MTEF5_ARATH
ID MTEF5_ARATH Reviewed; 493 AA.
AC F4JVI3;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Transcription termination factor MTERF5, chloroplastic {ECO:0000305};
DE AltName: Full=Mitochondrial transcription termination factor 5 {ECO:0000303|PubMed:23087700};
DE Short=mTERF5 {ECO:0000303|PubMed:23087700};
DE AltName: Full=Protein MTERF DEFECTIVE IN ARABIDOPSIS 1 {ECO:0000303|PubMed:22905186};
DE Flags: Precursor;
GN Name=MTERF5 {ECO:0000303|PubMed:23087700};
GN Synonyms=MDA1 {ECO:0000303|PubMed:22905186};
GN OrderedLocusNames=At4g14605 {ECO:0000312|Araport:AT4G14605};
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
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 [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;
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=21464319; DOI=10.1073/pnas.1103442108;
RA Babiychuk E., Vandepoele K., Wissing J., Garcia-Diaz M., De Rycke R.,
RA Akbari H., Joubes J., Beeckman T., Jaensch L., Frentzen M.,
RA Van Montagu M.C., Kushnir S.;
RT "Plastid gene expression and plant development require a plastidic protein
RT of the mitochondrial transcription termination factor family.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:6674-6679(2011).
RN [6]
RP GENE FAMILY.
RX PubMed=23087700; DOI=10.3389/fpls.2012.00233;
RA Kleine T.;
RT "Arabidopsis thaliana mTERF proteins: evolution and functional
RT classification.";
RL Front. Plant Sci. 3:233-233(2012).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22905186; DOI=10.1371/journal.pone.0042924;
RA Robles P., Micol J.L., Quesada V.;
RT "Arabidopsis MDA1, a nuclear-encoded protein, functions in chloroplast
RT development and abiotic stress responses.";
RL PLoS ONE 7:E42924-E42924(2012).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH PTAC6, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=31128276; DOI=10.1016/j.molp.2019.05.007;
RA Ding S., Zhang Y., Hu Z., Huang X., Zhang B., Lu Q., Wen X., Wang Y.,
RA Lu C.;
RT "mTERF5 acts as a transcriptional pausing factor to positively regulate
RT transcription of chloroplast psbEFLJ.";
RL Mol. Plant 12:1259-1277(2019).
CC -!- FUNCTION: Transcription termination factor required for processing and
CC steady-state levels of plastid transcripts (PubMed:22905186). Involved
CC also in chloroplast transcriptional pausing, a general feature of
CC chloroplast genes (PubMed:31128276). Specifically and positively
CC regulates the transcription of chloroplast psbEFLJ encoding for
CC photosystem II (PSII) core subunits psbE, psbF, psbL and psbJ; causes
CC the plastid-encoded RNA polymerase (PEP) complex to pause at psbEFLJ by
CC binding to the +30 to +51 region of double-stranded DNA, and recruits
CC additional pTAC6 to the transcriptionally paused region of psbEFLJ
CC (PubMed:31128276). May play a role in response to abiotic stresses
CC (PubMed:22905186). {ECO:0000269|PubMed:22905186,
CC ECO:0000269|PubMed:31128276}.
CC -!- SUBUNIT: Interacts with pTAC6. {ECO:0000269|PubMed:31128276}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:21464319, ECO:0000269|PubMed:31128276}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette leaves, cauline leaves,
CC stems, flower buds and open flowers. {ECO:0000269|PubMed:22905186}.
CC -!- DISRUPTION PHENOTYPE: Pale-green phenotype, reduced growth and altered
CC structure of chloroplasts (PubMed:22905186, PubMed:31128276). Defect in
CC photosystem II (PSII) function with strongly reduced levels of core
CC subunits, including psbE, psbF, psbL and psbJ cotranscribed from
CC psbEFLJ (PubMed:31128276). Enhanced osmotic stress tolerance and
CC altered sugar responses during seedling establishment
CC (PubMed:22905186). {ECO:0000269|PubMed:22905186,
CC ECO:0000269|PubMed:31128276}.
CC -!- SIMILARITY: Belongs to the mTERF family. {ECO:0000305}.
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DR EMBL; Z97336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002687; AEE83465.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66035.1; -; Genomic_DNA.
DR EMBL; AK226653; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001327961.1; NM_001340949.1.
DR RefSeq; NP_567435.4; NM_117541.9.
DR AlphaFoldDB; F4JVI3; -.
DR SMR; F4JVI3; -.
DR IntAct; F4JVI3; 2.
DR STRING; 3702.AT4G14605.1; -.
DR PaxDb; F4JVI3; -.
DR PRIDE; F4JVI3; -.
DR ProteomicsDB; 250906; -.
DR EnsemblPlants; AT4G14605.1; AT4G14605.1; AT4G14605.
DR EnsemblPlants; AT4G14605.2; AT4G14605.2; AT4G14605.
DR GeneID; 827109; -.
DR Gramene; AT4G14605.1; AT4G14605.1; AT4G14605.
DR Gramene; AT4G14605.2; AT4G14605.2; AT4G14605.
DR KEGG; ath:AT4G14605; -.
DR Araport; AT4G14605; -.
DR TAIR; locus:505006461; AT4G14605.
DR eggNOG; KOG1267; Eukaryota.
DR HOGENOM; CLU_028077_0_0_1; -.
DR InParanoid; F4JVI3; -.
DR OMA; RYALMKE; -.
DR OrthoDB; 702815at2759; -.
DR PhylomeDB; F4JVI3; -.
DR PRO; PR:F4JVI3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JVI3; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0032502; P:developmental process; IBA:GO_Central.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
DR GO; GO:0042793; P:plastid transcription; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR Gene3D; 1.25.70.10; -; 1.
DR InterPro; IPR003690; MTERF.
DR InterPro; IPR038538; MTERF_sf.
DR PANTHER; PTHR13068; PTHR13068; 1.
DR Pfam; PF02536; mTERF; 2.
DR SMART; SM00733; Mterf; 8.
PE 1: Evidence at protein level;
KW Chloroplast; DNA-binding; Plastid; Reference proteome; Transcription;
KW Transcription regulation; Transcription termination; Transit peptide.
FT TRANSIT 1..43
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 44..493
FT /note="Transcription termination factor MTERF5,
FT chloroplastic"
FT /id="PRO_0000436198"
SQ SEQUENCE 493 AA; 55961 MW; 78EC32BA025C831E CRC64;
MQSLSQLGPS EIFLVARREK PSTRAQLWFT GRLSFRQETN GIRLKNRVEF SPRPVPPNLI
AAEKEEAKAV LTLFFKKQGL SNSLSSRLIN KSDLFIDHLV SRLHSVHKAR YLVGRELTTL
EIRDSLIPYL EQLHEEHGDL LAELVVSFPD PPAEPRLVAS SPVSVLPPRG DTDSAADTRK
LRAVSRVSEL DTEGALRPQT LYLLDLGLNL EQIKTITRKF AAFPYYSLDG KIKPVVEFLL
DLGIPKSDIP TILCKRPQIC GISLTDNLKP TMAFLETLGI DKNQWAKIIS RFPAILTYSR
QKLTSTVEFL SQTGLTEEQI GRILTRCPNI MSYSVEDKLR PTMEYFRSLN VDVAVLLHRC
PQTFGLSIES NLKPVTEFFL EKGFGLDEIG IMISRYGALY TFSLKENVMP KWDYFQTMDY
PKSELVKFPQ FFGYSLQERI KPRYELVQRS GVRLLLNQVL SLSGIEFEKV VKKKMMKLVS
NNVIAEQSSG GLL