MRL7_ARATH
ID MRL7_ARATH Reviewed; 331 AA.
AC F4JLC1; Q67XP3; Q9M0H2;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Thioredoxin-like fold domain-containing protein MRL7, chloroplastic {ECO:0000305};
DE AltName: Full=Protein EARLY CHLOROPLAST BIOGENESIS 1 {ECO:0000303|PubMed:23956074};
DE Short=AtECB1 {ECO:0000303|PubMed:23956074};
DE AltName: Full=Protein MESOPHYLL-CELL RNAI LIBRARY LINE 7 {ECO:0000303|PubMed:21515910};
DE Short=AtMRL7 {ECO:0000303|PubMed:21515910};
DE AltName: Full=Protein REGULATOR OF CHLOROPLAST BIOGENESIS {ECO:0000303|PubMed:31201314};
DE AltName: Full=Protein SUPPRESSOR OF VARIEGATION 4 {ECO:0000303|PubMed:21220584};
DE Flags: Precursor;
GN Name=MRL7 {ECO:0000303|PubMed:21515910};
GN Synonyms=ECB1 {ECO:0000303|PubMed:23956074},
GN RCB {ECO:0000303|PubMed:31201314}, SVR4 {ECO:0000303|PubMed:21220584};
GN OrderedLocusNames=At4g28590 {ECO:0000312|Araport:AT4G28590};
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] OF 5-331.
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP ARG-291.
RX PubMed=21220584; DOI=10.1093/mp/ssq074;
RA Yu F., Park S.S., Liu X., Foudree A., Fu A., Powikrowska M.,
RA Khrouchtchova A., Jensen P.E., Kriger J.N., Gray G.R., Rodermel S.R.;
RT "SUPPRESSOR OF VARIEGATION4, a new var2 suppressor locus, encodes a pioneer
RT protein that is required for chloroplast biogenesis.";
RL Mol. Plant 4:229-240(2011).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21515910; DOI=10.1093/pcp/pcr054;
RA Qiao J., Ma C., Wimmelbacher M., Boernke F., Luo M.;
RT "Two novel proteins, MRL7 and its paralog MRL7-L, have essential but
RT functionally distinct roles in chloroplast development and are involved in
RT plastid gene expression regulation in Arabidopsis.";
RL Plant Cell Physiol. 52:1017-1030(2011).
RN [6]
RP FUNCTION, INTERACTION WITH FSD2 AND PRDA1, AND SUBCELLULAR LOCATION.
RX PubMed=24132784; DOI=10.1093/pcp/pct148;
RA Qiao J., Li J., Chu W., Luo M.;
RT "PRDA1, a novel chloroplast nucleoid protein, is required for early
RT chloroplast development and is involved in the regulation of plastid gene
RT expression in Arabidopsis.";
RL Plant Cell Physiol. 54:2071-2084(2013).
RN [7]
RP FUNCTION, INTERACTION WITH FSD3 AND CITRX/TRXZ, INDUCTION BY LIGHT, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=23956074; DOI=10.1093/mp/sst092;
RA Yua Q.B., Ma Q., Kong M.M., Zhao T.T., Zhang X.L., Zhou Q., Huang C.,
RA Chong K., Yang Z.N.;
RT "AtECB1/MRL7, a thioredoxin-like fold protein with disulfide reductase
RT activity, regulates chloroplast gene expression and chloroplast biogenesis
RT in Arabidopsis thaliana.";
RL Mol. Plant 7:206-217(2014).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24111559; DOI=10.1111/ppl.12108;
RA Powikrowska M., Khrouchtchova A., Martens H.J., Zygadlo-Nielsen A.,
RA Melonek J., Schulz A., Krupinska K., Rodermel S., Jensen P.E.;
RT "SVR4 (suppressor of variegation 4) and SVR4-like: two proteins with a role
RT in proper organization of the chloroplast genetic machinery.";
RL Physiol. Plantarum 150:477-492(2014).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=31201314; DOI=10.1038/s41467-019-10517-1;
RA Yang E.J., Yoo C.Y., Liu J., Wang H., Cao J., Li F.W., Pryer K.M.,
RA Sun T.P., Weigel D., Zhou P., Chen M.;
RT "NCP activates chloroplast transcription by controlling phytochrome-
RT dependent dual nuclear and plastidial switches.";
RL Nat. Commun. 10:2630-2630(2019).
CC -!- FUNCTION: Plays an essential role in early steps of chloroplast
CC development (PubMed:21220584, PubMed:21515910, PubMed:23956074,
CC PubMed:24111559). Involved in the regulation of plastid gene expression
CC (PubMed:21515910, PubMed:23956074, PubMed:24111559). May positively
CC regulate plastid-encoded RNA polymerase (PEP) activity through binding
CC to FSD3 and CITRX/TRXZ (PubMed:23956074). Involved in redox-mediated
CC regulation of chloroplast development (PubMed:24132784,
CC PubMed:23956074). Possesses disulfide reductase activity in vitro
CC (PubMed:23956074). Required for the proper function of the plastid
CC transcriptional machinery and protein accumulation in thylakoid
CC membranes. May function as molecular chaperone to ensure proper
CC organization of the nucleoids in chloroplasts (PubMed:24111559). May
CC mediate some aspect of thylakoid structure or function that controls
CC non-photochemical quenching (NPQ) (PubMed:21220584, PubMed:21515910,
CC PubMed:23956074, PubMed:24111559, PubMed:24132784). Participates in the
CC early light signaling events of photobody biogenesis in chloroplasts
CC (PubMed:31201314). May mediate the degradation of two repressors of
CC chloroplast biogenesis, PIF1 and PIF3 in nucleus (PubMed:31201314).
