FLU_ARATH
ID FLU_ARATH Reviewed; 316 AA.
AC Q940U6; B9DI70; Q9LJH7;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Protein FLUORESCENT IN BLUE LIGHT, chloroplastic;
DE Flags: Precursor;
GN Name=FLU; OrderedLocusNames=At3g14110; ORFNames=MAG2.7;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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] (ISOFORM 1).
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] (ISOFORM 1).
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-316 (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ALA-146 AND ALA-262, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=11606728; DOI=10.1073/pnas.221252798;
RA Meskauskiene R., Nater M., Goslings D., Kessler F., op den Camp R.G.L.,
RA Apel K.;
RT "FLU: a negative regulator of chlorophyll biosynthesis in Arabidopsis
RT thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12826-12831(2001).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14508004; DOI=10.1105/tpc.014662;
RA op den Camp R.G.L., Przybyla D., Ochsenbein C., Laloi C., Kim C., Danon A.,
RA Wagner D., Hideg E., Goebel C., Feussner I., Nater M., Apel K.;
RT "Rapid induction of distinct stress responses after the release of singlet
RT oxygen in Arabidopsis.";
RL Plant Cell 15:2320-2332(2003).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ALA-262, AND INTERACTION
RP WITH HEMA1 AND HEMA2.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=15584960; DOI=10.1111/j.1365-313x.2004.02262.x;
RA Goslings D., Meskauskiene R., Kim C., Lee K.P., Nater M., Apel K.;
RT "Concurrent interactions of heme and FLU with Glu tRNA reductase (HEMA1),
RT the target of metabolic feedback inhibition of tetrapyrrole biosynthesis,
RT in dark- and light-grown Arabidopsis plants.";
RL Plant J. 40:957-967(2004).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=18182022; DOI=10.1111/j.1365-313x.2008.03409.x;
RA Przybyla D., Goebel C., Imboden A., Hamberg M., Feussner I., Apel K.;
RT "Enzymatic, but not non-enzymatic, 1O2-mediated peroxidation of
RT polyunsaturated fatty acids forms part of the EXECUTER1-dependent stress
RT response program in the flu mutant of Arabidopsis thaliana.";
RL Plant J. 54:236-248(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [11]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE FLU-CONTAINING CHLOROPLAST
RP MEMBRANE COMPLEX.
RX PubMed=22212719; DOI=10.1016/j.febslet.2011.12.029;
RA Kauss D., Bischof S., Steiner S., Apel K., Meskauskiene R.;
RT "FLU, a negative feedback regulator of tetrapyrrole biosynthesis, is
RT physically linked to the final steps of the Mg(++)-branch of this
RT pathway.";
RL FEBS Lett. 586:211-216(2012).
CC -!- FUNCTION: Negative regulator of tetrapyrrole biosynthesis (including
CC chlorophyll) in chloroplasts, probably via HEMA1 repression. Inhibits
CC especially the magnesium ion Mg(2+) branch of tetrapyrrole
CC biosynthesis, but independently of heme. {ECO:0000269|PubMed:11606728,
CC ECO:0000269|PubMed:14508004, ECO:0000269|PubMed:15584960,
CC ECO:0000269|PubMed:18182022}.
CC -!- SUBUNIT: Part of the FLU-containing chloroplast membrane complex
CC composed of FLU, CRD1, PORB, PORC, CHLP and HEMA1. Interacts with HEMA1
CC (via C-terminus) only in the absence of light. No interaction with
CC HEMA2. {ECO:0000269|PubMed:15584960, ECO:0000269|PubMed:22212719}.
CC -!- INTERACTION:
CC Q940U6; Q9M591: CRD1; NbExp=5; IntAct=EBI-2319882, EBI-7632098;
CC Q940U6; P42804: HEMA1; NbExp=3; IntAct=EBI-2319882, EBI-2319900;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:18431481}; Single-pass membrane protein. Plastid,
CC chloroplast thylakoid membrane; Single-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q940U6-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Loss of ability to restrict the accumulation of
CC protochloro-phyllide (Pchlide) and delta-amin-olevulinic acid (ALA) in
CC the dark, leading to a strong Pchlide fluorescence in etiolated mutant
CC seedlings exposed to blue light. Rapid bleaching and death of plants
CC transferred from the dark to the light, mediated by singlet oxygen
CC production and enzymatic peroxidation of linolenic acid.
CC {ECO:0000269|PubMed:11606728, ECO:0000269|PubMed:14508004,
CC ECO:0000269|PubMed:15584960, ECO:0000269|PubMed:18182022}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02975.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP000600; BAB02975.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75470.1; -; Genomic_DNA.
