MRF3_ARATH
ID MRF3_ARATH Reviewed; 702 AA.
AC Q8W4Q4; A0A178V3H6; Q56XH1; Q9SZX0;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=MA3 DOMAIN-CONTAINING TRANSLATION REGULATORY FACTOR 3 {ECO:0000303|PubMed:29084871};
DE AltName: Full=EIN2 C-terminus interacting protein 1 {ECO:0000303|PubMed:21631530};
DE AltName: Full=MA3 domain-containing protein 5 {ECO:0000303|PubMed:24041411};
GN Name=MRF3 {ECO:0000303|PubMed:29084871};
GN Synonyms=ECIP1 {ECO:0000303|PubMed:21631530},
GN MAT5 {ECO:0000303|PubMed:24041411};
GN OrderedLocusNames=At4g24800 {ECO:0000312|Araport:AT4G24800};
GN ORFNames=F6I7.10 {ECO:0000312|EMBL:CAB41120.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH EIN2; ETR2 AND EIN4,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=21631530; DOI=10.1111/j.1365-3040.2011.02363.x;
RA Lei G., Shen M., Li Z.G., Zhang B., Duan K.X., Wang N., Cao Y.R.,
RA Zhang W.K., Ma B., Ling H.Q., Chen S.Y., Zhang J.S.;
RT "EIN2 regulates salt stress response and interacts with a MA3 domain-
RT containing protein ECIP1 in Arabidopsis.";
RL Plant Cell Environ. 34:1678-1692(2011).
RN [6]
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 [7]
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 [8]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY DARK AND STARVATION, TISSUE
RP SPECIFICITY, INTERACTION WITH EIF4A1 AND RIBOSOMES, SUBCELLULAR LOCATION,
RP 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 (PubMed:29084871). Involved in the regulation of the ethylene-mediated
CC signaling pathway (PubMed:21631530). Involved in salt stress responses
CC (PubMed:21631530). Reduced cotyledons size and early flowering
CC (PubMed:21631530). {ECO:0000269|PubMed:21631530,
CC ECO:0000269|PubMed:29084871}.
CC -!- SUBUNIT: Interacts with EIN2, ETR2 and EIN4 (PubMed:21631530). Binds to
CC EIF4A1 (PubMed:29084871). The association with ribosomes is modulated
CC by cellular energy status and TOR activity (PubMed:29084871).
CC {ECO:0000269|PubMed:21631530, ECO:0000269|PubMed:29084871}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:21631530,
CC ECO:0000269|PubMed:29084871}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in vegetative tissues, such as
CC leaves and stems, and, to a lower extent, in roots and reproductive
CC tissues, such as flower buds and flowers (PubMed:29084871). Expressed
CC in seedlings, roots, cauline leaf tips and flowers (PubMed:21631530).
CC {ECO:0000269|PubMed:21631530, ECO:0000269|PubMed:29084871}.
CC -!- DEVELOPMENTAL STAGE: In seedlings, observed in the root tips, root
CC vascular tissues and at the junction region of hypocotyl and root. In
CC flowers, mainly detected at the connection of petiole and stem, and in
CC young flower buds. Also present at low levels in sepals and pistils.
CC {ECO:0000269|PubMed:21631530}.
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 -!- DISRUPTION PHENOTYPE: Enhanced ethylene response, but altered salt
CC response during seed germination and plant growth leading to an
CC increased tolerance to salt stress (PubMed:21631530). Increased
CC susceptibility to dark and starvation, and to treatment with the TOR
CC inhibitor (PubMed:29084871). Decreased translation activity associated
CC with altered ribosome patterns, especially in the dark and starvation
CC conditions, in which mRNAs distribution is altered and rRNA abnormally
CC degraded (PubMed:29084871). Slightly early flowering time under long-
CC day conditions (PubMed:29084871). {ECO:0000269|PubMed:21631530,
CC ECO:0000269|PubMed:29084871}.
CC -!- SIMILARITY: Belongs to the PDCD4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB41120.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79390.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL049657; CAB41120.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161562; CAB79390.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84959.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84960.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84961.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM68168.1; -; Genomic_DNA.
DR EMBL; AY062102; AAL32978.1; -; mRNA.
DR EMBL; AY124878; AAM70587.1; -; mRNA.
DR EMBL; AK221703; BAD95421.1; -; mRNA.
