MRL7L_ARATH
ID MRL7L_ARATH Reviewed; 350 AA.
AC Q9SKB6; Q84RF5;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Thioredoxin-like fold domain-containing protein MRL7L, chloroplastic {ECO:0000305};
DE AltName: Full=Protein MESOPHYLL-CELL RNAI LIBRARY LINE 7-LIKE {ECO:0000303|PubMed:21515910};
DE Short=AtMRL7-L {ECO:0000303|PubMed:21515910};
DE AltName: Full=Protein NUCLEAR CONTROL OF PEP ACTIVITY {ECO:0000303|PubMed:31201314};
DE AltName: Full=Protein SUPPRESSOR OF VARIEGATION 4-LIKE {ECO:0000303|PubMed:24111559};
DE Flags: Precursor;
GN Name=MRL7L {ECO:0000303|PubMed:21515910};
GN Synonyms=NCP {ECO:0000303|PubMed:31201314},
GN SVR4L {ECO:0000303|PubMed:24111559};
GN OrderedLocusNames=At2g31840 {ECO:0000312|Araport:AT2G31840};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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=12481096; DOI=10.1104/pp.010207;
RA Xiao Y.-L., Malik M., Whitelaw C.A., Town C.D.;
RT "Cloning and sequencing of cDNAs for hypothetical genes from chromosome 2
RT of Arabidopsis.";
RL Plant Physiol. 130:2118-2128(2002).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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 [6]
RP STRUCTURE BY NMR OF 208-350, FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
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:21515910, PubMed:24111559). Involved in the
CC regulation of plastid gene expression (PubMed:21515910,
CC PubMed:24111559). Required for the proper function of the plastid
CC transcriptional machinery and protein accumulation in thylakoid
CC membranes (PubMed:21515910, PubMed:24111559). May function as molecular
CC chaperone to ensure proper organization of the nucleoids in
CC chloroplasts (PubMed:21515910, PubMed:24111559). Is a necessary
CC component of phytochrome signaling for photosynthesis-associated
CC plastid-encoded genes (PhAPGs) activation (PubMed:31201314). Mediates
CC the degradation of two repressors of chloroplast biogenesis, PIF1 and
CC PIF3 in nucleus (PubMed:31201314). Promotes the assembly of the
CC plastid-encoded RNA polymerase (PEP) complex for PhAPG transcription in
CC plastids (PubMed:31201314). {ECO:0000269|PubMed:21515910,
CC ECO:0000269|PubMed:24111559, ECO:0000269|PubMed:31201314}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:21515910, ECO:0000269|PubMed:24111559,
CC ECO:0000269|PubMed:31201314}. Nucleus {ECO:0000269|PubMed:31201314}.
CC -!- DISRUPTION PHENOTYPE: Seedling lethality due to deficiency in
CC chloroplast development. {ECO:0000269|PubMed:24111559}.
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DR EMBL; AC006533; AAD32288.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08592.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62918.1; -; Genomic_DNA.
DR EMBL; AY247801; AAO89195.1; -; mRNA.
DR PIR; G84725; G84725.
DR RefSeq; NP_001325041.1; NM_001336349.1.
DR RefSeq; NP_180743.1; NM_128742.3.
DR PDB; 6NE8; NMR; -; A=208-350.
DR PDBsum; 6NE8; -.
DR AlphaFoldDB; Q9SKB6; -.
DR SMR; Q9SKB6; -.
DR STRING; 3702.AT2G31840.1; -.
DR iPTMnet; Q9SKB6; -.
DR PaxDb; Q9SKB6; -.
DR PRIDE; Q9SKB6; -.
DR ProteomicsDB; 250861; -.
DR EnsemblPlants; AT2G31840.1; AT2G31840.1; AT2G31840.
DR EnsemblPlants; AT2G31840.2; AT2G31840.2; AT2G31840.
DR GeneID; 817741; -.
DR Gramene; AT2G31840.1; AT2G31840.1; AT2G31840.
DR Gramene; AT2G31840.2; AT2G31840.2; AT2G31840.
DR KEGG; ath:AT2G31840; -.
DR Araport; AT2G31840; -.
DR TAIR; locus:2045208; AT2G31840.
DR eggNOG; ENOG502QPQP; Eukaryota.
DR HOGENOM; CLU_072426_0_1_1; -.
DR InParanoid; Q9SKB6; -.
DR OMA; DLTTVEW; -.
DR OrthoDB; 1314217at2759; -.
DR PhylomeDB; Q9SKB6; -.
DR PRO; PR:Q9SKB6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SKB6; baseline and differential.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
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 3D-structure; Chloroplast; Nucleus; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..350
FT /note="Thioredoxin-like fold domain-containing protein
FT MRL7L, chloroplastic"
FT /id="PRO_0000439382"
FT REGION 78..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..201
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 22
FT /note="S -> P (in Ref. 3; AAO89195)"
FT /evidence="ECO:0000305"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:6NE8"
FT HELIX 222..226
FT /evidence="ECO:0007829|PDB:6NE8"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:6NE8"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:6NE8"
FT HELIX 246..264
FT /evidence="ECO:0007829|PDB:6NE8"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:6NE8"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:6NE8"
FT HELIX 280..286
FT /evidence="ECO:0007829|PDB:6NE8"
FT STRAND 290..297
FT /evidence="ECO:0007829|PDB:6NE8"
FT STRAND 299..306
FT /evidence="ECO:0007829|PDB:6NE8"
FT HELIX 312..323
FT /evidence="ECO:0007829|PDB:6NE8"
FT HELIX 330..333
FT /evidence="ECO:0007829|PDB:6NE8"
SQ SEQUENCE 350 AA; 40540 MW; F40D6B229FE3569C CRC64;
MILPFSTQFT CPVQDNGFSP SSLLSHCKRD RFEVTSLRYD SFGSVKTASS SKWNVMRSRR
NVKAFGLVDK LGKKVWRKKE EDSDSEDEED EVKEETFGGK EASLDDPVER REWRKTIREV
IDKHPDIEED EEIDMVEKRR KMQKLLADYP LVVNEEDPNW PEDADGWGFS FNQFFNKITI
KNEKKEEEDD DEDSEGDDSE KEIVWQDDNY IRPIKDLTTA EWEEAVFKDI SPLMVLVHNR
YKRPKENEKF REELEKAIQV IWNCGLPSPR CVAVDAVVET DLVSALKVSV FPEIIFTKAG
KILYREKGIR TADELSKIMA FFYYGAAKPP CLNGVVNSQE QIPLVDVSVN
