expression and functions are
RT modulated by the TOR signaling pathway.";
RL Plant Cell 29:2895-2920(2017).
CC -!- FUNCTION: Involved in target of rapamycin (TOR)-regulated translation
CC control, especially under energy-deficient conditions.
CC {ECO:0000269|PubMed:29084871}.
CC -!- SUBUNIT: Binds to EIF4A1, S6K1 and S6K2 (PubMed:29084871). The
CC association with ribosomes is modulated by cellular energy status and
CC TOR activity (PubMed:29084871). {ECO:0000269|PubMed:29084871}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:29084871}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in vegetative tissues, such as
CC leaves, roots and stems, and, to a lower extent, in reproductive
CC tissues, such as flower buds and flowers.
CC {ECO:0000269|PubMed:29084871}.
CC -!- INDUCTION: Induced by dark and starvation but repressed by glucose
CC feeding subsequent to starvation in a TOR-dependent manner.
CC {ECO:0000269|PubMed:29084871}.
CC -!- PTM: Phosphorylation by S6 kinases (e.g. S6K1 and S6K2) is modulated by
CC cellular energy status and TOR activity. {ECO:0000269|PubMed:29084871}.
CC -!- DISRUPTION PHENOTYPE: Increased susceptibility to dark and starvation,
CC and to treatment with the TOR inhibitor (PubMed:29084871). Decreased
CC translation activity associated with altered ribosome patterns,
CC especially in the dark and starvation conditions, in which mRNAs
CC distribution is altered and rRNA abnormally degraded (PubMed:29084871).
CC Slightly early flowering time under long-day conditions
CC (PubMed:29084871). {ECO:0000269|PubMed:29084871}.
CC -!- SIMILARITY: Belongs to the PDCD4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10561.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB008265; BAB10561.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97716.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97717.1; -; Genomic_DNA.
DR EMBL; AY039947; AAK64051.1; -; mRNA.
DR EMBL; AY142667; AAN13205.1; -; mRNA.
DR EMBL; AY085894; AAM63106.1; -; mRNA.
DR RefSeq; NP_568968.1; NM_125714.3.
DR RefSeq; NP_851255.1; NM_180924.3.
DR AlphaFoldDB; Q94BR1; -.
DR SMR; Q94BR1; -.
DR IntAct; Q94BR1; 2.
DR STRING; 3702.AT5G63190.2; -.
DR iPTMnet; Q94BR1; -.
DR PaxDb; Q94BR1; -.
DR PRIDE; Q94BR1; -.
DR ProteomicsDB; 189753; -.
DR EnsemblPlants; AT5G63190.1; AT5G63190.1; AT5G63190.
DR EnsemblPlants; AT5G63190.2; AT5G63190.2; AT5G63190.
DR GeneID; 836440; -.
DR Gramene; AT5G63190.1; AT5G63190.1; AT5G63190.
DR Gramene; AT5G63190.2; AT5G63190.2; AT5G63190.
DR KEGG; ath:AT5G63190; -.
DR Araport; AT5G63190; -.
DR TAIR; locus:2162007; AT5G63190.
DR eggNOG; KOG0403; Eukaryota.
DR HOGENOM; CLU_013764_0_0_1; -.
DR InParanoid; Q94BR1; -.
DR OMA; TGWIVED; -.
DR OrthoDB; 434771at2759; -.
DR PhylomeDB; Q94BR1; -.
DR PRO; PR:Q94BR1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94BR1; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0009646; P:response to absence of light; IEP:TAIR.
DR GO; GO:0090549; P:response to carbon starvation; IEP:TAIR.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003891; Initiation_fac_eIF4g_MI.
DR InterPro; IPR039778; PDCD4.
DR PANTHER; PTHR12626; PTHR12626; 1.
DR Pfam; PF02847; MA3; 4.
DR SMART; SM00544; MA3; 4.
DR SUPFAM; SSF48371; SSF48371; 4.
DR PROSITE; PS51366; MI; 4.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Translation regulation.
FT CHAIN 1..702
FT /note="MA3 DOMAIN-CONTAINING TRANSLATION REGULATORY FACTOR
FT 1"
FT /id="PRO_0000447574"
FT DOMAIN 122..243
FT /note="MI 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 286..407
FT /note="MI 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 420..541
FT /note="MI 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 583..702
FT /note="MI 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT REGION 39..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 273..280
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 458..465
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
SQ SEQUENCE 702 AA; 77556 MW; 4FB63FB12263C6D9 CRC64;
MASGEGILTD GQWKKLEIAT HNSGSLSSSP KSHTLFADLN IKSPTGGKGP VAGIPNRHVR
RTHSGKHIRV KKEGAGGKGT WGKLLDTDDG DSCIDKNDPN YDSGEDAYDG LVDSPVSDPL
NDYKKSVVSI IDEYFSTGDV KVAASDLREL GSSEYHPYFT KRLVSMAMDR HDKEKEMASV
LLSALYADVI LPDQIRDGFI RLLRSVDDLA VDILDAVNVL ALFIARAIVD EILPPVFLVR
SKKILPESCK GFQVIVTAEK SYLSAPHHAE LVEKKWGGST HTTVEETKKK ISEILKEYVE
NGDTYEACRC IRELGVSFFH HEVVKRALVL AMDSPTAESL VLKLLKETAE EGLISSSQMV
KGFFRVAESL DDLALDIPSA KKLFDSIVPK AISGGWLDDS FKITSDQDGE KSSQDGKLRQ
YKKDTVNIIQ EYFLSDDIPE LIRSLQDLGA PEYNPVFLKR LITLALDRKN REKEMASVLL
SALHMELFST EDFINGFIML LESAEDTALD IMDASNELAL FLARAVIDDV LAPLNLEDIS
TKLPPKSTGT ETVRSARSLI SARHAGERLL RSWGGGTGWI VEDAKDKISK LLEEYETGGV
TSEACQCIRD LGMPFFNHEV VKKALVMAME KQNDRLLNLL EECFGEGLIT TNQMTKGFGR
VNDSLDDLSL DIPNAKEKFE LYASHAMDNG WILPEFGISA TQ