CC {ECO:0000269|PubMed:21220584, ECO:0000269|PubMed:21515910,
CC ECO:0000269|PubMed:23956074, ECO:0000269|PubMed:24111559,
CC ECO:0000269|PubMed:24132784, ECO:0000269|PubMed:31201314}.
CC -!- SUBUNIT: Component of the transcriptionally active chromosome (TAC)
CC complexes (PubMed:24111559). Interacts with FSD2 and PRDA1
CC (PubMed:24132784). Interacts with FSD3 and CITRX/TRXZ
CC (PubMed:23956074). {ECO:0000269|PubMed:23956074,
CC ECO:0000269|PubMed:24111559, ECO:0000269|PubMed:24132784}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:21220584, ECO:0000269|PubMed:24111559}. Plastid,
CC chloroplast stroma, chloroplast nucleoid {ECO:0000269|PubMed:21515910,
CC ECO:0000269|PubMed:24132784, ECO:0000269|PubMed:31201314}. Nucleus
CC {ECO:0000269|PubMed:31201314}. Note=Associated with punctuate
CC structures in chloroplasts. {ECO:0000269|PubMed:21220584}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, shoots, stems, cauline leaves,
CC flower buds, flowers and siliques. {ECO:0000269|PubMed:21515910}.
CC -!- INDUCTION: Induced by light. {ECO:0000269|PubMed:23956074}.
CC -!- DISRUPTION PHENOTYPE: Seedling lethality due to deficiency in
CC chloroplast development. {ECO:0000269|PubMed:21220584,
CC ECO:0000269|PubMed:21515910, ECO:0000269|PubMed:23956074}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB81447.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL161573; CAB81447.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85510.1; -; Genomic_DNA.
DR EMBL; AK176513; BAD44276.1; -; mRNA.
DR EMBL; AK176775; BAD44538.1; -; mRNA.
DR PIR; T10653; T10653.
DR RefSeq; NP_194588.2; NM_119001.4.
DR AlphaFoldDB; F4JLC1; -.
DR SMR; F4JLC1; -.
DR STRING; 3702.AT4G28590.1; -.
DR PaxDb; F4JLC1; -.
DR PRIDE; F4JLC1; -.
DR ProteomicsDB; 238993; -.
DR EnsemblPlants; AT4G28590.1; AT4G28590.1; AT4G28590.
DR GeneID; 828977; -.
DR Gramene; AT4G28590.1; AT4G28590.1; AT4G28590.
DR KEGG; ath:AT4G28590; -.
DR Araport; AT4G28590; -.
DR TAIR; locus:2139850; AT4G28590.
DR eggNOG; ENOG502QQCJ; Eukaryota.
DR HOGENOM; CLU_072426_1_0_1; -.
DR InParanoid; F4JLC1; -.
DR OMA; NWVKEIN; -.
DR OrthoDB; 1109560at2759; -.
DR PRO; PR:F4JLC1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JLC1; baseline and differential.
DR GO; GO:0042644; C:chloroplast nucleoid; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:TAIR.
DR InterPro; IPR044701; MRL7/MRL7L.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR34669; PTHR34669; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Nucleus; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..59
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 60..331
FT /note="Thioredoxin-like fold domain-containing protein
FT MRL7, chloroplastic"
FT /id="PRO_0000439380"
FT REGION 52..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..160
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 291
FT /note="R->W: In svr4-1; retarded growth, pale green leaves
FT and enhanced non-photochemical quenching (NPQ)."
FT /evidence="ECO:0000269|PubMed:21220584"
FT CONFLICT 145
FT /note="E -> G (in Ref. 3; BAD44276/BAD44538)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 331 AA; 38241 MW; 5F1F5E2927C0F419 CRC64;
MSFFAVACSA PRSSMLLTGL NSSFSDMHRS PLFVFPVTIS SRSVKRFAAV SSDSVLDPES
KNQTRSRRKN KEAVTPIAET ENNEKFPTKV PRKSKRGRRS EADAVEDYVR SSLERTFSTI
KEQNPEVFEN KEKANFIKDR GVDEEEEEEE EMVVEEEDPD WPVDTDVGWG IKASEYFDTH
PIKNVVGDDG SEIDWEGEID DSWVKEINCL EWESFAFHPS PLVVLVFERY KRASDNWKTL
KELEKAIKVY WDAKDRLPPR AVKIDLNIET DLAYALKAKE CPQILFLRGN RILYREKDFR
TADELVHMIA HFYYKAKRPS CVDKANVTPY C