DR EMBL; AF446890; AAL38623.1; -; mRNA.
DR EMBL; AY052677; AAK96581.1; -; mRNA.
DR EMBL; AY087529; AAM65071.1; -; mRNA.
DR EMBL; AK317782; BAH20437.1; -; mRNA.
DR RefSeq; NP_566478.1; NM_112267.4. [Q940U6-1]
DR PDB; 4YVO; X-ray; 1.45 A; A=189-316.
DR PDB; 4YVQ; X-ray; 2.40 A; C=195-316.
DR PDB; 5CHE; X-ray; 3.20 A; E/F=195-316.
DR PDBsum; 4YVO; -.
DR PDBsum; 4YVQ; -.
DR PDBsum; 5CHE; -.
DR AlphaFoldDB; Q940U6; -.
DR SMR; Q940U6; -.
DR BioGRID; 5962; 1.
DR IntAct; Q940U6; 5.
DR MINT; Q940U6; -.
DR STRING; 3702.AT3G14110.3; -.
DR PaxDb; Q940U6; -.
DR PRIDE; Q940U6; -.
DR ProteomicsDB; 230523; -. [Q940U6-1]
DR EnsemblPlants; AT3G14110.1; AT3G14110.1; AT3G14110. [Q940U6-1]
DR GeneID; 820628; -.
DR Gramene; AT3G14110.1; AT3G14110.1; AT3G14110. [Q940U6-1]
DR KEGG; ath:AT3G14110; -.
DR Araport; AT3G14110; -.
DR eggNOG; ENOG502QTEG; Eukaryota.
DR InParanoid; Q940U6; -.
DR PhylomeDB; Q940U6; -.
DR PRO; PR:Q940U6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q940U6; baseline and differential.
DR Genevisible; Q940U6; AT.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:InterPro.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR044243; FLU.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR47310; PTHR47310; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chloroplast; Coiled coil; Membrane;
KW Plastid; Reference proteome; Repeat; Thylakoid; TPR repeat;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..26
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 27..316
FT /note="Protein FLUORESCENT IN BLUE LIGHT, chloroplastic"
FT /id="PRO_0000407552"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 203..236
FT /note="TPR 1"
FT REPEAT 243..276
FT /note="TPR 2"
FT REPEAT 283..316
FT /note="TPR 3"
FT COILED 144..175
FT /evidence="ECO:0000255"
FT MUTAGEN 146
FT /note="A->V: In flu1-4; rapid bleaching and death when
FT transferred from the dark to the light, accumulation of
FT Pchlide and ALA."
FT /evidence="ECO:0000269|PubMed:11606728"
FT MUTAGEN 262
FT /note="A->V: In flu1-1; rapid bleaching and death when
FT transferred from the dark to the light, accumulation of
FT Pchlide and ALA, and impaired HEMA1 interaction."
FT /evidence="ECO:0000269|PubMed:11606728,
FT ECO:0000269|PubMed:15584960"
FT CONFLICT 97
FT /note="M -> L (in Ref. 5; BAH20437)"
FT /evidence="ECO:0000305"
FT HELIX 199..215
FT /evidence="ECO:0007829|PDB:4YVO"
FT HELIX 219..235
FT /evidence="ECO:0007829|PDB:4YVO"
FT HELIX 239..255
FT /evidence="ECO:0007829|PDB:4YVO"
FT HELIX 259..276
FT /evidence="ECO:0007829|PDB:4YVO"
FT HELIX 282..295
FT /evidence="ECO:0007829|PDB:4YVO"
FT HELIX 299..313
FT /evidence="ECO:0007829|PDB:4YVO"
SQ SEQUENCE 316 AA; 34587 MW; 8A647B74684B6514 CRC64;
MAALIRCCSS FSHTSGGQPP PRDKSRAPEI GKFATSIGYS VVRKPGDHPP FSKIIHSSSQ
PKERQGKGIL QTPFASVGSL DKFSAFEGIG RLKLPVMAVL LTNSLQMATP LEALAAEICE
PESSMFSMPI LLLVALIGAT VGGLLARQRK GELQRLNEQL RQINAALRRQ AKIESYAPSL
SYAPVGARIP DSEIIVEPKK QELISKLKTG KTFLRNQEPE KAYTEFKIAL ELAQSLKDPT
EEKKAARGLG ASLQRQGKYR EAIQYHSMVL AISKRESEDS GITEAYGAIA DCYTELGDLE
KAGKFYDTYI ARLETD