DR PIR; T06664; T06664.
DR RefSeq; NP_001031708.1; NM_001036631.1.
DR RefSeq; NP_001190828.1; NM_001203899.1.
DR RefSeq; NP_001329945.1; NM_001341710.1.
DR RefSeq; NP_567708.1; NM_118613.3.
DR AlphaFoldDB; Q8W4Q4; -.
DR SMR; Q8W4Q4; -.
DR STRING; 3702.AT4G24800.3; -.
DR PaxDb; Q8W4Q4; -.
DR PRIDE; Q8W4Q4; -.
DR ProteomicsDB; 185731; -.
DR EnsemblPlants; AT4G24800.1; AT4G24800.1; AT4G24800.
DR EnsemblPlants; AT4G24800.2; AT4G24800.2; AT4G24800.
DR EnsemblPlants; AT4G24800.3; AT4G24800.3; AT4G24800.
DR EnsemblPlants; AT4G24800.4; AT4G24800.4; AT4G24800.
DR GeneID; 828582; -.
DR Gramene; AT4G24800.1; AT4G24800.1; AT4G24800.
DR Gramene; AT4G24800.2; AT4G24800.2; AT4G24800.
DR Gramene; AT4G24800.3; AT4G24800.3; AT4G24800.
DR Gramene; AT4G24800.4; AT4G24800.4; AT4G24800.
DR KEGG; ath:AT4G24800; -.
DR Araport; AT4G24800; -.
DR TAIR; locus:2126788; AT4G24800.
DR eggNOG; KOG0403; Eukaryota.
DR HOGENOM; CLU_013764_0_0_1; -.
DR InParanoid; Q8W4Q4; -.
DR OMA; IHEYFNS; -.
DR OrthoDB; 434771at2759; -.
DR PhylomeDB; Q8W4Q4; -.
DR PRO; PR:Q8W4Q4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8W4Q4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA: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:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
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 GO; GO:0009723; P:response to ethylene; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP: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; Ethylene signaling pathway; Nucleus; Reference proteome; Repeat;
KW Stress response; Translation regulation.
FT CHAIN 1..702
FT /note="MA3 DOMAIN-CONTAINING TRANSLATION REGULATORY FACTOR
FT 3"
FT /id="PRO_0000447576"
FT DOMAIN 116..237
FT /note="MI 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 280..401
FT /note="MI 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 414..535
FT /note="MI 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 577..697
FT /note="MI 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 267..274
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 615..622
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 11..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 633
FT /note="D -> G (in Ref. 4; BAD95421)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 702 AA; 77436 MW; B7A3BC9548854059 CRC64;
MEGFLTDQQR EMMKVATQTA DDLPPSQKPH SVLLEHLPKP SGGGKASGAS NAVKHRRSHA
GRSIRSKKDG GGGKGNWGKL IDTDGDYHID PNDPNYDSGE EPFELVGATL SDPLDDYKKA
AASIINEYFS TGDVDVAAAD LIELGSSEYH PYFIKRLVSV AMDRHDKEKE MASVLLSALY
ADVINPNQIR DGFVLLLESA DDFVVDIPDA VNVLALFLAR AVVDDILPPA FLPRAAKALP
ITSKGYQVVQ TAEKSYLSAA HHAELVERRW GGQTRTTVEE VKKKIADILN EYVETGETYE
ACRCVRELGV SFFHHEVVKR ALVTALENHA AEAPVLKLLN EAASENLISS SQMVKGFSRL
RESLDDLALD IPSARTKFGL IVPKAVSGGW LDASFGYPSG ECGRQQNEDE KLKRFKEDIV
TIIHEYFNSD DIPELIRSLE DLGAPEYNPI FLKKLITLAL DRKNHEKEMA SVLLSSLHIE
MFTTEDVADG FVMLLESAED TALDILDASN ELALFLARAV IDDVLAPFNL EEISSKLRPN
SSGTETVKMA RSLIFARHAG ERLLRCWGGG SGWAVEDAKD KISNLLEEYE SSGLVSEACK
CIHELGMPFF NHEVVKKALV MGMEKKKDKM MLDLLQESFS EGLITTNQMT KGFTRVKDGL
EDLALDIPNA KEKFNDYVEY GKKNGWVSSS FLTSLTEDAN VG
